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Conserved domains on  [gi|1370507705|ref|XP_024302145|]
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cyclin-dependent kinase 19 isoform X2 [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
1-275 0e+00

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd07867:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 318  Bit Score: 573.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd07867    44 MSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIH 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd07867   124 YLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKH 240
Cdd:cd07867   204 GCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKH 283
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 241 KVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07867   284 KVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 318
 
Name Accession Description Interval E-value
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
1-275 0e+00

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: 573.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd07867    44 MSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIH 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd07867   124 YLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKH 240
Cdd:cd07867   204 GCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKH 283
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 241 KVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07867   284 KVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 318
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
2-275 1.45e-65

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 210.85  E-value: 1.45e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705    2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIH 80
Cdd:smart00220  43 RILREIKILKKLKHPNIVRLYDVF--EDEDKLYLVMEYCEGgDLFDLLKKRGR---------LSEDEARFYLRQILSALE 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   81 YLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGaRHYTKAIDIWAI 160
Cdd:smart00220 112 YLHSKGIVHRDLKPENILLD----EDGHVKLADFGLARQLDPGEK----LTTFVGTPEYMAPEVLLG-KGYGKAVDIWSL 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  161 GCIFAELLTSEPIFHcrqediktsnpfHHDQLDRIFSVMGFPadkdweDIRKMPEYPTLQKDFRRttyansslikymekh 240
Cdd:smart00220 183 GVILYELLTGKPPFP------------GDDQLLELFKKIGKP------KPPFPPPEWDISPEAKD--------------- 229
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1370507705  241 kvkpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:smart00220 230 ----------LIRKLLVKDPEKRLTAEEALQHPFF 254
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
5-281 2.81e-59

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 196.91  E-value: 2.81e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEHDLWHIIkfhraskaNKKpMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:PTZ00024   69 RELKIMNEIKHENIMGLVDVYVEGD--FINLVMDIMASDLKKVV--------DRK-IRLTESQVKCILLQILNGLNVLHK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPL-----------KPLADLDPVVVTFWYRAPELLLGARHYTK 153
Cdd:PTZ00024  138 WYFMHRDLSPANIFI----NSKGICKIADFGLARRYGYPPysdtlskdetmQRREEMTSKVVTLWYRAPELLMGAEKYHF 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWEDIRKMPEY----PTLQKDFRRT-TY 228
Cdd:PTZ00024  214 AVDMWSVGCIFAELLTGKPLFPGENE---------IDQLGRIFELLGTPNEDNWPQAKKLPLYteftPRKPKDLKTIfPN 284
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370507705 229 ANSSLIKymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYFQEDPLP 281
Cdd:PTZ00024  285 ASDDAID---------------LLQSLLKLNPLERISAKEALKHEYFKSDPLP 322
Pkinase pfam00069
Protein kinase domain;
1-275 7.23e-31

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 118.12  E-value: 7.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAEH-DLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGi 79
Cdd:pfam00069  43 KNILREIKILKKLNHPNIVRLYDAFEDKDN--LYLVLEYVEGgSLFDLLSEKGA---------FSEREAKFIMKQILEG- 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 hylhanwvlhrdlkpanilvmgegpergrvkiadmgfarlfnspLKPLADLDPVVVTFWYRAPELLlGARHYTKAIDIWA 159
Cdd:pfam00069 111 --------------------------------------------LESGSSLTTFVGTPWYMAPEVL-GGNPYGPKVDVWS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 160 IGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFSVMGFpadkdwEDIRKMPEYPTLQKDFRRttyansslikymek 239
Cdd:pfam00069 146 LGCILYELLTGKP-------------PFPGINGNEIYELIID------QPYAFPELPSNLSEEAKD-------------- 192
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1370507705 240 hkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:pfam00069 193 -----------LLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
5-175 1.03e-30

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 123.58  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAE-HDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:COG0515    56 REARALARLNHPNIVRVYDVG--EEDGRPYLVMEYVEgESLADLLRRRGP---------LPPAEALRILAQLAEALAAAH 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPlkPLADLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCI 163
Cdd:COG0515   125 AAGIVHRDIKPANILLT----PDGRVKLIDFGIARALGGA--TLTQTGTVVGTPGYMAPEQARGEP-VDPRSDVYSLGVT 197
                         170
                  ....*....|..
gi 1370507705 164 FAELLTSEPIFH 175
Cdd:COG0515   198 LYELLTGRPPFD 209
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
5-173 1.09e-12

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 70.26  E-value: 1.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705    5 REIALLRELKHPNVIALqkvfLSHSDRKVWLLFDYAEHDLWHIIkfhRASKANKKPmqLPRSMVKSLLYQILDGIHYLHA 84
Cdd:TIGR03903   27 RETALCARLYHPNIVAL----LDSGEAPPGLLFAVFEYVPGRTL---REVLAADGA--LPAGETGRLMLQVLDALACAHN 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   85 NWVLHRDLKPANILVMGEGPERgRVKIADMGFARLfnspLKPLADLD--------PVVVTFWYRAPELLLGaRHYTKAID 156
Cdd:TIGR03903   98 QGIVHRDLKPQNIMVSQTGVRP-HAKVLDFGIGTL----LPGVRDADvatltrttEVLGTPTYCAPEQLRG-EPVTPNSD 171
                          170
                   ....*....|....*..
gi 1370507705  157 IWAIGCIFAELLTSEPI 173
Cdd:TIGR03903  172 LYAWGLIFLECLTGQRV 188
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
74-174 5.81e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 67.51  E-value: 5.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPlkPLADLDPVVVTFWYRAPELllgARH--Y 151
Cdd:NF033483  115 QILSALEHAHRNGIVHRDIKPQNILIT----KDGRVKVTDFGIARALSST--TMTQTNSVLGTVHYLSPEQ---ARGgtV 185
                          90       100
                  ....*....|....*....|...
gi 1370507705 152 TKAIDIWAIGCIFAELLTSEPIF 174
Cdd:NF033483  186 DARSDIYSLGIVLYEMLTGRPPF 208
 
Name Accession Description Interval E-value
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
1-275 0e+00

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: 573.94  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd07867    44 MSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIH 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd07867   124 YLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKH 240
Cdd:cd07867   204 GCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKH 283
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 241 KVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07867   284 KVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 318
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
1-275 0e+00

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: 553.43  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKAnkkpMQLPRSMVKSLLYQILDGIH 80
Cdd:cd07842    47 QSACREIALLRELKHENVVSLVEVFLEHADKSVYLLFDYAEHDLWQIIKFHRQAKR----VSIPPSMVKSLLWQILNGIH 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd07842   123 YLHSNWVLHRDLKPANILVMGEGPERGVVKIGDLGLARLFNAPLKPLADLDPVVVTIWYRAPELLLGARHYTKAIDIWAI 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKH 240
Cdd:cd07842   203 GCIFAELLTLEPIFKGREAKIKKSNPFQRDQLERIFEVLGTPTEKDWPDIKKMPEYDTLKSDTKASTYPNSLLAKWMHKH 282
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 241 KvKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07842   283 K-KPDSQGFDLLRKLLEYDPTKRITAEEALEHPYF 316
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
1-275 0e+00

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: 535.41  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd07868    59 MSACREIALLRELKHPNVISLQKVFLSHADRKVWLLFDYAEHDLWHIIKFHRASKANKKPVQLPRGMVKSLLYQILDGIH 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd07868   139 YLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKYMEKH 240
Cdd:cd07868   219 GCIFAELLTSEPIFHCRQEDIKTSNPYHHDQLDRIFNVMGFPADKDWEDIKKMPEHSTLMKDFRRNTYTNCSLIKYMEKH 298
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 241 KVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07868   299 KVKPDSKAFHLLQKLLTMDPIKRITSEQAMQDPYF 333
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
1-275 6.28e-110

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: 6.28e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIKfhraskanKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd07829    43 STALREISLLKELKHPNIVKLLDVI--HTENKLYLVFEYCDQDLKKYLD--------KRPGPLPPNLIKSIMYQLLRGLA 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKPLadlDPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd07829   113 YCHSHRILHRDLKPQNLLIN----RDGVLKLADFGLARAFGIPLRTY---THEVVTLWYRAPEILLGSKHYSTAVDIWSV 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWEDIRKMPEYptlQKDFRRttYANSSLIKYMEKH 240
Cdd:cd07829   186 GCIFAELITGKPLFPGDSE---------IDQLFKIFQILGTPTEESWPGVTKLPDY---KPTFPK--WPKNDLEKVLPRL 251
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 241 kvkpDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07829   252 ----DPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
3-275 6.51e-86

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: 264.43  E-value: 6.51e-86
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLSHSDRK----VWLLFDYAEHDLwhiikfhrASKANKKPMQLPRSMVKSLLYQILDG 78
Cdd:cd07840    45 AIREIKLLQKLDHPNVVRLKEIVTSKGSAKykgsIYMVFEYMDHDL--------TGLLDNPEVKFTESQIKCYMKQLLEG 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVMGegpeRGRVKIADMGFARLFNSPLKPlaDLDPVVVTFWYRAPELLLGARHYTKAIDIW 158
Cdd:cd07840   117 LQYLHSNGILHRDIKGSNILINN----DGVLKLADFGLARPYTKENNA--DYTNRVITLWYRPPELLLGATRYGPEVDMW 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 159 AIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKdfrRTTYANSSLIKYme 238
Cdd:cd07840   191 SVGCILAELFTGKPIFQGKTE---------LEQLEKIFELCGSPTEENWPGVSDLPWFENLKP---KKPYKRRLREVF-- 256
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1370507705 239 khKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07840   257 --KNVIDPSALDLLDKLLTLDPKKRISADQALQHEYF 291
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
1-282 8.51e-84

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: 259.04  E-value: 8.51e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEHDLWHIIKfhraskanKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd07841    47 FTALREIKLLQELKHPNIIGLLDVFGH--KSNINLVFEFMETDLEKVIK--------DKSIVLTPADIKSYMLMTLRGLE 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLAdldPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd07841   117 YLHSNWILHRDLKPNNLLI----ASDGVLKLADFGLARSFGSPNRKMT---HQVVTRWYRAPELLFGARHYGVGVDMWSV 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFHcRQEDIktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEY----PTLQKDFRRT-TYANSSLIK 235
Cdd:cd07841   190 GCIFAELLLRVPFLP-GDSDI--------DQLGKIFEALGTPTEENWPGVTSLPDYvefkPFPPTPLKQIfPAASDDALD 260
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1370507705 236 ymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYFQEDPLPT 282
Cdd:cd07841   261 ---------------LLQRLLTLNPNKRITARQALEHPYFSNDPAPT 292
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
1-275 2.42e-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: 257.92  E-value: 2.42e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHraskanKKPMQLprSMVKSLLYQILDGIH 80
Cdd:cd07843    49 ITSLREINILLKLQHPNIVTVKEVVVGSNLDKIYMVMEYVEHDLKSLMETM------KQPFLQ--SEVKCLMLQLLSGVA 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLAdldPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd07843   121 HLHDNWILHRDLKTSNLLL----NNRGILKICDFGLAREYGSPLKPYT---QLVVTLWYRAPELLLGAKEYSTAIDMWSV 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWedirkmPEYPTLQ--KDFRRTTYANSSLikyme 238
Cdd:cd07843   194 GCIFAELLTKKPLFPGKSE---------IDQLNKIFKLLGTPTEKIW------PGFSELPgaKKKTFTKYPYNQL----- 253
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1370507705 239 KHKVKPDS---KVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07843   254 RKKFPALSlsdNGFDLLNRLLTYDPAKRISAEDALKHPYF 293
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
2-275 3.43e-74

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: 234.11  E-value: 3.43e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIKFHRAskankkpMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd07835    44 TAIREISLLKELNHPNIVRLLDVV--HSENKLYLVFEFLDLDLKKYMDSSPL-------TGLDPPLIKSYLYQLLQGIAF 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldpVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07835   115 CHSHRVLHRDLKPQNLLI----DTEGALKLADFGLARAFGVPVRTYTH---EVVTLWYRAPEILLGSKHYSTPVDIWSVG 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFHCRQEdIktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYanSSLIKYMEKHK 241
Cdd:cd07835   188 CIFAEMVTRRPLFPGDSE-I--------DQLFRIFRTLGTPDEDVWPGVTSLPDYKPTFPKWARQDL--SKVVPSLDEDG 256
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370507705 242 VKpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07835   257 LD-------LLSQMLVYDPAKRISAKAALQHPYF 283
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
1-281 1.03e-72

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: 231.10  E-value: 1.03e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLwhiikfhrASKANKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd07845    51 ISSLREITLLLNLRHPNIVELKEVVVGKHLDSIFLVMEYCEQDL--------ASLLDNMPTPFSESQVKCLMLQLLRGLQ 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKPLAdldPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd07845   123 YLHENFIIHRDLKVSNLLLT----DKGCLKIADFGLARTYGLPAKPMT---PKVVTLWYRAPELLLGCTTYTTAIDMWAV 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQkdFRRTTYANSslikymeKH 240
Cdd:cd07845   196 GCILAELLAHKPLLPGKSE---------IEQLDLIIQLLGTPNESIWPGFSDLPLVGKFT--LPKQPYNNL-------KH 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 241 KVKPDSKVFL-LLQKLLTMDPTKRITSEQALQDPYFQEDPLP 281
Cdd:cd07845   258 KFPWLSEAGLrLLNFLLMYDPKKRATAEEALESSYFKEKPLP 299
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
5-306 2.48e-68

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: 220.47  E-value: 2.48e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFL---SHSDRKVWLLFDYAEHDLWHIIKfhraskaNKKPMQLPRsmVKSLLYQILDGIHY 81
Cdd:cd07834    48 REIKILRHLKHENIIGLLDILRppsPEEFNDVYIVTELMETDLHKVIK-------SPQPLTDDH--IQYFLYQILRGLKY 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLaDLDPVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07834   119 LHSAGVIHRDLKPSNILV----NSNCDLKICDFGLARGVDPDEDKG-FLTEYVVTRWYRAPELLLSSKKYTKAIDIWSVG 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFhcrqediKTSNPFHhdQLDRIFSVMGFPADKDWEDIRkmpeyptlqkdfrrttyaNSSLIKYME--- 238
Cdd:cd07834   194 CIFAELLTRKPLF-------PGRDYID--QLNLIVEVLGTPSEEDLKFIS------------------SEKARNYLKslp 246
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370507705 239 KHKVKPDSKVFL--------LLQKLLTMDPTKRITSEQALQDPYFQE--DPLPTldvfAGCQIPYPKREFLNEDDPEE 306
Cdd:cd07834   247 KKPKKPLSEVFPgaspeaidLLEKMLVFNPKKRITADEALAHPYLAQlhDPEDE----PVAKPPFDFPFFDDEELTIE 320
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
2-275 8.28e-67

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: 215.26  E-value: 8.28e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEHDLWHIIKfhraskanKKPMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd07833    46 TALREVKVLRQLRHENIVNLKEAFRR--KGRLYLVFEYVERTLLELLE--------ASPGGLPPDAVRSYIWQLLQAIAY 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPlkPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07833   116 CHSHNIIHRDIKPENILV----SESGVLKLCDFGFARALTAR--PASPLTDYVATRWYRAPELLVGDTNYGKPVDVWAIG 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWEDIRKMPEyptlqkdFRRTTYANSSLIKYME-KH 240
Cdd:cd07833   190 CIMAELLDGEPLFPGDSD---------IDQLYLIQKCLGPLPPSHQELFSSNPR-------FAGVAFPEPSQPESLErRY 253
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 241 KVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07833   254 PGKVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
2-275 4.65e-66

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: 213.11  E-value: 4.65e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIKFHRASKAnkkpmqLPRSMVKSLLYQILDGIHY 81
Cdd:cd07836    44 TAIREISLMKELKHENIVRLHDVI--HTENKLMLVFEYMDKDLKKYMDTHGVRGA------LDPNTVKSFTYQLLKGIAF 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGegpeRGRVKIADMGFARLFNSPLKPLADldpVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07836   116 CHENRVLHRDLKPQNLLINK----RGELKLADFGLARAFGIPVNTFSN---EVVTLWYRAPDVLLGSRTYSTSIDIWSVG 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFHCRQEDiktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYptlQKDFRRttYANSSLiKYMEKHK 241
Cdd:cd07836   189 CIMAEMITGRPLFPGTNNE---------DQLLKIFRIMGTPTESTWPGISQLPEY---KPTFPR--YPPQDL-QQLFPHA 253
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370507705 242 vkpDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07836   254 ---DPLGIDLLHRLLQLNPELRISAHDALQHPWF 284
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
2-275 1.42e-65

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: 211.98  E-value: 1.42e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLwhiIKFHRASKankkPMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd07860    45 TAIREISLLKELNHPNIVKLLDVI--HTENKLYLVFEFLHQDL---KKFMDASA----LTGIPLPLIKSYLFQLLQGLAF 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldpVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07860   116 CHSHRVLHRDLKPQNLLI----NTEGAIKLADFGLARAFGVPVRTYTH---EVVTLWYRAPEILLGCKYYSTAVDIWSLG 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFHCRQEDiktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYAnsslikymekhK 241
Cdd:cd07860   189 CIFAEMVTRRALFPGDSEI---------DQLFRIFRTLGTPDEVVWPGVTSMPDYKPSFPKWARQDFS-----------K 248
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1370507705 242 VKP--DSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07860   249 VVPplDEDGRDLLSQMLHYDPNKRISAKAALAHPFF 284
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
2-275 1.45e-65

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 210.85  E-value: 1.45e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705    2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIH 80
Cdd:smart00220  43 RILREIKILKKLKHPNIVRLYDVF--EDEDKLYLVMEYCEGgDLFDLLKKRGR---------LSEDEARFYLRQILSALE 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   81 YLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGaRHYTKAIDIWAI 160
Cdd:smart00220 112 YLHSKGIVHRDLKPENILLD----EDGHVKLADFGLARQLDPGEK----LTTFVGTPEYMAPEVLLG-KGYGKAVDIWSL 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  161 GCIFAELLTSEPIFHcrqediktsnpfHHDQLDRIFSVMGFPadkdweDIRKMPEYPTLQKDFRRttyansslikymekh 240
Cdd:smart00220 183 GVILYELLTGKPPFP------------GDDQLLELFKKIGKP------KPPFPPPEWDISPEAKD--------------- 229
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1370507705  241 kvkpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:smart00220 230 ----------LIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
5-284 3.08e-64

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: 210.11  E-value: 3.08e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELK-HPNVIALQKVFLSHSDRKVWLLFDYAEHDLwhiikfHRASKAN-KKPMQlprsmVKSLLYQILDGIHYL 82
Cdd:cd07852    55 REIMFLQELNdHPNIIKLLNVIRAENDKDIYLVFEYMETDL------HAVIRANiLEDIH-----KQYIMYQLLKALKYL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMGEGpergRVKIADMGFARLFNSplKPLADLDPV----VVTFWYRAPELLLGARHYTKAIDIW 158
Cdd:cd07852   124 HSGGVIHRDLKPSNILLNSDC----RVKLADFGLARSLSQ--LEEDDENPVltdyVATRWYRAPEILLGSTRYTKGVDMW 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 159 AIGCIFAELLTSEPIFHcrqediKTSNpfhHDQLDRIFSVMGFPADKDWEDIrkmpeyptlqkdfrRTTYAnSSLIKYME 238
Cdd:cd07852   198 SVGCILGEMLLGKPLFP------GTST---LNQLEKIIEVIGRPSAEDIESI--------------QSPFA-ATMLESLP 253
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370507705 239 KHKVKPDSKVFL--------LLQKLLTMDPTKRITSEQALQDPYFQE----DPLPTLD 284
Cdd:cd07852   254 PSRPKSLDELFPkaspdaldLLKKLLVFNPNKRLTAEEALRHPYVAQfhnpADEPSLP 311
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
2-275 3.13e-64

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: 209.09  E-value: 3.13e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFLSHSDRK------VWLLFDYAEHDLWHIIKFHRaskankkpMQLPRSMVKSLLYQI 75
Cdd:cd07866    53 TALREIKILKKLKHPNVVPLIDMAVERPDKSkrkrgsVYMVTPYMDHDLSGLLENPS--------VKLTESQIKCYMLQL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  76 LDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPL--------ADLDPVVVTFWYRAPELLLG 147
Cdd:cd07866   125 LEGINYLHENHILHRDIKAANILI----DNQGILKIADFGLARPYDGPPPNPkggggggtRKYTNLVVTRWYRPPELLLG 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 148 ARHYTKAIDIWAIGCIFAELLTSEPIFHcRQEDIktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYPTLqkdFRRTT 227
Cdd:cd07866   201 ERRYTTAVDIWGIGCVFAEMFTRRPILQ-GKSDI--------DQLHLIFKLCGTPTEETWPGWRSLPGCEGV---HSFTN 268
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1370507705 228 YANSslikyMEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07866   269 YPRT-----LEERFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPYF 311
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
1-275 5.65e-64

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: 207.51  E-value: 5.65e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELK---HPNVIALQKVFL-SHSDR--KVWLLFDYAEHDLWHIIKFHRASKankkpmqLPRSMVKSLLYQ 74
Cdd:cd07838    43 LSTIREIALLKQLEsfeHPNVVRLLDVCHgPRTDRelKLTLVFEHVDQDLATYLDKCPKPG-------LPPETIKDLMRQ 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGArHYTKA 154
Cdd:cd07838   116 LLRGLDFLHSHRIVHRDLKPQNILV----TSDGQVKLADFGLARIYSFEMA----LTSVVVTLWYRAPEVLLQS-SYATP 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 155 IDIWAIGCIFAELLTSEPIFhCRQEDIktsnpfhhDQLDRIFSVMGFPADKDWedirkmPEYPTLQKD-FRRTTYAN-SS 232
Cdd:cd07838   187 VDMWSVGCIFAELFNRRPLF-RGSSEA--------DQLGKIFDVIGLPSEEEW------PRNSALPRSsFPSYTPRPfKS 251
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1370507705 233 LIKYMEKHKVKpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07838   252 FVPEIDEEGLD-------LLKKMLTFNPHKRISAFEALQHPYF 287
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
2-275 1.11e-63

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: 206.89  E-value: 1.11e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLwhiikfHRASKANKKPMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd07861    45 TAIREISLLKELQHPNIVCLEDVL--MQENRLYLVFEFLSMDL------KKYLDSLPKGKYMDAELVKSYLYQILQGILF 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldpVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07861   117 CHSRRVLHRDLKPQNLLI----DNKGVIKLADFGLARAFGIPVRVYTH---EVVTLWYRAPEVLLGSPRYSTPVDIWSIG 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFHCRQEDiktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEY----PTLQKDFRRTTYANSslikym 237
Cdd:cd07861   190 TIFAEMATKKPLFHGDSEI---------DQLFRIFRILGTPTEDIWPGVTSLPDYkntfPKWKKGSLRTAVKNL------ 254
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370507705 238 ekhkvkpDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07861   255 -------DEDGLDLLEKMLIYDPAKRISAKKALVHPYF 285
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
2-275 7.55e-63

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: 204.87  E-value: 7.55e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELK-HPNVIALQKVFLSHSDrkVWLLFDYAEHDLWHIIKFHRaskankKPmqLPRSMVKSLLYQILDGIH 80
Cdd:cd07832    45 QALREIKALQACQgHPYVVKLRDVFPHGTG--FVLVFEYMLSSLSEVLRDEE------RP--LTEAQVKRYMRMLLKGVA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLadLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd07832   115 YMHANRIMHRDLKPANLLI----SSTGVLKIADFGLARLFSEEDPRL--YSHQVATRWYRAPELLYGSRKYDEGVDLWAV 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFHCRqEDIktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYPTLqkdfrrtTYANSSLIKyMEKH 240
Cdd:cd07832   189 GCIFAELLNGSPLFPGE-NDI--------EQLAIVLRTLGTPNEKTWPELTSLPDYNKI-------TFPESKGIR-LEEI 251
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 241 KVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07832   252 FPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
2-275 5.21e-60

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: 196.30  E-value: 5.21e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELK----HPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKfhraskanKKPMQLPRSMVKSLLYQILD 77
Cdd:cd05118    41 AALREIKLLKHLNdvegHPNIVKLLDVFEHRGGNHLCLVFELMGMNLYELIK--------DYPRGLPLDLIKSYLYQLLQ 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANWVLHRDLKPANILVMGEgpeRGRVKIADMGFARLFNSPLkpladLDPVVVTFWYRAPELLLGARHYTKAIDI 157
Cdd:cd05118   113 ALDFLHSNGIIHRDLKPENILINLE---LGQLKLADFGLARSFTSPP-----YTPYVATRWYRAPEVLLGAKPYGSSIDI 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 158 WAIGCIFAELLTSEPIFhcrqediktSNPFHHDQLDRIFSVMGFPADKDwedirkmpeyptlqkdfrrttyansslikym 237
Cdd:cd05118   185 WSLGCILAELLTGRPLF---------PGDSEVDQLAKIVRLLGTPEALD------------------------------- 224
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370507705 238 ekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd05118   225 -------------LLSKMLKYDPAKRITASQALAHPYF 249
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
5-277 7.14e-60

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: 197.34  E-value: 7.14e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRK----VWLLFDYAEHDLWHIIKFHRASKankkpMQLPRSMVKSLLYQILDGIH 80
Cdd:cd14137    46 RELQIMRRLKHPNIVKLKYFFYSSGEKKdevyLNLVMEYMPETLYRVIRHYSKNK-----QTIPIIYVKLYSYQLFRGLA 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLfnspLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd14137   121 YLHSLGICHRDIKPQNLLV---DPETGVLKLCDFGSAKR----LVPGEPNVSYICSRYYRAPELIFGATDYTTAIDIWSA 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFHCRqedikTSNpfhhDQLDRIFSVMGFPADkdwEDIRKM-PEYPtlqkDFRRTTYANSSLIKYMEK 239
Cdd:cd14137   194 GCVLAELLLGQPLFPGE-----SSV----DQLVEIIKVLGTPTR---EQIKAMnPNYT----EFKFPQIKPHPWEKVFPK 257
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370507705 240 HkvkPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQE 277
Cdd:cd14137   258 R---TPPDAIDLLSKILVYNPSKRLTALEALAHPFFDE 292
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
5-275 7.33e-60

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: 196.99  E-value: 7.33e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELK-HPNVIALQKVFLSHsdRKVWLLFDYAEHDLWHIIKfhraskaNKKPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd07830    46 REVKSLRKLNeHPNIVKLKEVFREN--DELYFVFEYMEGNLYQLMK-------DRKGKPFSESVIRSIIYQILQGLAHIH 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGegpeRGRVKIADMGFAR-LFNSPlkPLADLdpvVVTFWYRAPELLLGARHYTKAIDIWAIGC 162
Cdd:cd07830   117 KHGFFHRDLKPENLLVSG----PEVVKIADFGLAReIRSRP--PYTDY---VSTRWYRAPEILLRSTSYSSPVDIWALGC 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWedirkmPEYPTL--QKDFRRTTYANSSLikymekH 240
Cdd:cd07830   188 IMAELYTLRPLFPGSSE---------IDQLYKICSVLGTPTKQDW------PEGYKLasKLGFRFPQFAPTSL------H 246
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1370507705 241 KVKPDSKVFL--LLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07830   247 QLIPNASPEAidLIKDMLRWDPKKRPTASQALQHPYF 283
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
5-281 2.81e-59

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 196.91  E-value: 2.81e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEHDLWHIIkfhraskaNKKpMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:PTZ00024   69 RELKIMNEIKHENIMGLVDVYVEGD--FINLVMDIMASDLKKVV--------DRK-IRLTESQVKCILLQILNGLNVLHK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPL-----------KPLADLDPVVVTFWYRAPELLLGARHYTK 153
Cdd:PTZ00024  138 WYFMHRDLSPANIFI----NSKGICKIADFGLARRYGYPPysdtlskdetmQRREEMTSKVVTLWYRAPELLMGAEKYHF 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWEDIRKMPEY----PTLQKDFRRT-TY 228
Cdd:PTZ00024  214 AVDMWSVGCIFAELLTGKPLFPGENE---------IDQLGRIFELLGTPNEDNWPQAKKLPLYteftPRKPKDLKTIfPN 284
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370507705 229 ANSSLIKymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYFQEDPLP 281
Cdd:PTZ00024  285 ASDDAID---------------LLQSLLKLNPLERISAKEALKHEYFKSDPLP 322
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
2-275 3.07e-59

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: 195.34  E-value: 3.07e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLwhiIKFHRASKAnkkpmQLPRSMVKSLLYQILDGIHY 81
Cdd:cd07839    45 SALREICLLKELKHKNIVRLYDVL--HSDKKLTLVFEYCDQDL---KKYFDSCNG-----DIDPEIVKSFMFQLLKGLAF 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGegpeRGRVKIADMGFARLFNSPLKPLAdldPVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07839   115 CHSHNVLHRDLKPQNLLINK----NGELKLADFGLARAFGIPVRCYS---AEVVTLWYRPPDVLFGAKLYSTSIDMWSAG 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTS-EPIFHCRQEDiktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYPTLqkdfrrtTYANSSLIKYMEKH 240
Cdd:cd07839   188 CIFAELANAgRPLFPGNDVD---------DQLKRIFRLLGTPTEESWPGVSKLPDYKPY-------PMYPATTSLVNVVP 251
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 241 KVKPDSKVflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07839   252 KLNSTGRD--LLQNLLVCNPVQRISAEEALQHPYF 284
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
2-277 1.38e-58

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 193.88  E-value: 1.38e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLwhiiKFHRASKAN--KKPmqlprSMVKSLLYQILDGI 79
Cdd:PLN00009   47 TAIREISLLKEMQHGNIVRLQDVV--HSEKRLYLVFEYLDLDL----KKHMDSSPDfaKNP-----RLIKTYLYQILRGI 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLFNSPLKPLADldpVVVTFWYRAPELLLGARHYTKAIDIWA 159
Cdd:PLN00009  116 AYCHSHRVLHRDLKPQNLLI---DRRTNALKLADFGLARAFGIPVRTFTH---EVVTLWYRAPEILLGSRHYSTPVDIWS 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 160 IGCIFAELLTSEPIFHCRQEDiktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYAnsSLIKYMEK 239
Cdd:PLN00009  190 VGCIFAEMVNQKPLFPGDSEI---------DELFKIFRILGTPNEETWPGVTSLPDYKSAFPKWPPKDLA--TVVPTLEP 258
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370507705 240 HKVKpdskvflLLQKLLTMDPTKRITSEQALQDPYFQE 277
Cdd:PLN00009  259 AGVD-------LLSKMLRLDPSKRITARAALEHEYFKD 289
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
1-275 2.72e-57

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: 190.56  E-value: 2.72e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELK---HPNVIALQKVFLS-HSDR--KVWLLFDYAEHDLwhiikfhRASKANKKPMQLPRSMVKSLLYQ 74
Cdd:cd07863    44 LSTVREVALLKRLEafdHPNIVRLMDVCATsRTDRetKVTLVFEHVDQDL-------RTYLDKVPPPGLPAETIKDLMRQ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGARhYTKA 154
Cdd:cd07863   117 FLRGLDFLHANCIVHRDLKPENILVT----SGGQVKLADFGLARIYSCQMA----LTPVVVTLWYRAPEVLLQST-YATP 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 155 IDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWedirkmPEYPTLQK-DFR-RTTYANSS 232
Cdd:cd07863   188 VDMWSVGCIFAEMFRRKPLFCGNSE---------ADQLGKIFDLIGLPPEDDW------PRDVTLPRgAFSpRGPRPVQS 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1370507705 233 LIKYMEKHKVKpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07863   253 VVPEIEESGAQ-------LLLEMLTFNPHKRISAFRALQHPFF 288
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
5-279 1.64e-56

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: 190.20  E-value: 1.64e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFL--SHSD--RKVWLLFDYAEHDLWHIIKFHRaskankkpmqLPRSMVKSLLYQILDGIH 80
Cdd:cd07851    63 RELRLLKHMKHENVIGLLDVFTpaSSLEdfQDVYLVTHLMGADLNNIVKCQK----------LSDDHIQFLVYQILRGLK 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplkplaDLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd07851   133 YIHSAGIIHRDLKPSNLAV----NEDCELKILDFGLARHTDD------EMTGYVATRWYRAPEIMLNWMHYNQTVDIWSV 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFhcRQEDiktsnpfHHDQLDRIFSVMGFPADK-----DWED----IRKMPEYPtlQKDFRRT-TYAN 230
Cdd:cd07851   203 GCIMAELLTGKTLF--PGSD-------HIDQLKRIMNLVGTPDEEllkkiSSESarnyIQSLPQMP--KKDFKEVfSGAN 271
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370507705 231 SSLIKymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYFQE--DP 279
Cdd:cd07851   272 PLAID---------------LLEKMLVLDPDKRITAAEALAHPYLAEyhDP 307
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
2-275 7.75e-54

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: 181.43  E-value: 7.75e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIKFHraskankkPMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd07844    44 TAIREASLLKDLKHANIVTLHDII--HTKKTLTLVFEYLDTDLKQYMDDC--------GGGLSMHNVRLFLFQLLRGLAY 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldpVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07844   114 CHQRRVLHRDLKPQNLLI----SERGELKLADFGLARAKSVPSKTYSN---EVVTLWYRPPDVLLGSTEYSTSLDMWGVG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFhcrqEDIKTSNpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYptlqKDFRRTTYANSSLIKYMEKHK 241
Cdd:cd07844   187 CIFYEMATGRPLF----PGSTDVE----DQLHKIFRVLGTPTEETWPGVSSNPEF----KPYSFPFYPPRPLINHAPRLD 254
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370507705 242 VKPDSkvFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07844   255 RIPHG--EELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
5-307 1.43e-53

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: 182.12  E-value: 1.43e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSD---RKVWLLFDYAEHDLWHIIKfhraskankkPMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd07849    52 REIKILLRFKHENIIGILDIQRPPTFesfKDVYIVQELMETDLYKLIK----------TQHLSNDHIQYFLYQILRGLKY 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07849   122 IHSANVLHRDLKPSNLLL----NTNCDLKICDFGLARIADPEHDHTGFLTEYVATRWYRAPEIMLNSKGYTKAIDIWSVG 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFHCRQediktsnpfHHDQLDRIFSVMGFPADKDWEDI---------RKMPEYPTLqkdfrrttyansS 232
Cdd:cd07849   198 CILAEMLSNRPLFPGKD---------YLHQLNLILGILGTPSQEDLNCIislkarnyiKSLPFKPKV------------P 256
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370507705 233 LIKYMEKHkvkpDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQE--DPL--PTLDVfagcqiPYPKREFLNEDDPEEK 307
Cdd:cd07849   257 WNKLFPNA----DPKALDLLDKMLTFNPHKRITVEEALAHPYLEQyhDPSdePVAEE------PFPFDMELFDDLPKEK 325
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
3-275 2.41e-52

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: 177.56  E-value: 2.41e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIKFHraskankkPMQLPRSMVKSLLYQILDGIHYL 82
Cdd:cd07847    47 ALREIRMLKQLKHPNLVNLIEVF--RRKRKLHLVFEYCDHTVLNELEKN--------PRGVPEHLIKKIIWQTLQAVNFC 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMGEGpergRVKIADMGFARLFNSPLKPLADLdpvVVTFWYRAPELLLGARHYTKAIDIWAIGC 162
Cdd:cd07847   117 HKHNCIHRDVKPENILITKQG----QIKLCDFGFARILTGPGDDYTDY---VATRWYRAPELLVGDTQYGPPVDVWAIGC 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLTSEPIFHCRQE-D-----IKTSNPF--HHDQL---DRIFSVMGFPADKDWEDIR-KMPEYPTLQKDFrrttyan 230
Cdd:cd07847   190 VFAELLTGQPLWPGKSDvDqlyliRKTLGDLipRHQQIfstNQFFKGLSIPEPETREPLEsKFPNISSPALSF------- 262
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1370507705 231 sslikymekhkvkpdskvfllLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07847   263 ---------------------LKGCLQMDPTERLSCEELLEHPYF 286
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
1-275 2.61e-52

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: 177.95  E-value: 2.61e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLSHSDR------KVWLLFDYAEHDLwhiikfhrASKANKKPMQLPRSMVKSLLYQ 74
Cdd:cd07865    56 ITALREIKILQLLKHENVVNLIEICRTKATPynrykgSIYLVFEFCEHDL--------AGLLSNKNVKFTLSEIKKVMKM 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVMGEGPergrVKIADMGFARLFNSPLKPLADL-DPVVVTFWYRAPELLLGARHYTK 153
Cdd:cd07865   128 LLNGLYYIHRNKILHRDMKAANILITKDGV----LKLADFGLARAFSLAKNSQPNRyTNRVVTLWYRPPELLLGERDYGP 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWEDIRKMPEYPT--LQKDFRRTtyans 231
Cdd:cd07865   204 PIDMWGAGCIMAEMWTRSPIMQGNTE---------QHQLTLISQLCGSITPEVWPGVDKLELFKKmeLPQGQKRK----- 269
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1370507705 232 slIKYMEKHKVKpDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07865   270 --VKERLKPYVK-DPYALDLIDKLLVLDPAKRIDADTALNHDFF 310
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
1-274 9.20e-52

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: 176.53  E-value: 9.20e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLSHSD--------RKVWLLFDYAEHDLWHIIKfhraskanKKPMQLPRSMVKSLL 72
Cdd:cd07864    51 ITAIREIKILRQLNHRSVVNLKEIVTDKQDaldfkkdkGAFYLVFEYMDHDLMGLLE--------SGLVHFSEDHIKSFM 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  73 YQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNS-PLKPLADLdpvVVTFWYRAPELLLGARHY 151
Cdd:cd07864   123 KQLLEGLNYCHKKNFLHRDIKCSNILL----NNKGQIKLADFGLARLYNSeESRPYTNK---VITLWYRPPELLLGEERY 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 152 TKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWEDIRKMPEYPTL--QKDFRRTTYA 229
Cdd:cd07864   196 GPAIDVWSCGCILGELFTKKPIFQANQE---------LAQLELISRLCGSPCPAVWPDVIKLPYFNTMkpKKQYRRRLRE 266
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1370507705 230 NSSLIKymekhkvkpdSKVFLLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd07864   267 EFSFIP----------TPALDLLDHMLTLDPSKRCTAEQALNSPW 301
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
2-275 1.22e-51

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: 175.79  E-value: 1.22e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIaLQKVFLSHSDRK----VWLLFDYAEHDLWHIIKFHRASKANKkpmqLPRSMVKSLLYQILD 77
Cdd:cd07837    46 TALREVSLLQMLSQSIYI-VRLLDVEHVEENgkplLYLVFEYLDTDLKKFIDSYGRGPHNP----LPAKTIQSFMYQLCK 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLFNSPLKPLADldpVVVTFWYRAPELLLGARHYTKAIDI 157
Cdd:cd07837   121 GVAHCHSHGVMHRDLKPQNLLV---DKQKGLLKIADLGLGRAFTIPIKSYTH---EIVTLWYRAPEVLLGSTHYSTPVDM 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 158 WAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWEDIRKMP---EYPTLQ-KDFrrttyanSSL 233
Cdd:cd07837   195 WSVGCIFAEMSRKQPLFPGDSE---------LQQLLHIFRLLGTPNEEVWPGVSKLRdwhEYPQWKpQDL-------SRA 258
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 234 IKYMEKHKVKpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07837   259 VPDLEPEGVD-------LLTKMLAYDPAKRISAKAALQHPYF 293
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
5-306 1.25e-51

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: 177.18  E-value: 1.25e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRK---VWLLFDYAEHDLWHIIKfhraskankKPMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd07858    53 REIKLLRHLDHENVIAIKDIMPPPHREAfndVYIVYELMDTDLHQIIR---------SSQTLSDDHCQYFLYQLLRGLKY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLdpvVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07858   124 IHSANVLHRDLKPSNLLL----NANCDLKICDFGLARTTSEKGDFMTEY---VVTRWYRAPELLLNCSEYTTAIDVWSVG 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFHCRQediktsnpfHHDQLDRIFSVMGFPADKDWED---------IRKMPEYPtlQKDFRRttyanss 232
Cdd:cd07858   197 CIFAELLGRKPLFPGKD---------YVHQLKLITELLGSPSEEDLGFirnekarryIRSLPYTP--RQSFAR------- 258
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370507705 233 liKYMEKHKVKPDskvflLLQKLLTMDPTKRITSEQALQDPYFQedPLPTLDVFAGCQIPYP---KREFLNEDDPEE 306
Cdd:cd07858   259 --LFPHANPLAID-----LLEKMLVFDPSKRITVEEALAHPYLA--SLHDPSDEPVCQTPFSfdfEEDALTEEDIKE 326
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
5-281 3.74e-51

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: 175.63  E-value: 3.74e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSD----RKVWLLFDYAEHDLWHIIKfhraskaNKKPMQLprSMVKSLLYQILDGIH 80
Cdd:cd07855    53 RELKILRHFKHDNIIAIRDILRPKVPyadfKDVYVVLDLMESDLHHIIH-------SDQPLTL--EHIRYFLYQLLRGLK 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFAR-LFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWA 159
Cdd:cd07855   124 YIHSANVIHRDLKPSNLLV----NENCELKIGDFGMARgLCTSPEEHKYFMTEYVATRWYRAPELMLSLPEYTQAIDMWS 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 160 IGCIFAELLTSEPIFHCRqediktsNPFHhdQLDRIFSVMGFPADKDWEDIRkmpeyptlqKDFRRTTYANSSLIKYMEK 239
Cdd:cd07855   200 VGCIFAEMLGRRQLFPGK-------NYVH--QLQLILTVLGTPSQAVINAIG---------ADRVRRYIQNLPNKQPVPW 261
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1370507705 240 HKVKPDS--KVFLLLQKLLTMDPTKRITSEQALQDPYFQEDPLP 281
Cdd:cd07855   262 ETLYPKAdqQALDLLSQMLRFDPSERITVAEALQHPFLAKYHDP 305
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
2-277 1.12e-50

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: 173.26  E-value: 1.12e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDL-------WHIIKFHRaskankkpmqlprsmVKSLLYQ 74
Cdd:cd07873    46 TAIREVSLLKDLKHANIVTLHDII--HTEKSLTLVFEYLDKDLkqylddcGNSINMHN---------------VKLFLFQ 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldpVVVTFWYRAPELLLGARHYTKA 154
Cdd:cd07873   109 LLRGLAYCHRRKVLHRDLKPQNLLI----NERGELKLADFGLARAKSIPTKTYSN---EVVTLWYRPPDILLGSTDYSTQ 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 155 IDIWAIGCIFAELLTSEPIFHCRQEDiktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYptlqKDFRRTTYANSSLI 234
Cdd:cd07873   182 IDMWGVGCIFYEMSTGRPLFPGSTVE---------EQLHFIFRILGTPTEETWPGILSNEEF----KSYNYPKYRADALH 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1370507705 235 kymeKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQE 277
Cdd:cd07873   249 ----NHAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHS 287
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
2-275 4.14e-49

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: 169.03  E-value: 4.14e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIKfhraSKANKKPMQlprsMVKSLLYQILDGIHY 81
Cdd:cd07871    49 TAIREVSLLKNLKHANIVTLHDII--HTERCLTLVFEYLDSDLKQYLD----NCGNLMSMH----NVKIFMFQLLRGLSY 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldpVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07871   119 CHKRKILHRDLKPQNLLI----NEKGELKLADFGLARAKSVPTKTYSN---EVVTLWYRPPDVLLGSTEYSTPIDMWGVG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFhcRQEDIKtsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYptlqKDFRRTTYANSSLIkymeKHK 241
Cdd:cd07871   192 CILYEMATGRPMF--PGSTVK-------EELHLIFRLLGTPTEETWPGVTSNEEF----RSYLFPQYRAQPLI----NHA 254
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370507705 242 VKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07871   255 PRLDTDGIDLLSSLLLYETKSRISAEAALRHSYF 288
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
3-309 1.08e-47

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: 166.43  E-value: 1.08e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELK-HPNVIALQKVFLSHSD--RKVWLLFDYAEHDLWHIIKfhraskankKPMQLPRSMVKSLLYQILDGI 79
Cdd:cd07857    48 ALRELKLLRHFRgHKNITCLYDMDIVFPGnfNELYLYEELMEADLHQIIR---------SGQPLTDAHFQSFIYQILCGL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILVMGEGpergRVKIADMGFARLFN-SPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIW 158
Cdd:cd07857   119 KYIHSANVLHRDLKPGNLLVNADC----ELKICDFGLARGFSeNPGENAGFMTEYVATRWYRAPEIMLSFQSYTKAIDVW 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 159 AIGCIFAELLTSEPIFHCRQediktsnpfHHDQLDRIFSVMGFPAD---------KDWEDIRKMPEYPtlQKDFrrttya 229
Cdd:cd07857   195 SVGCILAELLGRKPVFKGKD---------YVDQLNQILQVLGTPDEetlsrigspKAQNYIRSLPNIP--KKPF------ 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 230 nsslikymEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQE--DPlptlDVFAGCQIPYPKrEFLNEDDPEEK 307
Cdd:cd07857   258 --------ESIFPNANPLALDLLEKLLAFDPTKRISVEEALEHPYLAIwhDP----DDEPVCQKPFDF-SFESEDSMEEL 324

                  ..
gi 1370507705 308 GD 309
Cdd:cd07857   325 RD 326
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
3-275 8.12e-46

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: 160.28  E-value: 8.12e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIKfhraskanKKPMQLPRSMVKSLLYQILDGIHYL 82
Cdd:cd07846    47 AMREIKMLKQLRHENLVNLIEVF--RRKKRWYLVFEFVDHTVLDDLE--------KYPNGLDESRVRKYLFQILRGIDFC 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLdpvVVTFWYRAPELLLGARHYTKAIDIWAIGC 162
Cdd:cd07846   117 HSHNIIHRDIKPENILV----SQSGVVKLCDFGFARTLAAPGEVYTDY---VATRWYRAPELLVGDTKYGKAVDVWAVGC 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLTSEPIFHcRQEDIktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQkdfrrttYANSSLIKYMEKHKV 242
Cdd:cd07846   190 LVTEMLTGEPLFP-GDSDI--------DQLYHIIKCLGNLIPRHQELFQKNPLFAGVR-------LPEVKEVEPLERRYP 253
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370507705 243 KPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07846   254 KLSGVVIDLAKKCLHIDPDKRPSCSELLHHEFF 286
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
3-275 1.38e-45

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 159.36  E-value: 1.38e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELK-HPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRaskankKPmqLPRSMVKSLLYQILDGIHY 81
Cdd:cd07831    44 NLREIQALRRLSpHPNILRLIEVLFDRKTGRLALVFELMDMNLYELIKGRK------RP--LPEKRVKNYMYQLLKSLDH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEgpergRVKIADMGFARLFNSPLkPLADLdpvVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07831   116 MHRNGIFHRDIKPENILIKDD-----ILKLADFGSCRGIYSKP-PYTEY---ISTRWYRAPECLLTDGYYGPKMDIWAVG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPAdkdwedirkmpeyPTLQKDFRRTTYANSSLIKY----M 237
Cdd:cd07831   187 CVFFEILSLFPLFPGTNE---------LDQIAKIHDVLGTPD-------------AEVLKKFRKSRHMNYNFPSKkgtgL 244
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370507705 238 EKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07831   245 RKLLPNASAEGLDLLKKLLAYDPDERITAKQALRHPYF 282
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
2-276 3.19e-45

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: 159.39  E-value: 3.19e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLwhiiKFHRASKANKKPMQlprsMVKSLLYQILDGIHY 81
Cdd:cd07872    50 TAIREVSLLKDLKHANIVTLHDIV--HTDKSLTLVFEYLDKDL----KQYMDDCGNIMSMH----NVKIFLYQILRGLAY 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldpVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07872   120 CHRRKVLHRDLKPQNLLI----NERGELKLADFGLARAKSVPTKTYSN---EVVTLWYRPPDVLLGSSEYSTQIDMWGVG 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFHCRQEDiktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYptlqKDFRRTTYANSSLIkymeKHK 241
Cdd:cd07872   193 CIFFEMASGRPLFPGSTVE---------DELHLIFRLLGTPTEETWPGISSNDEF----KNYNFPKYKPQPLI----NHA 255
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 242 VKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQ 276
Cdd:cd07872   256 PRLDTEGIELLTKFLQYESKKRISAEEAMKHAYFR 290
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
2-275 4.29e-45

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: 158.20  E-value: 4.29e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIKFHraskankkPMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd07870    44 TAIREASLLKGLKHANIVLLHDII--HTKETLTFVFEYMHTDLAQYMIQH--------PGGLHPYNVRLFMFQLLRGLAY 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldpVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07870   114 IHGQHILHRDLKPQNLLI----SYLGELKLADFGLARAKSIPSQTYSS---EVVTLWYRPPDVLLGATDYSSALDIWGAG 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFHcrqediKTSNPFhhDQLDRIFSVMGFPADKDWEDIRKMPEY-PTLQKdfrrttYANSSLIKYMEKH 240
Cdd:cd07870   187 CIFIEMLQGQPAFP------GVSDVF--EQLEKIWTVLGVPTEDTWPGVSKLPNYkPEWFL------PCKPQQLRVVWKR 252
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 241 KVKPdSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07870   253 LSRP-PKAEDLASQMLMMFPKDRISAQDALLHPYF 286
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
3-277 5.42e-45

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: 159.73  E-value: 5.42e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLSHS--DR--KVWLLFDYAEHDLWHIIKFHRaskankkpmqLPRSMVKSLLYQILDG 78
Cdd:cd07880    61 AYRELRLLKHMKHENVIGLLDVFTPDLslDRfhDFYLVMPFMGTDLGKLMKHEK----------LSEDRIQFLVYQMLKG 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplkplaDLDPVVVTFWYRAPELLLGARHYTKAIDIW 158
Cdd:cd07880   131 LKYIHAAGIIHRDLKPGNLAV----NEDCELKILDFGLARQTDS------EMTGYVVTRWYRAPEVILNWMHYTQTVDIW 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 159 AIGCIFAELLTSEPIFhcrqediKTSNpfHHDQLDRIFSVMGFP---------ADKDWEDIRKMPEYPtlQKDFRrttya 229
Cdd:cd07880   201 SVGCIMAEMLTGKPLF-------KGHD--HLDQLMEIMKVTGTPskefvqklqSEDAKNYVKKLPRFR--KKDFR----- 264
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1370507705 230 nsSLIKYMEKHKVKpdskvflLLQKLLTMDPTKRITSEQALQDPYFQE 277
Cdd:cd07880   265 --SLLPNANPLAVN-------VLEKMLVLDAESRITAAEALAHPYFEE 303
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
1-275 2.77e-44

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: 156.35  E-value: 2.77e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELK---HPNVIALQKV-FLSHSDR--KVWLLFDYAEHDLwhiikfhrASKANKKPMQ-LPRSMVKSLLY 73
Cdd:cd07862    46 LSTIREVAVLRHLEtfeHPNVVRLFDVcTVSRTDRetKLTLVFEHVDQDL--------TTYLDKVPEPgVPTETIKDMMF 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGARhYTK 153
Cdd:cd07862   118 QLLRGLDFLHSHRVVHRDLKPQNILVTSS----GQIKLADFGLARIYSFQMA----LTSVVVTLWYRAPEVLLQSS-YAT 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFHcRQEDIktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPeyptlqkdfrRTTYAnSSL 233
Cdd:cd07862   189 PVDLWSVGCIFAEMFRRKPLFR-GSSDV--------DQLGKILDVIGLPGEEDWPRDVALP----------RQAFH-SKS 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 234 IKYMEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07862   249 AQPIEKFVTDIDELGKDLLLKCLTFNPAKRISAYSALSHPYF 290
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
5-306 4.97e-44

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: 156.87  E-value: 4.97e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRK---VWLLFDYAEHDLwhiikfHRASKANKkpmQLPRSMVKSLLYQILDGIHY 81
Cdd:cd07859    48 REIKLLRLLRHPDIVEIKHIMLPPSRREfkdIYVVFELMESDL------HQVIKAND---DLTPEHHQFFLYQLLRALKY 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEGpergRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLlGA--RHYTKAIDIWA 159
Cdd:cd07859   119 IHTANVFHRDLKPKNILANADC----KLKICDFGLARVAFNDTPTAIFWTDYVATRWYRAPELC-GSffSKYTPAIDIWS 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 160 IGCIFAELLTSEPIFHCRqediktsNPFHhdQLDRIFSVMGFPADKDWEDIRkmpeyptlQKDFRRttYANSslikyMEK 239
Cdd:cd07859   194 IGCIFAEVLTGKPLFPGK-------NVVH--QLDLITDLLGTPSPETISRVR--------NEKARR--YLSS-----MRK 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 240 HKVKP--------DSKVFLLLQKLLTMDPTKRITSEQALQDPYFQEdpLPTLDVFAGCQiPYPKREF------LNEDDPE 305
Cdd:cd07859   250 KQPVPfsqkfpnaDPLALRLLERLLAFDPKDRPTAEEALADPYFKG--LAKVEREPSAQ-PITKLEFeferrrLTKEDVR 326

                  .
gi 1370507705 306 E 306
Cdd:cd07859   327 E 327
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
5-305 5.67e-44

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: 157.60  E-value: 5.67e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVI-ALQKVFLSHSD--RKVWLLFDYAEHDLWHIIKfhraskankKPMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd07853    48 RELKMLCFFKHDNVLsALDILQPPHIDpfEEIYVVTELMQSDLHKIIV---------SPQPLSSDHVKVFLYQILRGLKY 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEGpergRVKIADMGFARLfnSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07853   119 LHSAGILHRDIKPGNLLVNSNC----VLKICDFGLARV--EEPDESKHMTQEVVTQYYRAPEILMGSRHYTSAVDIWSVG 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFhcrqediKTSNPFhhDQLDRIFSVMGFPAdkdwedirkmpeyptlQKDFRrttYANSSLIKYMEKHK 241
Cdd:cd07853   193 CIFAELLGRRILF-------QAQSPI--QQLDLITDLLGTPS----------------LEAMR---SACEGARAHILRGP 244
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370507705 242 VKPDS-------------KVFLLLQKLLTMDPTKRITSEQALQDPYFQEDPLPTLDVFAG-CQIPYPKREFLNEDDPE 305
Cdd:cd07853   245 HKPPSlpvlytlssqathEAVHLLCRMLVFDPDKRISAADALAHPYLDEGRLRYHTCMCKcCYTTSGGRVYTSDFEPS 322
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
2-276 1.15e-41

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: 150.70  E-value: 1.15e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFLSHSDR------------KVWLLFDYAEHDLWHIIKFHraskankkpmQLPRSMVK 69
Cdd:cd07854    48 HALREIKIIRRLDHDNIVKVYEVLGPSGSDltedvgsltelnSVYIVQEYMETDLANVLEQG----------PLSEEHAR 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  70 SLLYQILDGIHYLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGAR 149
Cdd:cd07854   118 LFMYQLLRGLKYIHSANVLHRDLKPANVFI---NTEDLVLKIGDFGLARIVDPHYSHKGYLSEGLVTKWYRSPRLLLSPN 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 150 HYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWEDI-RKMPEYptLQKDfrrTTY 228
Cdd:cd07854   195 NYTKAIDMWAAGCIFAEMLTGKPLFAGAHE---------LEQMQLILESVPVVREEDRNELlNVIPSF--VRND---GGE 260
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1370507705 229 ANSSLIKYMEkhkvKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQ 276
Cdd:cd07854   261 PRRPLRDLLP----GVNPEALDFLEQILTFNPMDRLTAEEALMHPYMS 304
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
5-279 1.36e-41

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: 150.58  E-value: 1.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRK----VWLLFDYAEHDLWHIIKFHRaskankkpmqLPRSMVKSLLYQILDGIH 80
Cdd:cd07877    65 RELRLLKHMKHENVIGLLDVFTPARSLEefndVYLVTHLMGADLNNIVKCQK----------LTDDHVQFLIYQILRGLK 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplkplaDLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd07877   135 YIHSADIIHRDLKPSNLAV----NEDCELKILDFGLARHTDD------EMTGYVATRWYRAPEIMLNWMHYNQTVDIWSV 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFhcrqediktSNPFHHDQLDRIFSVMGFPADkdwEDIRKMPEYPTlqkdfrrTTYANSslIKYMEKH 240
Cdd:cd07877   205 GCIMAELLTGRTLF---------PGTDHIDQLKLILRLVGTPGA---ELLKKISSESA-------RNYIQS--LTQMPKM 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1370507705 241 KVkpdSKVFL--------LLQKLLTMDPTKRITSEQALQDPYFQE--DP 279
Cdd:cd07877   264 NF---ANVFIganplavdLLEKMLVLDSDKRITAAQALAHAYFAQyhDP 309
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
3-277 3.24e-41

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: 149.67  E-value: 3.24e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLS----HSDRKVWLLFDYAEHDLWHIIKFHraskankkpmqLPRSMVKSLLYQILDG 78
Cdd:cd07879    61 AYRELTLLKHMQHENVIGLLDVFTSavsgDEFQDFYLVMPYMQTDLQKIMGHP-----------LSEDKVQYLVYQMLCG 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNsplkplADLDPVVVTFWYRAPELLLGARHYTKAIDIW 158
Cdd:cd07879   130 LKYIHSAGIIHRDLKPGNLAV----NEDCELKILDFGLARHAD------AEMTGYVVTRWYRAPEVILNWMHYNQTVDIW 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 159 AIGCIFAELLTSEPIFHCRQediktsnpfHHDQLDRIFSVMGFPAD---KDWED------IRKMPEYPtlQKDFrRTTYA 229
Cdd:cd07879   200 SVGCIMAEMLTGKTLFKGKD---------YLDQLTQILKVTGVPGPefvQKLEDkaaksyIKSLPKYP--RKDF-STLFP 267
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1370507705 230 NSSlikymekhkvkpdSKVFLLLQKLLTMDPTKRITSEQALQDPYFQE 277
Cdd:cd07879   268 KAS-------------PQAVDLLEKMLELDVDKRLTATEALEHPYFDS 302
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
2-279 5.70e-41

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: 147.92  E-value: 5.70e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIkfhraskaNKKPMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd07869    49 TAIREASLLKGLKHANIVLLHDII--HTKETLTLVFEYVHTDLCQYM--------DKHPGGLHPENVKLFLFQLLRGLSY 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldpVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd07869   119 IHQRYILHRDLKPQNLLI----SDTGELKLADFGLARAKSVPSHTYSN---EVVTLWYRPPDVLLGSTEYSTCLDMWGVG 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFHcRQEDIKtsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYptlqKDFRRTTYANSSLIKYMEKHK 241
Cdd:cd07869   192 CIFVEMIQGVAAFP-GMKDIQ-------DQLERIFLVLGTPNEDTWPGVHSLPHF----KPERFTLYSPKNLRQAWNKLS 259
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370507705 242 VKPDSKVflLLQKLLTMDPTKRITSEQALQDPYFQEDP 279
Cdd:cd07869   260 YVNHAED--LASKLLQCFPKNRLSAQAALSHEYFSDLP 295
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
5-279 1.07e-39

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


Pssm-ID: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 145.58  E-value: 1.07e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSD----RKVWLLFDYAEHDLWHIIKFHRASKANkkpmqlprsmVKSLLYQILDGIH 80
Cdd:cd07878    63 RELRLLKHMKHENVIGLLDVFTPATSienfNEVYLVTNLMGADLNNIVKCQKLSDEH----------VQFLIYQLLRGLK 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplkplaDLDPVVVTFWYRAPELLLGARHYTKAIDIWAI 160
Cdd:cd07878   133 YIHSAGIIHRDLKPSNVAV----NEDCELRILDFGLARQADD------EMTGYVATRWYRAPEIMLNWMHYNQTVDIWSV 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFHCRQediktsnpfHHDQLDRIFSVMGFP------------ADKDWEDIRKMPEyPTLQKDFRRtty 228
Cdd:cd07878   203 GCIMAELLKGKALFPGND---------YIDQLKRIMEVVGTPspevlkkissehARKYIQSLPHMPQ-QDLKKIFRG--- 269
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370507705 229 ANSSLIKymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYFQE--DP 279
Cdd:cd07878   270 ANPLAID---------------LLEKMLVLDSDKRISASEALAHPYFSQyhDP 307
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
5-274 1.58e-37

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: 139.24  E-value: 1.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDrKVWLLFDYAEHDLwhiikfHRASKAnkKPMQlpRSMVKSLLYQILDGIHYLHA 84
Cdd:cd07856    58 RELKLLKHLRHENIISLSDIFISPLE-DIYFVTELLGTDL------HRLLTS--RPLE--KQFIQYFLYQILRGLKYVHS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplkplaDLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIF 164
Cdd:cd07856   127 AGVIHRDLKPSNILV----NENCDLKICDFGLARIQDP------QMTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIF 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 165 AELLTSEPIFHCRQediktsnpfHHDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQKDFRRTTYANSSLIKymekhKVKP 244
Cdd:cd07856   197 AEMLEGKPLFPGKD---------HVNQFSIITELLGTPPDDVINTICSENTLRFVQSLPKRERVPFSEKFK-----NADP 262
                         250       260       270
                  ....*....|....*....|....*....|
gi 1370507705 245 DSkvFLLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd07856   263 DA--IDLLEKMLVFDPKKRISAAEALAHPY 290
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
3-274 2.25e-37

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: 139.09  E-value: 2.25e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLSHSD----RKVWLLFDYAEHDLWHIIKfhraskankkpMQLPRSMVKSLLYQILDG 78
Cdd:cd07850    46 AYRELVLMKLVNHKNIIGLLNVFTPQKSleefQDVYLVMELMDANLCQVIQ-----------MDLDHERMSYLLYQMLCG 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGArHYTKAIDIW 158
Cdd:cd07850   115 IKHLHSAGIIHRDLKPSNIVV----KSDCTLKILDFGLARTAGTSFM----MTPYVVTRYYRAPEVILGM-GYKENVDIW 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 159 AIGCIFAELLTSEPIFHCRQediktsnpfHHDQLDRIFSVMGFPADKDWED--------IRKMPEYP--TLQKDFRRTTY 228
Cdd:cd07850   186 SVGCIMGEMIRGTVLFPGTD---------HIDQWNKIIEQLGTPSDEFMSRlqptvrnyVENRPKYAgySFEELFPDVLF 256
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1370507705 229 ANSSlikyMEKHKVKPdSKVFLLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd07850   257 PPDS----EEHNKLKA-SQARDLLSKMLVIDPEKRISVDDALQHPY 297
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
1-167 6.67e-37

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: 134.32  E-value: 6.67e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKfhraskANKKPMQLPRsmVKSLLYQILDGI 79
Cdd:cd00180    36 EELLREIEILKKLNHPNIVKLYDVF--ETENFLYLVMEYCEGgSLKDLLK------ENKGPLSEEE--ALSILRQLLSAL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKPLADLDPvvVTFWYRAPELLLGARHYTKAIDIWA 159
Cdd:cd00180   106 EYLHSNGIIHRDLKPENILLD----SDGTVKLADFGLAKDLDSDDSLLKTTGG--TTPPYYAPPELLGGRYYGPKVDIWS 179

                  ....*...
gi 1370507705 160 IGCIFAEL 167
Cdd:cd00180   180 LGVILYEL 187
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
5-275 3.26e-36

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: 134.74  E-value: 3.26e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEHDLWHIIKFHraskankkPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd07848    49 RELKMLRTLKQENIVELKEAFRRRG--KLYLVFEYVEKNMLELLEEM--------PNGVPPEKVRSYIYQLIKAIHWCHK 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEGPergrVKIADMGFARlfNSPLKPLADLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCIF 164
Cdd:cd07848   119 NDIVHRDIKPENLLISHNDV----LKLCDFGFAR--NLSEGSNANYTEYVATRWYRSPELLLGAP-YGKAVDMWSVGCIL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 165 AELLTSEPIFHCRQEDiktsnpfhhDQLDRIFSVMGFPADKDWEDIRKMPEYPTLQkdFRRTTYANSslikyMEKHKVKP 244
Cdd:cd07848   192 GELSDGQPLFPGESEI---------DQLFTIQKVLGPLPAEQMKLFYSNPRFHGLR--FPAVNHPQS-----LERRYLGI 255
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1370507705 245 DSKVFL-LLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd07848   256 LSGVLLdLMKNLLKLNPTDRYLTEQCLNHPAF 287
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
4-276 3.64e-36

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: 134.98  E-value: 3.64e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELK-HPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHiikfHRASKANKKPMQLprsmvksLLYQILDGIHYL 82
Cdd:cd14132    60 KREIKILQNLRgGPNIVKLLDVVKDPQSKTPSLIFEYVNNTDFK----TLYPTLTDYDIRY-------YMYELLKALDYC 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVmgeGPERGRVKIADMGFARlFNSPLKplaDLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGC 162
Cdd:cd14132   129 HSKGIMHRDVKPHNIMI---DHEKRKLRLIDWGLAE-FYHPGQ---EYNVRVASRYYKGPELLVDYQYYDYSLDMWSLGC 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLT-SEPIFHCRQEDiktsnpfhhDQLDRIFSVMGFPADKDWED---IRKMPEYPTLQKDFRRTTYanSSLIKYME 238
Cdd:cd14132   202 MLASMIFrKEPFFHGHDNY---------DQLVKIAKVLGTDDLYAYLDkygIELPPRLNDILGRHSKKPW--ERFVNSEN 270
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370507705 239 KHKVKPDSkvFLLLQKLLTMDPTKRITSEQALQDPYFQ 276
Cdd:cd14132   271 QHLVTPEA--LDLLDKLLRYDHQERITAKEAMQHPYFD 306
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
5-273 5.20e-36

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: 133.37  E-value: 5.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLwhiikFHRASKANKkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd05117    48 REIEILKRLDHPNIVKLYEVF--EDDKNLYLVMELCTGgEL-----FDRIVKKGS----FSEREAAKIMKQILSAVAYLH 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEGPErGRVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCI 163
Cdd:cd05117   117 SQGIVHRDLKPENILLASKDPD-SPIKIIDFGLAKIFEEGEK----LKTVCGTPYYVAPEVLKGKG-YGKKCDIWSLGVI 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 164 FAELLTSEPifhcrqediktsnPFHHDQLDRIFS--VMG---FPaDKDWEDIRKMpeyptlQKDFrrttyansslikyme 238
Cdd:cd05117   191 LYILLCGYP-------------PFYGETEQELFEkiLKGkysFD-SPEWKNVSEE------AKDL--------------- 235
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 239 khkvkpdskvfllLQKLLTMDPTKRITSEQALQDP 273
Cdd:cd05117   236 -------------IKRLLVVDPKKRLTAAEALNHP 257
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
5-279 1.22e-34

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 134.01  E-value: 1.22e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRK----VWL--LFDYAEHDLWHIIKFHraSKANKkpmQLPRSMVKSLLYQILDG 78
Cdd:PTZ00036  108 RELLIMKNLNHINIIFLKDYYYTECFKKneknIFLnvVMEFIPQTVHKYMKHY--ARNNH---ALPLFLVKLYSYQLCRA 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLFNSPLKPLAdldpVVVTFWYRAPELLLGARHYTKAIDIW 158
Cdd:PTZ00036  183 LAYIHSKFICHRDLKPQNLLI---DPNTHTLKLCDFGSAKNLLAGQRSVS----YICSRFYRAPELMLGATNYTTHIDLW 255
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 159 AIGCIFAELLTSEPIFhcrqediktSNPFHHDQLDRIFSVMGFPADkdwEDIRKM-PEYPTLQ------KDFRRTTyans 231
Cdd:PTZ00036  256 SLGCIIAEMILGYPIF---------SGQSSVDQLVRIIQVLGTPTE---DQLKEMnPNYADIKfpdvkpKDLKKVF---- 319
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370507705 232 slikymekHKVKPDSKVFLLLQkLLTMDPTKRITSEQALQDPYFQE--DP 279
Cdd:PTZ00036  320 --------PKGTPDDAINFISQ-FLKYEPLKRLNPIEALADPFFDDlrDP 360
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
5-275 3.40e-34

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: 128.41  E-value: 3.40e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIalqKVFLSHSDRKVWLLF-DYAEH-DLWHIIKfhraskaNKKPmqLPRSMVKSLLYQILDGIHYL 82
Cdd:cd06606    48 REIRILSSLKHPNIV---RYLGTERTENTLNIFlEYVPGgSLASLLK-------KFGK--LPEPVVRKYTRQILEGLEYL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPLADLdPVVVTFWYRAPELLLGARHYTKAiDIWAIGC 162
Cdd:cd06606   116 HSNGIVHRDIKGANILVDSD----GVVKLADFGCAKRLAEIATGEGTK-SLRGTPYWMAPEVIRGEGYGRAA-DIWSLGC 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLTSEPIFhcrqediktsnPFHHDQLDRIFSVMGFPadkdwedirKMPEYPTLQ----KDFrrttyansslikyme 238
Cdd:cd06606   190 TVIEMATGKPPW-----------SELGNPVAALFKIGSSG---------EPPPIPEHLseeaKDF--------------- 234
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1370507705 239 khkvkpdskvfllLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd06606   235 -------------LRKCLQRDPKKRPTADELLQHPFL 258
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
3-274 1.31e-32

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: 126.68  E-value: 1.31e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLSHSDRKVWllfdyaeHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYL 82
Cdd:cd07876    67 AYRELVLLKCVNHKNIISLLNVFTPQKSLEEF-------QDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMGEGPergrVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGC 162
Cdd:cd07876   140 HSAGIIHRDLKPSNIVVKSDCT----LKILDFGLARTACTNFM----MTPYVVTRYYRAPEVILGMG-YKENVDIWSVGC 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLTSEPIFHCRQediktsnpfHHDQLDRIFSVMGFPA----DKDWEDIRKM----PEYP--TLQKDFRRTTYANSS 232
Cdd:cd07876   211 IMGELVKGSVIFQGTD---------HIDQWNKVIEQLGTPSaefmNRLQPTVRNYvenrPQYPgiSFEELFPDWIFPSES 281
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 233 likymEKHKVKpDSKVFLLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd07876   282 -----ERDKLK-TSQARDLLSKMLVIDPDKRISVDEALRHPY 317
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
5-275 1.73e-31

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: 121.12  E-value: 1.73e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEH-DLWHIIKFHRASkankkpmQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14008    53 REIAIMKKLDHPNIVRLYEVIDDPESDKLYLVLEYCEGgPVMELDSGDRVP-------PLPEETARKYFRDLVLGLEYLH 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNsplKPLADLDPVVVTFWYRAPELLLG-ARHY-TKAIDIWAIG 161
Cdd:cd14008   126 ENGIVHRDIKPENLLL----TADGTVKISDFGVSEMFE---DGNDTLQKTAGTPAFLAPELCDGdSKTYsGKAADIWALG 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 C-----IFAELltsepifhcrqediktsnPFHHDQLDRIFSVmgfpadkdwedIRKMPEYPTLQKDfrrttyANSSLIKy 236
Cdd:cd14008   199 VtlyclVFGRL------------------PFNGDNILELYEA-----------IQNQNDEFPIPPE------LSPELKD- 242
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370507705 237 mekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14008   243 --------------LLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
5-274 3.64e-31

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: 120.05  E-value: 3.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd14002    49 QEIEILRKLNHPNIIEMLDSF--ETKKEFVVVTEYAQGELFQILEDDGT---------LPEEEVRSIAKQLVSALHYLHS 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmGEGperGRVKIADMGFARL--FNSPLkpladLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGC 162
Cdd:cd14002   118 NRIIHRDMKPQNILI-GKG---GVVKLCDFGFARAmsCNTLV-----LTSIKGTPLYMAPE-LVQEQPYDHTADLWSLGC 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLTSEPifhcrqediktsnPFhhdqldrifsvmgfpadkdwedirkmpeyptlqkdfrrttYANS--SLIKYMEKH 240
Cdd:cd14002   188 ILYELFVGQP-------------PF----------------------------------------YTNSiyQLVQMIVKD 214
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1370507705 241 KVK------PDSKVFllLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14002   215 PVKwpsnmsPEFKSF--LQGLLNKDPSKRLSWPDLLEHPF 252
Pkinase pfam00069
Protein kinase domain;
1-275 7.23e-31

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 118.12  E-value: 7.23e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAEH-DLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGi 79
Cdd:pfam00069  43 KNILREIKILKKLNHPNIVRLYDAFEDKDN--LYLVLEYVEGgSLFDLLSEKGA---------FSEREAKFIMKQILEG- 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 hylhanwvlhrdlkpanilvmgegpergrvkiadmgfarlfnspLKPLADLDPVVVTFWYRAPELLlGARHYTKAIDIWA 159
Cdd:pfam00069 111 --------------------------------------------LESGSSLTTFVGTPWYMAPEVL-GGNPYGPKVDVWS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 160 IGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFSVMGFpadkdwEDIRKMPEYPTLQKDFRRttyansslikymek 239
Cdd:pfam00069 146 LGCILYELLTGKP-------------PFPGINGNEIYELIID------QPYAFPELPSNLSEEAKD-------------- 192
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1370507705 240 hkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:pfam00069 193 -----------LLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
5-175 1.03e-30

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 123.58  E-value: 1.03e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAE-HDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:COG0515    56 REARALARLNHPNIVRVYDVG--EEDGRPYLVMEYVEgESLADLLRRRGP---------LPPAEALRILAQLAEALAAAH 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPlkPLADLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCI 163
Cdd:COG0515   125 AAGIVHRDIKPANILLT----PDGRVKLIDFGIARALGGA--TLTQTGTVVGTPGYMAPEQARGEP-VDPRSDVYSLGVT 197
                         170
                  ....*....|..
gi 1370507705 164 FAELLTSEPIFH 175
Cdd:COG0515   198 LYELLTGRPPFD 209
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
5-174 1.39e-30

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: 118.46  E-value: 1.39e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAE-HDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14014    49 REARALARLSHPNIVRVYDVG--EDDGRPYIVMEYVEgGSLADLLRERGP---------LPPREALRILAQIADALAAAH 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLdpVVVTFWYRAPELLLGARhYTKAIDIWAIGCI 163
Cdd:cd14014   118 RAGIVHRDIKPANILL----TEDGRVKLTDFGIARALGDSGLTQTGS--VLGTPAYMAPEQARGGP-VDPRSDIYSLGVV 190
                         170
                  ....*....|.
gi 1370507705 164 FAELLTSEPIF 174
Cdd:cd14014   191 LYELLTGRPPF 201
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
5-276 3.34e-30

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: 117.19  E-value: 3.34e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKfhraskANKKpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14007    49 REIEIQSHLRHPNILRLYGYF--EDKKRIYLILEYAPNgELYKELK------KQKR---FDEKEAAKYIYQLALALDYLH 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGF-ARLFNSPLKPLADldpvvvTFWYRAPELLLGaRHYTKAIDIWAIGC 162
Cdd:cd14007   118 SKNIIHRDIKPENILL----GSNGELKLADFGWsVHAPSNRRKTFCG------TLDYLPPEMVEG-KEYDYKVDIWSLGV 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLTSEPIFHCRQEDiktsnpfhhDQLDRIFSVmgfpadkdweDIrKMPEY-PTLQKDFrrttyansslikymekhk 241
Cdd:cd14007   187 LCYELLVGKPPFESKSHQ---------ETYKRIQNV----------DI-KFPSSvSPEAKDL------------------ 228
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 242 vkpdskvfllLQKLLTMDPTKRITSEQALQDPYFQ 276
Cdd:cd14007   229 ----------ISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
3-274 4.24e-30

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: 119.81  E-value: 4.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLSHSD----RKVWLLFDYAEHDLWHIIKfhraskankkpMQLPRSMVKSLLYQILDG 78
Cdd:cd07874    63 AYRELVLMKCVNHKNIISLLNVFTPQKSleefQDVYLVMELMDANLCQVIQ-----------MELDHERMSYLLYQMLCG 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVMGEGPergrVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGArHYTKAIDIW 158
Cdd:cd07874   132 IKHLHSAGIIHRDLKPSNIVVKSDCT----LKILDFGLARTAGTSFM----MTPYVVTRYYRAPEVILGM-GYKENVDIW 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 159 AIGCIFAELLTSEPIFHCRQediktsnpfHHDQLDRIFSVMGFPADkdwEDIRKMPeyPTLQKDFR-RTTYAN------- 230
Cdd:cd07874   203 SVGCIMGEMVRHKILFPGRD---------YIDQWNKVIEQLGTPCP---EFMKKLQ--PTVRNYVEnRPKYAGltfpklf 268
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1370507705 231 -SSLIKYMEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd07874   269 pDSLFPADSEHNKLKASQARDLLSKMLVIDPAKRISVDEALQHPY 313
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
5-275 5.53e-30

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


Pssm-ID: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 117.45  E-value: 5.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLREL-KHPNVIALQKVFlsHSDRKVWL---------LFDYaehdLWHIIKFhrASKANKKPMQlprsmvksllyQ 74
Cdd:cd14093    57 REIEILRQVsGHPNIIELHDVF--ESPTFIFLvfelcrkgeLFDY----LTEVVTL--SEKKTRRIMR-----------Q 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLfnspLKPLADLDPVVVTFWYRAPELL-----LGAR 149
Cdd:cd14093   118 LFEAVEFLHSLNIVHRDLKPENILLDDN----LNVKISDFGFATR----LDEGEKLRELCGTPGYLAPEVLkcsmyDNAP 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 150 HYTKAIDIWAIGCIFAELLTSEPIFhcrqediktsnpFHHDQLDRIFSVM----GFPAdKDWEDIRKMPeyptlqKDfrr 225
Cdd:cd14093   190 GYGKEVDMWACGVIMYTLLAGCPPF------------WHRKQMVMLRNIMegkyEFGS-PEWDDISDTA------KD--- 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370507705 226 ttyansslikymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14093   248 -------------------------LISKLLVVDPKKRLTAEEALEHPFF 272
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
55-275 1.07e-29

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: 117.65  E-value: 1.07e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  55 KANK-KPMQLprSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgEGPERGRVKIADMGFARLFNSPlkpladldpv 133
Cdd:cd14210   106 KSNNfQGLSL--SLIRKFAKQILQALQFLHKLNIIHCDLKPENILL--KQPSKSSIKVIDFGSSCFEGEK---------- 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 134 VVTF----WYRAPELLLGARhYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGfpadkdwed 209
Cdd:cd14210   172 VYTYiqsrFYRAPEVILGLP-YDTAIDMWSLGCILAELYTGYPLFPGENE---------EEQLACIMEVLG--------- 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 210 irkMPEYPTLQKDFRRTTY---------ANSSLIKYME------KHKVKPDSKVFL-LLQKLLTMDPTKRITSEQALQDP 273
Cdd:cd14210   233 ---VPPKSLIDKASRRKKFfdsngkprpTTNSKGKKRRpgskslAQVLKCDDPSFLdFLKKCLRWDPSERMTPEEALQHP 309

                  ..
gi 1370507705 274 YF 275
Cdd:cd14210   310 WI 311
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
5-274 1.72e-29

Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AMPK-like subfamily is composed of AMPK, MARK, BRSK, NUAK, MELK, SNRK, TSSK, and SIK, among others. LKB1 serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. BRSKs play important roles in establishing neuronal polarity. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. The AMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 115.31  E-value: 1.72e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14003    48 REIEIMKLLNHPNIIKLYEVI--ETENKIYLVMEYASGgELFDYIVNNGR---------LSEDEARRFFQQLISAVDYCH 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFnsplKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCI 163
Cdd:cd14003   117 SNGIVHRDLKLENILL----DKNGNLKIIDFGLSNEF----RGGSLLKTFCGTPAYAAPEVLLGRKYDGPKADVWSLGVI 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 164 FAELLTSEPifhcrqediktsnPFHHDQLDRIFsvmgfpadkdWEDIRKMPEYP-TLQKDFRRttyansslikymekhkv 242
Cdd:cd14003   189 LYAMLTGYL-------------PFDDDNDSKLF----------RKILKGKYPIPsHLSPDARD----------------- 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1370507705 243 kpdskvflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14003   229 --------LIRRMLVVDPSKRITIEEILNHPW 252
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
3-280 1.78e-29

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: 118.22  E-value: 1.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLSHSDRKVWllfdyaeHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYL 82
Cdd:cd07875    70 AYRELVLMKCVNHKNIIGLLNVFTPQKSLEEF-------QDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMGEGPergrVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGArHYTKAIDIWAIGC 162
Cdd:cd07875   143 HSAGIIHRDLKPSNIVVKSDCT----LKILDFGLARTAGTSFM----MTPYVVTRYYRAPEVILGM-GYKENVDIWSVGC 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLTSEPIFHCRQediktsnpfHHDQLDRIFSVMGFPADkdwEDIRKMPeyPTLQKDFR-RTTYANSSLIKYM---- 237
Cdd:cd07875   214 IMGEMIKGGVLFPGTD---------HIDQWNKVIEQLGTPCP---EFMKKLQ--PTVRTYVEnRPKYAGYSFEKLFpdvl 279
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370507705 238 -----EKHKVKPdSKVFLLLQKLLTMDPTKRITSEQALQDPYFQ--EDPL 280
Cdd:cd07875   280 fpadsEHNKLKA-SQARDLLSKMLVIDASKRISVDEALQHPYINvwYDPS 328
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
5-275 1.85e-29

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: 115.74  E-value: 1.85e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14080    51 RELEILRKLRHPNIIQVYSIF--ERGSKVFIFMEYAEHgDLLEYIQKRGA---------LSESQARIWFRQLALAVQYLH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPlkplaDLDPVVVTFW----YRAPELLLGARHYTKAIDIWA 159
Cdd:cd14080   120 SLDIAHRDLKCENILLD----SNNNVKLSDFGFARLCPDD-----DGDVLSKTFCgsaaYAAPEILQGIPYDPKKYDIWS 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 160 IGCIFAELLTSEPIFhcRQEDIKTsnpFHHDQLDRIFsvmGFPadkdwedirkmpeyptlqkdfrrttyansslikymeK 239
Cdd:cd14080   191 LGVILYIMLCGSMPF--DDSNIKK---MLKDQQNRKV---RFP------------------------------------S 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1370507705 240 HKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14080   227 SVKKLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
4-174 3.74e-29

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: 114.17  E-value: 3.74e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELKHPNVIALqkVFLSHSDRKVWLLFDYAEH-DLWHIIkfhraskaNKKPMQLPRSMVKSLLYQILDGIHYL 82
Cdd:cd13999    38 RREVSILSKLRHPNIVQF--IGACLSPPPLCIVTEYMPGgSLYDLL--------HKKKIPLSWSLRLKIALDIARGMNYL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNsplKPLADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGC 162
Cdd:cd13999   108 HSPPIIHRDLKSLNILL----DENFTVKIADFGLSRIKN---STTEKMTGVVGTPRWMAPEVLRG-EPYTEKADVYSFGI 179
                         170
                  ....*....|..
gi 1370507705 163 IFAELLTSEPIF 174
Cdd:cd13999   180 VLWELLTGEVPF 191
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
2-175 3.80e-28

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: 111.79  E-value: 3.80e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKfhrASKANKKPmqLPRSMVKSLLYQILDGIH 80
Cdd:cd08215    45 EALNEVKLLSKLKHPNIVKYYESFEE--NGKLCIVMEYADGgDLAQKIK---KQKKKGQP--FPEEQILDWFVQICLALK 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLkPLAdlDPVVVTFWYRAPELLLGaRHYTKAIDIWAI 160
Cdd:cd08215   118 YLHSRKILHRDLKTQNIFLTKD----GVVKLGDFGISKVLESTT-DLA--KTVVGTPYYLSPELCEN-KPYNYKSDIWAL 189
                         170
                  ....*....|....*
gi 1370507705 161 GCIFAELLTSEPIFH 175
Cdd:cd08215   190 GCVLYELCTLKHPFE 204
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
1-175 6.53e-28

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: 111.16  E-value: 6.53e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACR-EIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKfhrasKANKkpmqLPRSMVKSLLYQILDG 78
Cdd:cd06627    43 LKSVMgEIDLLKKLNHPNIVKYIGSV--KTKDSLYIILEYVENgSLASIIK-----KFGK----FPESLVAVYIYQVLEG 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldpVVVTFWYRAPELLLGARHYTKAiDIW 158
Cdd:cd06627   112 LAYLHEQGVIHRDIKGANILT----TKDGLVKLADFGVATKLNEVEKDENS---VVGTPYWMAPEVIEMSGVTTAS-DIW 183
                         170
                  ....*....|....*..
gi 1370507705 159 AIGCIFAELLTSEPIFH 175
Cdd:cd06627   184 SVGCTVIELLTGNPPYY 200
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
5-275 1.05e-27

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: 110.37  E-value: 1.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKfhraskanKKPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd05122    46 NEIAILKKCKHPNIVKYYGSYLK--KDELWIVMEFCSGgSLKDLLK--------NTNKTLTEQQIAYVCKEVLKGLEYLH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgegpERGRVKIADMGFArlfnSPLKPLADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCI 163
Cdd:cd05122   116 SHGIIHRDIKAANILLT----SDGEVKLIDFGLS----AQLSDGKTRNTFVGTPYWMAPEVIQG-KPYGFKADIWSLGIT 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 164 FAELLTSEPifhcrqediktsnPFHHdqlDRIFSVMGFPADKDwedirkmpeYPTLQkdfrrttyansslikymEKHKVK 243
Cdd:cd05122   187 AIEMAEGKP-------------PYSE---LPPMKALFLIATNG---------PPGLR-----------------NPKKWS 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1370507705 244 PDSKVFLLlqKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd05122   225 KEFKDFLK--KCLQKDPEKRPTAEQLLKHPFI 254
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
5-274 1.96e-26

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: 107.48  E-value: 1.96e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKfhraskankKPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14084    60 TEIEILKKLSHPCIIKIEDFF--DAEDDYYIVLELMEGgELFDRVV---------SNKRLKEAICKLYFYQMLLAVKYLH 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEGpERGRVKIADMGFARLF--NSPLKPLADldpvvvTFWYRAPELLL--GARHYTKAIDIWA 159
Cdd:cd14084   129 SNGIIHRDLKPENVLLSSQE-EECLIKITDFGLSKILgeTSLMKTLCG------TPTYLAPEVLRsfGTEGYTRAVDCWS 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 160 IGCIFAELLTSEPIF--HCRQEDIKtsnpfhhdqlDRIFSvmgfpadkdwedirkmPEYPTLQKDFRRTTyansslikym 237
Cdd:cd14084   202 LGVILFICLSGYPPFseEYTQMSLK----------EQILS----------------GKYTFIPKAWKNVS---------- 245
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1370507705 238 ekhkvkpdSKVFLLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14084   246 --------EEAKDLVKKMLVVDPSRRPSIEEALEHPW 274
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
6-275 7.27e-26

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: 105.81  E-value: 7.27e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELK------HPNVIALQKVFLSHSDrkVWLLFDYAEHDLWHIIKFHRaskanKKPMQLPRsmVKSLLYQILDGI 79
Cdd:cd14133    45 EIRLLELLNkkdkadKYHIVRLKDVFYFKNH--LCIVFELLSQNLYEFLKQNK-----FQYLSLPR--IRKIAQQILEAL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILVmgEGPERGRVKIADmgfarlFNSPLKPLADLDPVVVTFWYRAPELLLGARhYTKAIDIWA 159
Cdd:cd14133   116 VFLHSLGLIHCDLKPENILL--ASYSRCQIKIID------FGSSCFLTQRLYSYIQSRYYRAPEVILGLP-YDEKIDMWS 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 160 IGCIFAELLTSEPIFhcrqediktSNPFHHDQLDRIFSVMGFPAdkdwedirkmpeyptlqkdfrrttyanssliKYMEK 239
Cdd:cd14133   187 LGCILAELYTGEPLF---------PGASEVDQLARIIGTIGIPP-------------------------------AHMLD 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1370507705 240 HKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14133   227 QGKADDELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
5-174 1.14e-25

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: 105.00  E-value: 1.14e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVflSHSDRKVWLLFDY-AEHDLWHIIKFHRaskankkpmQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14009    41 SEIAILKSIKHPNIVRLYDV--QKTEDFIYLVLEYcAGGDLSQYIRKRG---------RLPEAVARHFMQQLASGLKFLR 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILvMGEGPERGRVKIADMGFAR----------LFNSPLkpladldpvvvtfwYRAPELLLGARHYTK 153
Cdd:cd14009   110 SKNIIHRDLKPQNLL-LSTSGDDPVLKIADFGFARslqpasmaetLCGSPL--------------YMAPEILQFQKYDAK 174
                         170       180
                  ....*....|....*....|.
gi 1370507705 154 AiDIWAIGCIFAELLTSEPIF 174
Cdd:cd14009   175 A-DLWSVGAILFEMLVGKPPF 194
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
6-275 2.86e-24

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: 101.09  E-value: 2.86e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKfhraskaNKKPMQLPRsmVKSLLYQILDGIHYLHA 84
Cdd:cd14099    51 EIKIHRSLKHPNIVKFHDCF--EDEENVYILLELCSNgSLMELLK-------RRKALTEPE--VRYFMRQILSGVKYLHS 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmgegPERGRVKIADMGFArlfnsplkplADLDP-------VVVTFWYRAPELLLGARHYTKAIDI 157
Cdd:cd14099   120 NRIIHRDLKLGNLFL----DENMNVKIGDFGLA----------ARLEYdgerkktLCGTPNYIAPEVLEKKKGHSFEVDI 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 158 WAIGCIFAELLTSEPIFHCRqeDIKtsnpfhhdqldrifsvmgfpadkdwedirkmpeyptlqkdfrrTTYANSSLIKY- 236
Cdd:cd14099   186 WSLGVILYTLLVGKPPFETS--DVK-------------------------------------------ETYKRIKKNEYs 220
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370507705 237 MEKHKVKPDSKVfLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14099   221 FPSHLSISDEAK-DLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
5-274 6.32e-24

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 100.03  E-value: 6.32e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDY-AEHDLwhiikFHRASKankkPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14006    38 REISILNQLQHPRIIQLHEAYES--PTELVLILELcSGGEL-----LDRLAE----RGSLSEEEVRTYMRQLLEGLQYLH 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgEGPERGRVKIADMGFARlfnsPLKPLADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCI 163
Cdd:cd14006   107 NHHILHLDLKPENILL--ADRPSPQIKIIDFGLAR----KLNPGEELKEIFGTPEFVAPEIVNG-EPVSLATDMWSIGVL 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 164 FAELLTSEpifhcrqediktsNPFHhdqldrifsvmgfpADKDWEDIRKMPEYptlQKDFRRTTYANSSlikymekhkvk 243
Cdd:cd14006   180 TYVLLSGL-------------SPFL--------------GEDDQETLANISAC---RVDFSEEYFSSVS----------- 218
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370507705 244 PDSKVFllLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14006   219 QEAKDF--IRKLLVKEPRKRPTAQEALQHPW 247
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
2-267 1.07e-23

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: 99.98  E-value: 1.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKFHRaskankkpmQLPRSMVKSLLYQILDGIH 80
Cdd:cd05581    47 YVTIEKEVLSRLAHPGIVKLYYTF--QDESKLYFVLEYAPNgDLLEYIRKYG---------SLDEKCTRFYTAEIVLALE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLDP--------------VVVTFWYRAPELLL 146
Cdd:cd05581   116 YLHSKGIIHRDLKPENILL----DEDMHIKITDFGTAKVLGPDSSPESTKGDadsqiaynqaraasFVGTAEYVSPELLN 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 147 GaRHYTKAIDIWAIGCIFAELLTSEPIFHCrqediktSNPFHhdqldrIFsvmgfpadkdwEDIRKM-PEYPtlqkdfrr 225
Cdd:cd05581   192 E-KPAGKSSDLWALGCIIYQMLTGKPPFRG-------SNEYL------TF-----------QKIVKLeYEFP-------- 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 226 ttyansslikymekHKVKPDSKVflLLQKLLTMDPTKRITSE 267
Cdd:cd05581   239 --------------ENFPPDAKD--LIQKLLVLDPSKRLGVN 264
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
5-275 1.24e-23

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: 99.13  E-value: 1.24e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLW-HIIKFHRaskankkpmqLPRSMVKslLY--QILDGIH 80
Cdd:cd05123    42 NERNILERVNHPFIVKLHYAF--QTEEKLYLVLDYVPGgELFsHLSKEGR----------FPEERAR--FYaaEIVLALE 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFArlfnsplKPLADLDPVVVTFW----YRAPELLLGARhYTKAID 156
Cdd:cd05123   108 YLHSLGIIYRDLKPENILL----DSDGHIKLTDFGLA-------KELSSDGDRTYTFCgtpeYLAPEVLLGKG-YGKAVD 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 157 IWAIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFsvmgfpaDKDWEDIRKMPEYptlqkdfrrttyanssliky 236
Cdd:cd05123   176 WWSLGVLLYEMLTGKP-------------PFYAENRKEIY-------EKILKSPLKFPEY-------------------- 215
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 237 mekhkVKPDSKvfLLLQKLLTMDPTKRITS---EQALQDPYF 275
Cdd:cd05123   216 -----VSPEAK--SLISGLLQKDPTKRLGSggaEEIKAHPFF 250
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
5-274 1.33e-23

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: 99.47  E-value: 1.33e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14098    50 REINILKSLEHPGIVRLIDWY--EDDQHIYLVMEYVEGgDLMDFIMAWGA---------IPEQHARELTKQILEAMAYTH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEGPErgRVKIADMGFARLF--NSPLKPLadldpvVVTFWYRAPELLLGARH-----YTKAID 156
Cdd:cd14098   119 SMGITHRDLKPENILITQDDPV--IVKISDFGLAKVIhtGTFLVTF------CGTMAYLAPEILMSKEQnlqggYSNLVD 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 157 IWAIGCIFAELLTSepifhcrqediktSNPFHHDQLDRIFsvmgfpadkdwedirkmpeyptlqKDFRRTTYANSSLIKY 236
Cdd:cd14098   191 MWSVGCLVYVMLTG-------------ALPFDGSSQLPVE------------------------KRIRKGRYTQPPLVDF 233
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370507705 237 mekhKVKPDSKVFLLlqKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14098   234 ----NISEEAIDFIL--RLLDVDPEKRMTAAQALDHPW 265
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
2-177 1.63e-23

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: 99.00  E-value: 1.63e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAE-HDLWHIIkfhraSKANKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd08530    45 DSVNEIRLLASVNHPNIIRYKEAFLD--GNRLCIVMEYAPfGDLSKLI-----SKRKKKRRLFPEDDIWRIFIQMLRGLK 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLkpladLDPVVVTFWYRAPELLLGaRHYTKAIDIWAI 160
Cdd:cd08530   118 ALHDQKILHRDLKSANILLS----AGDLVKIGDLGISKVLKKNL-----AKTQIGTPLYAAPEVWKG-RPYDYKSDIWSL 187
                         170
                  ....*....|....*..
gi 1370507705 161 GCIFAELLTSEPIFHCR 177
Cdd:cd08530   188 GCLLYEMATFRPPFEAR 204
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
6-274 2.74e-23

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: 98.21  E-value: 2.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSdrKVWL---------LFD-------YAEHDLWHIIKfhraskankkpmqlprsmvk 69
Cdd:cd14083    51 EIAVLRKIKHPNIVQLLDIYESKS--HLYLvmelvtggeLFDrivekgsYTEKDASHLIR-------------------- 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  70 sllyQILDGIHYLHANWVLHRDLKPANILVMGEGpERGRVKIADMGFARLFNSplkplADLDPVVVTFWYRAPElLLGAR 149
Cdd:cd14083   109 ----QVLEAVDYLHSLGIVHRDLKPENLLYYSPD-EDSKIMISDFGLSKMEDS-----GVMSTACGTPGYVAPE-VLAQK 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 150 HYTKAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFS-VMGFPADKD---WEDIRKMpeyptlQKDFrr 225
Cdd:cd14083   178 PYGKAVDCWSIGVISYILLCGYP-------------PFYDENDSKLFAqILKAEYEFDspyWDDISDS------AKDF-- 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1370507705 226 ttyansslikymekhkvkpdskvfllLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14083   237 --------------------------IRHLMEKDPNKRYTCEQALEHPW 259
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
3-275 4.30e-23

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 98.11  E-value: 4.30e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLREL-KHPNVIalqKVFLSHSDRK-VWLLFDYAEHDLWHIIKFHRASKANKKPMQLPrsmvKSLLYQILDGIH 80
Cdd:cd13982    41 ADREVQLLRESdEHPNVI---RYFCTEKDRQfLYIALELCAASLQDLVESPRESKLFLRPGLEP----VRLLRQIASGLA 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILV-MGEGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLG--ARHYTKAIDI 157
Cdd:cd13982   114 HLHSLNIVHRDLKPQNILIsTPNAHGNVRAMISDFGLCKKLDVGRSSFSRRSGVAGTSGWIAPEMLSGstKRRQTRAVDI 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 158 WAIGCIFAELLTsepifhcrqediKTSNPFhHDQLDRIFSVMG--FPADKDWEDIRKMPEyptlqkdfrrttyaNSSLIK 235
Cdd:cd13982   194 FSLGCVFYYVLS------------GGSHPF-GDKLEREANILKgkYSLDKLLSLGEHGPE--------------AQDLIE 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1370507705 236 YMekhkvkpdskvflllqklLTMDPTKRITSEQALQDPYF 275
Cdd:cd13982   247 RM------------------IDFDPEKRPSAEEVLNHPFF 268
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
2-275 5.79e-23

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 98.12  E-value: 5.79e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELK-HPNVIALQKVFLSHSdrKVWLLFDYAEHDLWHIIKFHRASKANKKPmqlpRSMVKSLLyqilDGIH 80
Cdd:cd14181    61 STLKEIHILRQVSgHPSIITLIDSYESST--FIFLVFDLMRRGELFDYLTEKVTLSEKET----RSIMRSLL----EAVS 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFArlfnSPLKPLADLDPVVVTFWYRAPELL---LGARH--YTKAI 155
Cdd:cd14181   131 YLHANNIVHRDLKPENILL----DDQLHIKLSDFGFS----CHLEPGEKLRELCGTPGYLAPEILkcsMDETHpgYGKEV 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 156 DIWAIGCIFAELLTSEPIFhcrqediktsnpFHHDQLDRIFSVM------GFPadkDWEDirkmpeyptlqkdfrrttya 229
Cdd:cd14181   203 DLWACGVILFTLLAGSPPF------------WHRRQMLMLRMIMegryqfSSP---EWDD-------------------- 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1370507705 230 NSSLIKYmekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14181   248 RSSTVKD--------------LISRLLVVDPEIRLTAEQALQHPFF 279
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
6-274 6.81e-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: 97.41  E-value: 6.81e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDRKVWL-------LFD-------YAEHDlwhiikfhrASKankkpmqlprsmvksL 71
Cdd:cd14167    51 EIAVLHKIKHPNIVALDDIYESGGHLYLIMqlvsggeLFDrivekgfYTERD---------ASK---------------L 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  72 LYQILDGIHYLHANWVLHRDLKPANILVMGEgPERGRVKIADMGFARLFNSPlkplADLDPVVVTFWYRAPElLLGARHY 151
Cdd:cd14167   107 IFQILDAVKYLHDMGIVHRDLKPENLLYYSL-DEDSKIMISDFGLSKIEGSG----SVMSTACGTPGYVAPE-VLAQKPY 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 152 TKAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIF-SVMGFPADKD---WEDIRKMpeyptlQKDFrrtt 227
Cdd:cd14167   181 SKAVDCWSIGVIAYILLCGYP-------------PFYDENDAKLFeQILKAEYEFDspyWDDISDS------AKDF---- 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1370507705 228 yansslikymekhkvkpdskvfllLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14167   238 ------------------------IQHLMEKDPEKRFTCEQALQHPW 260
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
5-276 7.08e-23

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: 97.28  E-value: 7.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKFHraskankkPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd06614    45 NEILIMKECKHPNIVDYYDSYLV--GDELWVVMEYMDGgSLTDIITQN--------PVRMNESQIAYVCREVLQGLEYLH 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFArlfnsplkplADLDP-------VVVTFWYRAPELLLGARhYTKAID 156
Cdd:cd06614   115 SQNVIHRDIKSDNILL----SKDGSVKLADFGFA----------AQLTKekskrnsVVGTPYWMAPEVIKRKD-YGPKVD 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 157 IWAIGCIFAELLTSEPifhcrqediktsnPFhhdqldrifsvMGFPADKDWEDIRKMPeYPTLQkdfrrttyanssliky 236
Cdd:cd06614   180 IWSLGIMCIEMAEGEP-------------PY-----------LEEPPLRALFLITTKG-IPPLK---------------- 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1370507705 237 mEKHKVKPDSKVFllLQKLLTMDPTKRITSEQALQDPYFQ 276
Cdd:cd06614   219 -NPEKWSPEFKDF--LNKCLVKDPEKRPSAEELLQHPFLK 255
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
5-275 4.77e-22

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: 95.09  E-value: 4.77e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIAlqkvFLSHSDRK--VWLLFDYAEH-DLWHIIKFHraskankkpMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd14069    49 KEVCIQKMLSHKNVVR----FYGHRREGefQYLFLEYASGgELFDKIEPD---------VGMPEDVAQFYFQQLMAGLKY 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLAdLDPVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd14069   116 LHSCGITHRDIKPENLLL----DENDNLKISDFGLATVFRYKGKERL-LNKMCGTLPYVAPELLAKKKYRAEPVDVWSCG 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEpifhcrqediktsnpfhhdqldrifsvmgFPADkdwEDIRKMPEYpTLQKDFRRTTYANSSLIkymekhk 241
Cdd:cd14069   191 IVLFAMLAGE-----------------------------LPWD---QPSDSCQEY-SDWKENKKTYLTPWKKI------- 230
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370507705 242 vkpDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14069   231 ---DTAALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
6-275 5.70e-22

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: 94.92  E-value: 5.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEH-DLWHIIKfhRASKANKKpmqLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd08217    49 EVNILRELKHPNIVRYYDRIVDRANTTLYIVMEYCEGgDLAQLIK--KCKKENQY---IPEEFIWKIFTQLLLALYECHN 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 -----NWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKpLAdlDPVVVTFWYRAPELLLGARhYTKAIDIWA 159
Cdd:cd08217   124 rsvggGKILHRDLKPANIFL----DSDNNVKLGDFGLARVLSHDSS-FA--KTYVGTPYYMSPELLNEQS-YDEKSDIWS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 160 IGCIFAELLTSEPIFHCRQediktsnpfhHDQLdrifsvmgfpADKdwedIRKMPeyptlqkdFRRTTYANSslikymek 239
Cdd:cd08217   196 LGCLIYELCALHPPFQAAN----------QLEL----------AKK----IKEGK--------FPRIPSRYS-------- 235
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1370507705 240 hkvkpdSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd08217   236 ------SELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
6-274 5.71e-22

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: 94.66  E-value: 5.71e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd14121    45 EIELLKKLKHPHIVELKDFQWD--EEHIYLIMEYCSGgDLSRFIRSRRT---------LPESTVRRFLQQLASALQFLRE 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMgeGPERGRVKIADMGFARLfnspLKPLADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCIF 164
Cdd:cd14121   114 HNISHMDLKPQNLLLS--SRYNPVLKLADFGFAQH----LKPNDEAHSLRGSPLYMAPEMILK-KKYDARVDLWSVGVIL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 165 AELLTSEPIFHCR-----QEDIKTSNPFhhdqldrifsvmgfpadkdwedirKMPEYPTLQKDFRRttyansslikymek 239
Cdd:cd14121   187 YECLFGRAPFASRsfeelEEKIRSSKPI------------------------EIPTRPELSADCRD-------------- 228
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 240 hkvkpdskvflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14121   229 -----------LLLRLLQRDPDRRISFEEFFAHPF 252
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
5-275 1.60e-21

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: 93.48  E-value: 1.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKfhraSKANKKpmqLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd14119    43 REIQILRRLNHRNVIKLVDVLYNEEKQKLYMVMEYCVGGLQEMLD----SAPDKR---LPIWQAHGYFVQLIDGLEYLHS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEgperGRVKIADMGFARLfnspLKPLADLDPVVV---TFWYRAPELLLGARHYT-KAIDIWAI 160
Cdd:cd14119   116 QGIIHKDIKPGNLLLTTD----GTLKISDFGVAEA----LDLFAEDDTCTTsqgSPAFQPPEIANGQDSFSgFKVDIWSA 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEpifhcrqediktsNPFHHDQLDRIFSVMGfpaDKDWEdirkMPeyPTLQKDFRrttyansSLIKYMekh 240
Cdd:cd14119   188 GVTLYNMTTGK-------------YPFEGDNIYKLFENIG---KGEYT----IP--DDVDPDLQ-------DLLRGM--- 235
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 241 kvkpdskvflllqklLTMDPTKRITSEQALQDPYF 275
Cdd:cd14119   236 ---------------LEKDPEKRFTIEQIRQHPWF 255
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
5-274 1.61e-21

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: 93.24  E-value: 1.61e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLwhiikFHRASKANKkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14663    49 REIAIMKLLRHPNIVELHEVM--ATKTKIFFVMELVTGgEL-----FSKIAKNGR----LKEDKARKYFQQLIDAVDYCH 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFARLfNSPLKPLADLDPVVVTFWYRAPElLLGARHYTKAI-DIWAIGC 162
Cdd:cd14663   118 SRGVFHRDLKPENLLL----DEDGNLKISDFGLSAL-SEQFRQDGLLHTTCGTPNYVAPE-VLARRGYDGAKaDIWSCGV 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLTSepifhcrqediktSNPFHHDQLDRIFSVMGfpadkdwediRKMPEYPT-LQKDFRRttyansslikymekhk 241
Cdd:cd14663   192 ILFVLLAG-------------YLPFDDENLMALYRKIM----------KGEFEYPRwFSPGAKS---------------- 232
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370507705 242 vkpdskvflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14663   233 ---------LIKRILDPNPSTRITVEQIMASPW 256
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
5-275 1.79e-21

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: 93.10  E-value: 1.79e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIalqKVFLS-HSDRKVWLLFDYAE----HDLWHIIkfhraskaNKkpmQLPRSMVKSLLYQILDGI 79
Cdd:cd06612    47 KEISILKQCDSPYIV---KYYGSyFKNTDLWIVMEYCGagsvSDIMKIT--------NK---TLTEEEIAAILYQTLKGL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFA-RLFNSplkpLADLDPVVVTFWYRAPELLLGARHYTKAiDIW 158
Cdd:cd06612   113 EYLHSNKKIHRDIKAGNILL----NEEGQAKLADFGVSgQLTDT----MAKRNTVIGTPFWMAPEVIQEIGYNNKA-DIW 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 159 AIGCIFAELLTSEPifhcrqediktsnPFHHDQLDR-IFSvmgfpadkdwedIRKMPEyPTLQkdfrrttyansslikym 237
Cdd:cd06612   184 SLGITAIEMAEGKP-------------PYSDIHPMRaIFM------------IPNKPP-PTLS----------------- 220
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370507705 238 EKHKVKPDSKVFllLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd06612   221 DPEKWSPEFNDF--VKKCLVKDPEERPSAIQLLQHPFI 256
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
3-274 4.05e-21

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: 92.77  E-value: 4.05e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYL 82
Cdd:cd13990    51 ALREYEIHKSLDHPRIVKLYDVFEIDTDSFCTVLEYCDGNDLDFYLKQHKS---------IPEREARSIIMQVVSALKYL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 --HANWVLHRDLKPANILvMGEGPERGRVKIADMGFARLFNSPLKPLADLDPV---VVTFWYRAPELLL---GARHYTKA 154
Cdd:cd13990   122 neIKPPIIHYDLKPGNIL-LHSGNVSGEIKITDFGLSKIMDDESYNSDGMELTsqgAGTYWYLPPECFVvgkTPPKISSK 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 155 IDIWAIGCIFAELLtsepifHCRQediktsnPFHHDQldrifsvmgfpadkdwedirkmpeypTLQKDFRRTTYANSSLI 234
Cdd:cd13990   201 VDVWSVGVIFYQML------YGRK-------PFGHNQ--------------------------SQEAILEENTILKATEV 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1370507705 235 KYMEKHKVKPDSKVFllLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd13990   242 EFPSKPVVSSEAKDF--IRRCLTYRKEDRPDVLQLANDPY 279
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
63-275 5.73e-21

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: 93.08  E-value: 5.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  63 LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGegPERGRVKIADMGFARLFNSplkpladldpVVVTF----W 138
Cdd:cd14212   100 LSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVN--LDSPEIKLIDFGSACFENY----------TLYTYiqsrF 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 139 YRAPELLLGArHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWEDIRKMPEYPT 218
Cdd:cd14212   168 YRSPEVLLGL-PYSTAIDMWSLGCIAAELFLGLPLFPGNSE---------YNQLSRIIEMLGMPPDWMLEKGKNTNKFFK 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 219 L-QKDFRRTTYANSSLIKYMEKHKVKPDS----------------------------------KVFL-LLQKLLTMDPTK 262
Cdd:cd14212   238 KvAKSGGRSTYRLKTPEEFEAENNCKLEPgkryfkyktlediimnypmkkskkeqidkemetrLAFIdFLKGLLEYDPKK 317
                         250
                  ....*....|...
gi 1370507705 263 RITSEQALQDPYF 275
Cdd:cd14212   318 RWTPDQALNHPFI 330
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
5-274 6.20e-21

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: 91.98  E-value: 6.20e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLsHSDrKVWLLFDY-AEHDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd06626    48 DEMKVLEGLDHPNLVRYYGVEV-HRE-EVYIFMEYcQEGTLEELLRHGRI---------LDEAVIRVYTLQLLEGLAYLH 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGegpeRGRVKIADMGFARLFNSPLKPLAD--LDPVVVTFWYRAPELLLGAR--HYTKAIDIWA 159
Cdd:cd06626   117 ENGIVHRDIKPANIFLDS----NGLIKLGDFGSAVKLKNNTTTMAPgeVNSLVGTPAYMAPEVITGNKgeGHGRAADIWS 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 160 IGCIFAELLTSEPifhcrqediktsnPFHhdQLDRIFSVMGFPAdkdwedirkMPEYPTLQkdfrrttyansslikymEK 239
Cdd:cd06626   193 LGCVVLEMATGKR-------------PWS--ELDNEWAIMYHVG---------MGHKPPIP-----------------DS 231
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 240 HKVKPDSKVFllLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd06626   232 LQLSPEGKDF--LSRCLESDPKKRPTASELLDHPF 264
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
63-275 6.89e-21

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: 91.89  E-value: 6.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  63 LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARL------FNSPLKPLADLDP---- 132
Cdd:cd05579    90 LDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDAN----GHLKLTDFGLSKVglvrrqIKLSIQKKSNGAPeked 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 133 --VVVTFWYRAPELLLGaRHYTKAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFSVmgfpadkdwedi 210
Cdd:cd05579   166 rrIVGTPDYLAPEILLG-QGHGKTVDWWSLGVILYEFLVGIP-------------PFHAETPEEIFQN------------ 219
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370507705 211 rkmpeypTLQKDfrrttyansslIKYMEKHKVKPDSKVflLLQKLLTMDPTKRI---TSEQALQDPYF 275
Cdd:cd05579   220 -------ILNGK-----------IEWPEDPEVSDEAKD--LISKLLTPDPEKRLgakGIEEIKNHPFF 267
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
5-168 1.06e-20

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: 91.20  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEH-DLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14162    49 REIEVIKGLKHPNLICFYEAIETTS--RVYIIMELAENgDLLDYIRKNGA---------LPEPQARRWFRQLVAGVEYCH 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFARlfnSPLKPLADLDPVVVTFW----YRAPELLLGARHYTKAIDIWA 159
Cdd:cd14162   118 SKGVVHRDLKCENLLL----DKNNNLKITDFGFAR---GVMKTKDGKPKLSETYCgsyaYASPEILRGIPYDPFLSDIWS 190

                  ....*....
gi 1370507705 160 IGCIFAELL 168
Cdd:cd14162   191 MGVVLYTMV 199
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
66-276 1.33e-20

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: 92.38  E-value: 1.33e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  66 SMVKSLLYQILDGIHYLHAN--WVLHRDLKPANILVMGegPERGRVKIADmgfarlFNSPLKPLADLDPVVVTFWYRAPE 143
Cdd:cd14226   116 NLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLCN--PKRSAIKIID------FGSSCQLGQRIYQYIQSRFYRSPE 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 144 LLLGARhYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFP----------ADKDWEDIRKM 213
Cdd:cd14226   188 VLLGLP-YDLAIDMWSLGCILVEMHTGEPLFSGANE---------VDQMNKIVEVLGMPpvhmldqapkARKFFEKLPDG 257
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370507705 214 PEYPTLQKDFRRTTYANSSLIKYM---------------EKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQ 276
Cdd:cd14226   258 TYYLKKTKDGKKYKPPGSRKLHEIlgvetggpggrragePGHTVEDYLKFKDLILRMLDYDPKTRITPAEALQHSFFK 335
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
5-274 1.36e-20

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: 90.92  E-value: 1.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIalQKVFLSHSDRKVWLLFDYaehdlwhiIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd06632    51 QEIALLSKLRHPNIV--QYYGTEREEDNLYIFLEY--------VPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHS 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLAdldpVVVTFWYRAPELLLGA-RHYTKAIDIWAIGCI 163
Cdd:cd06632   121 RNTVHRDIKGANILV----DTNGVVKLADFGMAKHVEAFSFAKS----FKGSPYWMAPEVIMQKnSGYGLAVDIWSLGCT 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 164 FAELLTSEPifhcrqediktsnPFHH-DQLDRIFSvmgfpadkdwedIRKMPEYPTLQKDfrrttyansslikymekhkV 242
Cdd:cd06632   193 VLEMATGKP-------------PWSQyEGVAAIFK------------IGNSGELPPIPDH-------------------L 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1370507705 243 KPDSKVFLLLqkLLTMDPTKRITSEQALQDPY 274
Cdd:cd06632   229 SPDAKDFIRL--CLQRDPEDRPTASQLLEHPF 258
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
5-275 1.47e-20

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: 90.39  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHsdRKVWLLFDYAEH-DLWHIIKFHRaskankkpmQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14081    50 REIAIMKLIEHPNVLKLYDVYENK--KYLYLVLEYVSGgELFDYLVKKG---------RLTEKEARKFFRQIISALDYCH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFARL--FNSPLKpladldpvvvTFW----YRAPELLLGARHYTKAIDI 157
Cdd:cd14081   119 SHSICHRDLKPENLLL----DEKNNIKIADFGMASLqpEGSLLE----------TSCgsphYACPEVIKGEKYDGRKADI 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 158 WAIGCIFAELLTSepifhcrqediktSNPFHHDQLDRIFsvmgfpadkdwEDIRK-MPEYPtlqkdfrrttyanssliky 236
Cdd:cd14081   185 WSCGVILYALLVG-------------ALPFDDDNLRQLL-----------EKVKRgVFHIP------------------- 221
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370507705 237 mekHKVKPDSKVflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14081   222 ---HFISPDAQD--LLRRMLEVNPEKRITIEEIKKHPWF 255
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
4-169 1.89e-20

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: 90.30  E-value: 1.89e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705    4 CREIALLRELKHPNVIALQKVflSHSDRKVWLLFDYAEH-DLWHIIKFHRASKankkpmqLPRSMVKSLLYQILDGIHYL 82
Cdd:smart00221  49 LREARIMRKLDHPNIVKLLGV--CTEEEPLMIVMEYMPGgDLLDYLRKNRPKE-------LSLSDLLSFALQIARGMEYL 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFAR-LFNSPLKPLADLD-PVvvtFWYrAPELLLgARHYTKAIDIWAI 160
Cdd:smart00221 120 ESKNFIHRDLAARNCLV----GENLVVKISDFGLSRdLYDDDYYKVKGGKlPI---RWM-APESLK-EGKFTSKSDVWSF 190

                   ....*....
gi 1370507705  161 GCIFAELLT 169
Cdd:smart00221 191 GVLLWEIFT 199
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
5-271 2.49e-20

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: 90.10  E-value: 2.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLREL-KHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKfhraskaNKKPMQLPRSMVKSLLYQILDGIHYL 82
Cdd:cd13993    53 REIDLHRRVsRHPNIITLHDVF--ETEVAIYIVLEYCPNgDLFEAIT-------ENRIYVGKTELIKNVFLQLIDAVKHC 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMGEGperGRVKIADMGFARlfNSPLKPladlDPVVVTFWYRAPELL-----LGARHYTKAIDI 157
Cdd:cd13993   124 HSLGIYHRDIKPENILLSQDE---GTVKLCDFGLAT--TEKISM----DFGVGSEFYMAPECFdevgrSLKGYPCAAGDI 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 158 WAIGCIFAELltsepIFHcrqediktSNPFHH-DQLDRIFSVMgFPADKDWEDIrkmpeYPTLQKDFrrttyanssliky 236
Cdd:cd13993   195 WSLGIILLNL-----TFG--------RNPWKIaSESDPIFYDY-YLNSPNLFDV-----ILPMSDDF------------- 242
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 237 mekhkvkpdskvFLLLQKLLTMDPTKRITSEQALQ 271
Cdd:cd13993   243 ------------YNLLRQIFTVNPNNRILLPELQL 265
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
5-275 2.68e-20

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: 90.11  E-value: 2.68e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDY-AEHDLWHIIKFHRASKAnkkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd06610    48 KEIQAMSQCNHPNVVSYYTSFVV--GDELWLVMPLlSGGSLLDIMKSSYPRGG------LDEAIIATVLKEVLKGLEYLH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGF-ARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGC 162
Cdd:cd06610   120 SNGQIHRDVKAGNILL----GEDGSVKIADFGVsASLATGGDRTRKVRKTFVGTPCWMAPEVMEQVRGYDFKADIWSFGI 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLTSEPifhcrqediktsnPFHHdqldrifsvmgFPADKdwedIRKMpeypTLQKDFRrttyanssliKYMEKHKV 242
Cdd:cd06610   196 TAIELATGAA-------------PYSK-----------YPPMK----VLML----TLQNDPP----------SLETGADY 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370507705 243 KPDSKVFL-LLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd06610   234 KKYSKSFRkMISLCLQKDPSKRPTAEELLKHKFF 267
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
4-185 2.82e-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: 89.98  E-value: 2.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELKHPNVIALQKVFlshSDRK-VWLLFDY-AEHDLWHIIKFHRaskankkpmQLPRSMVKSLLYQILDGIHY 81
Cdd:cd05572    41 FSEKEILEECNSPFIVKLYRTF---KDKKyLYMLMEYcLGGELWTILRDRG---------LFDEYTARFYTACVVLAFEY 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKpladldpvVVTFW----YRAPELLLGaRHYTKAIDI 157
Cdd:cd05572   109 LHSRGIIYRDLKPENLLLD----SNGYVKLVDFGFAKKLGSGRK--------TWTFCgtpeYVAPEIILN-KGYDFSVDY 175
                         170       180
                  ....*....|....*....|....*....
gi 1370507705 158 WAIGCIFAELLTSEPIFHCRQED-IKTSN 185
Cdd:cd05572   176 WSLGILLYELLTGRPPFGGDDEDpMKIYN 204
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
4-169 2.88e-20

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 89.90  E-value: 2.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705    4 CREIALLRELKHPNVIALQKVflSHSDRKVWLLFDYAEH-DLWHIIKFHRaskankkpMQLPRSMVKSLLYQILDGIHYL 82
Cdd:smart00219  49 LREARIMRKLDHPNVVKLLGV--CTEEEPLYIVMEYMEGgDLLSYLRKNR--------PKLSLSDLLSFALQIARGMEYL 118
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFAR-LFNSPLKPLADLD-PVvvtFWYrAPELLLgARHYTKAIDIWAI 160
Cdd:smart00219 119 ESKNFIHRDLAARNCLV----GENLVVKISDFGLSRdLYDDDYYRKRGGKlPI---RWM-APESLK-EGKFTSKSDVWSF 189

                   ....*....
gi 1370507705  161 GCIFAELLT 169
Cdd:smart00219 190 GVLLWEIFT 198
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
5-275 3.16e-20

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: 90.10  E-value: 3.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELK-HPNVIALQKVFLSHSDrkVWLLFDYAEH-DLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYL 82
Cdd:cd14106    56 HEIAVLELCKdCPRVVNLHEVYETRSE--LILILELAAGgELQTLLDEEEC---------LTEADVRRLMRQILEGVQYL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMGEGPErGRVKIADMGFARLfnspLKPLADLDPVVVTFWYRAPELLlgarHY---TKAIDIWA 159
Cdd:cd14106   125 HERNIVHLDLKPQNILLTSEFPL-GDIKLCDFGISRV----IGEGEEIREILGTPDYVAPEIL----SYepiSLATDMWS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 160 IGCIFAELLTSepifhcrqediktSNPFHHDQLDRIFSvmgfpadkdweDIRKMpeyptlQKDFRRTTYansslikymek 239
Cdd:cd14106   196 IGVLTYVLLTG-------------HSPFGGDDKQETFL-----------NISQC------NLDFPEELF----------- 234
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1370507705 240 HKVKPDSKVFllLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14106   235 KDVSPLAIDF--IKRLLVKDPEKRLTAKECLEHPWL 268
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
5-175 5.43e-20

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 89.15  E-value: 5.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKvFLSHSDRKVWLLFDYAEHDLWHiiKFHRaskaNKKPmqlPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd14164    49 RELSILRRVNHPNIVQMFE-CIEVANGRLYIVMEAAATDLLQ--KIQE----VHHI---PKDLARDMFAQMVGAVNYLHD 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmgeGPERGRVKIADMGFARLFNSPlkplADLDPVVV-TFWYRAPELLLGARHYTKAIDIWAIGCI 163
Cdd:cd14164   119 MNIVHRDLKCENILL---SADDRKIKIADFGFARFVEDY----PELSTTFCgSRAYTPPEVILGTPYDPKKYDVWSLGVV 191
                         170
                  ....*....|..
gi 1370507705 164 FAELLTSEPIFH 175
Cdd:cd14164   192 LYVMVTGTMPFD 203
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
5-272 6.11e-20

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 89.27  E-value: 6.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAE-HDLWHIIKFHRASKANKKPMQLprsmvkSLLYQILDGIHYLH 83
Cdd:cd13996    53 REVKALAKLNHPNIVRYYTAWVE--EPPLYIQMELCEgGTLRDWIDRRNSSSKNDRKLAL------ELFKQILKGVSYIH 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLF-----------NSPLKPLADLDPVVVTFWYRAPELLLGaRHYT 152
Cdd:cd13996   125 SKGIVHRDLKPSNIFL---DNDDLQVKIGDFGLATSIgnqkrelnnlnNNNNGNTSNNSVGIGTPLYASPEQLDG-ENYN 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 153 KAIDIWAIGCIFAELLTSepifhcrqedIKTsnpfhhdqldrifsVMgfpadkdwEDIRKMpeyptlqKDFRRTTYANSS 232
Cdd:cd13996   201 EKADIYSLGIILFEMLHP----------FKT--------------AM--------ERSTIL-------TDLRNGILPESF 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1370507705 233 LIKYMEKHKvkpdskvflLLQKLLTMDPTKRITSEQALQD 272
Cdd:cd13996   242 KAKHPKEAD---------LIQSLLSKNPEERPSAEQLLRS 272
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
6-274 8.25e-20

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: 89.28  E-value: 8.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDRKVWL-------LFD-------YAEHDLWHIIKfhraskankkpmqlprsmvksl 71
Cdd:cd14166    50 EIAVLKRIKHENIVTLEDIYESTTHYYLVMqlvsggeLFDrilergvYTEKDASRVIN---------------------- 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  72 lyQILDGIHYLHANWVLHRDLKPANILVMGEgPERGRVKIADMGFARLFNSPLKPLADLDPvvvtfWYRAPElLLGARHY 151
Cdd:cd14166   108 --QVLSAVKYLHENGIVHRDLKPENLLYLTP-DENSKIMITDFGLSKMEQNGIMSTACGTP-----GYVAPE-VLAQKPY 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 152 TKAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFSVM--GFPADKD--WEDIRKMpeyptlQKDFrrtt 227
Cdd:cd14166   179 SKAVDCWSIGVITYILLCGYP-------------PFYEETESRLFEKIkeGYYEFESpfWDDISES------AKDF---- 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1370507705 228 yansslikymekhkvkpdskvfllLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14166   236 ------------------------IRHLLEKNPSKRYTCEKALSHPW 258
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
33-275 9.17e-20

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: 89.56  E-value: 9.17e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  33 VWLLFDYAEHDLWHIIKFHraskaNKKPMQLPrsMVKSLLYQILDGIHYLHANW-VLHRDLKPANILVMgegPERGRVKI 111
Cdd:cd14136    93 VCMVFEVLGPNLLKLIKRY-----NYRGIPLP--LVKKIARQVLQGLDYLHTKCgIIHTDIKPENVLLC---ISKIEVKI 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 112 ADMGFARLFNsplKPLADldpVVVTFWYRAPELLLGArHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNpfhHDQ 191
Cdd:cd14136   163 ADLGNACWTD---KHFTE---DIQTRQYRSPEVILGA-GYGTPADIWSTACMAFELATGDYLFDPHSGEDYSRD---EDH 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 192 LDRIFSVMG-FP---ADKDwediRKMPEYPTLQKDFRRttyaNSSLIKY------MEKHKVKP-DSKVF-LLLQKLLTMD 259
Cdd:cd14136   233 LALIIELLGrIPrsiILSG----KYSREFFNRKGELRH----ISKLKPWpledvlVEKYKWSKeEAKEFaSFLLPMLEYD 304
                         250
                  ....*....|....*.
gi 1370507705 260 PTKRITSEQALQDPYF 275
Cdd:cd14136   305 PEKRATAAQCLQHPWL 320
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
6-278 1.07e-19

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: 88.79  E-value: 1.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEH-DLWHIIkFHRASKANKKPMQLprsmvkslLYQILDGIHYLHA 84
Cdd:cd14169    51 EIAVLRRINHENIVSLEDIYESPT--HLYLAMELVTGgELFDRI-IERGSYTEKDASQL--------IGQVLQAVKYLHQ 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmgEGP-ERGRVKIADMGFARLFNSPLKPLADLDPVvvtfwYRAPElLLGARHYTKAIDIWAIGCI 163
Cdd:cd14169   120 LGIVHRDLKPENLLY--ATPfEDSKIMISDFGLSKIEAQGMLSTACGTPG-----YVAPE-LLEQKPYGKAVDVWAIGVI 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 164 FAELLTSEPifhcrqediktsnPFHHDQLDRIFSVMgFPADKD-----WEDIRKMpeyptlQKDFRRttyansslikyme 238
Cdd:cd14169   192 SYILLCGYP-------------PFYDENDSELFNQI-LKAEYEfdspyWDDISES------AKDFIR------------- 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1370507705 239 khkvkpdskvflllqKLLTMDPTKRITSEQALQDPYFQED 278
Cdd:cd14169   239 ---------------HLLERDPEKRFTCEQALQHPWISGD 263
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
64-275 1.26e-19

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: 89.55  E-value: 1.26e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  64 PRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEG---------------PERGRVKIADMG---FARLFNSPlk 125
Cdd:cd14134   113 PLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDSDyvkvynpkkkrqirvPKSTDIKLIDFGsatFDDEYHSS-- 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 126 pladldpVVVTFWYRAPELLLGARhYTKAIDIWAIGCIFAELLTSEPIFHcrqedikTSNPFHHDQLdrIFSVMGfPADK 205
Cdd:cd14134   191 -------IVSTRHYRAPEVILGLG-WSYPCDVWSIGCILVELYTGELLFQ-------THDNLEHLAM--MERILG-PLPK 252
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 206 DWedIRKMPeYPTLQKDFRRTTYA---NSSLIKYMEKHK---------VKPDSKVFL-LLQKLLTMDPTKRITSEQALQD 272
Cdd:cd14134   253 RM--IRRAK-KGAKYFYFYHGRLDwpeGSSSGRSIKRVCkplkrlmllVDPEHRLLFdLIRKMLEYDPSKRITAKEALKH 329

                  ...
gi 1370507705 273 PYF 275
Cdd:cd14134   330 PFF 332
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
3-274 1.85e-19

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: 89.42  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHP------NVIALQK--VFLSHsdrkVWLLFDYAEHDLWHIIKfhrASKANKKPMQLPRSMVKSLLyQ 74
Cdd:cd14224   108 AAEEIRILEHLKKQdkdntmNVIHMLEsfTFRNH----ICMTFELLSMNLYELIK---KNKFQGFSLQLVRKFAHSIL-Q 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGihyLHANWVLHRDLKPANILVMGEGpeRGRVKIADMGFA-----RLFNsplkpladldpVVVTFWYRAPELLLGAR 149
Cdd:cd14224   180 CLDA---LHRNKIIHCDLKPENILLKQQG--RSGIKVIDFGSScyehqRIYT-----------YIQSRFYRAPEVILGAR 243
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 150 hYTKAIDIWAIGCIFAELLTSEPIFHCRQEDiktsnpfhhDQLDRIFSVMGFPADKDWEDIRKM---------PEYPTLQ 220
Cdd:cd14224   244 -YGMPIDMWSFGCILAELLTGYPLFPGEDEG---------DQLACMIELLGMPPQKLLETSKRAknfisskgyPRYCTVT 313
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370507705 221 KDFRRTTYANSSLIKyMEKHKVKPDSK------------VFL-LLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14224   314 TLPDGSVVLNGGRSR-RGKMRGPPGSKdwvtalkgcddpLFLdFLKRCLEWDPAARMTPSQALRHPW 379
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
4-169 1.90e-19

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: 87.59  E-value: 1.90e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELKHPNVIALQKVflSHSDRKVWLLFDYAEH-DLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYL 82
Cdd:cd00192    44 LKEARVMKKLGHPNVVRLLGV--CTEEEPLYLVMEYMEGgDLLDFLRKSRPVFPSPEPSTLSLKDLLSFAIQIAKGMEYL 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYrAPELLLGaRHYTKAIDIWAIGC 162
Cdd:cd00192   122 ASKKFVHRDLAARNCLV----GEDLVVKISDFGLSRDIYDDDYYRKKTGGKLPIRWM-APESLKD-GIFTSKSDVWSFGV 195

                  ....*..
gi 1370507705 163 IFAELLT 169
Cdd:cd00192   196 LLWEIFT 202
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
6-278 3.73e-19

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: 87.19  E-value: 3.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDRKVWL-------LFD-------YAEHDlwhiikfhrASKANKkpmqlprsmvksl 71
Cdd:cd14085    48 EIGVLLRLSHPNIIKLKEIFETPTEISLVLelvtggeLFDrivekgyYSERD---------AADAVK------------- 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  72 lyQILDGIHYLHANWVLHRDLKPANILVMGEGPErGRVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGARhY 151
Cdd:cd14085   106 --QILEAVAYLHENGIVHRDLKPENLLYATPAPD-APLKIADFGLSKIVDQQVT----MKTVCGTPGYCAPEILRGCA-Y 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 152 TKAIDIWAIGCIFAELLtsepifhCRQEdiktsnPFHHDQLDRIFSVMGFPADKD-----WEDIRKMpeyptlQKDfrrt 226
Cdd:cd14085   178 GPEVDMWSVGVITYILL-------CGFE------PFYDERGDQYMFKRILNCDYDfvspwWDDVSLN------AKD---- 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370507705 227 tyansslikymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYFQED 278
Cdd:cd14085   235 ------------------------LVKKLIVLDPKKRLTTQQALQHPWVTGK 262
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
5-183 4.13e-19

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


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 87.79  E-value: 4.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEHDLWHIIKFHraskanKKPMQlpRSMVKSLLYQILDGIHYLHA 84
Cdd:cd06633    70 KEVKFLQQLKHPNTIEYKGCYLK--DHTAWLVMEYCLGSASDLLEVH------KKPLQ--EVEIAAITHGALQGLAYLHS 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMgegpERGRVKIADMGFARLfNSPlkpladLDPVVVTFWYRAPELLLGAR--HYTKAIDIWAIGC 162
Cdd:cd06633   140 HNMIHRDIKAGNILLT----EPGQVKLADFGSASI-ASP------ANSFVGTPYWMAPEVILAMDegQYDGKVDIWSLGI 208
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1370507705 163 IFAELLTSEP----------IFHCRQEDIKT 183
Cdd:cd06633   209 TCIELAERKPplfnmnamsaLYHIAQNDSPT 239
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
5-172 4.44e-19

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: 86.64  E-value: 4.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIalQKVFLSHSDRKVWLLFDYAE----HDlwHIikfhraskanKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd06625    51 CEIQLLKNLQHERIV--QYYGCLQDEKSLSIFMEYMPggsvKD--EI----------KAYGALTENVTRKYTRQILEGLA 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSpLKPLADLDPVVVTFWYRAPELLLGARHYTKAiDIWAI 160
Cdd:cd06625   117 YLHSNMIVHRDIKGANILRDSN----GNVKLGDFGASKRLQT-ICSSTGMKSVTGTPYWMSPEVINGEGYGRKA-DIWSV 190
                         170
                  ....*....|..
gi 1370507705 161 GCIFAELLTSEP 172
Cdd:cd06625   191 GCTVVEMLTTKP 202
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
6-274 4.92e-19

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: 86.23  E-value: 4.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIkfhraSKANKKPMQLPRSMVKSLLyQILDgihYLHA 84
Cdd:cd14095    48 EVAILRRVKHPNIVQLIEEY--DTDTELYLVMELVKGgDLFDAI-----TSSTKFTERDASRMVTDLA-QALK---YLHS 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKpladldPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIF 164
Cdd:cd14095   117 LSIVHRDIKPENLLVVEHEDGSKSLKLADFGLATEVKEPLF------TVCGTPTYVAPE-ILAETGYGLKVDIWAAGVIT 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 165 AELLTSEPIFhcRQEDiktsnpfhHDQlDRIFS--VMG---FPADKdWEDIrkmpeyptlqkdfrrTTYAnsslikymeK 239
Cdd:cd14095   190 YILLCGFPPF--RSPD--------RDQ-EELFDliLAGefeFLSPY-WDNI---------------SDSA---------K 233
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 240 HkvkpdskvflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14095   234 D----------LISRMLVVDPEKRYSAGQVLDHPW 258
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
5-274 5.82e-19

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: 86.72  E-value: 5.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWH-IIKFHRASKAnkkpmqLPRSMVKsllyQILDGIHYL 82
Cdd:cd14096    55 KEVQIMKRLSHPNIVKLLDFQ--ESDEYYYIVLELADGgEIFHqIVRLTYFSED------LSRHVIT----QVASAVKYL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANIL-------------VMGEGPER----------------GRVKIADMGFAR-LFNSPLK-PLAdld 131
Cdd:cd14096   123 HEIGVVHRDIKPENLLfepipfipsivklRKADDDETkvdegefipgvggggiGIVKLADFGLSKqVWDSNTKtPCG--- 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 132 pvvvTFWYRAPELLlGARHYTKAIDIWAIGCIFAELLTSEPIFHcrQEDIKTSNpfhhDQLDRIFSVMGFPAdkdWEDIR 211
Cdd:cd14096   200 ----TVGYTAPEVV-KDERYSKKVDMWALGCVLYTLLCGFPPFY--DESIETLT----EKISRGDYTFLSPW---WDEIS 265
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370507705 212 KMpeyptlQKDfrrttyansslikymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14096   266 KS------AKD----------------------------LISHLLTVDPAKRYDIDEFLAHPW 294
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
5-275 7.42e-19

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: 85.82  E-value: 7.42e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDrKVWLLFDYAEH-DLWHIIKfhraskankKPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd13994    46 SEYIISSKLHHPNIVKVLDLCQDLHG-KWCLVMEYCPGgDLFTLIE---------KADSLSLEEKDCFFKQILRGVAYLH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLA-DLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGC 162
Cdd:cd13994   116 SHGIAHRDLKPENILL----DEDGVLKLTDFGTAEVFGMPAEKESpMSAGLCGSEPYMAPEVFTSGSYDGRAVDVWSCGI 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLTSE-PIFHCRQEDiktsnpfhhdqldrifsvmgfPADKDWEDIRKMPEYPTLQkdfrrttyANSSLIKYMEKhk 241
Cdd:cd13994   192 VLFALFTGRfPWRSAKKSD---------------------SAYKAYEKSGDFTNGPYEP--------IENLLPSECRR-- 240
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370507705 242 vkpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd13994   241 ---------LIYRMLHPDPEKRITIDEALNDPWV 265
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
5-162 7.73e-19

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: 86.26  E-value: 7.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVflshsdrkvwlLFDYAEHDLWHIIKFHRASKANKKPMQLPRS--MVKSLLYQILDGIHYL 82
Cdd:cd14118    63 REIAILKKLDHPNVVKLVEV-----------LDDPNEDNLYMVFELVDKGAVMEVPTDNPLSeeTARSYFRDIVLGIEYL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplkPLADLDPVVVTFWYRAPELLLGARHYT--KAIDIWAI 160
Cdd:cd14118   132 HYQKIIHRDIKPSNLLL----GDDGHVKIADFGVSNEFEG---DDALLSSTAGTPAFMAPEALSESRKKFsgKALDIWAM 204

                  ..
gi 1370507705 161 GC 162
Cdd:cd14118   205 GV 206
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
5-175 8.01e-19

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: 85.83  E-value: 8.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKvfLSHSDRKVWLLFDYAEH-DLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14202    50 KEIKILKELKHENIVALYD--FQEIANSVYLVMEYCNGgDLADYLHTMRT---------LSEDTIRLFLQQIAGAMKMLH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEG-----PERGRVKIADMGFARLFNSPLKPlADL--DPVvvtfwYRAPELLLgARHYTKAID 156
Cdd:cd14202   119 SKGIIHRDLKPQNILLSYSGgrksnPNNIRIKIADFGFARYLQNNMMA-ATLcgSPM-----YMAPEVIM-SQHYDAKAD 191
                         170
                  ....*....|....*....
gi 1370507705 157 IWAIGCIFAELLTSEPIFH 175
Cdd:cd14202   192 LWSIGTIIYQCLTGKAPFQ 210
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
5-274 8.48e-19

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: 86.32  E-value: 8.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHII---KFHRASKANKkpmqlprsmvksLLYQILDGIH 80
Cdd:cd14086    49 REARICRLLKHPNIVRLHDSI--SEEGFHYLVFDLVTGgELFEDIvarEFYSEADASH------------CIQQILESVN 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEGPErGRVKIADMGFARLFNSPLKPLADLdpvVVTFWYRAPElLLGARHYTKAIDIWAI 160
Cdd:cd14086   115 HCHQNGIVHRDLKPENLLLASKSKG-AAVKLADFGLAIEVQGDQQAWFGF---AGTPGYLSPE-VLRKDPYGKPVDIWAC 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFSVM-----GFPAdkdwedirkmPEYPTlqkdfrrttyansslik 235
Cdd:cd14086   190 GVILYILLVGYP-------------PFWDEDQHRLYAQIkagayDYPS----------PEWDT----------------- 229
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370507705 236 ymekhkVKPDSKVflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14086   230 ------VTPEAKD--LINQMLTVNPAKRITAAEALKHPW 260
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
5-274 1.12e-18

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: 85.46  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWL-------LFDY-AEHDlwhiikfhraskankkpmQLPRSMVKSLLYQIL 76
Cdd:cd14194    57 REVSILKEIQHPNVITLHEVYENKTDVILILelvaggeLFDFlAEKE------------------SLTEEEATEFLKQIL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  77 DGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPlkplADLDPVVVTFWYRAPELL----LGARHyt 152
Cdd:cd14194   119 NGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDFGLAHKIDFG----NEFKNIFGTPEFVAPEIVnyepLGLEA-- 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 153 kaiDIWAIGCIFAELLTSEPIF--HCRQEDIKTSNPFHHDQLDRIFSvmgfpadkdwedirkmpEYPTLQKDFrrttyan 230
Cdd:cd14194   193 ---DMWSIGVITYILLSGASPFlgDTKQETLANVSAVNYEFEDEYFS-----------------NTSALAKDF------- 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1370507705 231 sslikymekhkvkpdskvfllLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14194   246 ---------------------IRRLLVKDPKKRMTIQDSLQHPW 268
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
6-175 1.14e-18

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: 85.54  E-value: 1.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIalqKVFLSHSDRKVWLLFdyAEH----DLWHIIKfhraSKANkkPMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd06624    55 EIALHSRLSHKNIV---QYLGSVSEDGFFKIF--MEQvpggSLSALLR----SKWG--PLKDNENTIGYYTKQILEGLKY 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgeGPERGRVKIADMGFArlfnsplKPLADLDPVVVTF----WYRAPELL-LGARHYTKAID 156
Cdd:cd06624   124 LHDNKIVHRDIKGDNVLV---NTYSGVVKISDFGTS-------KRLAGINPCTETFtgtlQYMAPEVIdKGQRGYGPPAD 193
                         170
                  ....*....|....*....
gi 1370507705 157 IWAIGCIFAELLTSEPIFH 175
Cdd:cd06624   194 IWSLGCTIIEMATGKPPFI 212
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
5-174 1.34e-18

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: 85.16  E-value: 1.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAE-HDLWHIIKFHraskankkPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14074    51 QEVRCMKLVQHPNVVRLYEVIDTQT--KLYLILELGDgGDMYDYIMKH--------ENGLNEDLARKYFRQIVSAISYCH 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGegpERGRVKIADMGFARLFNsplkPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCI 163
Cdd:cd14074   121 KLHVVHRDLKPENVVFFE---KQGLVKLTDFGFSNKFQ----PGEKLETSCGSLAYSAPEILLGDEYDAPAVDIWSLGVI 193
                         170
                  ....*....|.
gi 1370507705 164 FAELLTSEPIF 174
Cdd:cd14074   194 LYMLVCGQPPF 204
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
6-281 1.69e-18

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


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 85.38  E-value: 1.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIaLLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHD--LWHIIKfhraskanKKpmQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14091    45 EI-LLRYGQHPNIITLRDVY--DDGNSVYLVTELLRGGelLDRILR--------QK--FFSEREASAVMKTLTKTVEYLH 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEGPERGRVKIADMGFArlfnsplKPLADLDPVVVTFWYR----APElLLGARHYTKAIDIWA 159
Cdd:cd14091   112 SQGVVHRDLKPSNILYADESGDPESLRICDFGFA-------KQLRAENGLLMTPCYTanfvAPE-VLKKQGYDAACDIWS 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 160 IGCIFAELLTSEPIFHCRQEDikTSnpfhHDQLDRI----FSVMGfpadKDWedirkmpeyptlqkdfrrttyansslik 235
Cdd:cd14091   184 LGVLLYTMLAGYTPFASGPND--TP----EVILARIgsgkIDLSG----GNW---------------------------- 225
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1370507705 236 ymekHKVKPDSKVflLLQKLLTMDPTKRITSEQALQDPYFQE-DPLP 281
Cdd:cd14091   226 ----DHVSDSAKD--LVRKMLHVDPSQRPTAAQVLQHPWIRNrDSLP 266
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
5-274 2.03e-18

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: 84.65  E-value: 2.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAE-HDLWHIIKfhraskANKKpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14010    43 NEVRLTHELKHPNVLKFYEWY--ETSNHLWLVVEYCTgGDLETLLR------QDGN---LPESSVRKFGRDLVRGLHYIH 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgEGPerGRVKIADMGFARLFNSPLKPLADLD-------------PVVVTFWYRAPELLLGARH 150
Cdd:cd14010   112 SKGIIYCDLKPSNILL--DGN--GTLKLSDFGLARREGEILKELFGQFsdegnvnkvskkqAKRGTPYYMAPELFQGGVH 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 151 yTKAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFsvmgfpadkdwEDIrkmpeyptLQKDFRRTTyan 230
Cdd:cd14010   188 -SFASDLWALGCVLYEMFTGKP-------------PFVAESFTELV-----------EKI--------LNEDPPPPP--- 231
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1370507705 231 sslikymEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14010   232 -------PKVSSKPSPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
5-161 2.55e-18

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: 84.31  E-value: 2.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLwhiikFHRASKANKkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14075    50 REISSMEKLHHPNIIRLYEVV--ETLSKLHLVMEYASGgEL-----YTKISTEGK----LSESEAKPLFAQIVSAVKHMH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEgperGRVKIADMGFARLfnspLKPLADLDpvvvTFW----YRAPELLLGARHYTKAIDIWA 159
Cdd:cd14075   119 ENNIIHRDLKAENVFYASN----NCVKVGDFGFSTH----AKRGETLN----TFCgsppYAAPELFKDEHYIGIYVDIWA 186

                  ..
gi 1370507705 160 IG 161
Cdd:cd14075   187 LG 188
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
6-274 3.13e-18

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: 83.84  E-value: 3.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKfhraskankKPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd14185    48 EILIIKSLSHPNIVKLFEVY--ETEKEIYLILEYVRGgDLFDAII---------ESVKFTEHDAALMIIDLCEALVYIHS 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKpladldPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCIF 164
Cdd:cd14185   117 KHIVHRDLKPENLLVQHNPDKSTTLKLADFGLAKYVTGPIF------TVCGTPTYVAPEILSE-KGYGLEVDMWAAGVIL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 165 AELLTSEPIFHCRQEDiktsnpfhhdqLDRIFSVMgfpadkdwedirKMPEYPTLQKDFRRTTYANSSLIkymekhkvkp 244
Cdd:cd14185   190 YILLCGFPPFRSPERD-----------QEELFQII------------QLGHYEFLPPYWDNISEAAKDLI---------- 236
                         250       260       270
                  ....*....|....*....|....*....|
gi 1370507705 245 dskvflllQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14185   237 --------SRLLVVDPEKRYTAKQVLQHPW 258
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
2-167 3.21e-18

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 83.86  E-value: 3.21e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SAC-REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKfHRASKanKKPmqLPRSMVKSLLYQILDGI 79
Cdd:cd08224    45 QDClKEIDLLQQLNHPNIIKYLASFIE--NNELNIVLELADAgDLSRLIK-HFKKQ--KRL--IPERTIWKYFVQLCSAL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSplKPLAdLDPVVVTFWYRAPELLLGArHYTKAIDIWA 159
Cdd:cd08224   118 EHMHSKRIMHRDIKPANVFITAN----GVVKLGDLGLGRFFSS--KTTA-AHSLVGTPYYMSPERIREQ-GYDFKSDIWS 189

                  ....*...
gi 1370507705 160 IGCIFAEL 167
Cdd:cd08224   190 LGCLLYEM 197
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
5-285 3.29e-18

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: 85.04  E-value: 3.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELK-HPNVIALQKVFlshsdrkvwllfdyaeHDLWH---IIKFHRASKANKKPMQLPR---SMVKSLLYQILD 77
Cdd:cd14092    47 REVQLLRLCQgHPNIVKLHEVF----------------QDELHtylVMELLRGGELLERIRKKKRfteSEASRIMRQLVS 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANWVLHRDLKPANILVMGEgPERGRVKIADMGFARLF--NSPLK-PladldpvVVTFWYRAPELLLGARH---Y 151
Cdd:cd14092   111 AVSFMHSKGVVHRDLKPENLLFTDE-DDDAEIKIVDFGFARLKpeNQPLKtP-------CFTLPYAAPEVLKQALStqgY 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 152 TKAIDIWAIGCIFAELLTSEPIFHcrqediktsnpfHHDQLDRIFSVMgfpadkdwEDIRKmpeyptlqKDFRRTTYANS 231
Cdd:cd14092   183 DESCDLWSLGVILYTMLSGQVPFQ------------SPSRNESAAEIM--------KRIKS--------GDFSFDGEEWK 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 232 SlikymekhkVKPDSKVflLLQKLLTMDPTKRITSEQALQDPYFQED------PLPTLDV 285
Cdd:cd14092   235 N---------VSSEAKS--LIQGLLTVDPSKRLTMSELRNHPWLQGSsspsstPLMTPGV 283
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
5-274 3.51e-18

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: 84.08  E-value: 3.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWL-------LFDYAehdlwhiikfhraskANKKPMQLPRSMvkSLLYQILD 77
Cdd:cd14105    57 REVSILRQVLHPNIITLHDVFENKTDVVLILelvaggeLFDFL---------------AEKESLSEEEAT--EFLKQILD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARLfnspLKPLADLDPVVVTFWYRAPELL----LGArhytk 153
Cdd:cd14105   120 GVNYLHTKNIAHFDLKPENIMLLDKNVPIPRIKLIDFGLAHK----IEDGNEFKNIFGTPEFVAPEIVnyepLGL----- 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIF--HCRQEDIKTSNPFHHDQLDRIFSvmgfpadkdwedirkmpEYPTLQKDFrrttyans 231
Cdd:cd14105   191 EADMWSIGVITYILLSGASPFlgDTKQETLANITAVNYDFDDEYFS-----------------NTSELAKDF-------- 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1370507705 232 slikymekhkvkpdskvfllLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14105   246 --------------------IRQLLVKDPRKRMTIQESLRHPW 268
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
6-172 4.31e-18

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: 83.63  E-value: 4.31e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVI----ALQK-----VFLShsdrkvWLlfdyAEHDLWHIIKFHRAskankkpmqLPRSMVKSLLYQIL 76
Cdd:cd06630    53 EIRMMARLNHPNIVrmlgATQHkshfnIFVE------WM----AGGSVASLLSKYGA---------FSENVIINYTLQIL 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  77 DGIHYLHANWVLHRDLKPANILVMGEGPergRVKIADMGFARLFNSPLKPLADLDPVVV-TFWYRAPELLLGaRHYTKAI 155
Cdd:cd06630   114 RGLAYLHDNQIIHRDLKGANLLVDSTGQ---RLRIADFGAAARLASKGTGAGEFQGQLLgTIAFMAPEVLRG-EQYGRSC 189
                         170
                  ....*....|....*..
gi 1370507705 156 DIWAIGCIFAELLTSEP 172
Cdd:cd06630   190 DVWSVGCVIIEMATAKP 206
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
5-169 4.72e-18

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: 83.48  E-value: 4.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKFHRASkankkpmQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd08219    47 KEAVLLAKMKHPNIVAFKESF--EADGHLYIVMEYCDGgDLMQKIKLQRGK-------LFPEDTILQWFVQMCLGVQHIH 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSplkPLADLDPVVVTFWYRAPELLLGARHYTKAiDIWAIGCI 163
Cdd:cd08219   118 EKRVLHRDIKSKNIFLT----QNGKVKLGDFGSARLLTS---PGAYACTYVGTPYYVPPEIWENMPYNNKS-DIWSLGCI 189

                  ....*.
gi 1370507705 164 FAELLT 169
Cdd:cd08219   190 LYELCT 195
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
5-178 4.73e-18

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: 83.74  E-value: 4.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIalQKVFLSHSDRKVWLLFDYAEHdlwhiikfhrASKANKKPM--QLPRSMVKSLLYQILDGIHYL 82
Cdd:cd06628    55 REIALLRELQHENIV--QYLGSSSDANHLNIFLEYVPG----------GSVATLLNNygAFEESLVRNFVRQILKGLNYL 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFARLF--NSPLKPLADLDPVV--VTFWYrAPELLLGARHYTKAiDIW 158
Cdd:cd06628   123 HNRGIIHRDIKGANILV----DNKGGIKISDFGISKKLeaNSLSTKNNGARPSLqgSVFWM-APEVVKQTSYTRKA-DIW 196
                         170       180
                  ....*....|....*....|.
gi 1370507705 159 AIGCIFAELLTSE-PIFHCRQ 178
Cdd:cd06628   197 SLGCLVVEMLTGThPFPDCTQ 217
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
68-275 6.37e-18

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: 84.20  E-value: 6.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  68 VKSLLYQILDGIHYLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLFNSplkplADLDPVVVTFWYRAPELLLG 147
Cdd:cd14135   107 VRSYAQQLFLALKHLKKCNILHADIKPDNILV---NEKKNTLKLCDFGSASDIGE-----NEITPYLVSRFYRAPEIILG 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 148 ARhYTKAIDIWAIGCIFAELLTSEPIFhcrqeDIKTSN-----------PFHHDQLDR-IFSVMGFPADKDW----ED-- 209
Cdd:cd14135   179 LP-YDYPIDMWSVGCTLYELYTGKILF-----PGKTNNhmlklmmdlkgKFPKKMLRKgQFKDQHFDENLNFiyreVDkv 252
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370507705 210 ----IRKMPEYPTLQKDFRrttyanSSLIKYmeKHKVKPDSKVFL----LLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14135   253 tkkeVRRVMSDIKPTKDLK------TLLIGK--QRLPDEDRKKLLqlkdLLDKCLMLDPEKRITPNEALQHPFI 318
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
5-175 6.75e-18

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: 83.15  E-value: 6.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAeHDLWHIIKFHRaskanKKPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd08228    51 KEIDLLKQLNHPNVIKYLDSFIEDNELNIVLELADA-GDLSQMIKYFK-----KQKRLIPERTVWKYFVQLCSAVEHMHS 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPLADLdpvVVTFWYRAPElLLGARHYTKAIDIWAIGCIF 164
Cdd:cd08228   125 RRVMHRDIKPANVFITAT----GVVKLGDLGLGRFFSSKTTAAHSL---VGTPYYMSPE-RIHENGYNFKSDIWSLGCLL 196
                         170
                  ....*....|.
gi 1370507705 165 AELLTSEPIFH 175
Cdd:cd08228   197 YEMAALQSPFY 207
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
6-274 6.99e-18

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: 83.03  E-value: 6.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKH-PNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKfhraskaNKKPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd14131    49 EIELLKKLKGsDRIIQLYDYEVTDEDDYLYMVMECGEIDLATILK-------KKRPKPIDPNFIRYYWKQMLEAVHTIHE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMgegpeRGRVKIADMGFARLFN----SPLKpladlDPVVVTFWYRAPELLLGARHYT-------- 152
Cdd:cd14131   122 EGIVHSDLKPANFLLV-----KGRLKLIDFGIAKAIQndttSIVR-----DSQVGTLNYMSPEAIKDTSASGegkpkski 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 153 -KAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQldRIFSVMGFPADKDWEdIrkmpEYPTLqkdfrrttyANS 231
Cdd:cd14131   192 gRPSDVWSLGCILYQMVYGKT-------------PFQHIT--NPIAKLQAIIDPNHE-I----EFPDI---------PNP 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1370507705 232 SLIKymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14131   243 DLID---------------VMKRCLQRDPKKRPSIPELLNHPF 270
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
5-178 7.14e-18

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: 83.77  E-value: 7.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELK-HPNVIALQKVFlsHSDRKVWLLFDYAEHD--LWHIIKFHRASKANKKpmQLPRSMVKSllyqildgIHY 81
Cdd:cd14180    49 REVAALRLCQsHPNIVALHEVL--HDQYHTYLVMELLRGGelLDRIKKKARFSESEAS--QLMRSLVSA--------VSF 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEGPErGRVKIADMGFARLFNSPLKPladLDPVVVTFWYRAPElLLGARHYTKAIDIWAIG 161
Cdd:cd14180   117 MHEAGVVHRDLKPENILYADESDG-AVLKVIDFGFARLRPQGSRP---LQTPCFTLQYAAPE-LFSNQGYDESCDLWSLG 191
                         170
                  ....*....|....*..
gi 1370507705 162 CIFAELLTSEPIFHCRQ 178
Cdd:cd14180   192 VILYTMLSGQVPFQSKR 208
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
5-175 7.88e-18

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: 82.80  E-value: 7.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALqkVFLSHSDRKVWLLFDYAEH-DLwhiikfhrASKANKKPMqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14120    41 KEIKILKELSHENVVAL--LDCQETSSSVYLVMEYCNGgDL--------ADYLQAKGT-LSEDTIRVFLQQIAAAMKALH 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILV-----MGEGPERGRVKIADMGFARLFN----------SPLkpladldpvvvtfwYRAPELLLGa 148
Cdd:cd14120   110 SKGIVHRDLKPQNILLshnsgRKPSPNDIRLKIADFGFARFLQdgmmaatlcgSPM--------------YMAPEVIMS- 174
                         170       180
                  ....*....|....*....|....*..
gi 1370507705 149 RHYTKAIDIWAIGCIFAELLTSEPIFH 175
Cdd:cd14120   175 LQYDAKADLWSIGTIVYQCLTGKAPFQ 201
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
66-275 8.37e-18

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: 83.98  E-value: 8.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  66 SMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGpeRGRVKIADMGfarlfNSPLKpladlDPVVVTF----WYRA 141
Cdd:cd14225   146 SLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRG--QSSIKVIDFG-----SSCYE-----HQRVYTYiqsrFYRS 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 142 PELLLGARhYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDRIFSVMGFPADKDWE---------DIRK 212
Cdd:cd14225   214 PEVILGLP-YSMAIDMWSLGCILAELYTGYPLFPGENE---------VEQLACIMEVLGLPPPELIEnaqrrrlffDSKG 283
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370507705 213 MPEYPTLQKDFRRttYANSSLIKYMekhkVKPDSKVFL-LLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14225   284 NPRCITNSKGKKR--RPNSKDLASA----LKTSDPLFLdFIRRCLEWDPSKRMTPDEALQHEWI 341
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
5-163 9.83e-18

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: 82.44  E-value: 9.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYA-EHDLWHIIkfhraskANKKpmQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14073    50 REIEIMSSLNHPHIIRIYEVF--ENKDKIVIVMEYAsGGELYDYI-------SERR--RLPEREARRIFRQIVSAVHYCH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFnsplkplaDLDPVVVTF----WYRAPELLLGARHYTKAIDIWA 159
Cdd:cd14073   119 KNGVVHRDLKLENILL----DQNGNAKIADFGLSNLY--------SKDKLLQTFcgspLYASPEIVNGTPYQGPEVDCWS 186

                  ....
gi 1370507705 160 IGCI 163
Cdd:cd14073   187 LGVL 190
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
5-172 1.02e-17

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: 82.50  E-value: 1.02e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEHDLWHIIKFHraskanKKPMQlpRSMVKSLLYQILDGIHYLHA 84
Cdd:cd06607    50 KEVKFLRQLRHPNTIEYKGCYLR--EHTAWLVMEYCLGSASDIVEVH------KKPLQ--EVEIAAICHGALQGLAYLHS 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMgegpERGRVKIADMGFARLFnSPLKPLadldpvVVTFWYRAPELLLGAR--HYTKAIDIWAIG- 161
Cdd:cd06607   120 HNRIHRDVKAGNILLT----EPGTVKLADFGSASLV-CPANSF------VGTPYWMAPEVILAMDegQYDGKVDVWSLGi 188
                         170
                  ....*....|..
gi 1370507705 162 -CIfaELLTSEP 172
Cdd:cd06607   189 tCI--ELAERKP 198
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
6-175 1.05e-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: 83.15  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlshsdrkvwllfdYAEHDLWHIIKFHRASKANKKPMQLPRSM----VKSLLYQILDGIHY 81
Cdd:cd06643    52 EIDILASCDHPNIVKLLDAF-------------YYENNLWILIEFCAGGAVDAVMLELERPLtepqIRVVCKQTLEALVY 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEgperGRVKIADMGFARlfnSPLKPLADLDPVVVTFWYRAPELLL----GARHYTKAIDI 157
Cdd:cd06643   119 LHENKIIHRDLKAGNILFTLD----GDIKLADFGVSA---KNTRTLQRRDSFIGTPYWMAPEVVMcetsKDRPYDYKADV 191
                         170
                  ....*....|....*...
gi 1370507705 158 WAIGCIFAELLTSEPIFH 175
Cdd:cd06643   192 WSLGVTLIEMAQIEPPHH 209
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
35-274 1.13e-17

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: 83.54  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  35 LLFDYAEHDLWHIIKFHRASKankkpmqLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADM 114
Cdd:cd14229    78 LVFEMLEQNLYDFLKQNKFSP-------LPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDF 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 115 GFARLFNSPLkpladLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDR 194
Cdd:cd14229   151 GSASHVSKTV-----CSTYLQSRYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGALE---------YDQIRY 215
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 195 IFSVMGFPADK---------------------DWEdIRKMPEYPT----LQKDFRRTTYAN------SSLIKYMEKHKV- 242
Cdd:cd14229   216 ISQTQGLPGEQllnvgtktsrffcretdapysSWR-LKTLEEHEAetgmKSKEARKYIFNSlddiahVNMVMDLEGSDLl 294
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 243 --KPDSKVFL-LLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14229   295 aeKADRREFVaLLKKMLLIDADLRITPADTLSHPF 329
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
4-275 1.31e-17

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: 82.35  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAE----HDLWHIIKfhraskankkpmQLPRSMVKSLLYQILDGI 79
Cdd:cd06613    45 QQEISMLKECRHPNIVAYFGSYLR--RDKLWIVMEYCGggslQDIYQVTG------------PLSELQIAYVCRETLKGL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILVMgegpERGRVKIADMGF-ARLFNSplkpLADLDPVVVTFWYRAPELLLGARH--YTKAID 156
Cdd:cd06613   111 AYLHSTGKIHRDIKGANILLT----EDGDVKLADFGVsAQLTAT----IAKRKSFIGTPYWMAPEVAAVERKggYDGKCD 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 157 IWAIG--CI-FAELLTsePIFhcrqeDIktsnpfHHDQLDRIFSVMGFPAdkdwedirkmpeyPTLQkdfrrttyanssl 233
Cdd:cd06613   183 IWALGitAIeLAELQP--PMF-----DL------HPMRALFLIPKSNFDP-------------PKLK------------- 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 234 ikymEKHKVKPDSKVFllLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd06613   224 ----DKEKWSPDFHDF--IKKCLTKNPKKRPTATKLLQHPFV 259
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
5-179 1.31e-17

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: 82.35  E-value: 1.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVfLSHSDRKVWLLFDYAEH-DLWHIIkfhraskANKKPmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14163    49 RELQIVERLDHKNIIHVYEM-LESADGKIYLVMELAEDgDVFDCV-------LHGGP--LPEHRAKALFRQLVEAIRYCH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEgpergRVKIADMGFARLFNSPLKPLADldpvvvTFW----YRAPELLLGARHYTKAIDIWA 159
Cdd:cd14163   119 GCGVAHRDLKCENALLQGF-----TLKLTDFGFAKQLPKGGRELSQ------TFCgstaYAAPEVLQGVPHDSRKGDIWS 187
                         170       180
                  ....*....|....*....|....*...
gi 1370507705 160 IGCIFAELL--------TSEPIFHCRQE 179
Cdd:cd14163   188 MGVVLYVMLcaqlpfddTDIPKMLCQQQ 215
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
3-169 1.40e-17

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: 82.07  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKFHRASkankkpmQLPRSMVKSLLYQILDGIHY 81
Cdd:cd08529    46 AIDEARVLSKLNSPYVIKYYDSFVD--KGKLNIVMEYAENgDLHSLIKSQRGR-------PLPEDQIWKFFIQTLLGLSH 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLfnspLKPLADLDPVVV-TFWYRAPELLLGaRHYTKAIDIWAI 160
Cdd:cd08529   117 LHSKKILHRDIKSMNIFL----DKGDNVKIGDLGVAKI----LSDTTNFAQTIVgTPYYLSPELCED-KPYNEKSDVWAL 187

                  ....*....
gi 1370507705 161 GCIFAELLT 169
Cdd:cd08529   188 GCVLYELCT 196
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
4-188 1.40e-17

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: 82.66  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELKHPNVIALQKVFLShsdrkvwllFDYAEHDLWHIIKFHRASKANKKPMQLPR-------SMVKSLLYQIL 76
Cdd:cd14039    39 CHEIQIMKKLNHPNVVKACDVPEE---------MNFLVNDVPLLAMEYCSGGDLRKLLNKPEnccglkeSQVLSLLSDIG 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  77 DGIHYLHANWVLHRDLKPANILVMGEGperGRV--KIADMGFARlfnsplkplaDLD------PVVVTFWYRAPELLLGa 148
Cdd:cd14039   110 SGIQYLHENKIIHRDLKPENIVLQEIN---GKIvhKIIDLGYAK----------DLDqgslctSFVGTLQYLAPELFEN- 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370507705 149 RHYTKAIDIWAIGCIFAELLTS-EPIFHCRQ-----EDIKTSNPFH 188
Cdd:cd14039   176 KSYTVTVDYWSFGTMVFECIAGfRPFLHNLQpftwhEKIKKKDPKH 221
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
5-276 1.62e-17

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: 82.36  E-value: 1.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWL-------LFDYAehdlwhiikfhraskANKKpmQLPRSMVKSLLYQILD 77
Cdd:cd14195    57 REVNILREIQHPNIITLHDIFENKTDVVLILelvsggeLFDFL---------------AEKE--SLTEEEATQFLKQILD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARlfnsPLKPLADLDPVVVTFWYRAPELL----LGARhytk 153
Cdd:cd14195   120 GVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDFGIAH----KIEAGNEFKNIFGTPEFVAPEIVnyepLGLE---- 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 154 aIDIWAIGCIFAELLTSEPIF--HCRQEDIKTSNPFHHDQLDRIFSvmgfpadkdwedirkmpEYPTLQKDFRRttyans 231
Cdd:cd14195   192 -ADMWSIGVITYILLSGASPFlgETKQETLTNISAVNYDFDEEYFS-----------------NTSELAKDFIR------ 247
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1370507705 232 slikymekhkvkpdskvflllqKLLTMDPTKRITSEQALQDPYFQ 276
Cdd:cd14195   248 ----------------------RLLVKDPKKRMTIAQSLEHSWIK 270
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
4-263 1.73e-17

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: 82.50  E-value: 1.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELKHPNVIALQKV----FLSHSDRKVWLLFDYAEH-DLWHIIkfHRASKANKkpmqLPRSMVKSLLYQILDG 78
Cdd:cd13989    41 CLEVQIMKKLNHPNVVSARDVppelEKLSPNDLPLLAMEYCSGgDLRKVL--NQPENCCG----LKESEVRTLLSDISSA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANIlVMGEGPERGRVKIADMGFARlfnsplkplaDLD------PVVVTFWYRAPELLLGARhYT 152
Cdd:cd13989   115 ISYLHENRIIHRDLKPENI-VLQQGGGRVIYKLIDLGYAK----------ELDqgslctSFVGTLQYLAPELFESKK-YT 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 153 KAIDIWAIGCIfaelltsepIFHCrqedIKTSNPF-HHDQldrIFSVMGFPADKDWEDIR---KMPEYPTLQKDFRRTTY 228
Cdd:cd13989   183 CTVDYWSFGTL---------AFEC----ITGYRPFlPNWQ---PVQWHGKVKQKKPEHICayeDLTGEVKFSSELPSPNH 246
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 229 ANSSLIKYMEKhkvkpdskvflLLQKLLTMDPTKR 263
Cdd:cd13989   247 LSSILKEYLES-----------WLQLMLRWDPRQR 270
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
5-275 2.27e-17

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: 81.55  E-value: 2.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAEH-DLW-HIIKFHRaskankkpmqLPRSMVKSLLYQILDGIHYL 82
Cdd:cd14079    51 REIQILKLFRHPHIIRLYEVIETPTD--IFMVMEYVSGgELFdYIVQKGR----------LSEDEARRFFQQIISGVEYC 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFN----------SPLkpladldpvvvtfwYRAPELLLGARHYT 152
Cdd:cd14079   119 HRHMVVHRDLKPENLLL----DSNMNVKIADFGLSNIMRdgeflktscgSPN--------------YAAPEVISGKLYAG 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 153 KAIDIWAIGCIFAELLtsepifhCRqediktSNPFhhdqldrifsvmgfpadkDWEDIrkmpeyPTLQKDFRRTTYanss 232
Cdd:cd14079   181 PEVDVWSCGVILYALL-------CG------SLPF------------------DDEHI------PNLFKKIKSGIY---- 219
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1370507705 233 likYMEKHkVKPDSKVflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14079   220 ---TIPSH-LSPGARD--LIKRMLVVDPLKRITIPEIRQHPWF 256
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
6-175 2.70e-17

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


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 81.39  E-value: 2.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRE-LKHPNVIALQKVFLsHSDRkVWLLFDYAE----HDLWHIIKfhraskanKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd08528    58 EVNIIKEqLRHPNIVRYYKTFL-ENDR-LYIVMELIEgaplGEHFSSLK--------EKNEHFTEDRIWNIFVQMVLALR 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHA-NWVLHRDLKPANILvMGEGPergRVKIADMGFARlfnSPLKPLADLDPVVVTFWYRAPELLlGARHYTKAIDIWA 159
Cdd:cd08528   128 YLHKeKQIVHRDLKPNNIM-LGEDD---KVTITDFGLAK---QKGPESSKMTSVVGTILYSCPEIV-QNEPYGEKADIWA 199
                         170
                  ....*....|....*.
gi 1370507705 160 IGCIFAELLTSEPIFH 175
Cdd:cd08528   200 LGCILYQMCTLQPPFY 215
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
6-174 3.20e-17

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: 81.51  E-value: 3.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELK-HPNVIALQKVFlsHSDRKVWLLFDYAEHDlwHIIKFHRASKANKkpmqLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd14198    57 EIAVLELAKsNPRVVNLHEVY--ETTSEIILILEYAAGG--EIFNLCVPDLAEM----VSENDIIRLIRQILEGVYYLHQ 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEGPeRGRVKIADMGFARLFNSPlkplADLDPVVVTFWYRAPELLlgarHY---TKAIDIWAIG 161
Cdd:cd14198   129 NNIVHLDLKPQNILLSSIYP-LGDIKIVDFGMSRKIGHA----CELREIMGTPEYLAPEIL----NYdpiTTATDMWNIG 199
                         170
                  ....*....|...
gi 1370507705 162 CIFAELLTSEPIF 174
Cdd:cd14198   200 VIAYMLLTHESPF 212
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
4-171 3.83e-17

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: 81.10  E-value: 3.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAE----HDlwhIIKFHRAskankkpmqLPRSMVKSLLYQILDGI 79
Cdd:cd06623    47 LRELKTLRSCESPYVVKCYGAF--YKEGEISIVLEYMDggslAD---LLKKVGK---------IPEPVLAYIARQILKGL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANW-VLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLdpvVVTFWYRAPELLLGaRHYTKAIDIW 158
Cdd:cd06623   113 DYLHTKRhIIHRDIKPSNLLI----NSKGEVKIADFGISKVLENTLDQCNTF---VGTVTYMSPERIQG-ESYSYAADIW 184
                         170
                  ....*....|...
gi 1370507705 159 AIGCIFAELLTSE 171
Cdd:cd06623   185 SLGLTLLECALGK 197
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
5-286 6.60e-17

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 81.24  E-value: 6.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELK-HPNVIALQKVFlsHSDRKVWLLFDyaehdlwhIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14179    50 REIAALKLCEgHPNIVKLHEVY--HDQLHTFLVME--------LLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEGpERGRVKIADMGFARLF---NSPLKpladlDPvVVTFWYRAPElLLGARHYTKAIDIWAI 160
Cdd:cd14179   120 DVGVVHRDLKPENLLFTDES-DNSEIKIIDFGFARLKppdNQPLK-----TP-CFTLHYAAPE-LLNYNGYDESCDLWSL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSEPIFHCRQEDIKTSNPfhhdqldrifsvmgfpadkdwEDIRKMPEyptlQKDFrrtTYANSSLIKYMEKH 240
Cdd:cd14179   192 GVILYTMLSGQVPFQCHDKSLTCTSA---------------------EEIMKKIK----QGDF---SFEGEAWKNVSQEA 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370507705 241 KVkpdskvflLLQKLLTMDPTKRITSEQALQDPYFQED------PLPTLDVF 286
Cdd:cd14179   244 KD--------LIQGLLTVDPNKRIKMSGLRYNEWLQDGsqlssnPLMTPDIL 287
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
5-275 6.64e-17

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 79.96  E-value: 6.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELK-HPNVIALQKVFlSHSDrKVWLLFDYAEHDLWHIIkFHRASKANkkpmqlprsmVKSLLYQILDGIHYLH 83
Cdd:cd14019    52 NELECLERLGgSNNVSGLITAF-RNED-QVVAVLPYIEHDDFRDF-YRKMSLTD----------IRIYLRNLFKALKHVH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLFNSPLKPLAdldPVVVTFWYRAPELLLGARHYTKAIDIWAIGCI 163
Cdd:cd14019   119 SFGIIHRDVKPGNFLY---NRETGKGVLVDFGLAQREEDRPEQRA---PRAGTRGFRAPEVLFKCPHQTTAIDIWSAGVI 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 164 FAELLTSEPIFHCRQEDIktsnpfhhDQLDRIFSVMGfpadKDWedirkmpeyptlqkdfrrttyansslikymekhkvk 243
Cdd:cd14019   193 LLSILSGRFPFFFSSDDI--------DALAEIATIFG----SDE------------------------------------ 224
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1370507705 244 pdskVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14019   225 ----AYDLLDKLLELDPSKRITAEEALKHPFF 252
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
5-161 7.48e-17

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: 79.74  E-value: 7.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKFHRaskankkpmQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14071    48 REVQIMKMLNHPHIIKLYQVM--ETKDMLYLVTEYASNgEIFDYLAQHG---------RMSEKEARKKFWQILSAVEYCH 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNS--PLKPLADLDPvvvtfwYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd14071   117 KRHIVHRDLKAENLLL----DANMNIKIADFGFSNFFKPgeLLKTWCGSPP------YAAPEVFEGKEYEGPQLDIWSLG 186
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
6-275 8.26e-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: 79.74  E-value: 8.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELK---HPNVIALQKVFlshsDRKVWLLFDYAEH----DLWHIIKFHRaskankkpmQLPRSMVKSLLYQILDG 78
Cdd:cd14004    55 EIHILDTLNkrsHPNIVKLLDFF----EDDEFYYLVMEKHgsgmDLFDFIERKP---------NMDEKEAKYIFRQVADA 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSplkplADLDPVVVTFWYRAPELLLGARHYTKAIDIW 158
Cdd:cd14004   122 VKHLHDQGIVHRDIKDENVILDGN----GTIKLIDFGSAAYIKS-----GPFDTFVGTIDYAAPEVLRGNPYGGKEQDIW 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 159 AIGCIFAELLTSEpifhcrqediktsNPFHhdQLDRIFSvmgfpadkdwediRKMPEYPTLQKDfrrttyaNSSLIKyme 238
Cdd:cd14004   193 ALGVLLYTLVFKE-------------NPFY--NIEEILE-------------ADLRIPYAVSED-------LIDLIS--- 234
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1370507705 239 khkvkpdskvflllqKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14004   235 ---------------RMLNRDVGDRPTIEELLTDPWL 256
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
63-276 1.13e-16

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: 79.45  E-value: 1.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  63 LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFAR--LFNSPLKPLadldpvVVTFWYR 140
Cdd:cd05611    94 LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLI----DQTGHLKLTDFGLSRngLEKRHNKKF------VGTPDYL 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 141 APELLLGARHyTKAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFsvmgfpadkdwedirkmpeyptlQ 220
Cdd:cd05611   164 APETILGVGD-DKMSDWWSLGCVIFEFLFGYP-------------PFHAETPDAVF-----------------------D 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370507705 221 KDFRRTtyansslIKYMEKHKVKPDSKVFLLLQKLLTMDPTKRITS---EQALQDPYFQ 276
Cdd:cd05611   207 NILSRR-------INWPEEVKEFCSPEAVDLINRLLCMDPAKRLGAngyQEIKSHPFFK 258
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
6-274 1.24e-16

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: 79.50  E-value: 1.24e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAE-HDLW-HIIKFHRASKANkkpmqlprsmVKSLLYQILDGIHYLH 83
Cdd:cd14087    47 ELNVLRRVRHTNIIQLIEVFETKE--RVYMVMELATgGELFdRIIAKGSFTERD----------ATRVLQMVLDGVKYLH 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEGPErGRVKIADMGFArlFNSPLKPLADLDPVVVTFWYRAPELLLgARHYTKAIDIWAIGCI 163
Cdd:cd14087   115 GLGITHRDLKPENLLYYHPGPD-SKIMITDFGLA--STRKKGPNCLMKTTCGTPEYIAPEILL-RKPYTQSVDMWAVGVI 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 164 FAELLTSepifhcrqediktSNPFHHDQLDRI--------FSVMGFPadkdWEDIRKmpeyptLQKDFrrttyansslik 235
Cdd:cd14087   191 AYILLSG-------------TMPFDDDNRTRLyrqilrakYSYSGEP----WPSVSN------LAKDF------------ 235
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370507705 236 ymekhkvkpdskvfllLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14087   236 ----------------IDRLLTVNPGERLSATQALKHPW 258
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
2-167 1.36e-16

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: 79.01  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKfhraskaNKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd08220    45 AALNEVKVLSMLHHPNIIEYYESFLE--DKALMIVMEYAPGgTLFEYIQ-------QRKGSLLSEEEILHFFVQILLALH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLFNSPLKPLAdldpVVVTFWYRAPELLLGaRHYTKAIDIWAI 160
Cdd:cd08220   116 HVHSKQILHRDLKTQNILL---NKKRTVVKIGDFGISKILSSKSKAYT----VVGTPCYISPELCEG-KPYNQKSDIWAL 187

                  ....*..
gi 1370507705 161 GCIFAEL 167
Cdd:cd08220   188 GCVLYEL 194
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
5-175 1.52e-16

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: 79.28  E-value: 1.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVflSHSDRKVWLLFDYAEH-DLWHIIKfhraSKANkkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14201    54 KEIKILKELQHENIVALYDV--QEMPNSVFLVMEYCNGgDLADYLQ----AKGT-----LSEDTIRVFLQQIAAAMRILH 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEGPERG-----RVKIADMGFARLFNSPLKPLAdldpVVVTFWYRAPELLLgARHYTKAIDIW 158
Cdd:cd14201   123 SKGIIHRDLKPQNILLSYASRKKSsvsgiRIKIADFGFARYLQSNMMAAT----LCGSPMYMAPEVIM-SQHYDAKADLW 197
                         170
                  ....*....|....*..
gi 1370507705 159 AIGCIFAELLTSEPIFH 175
Cdd:cd14201   198 SIGTVIYQCLVGKPPFQ 214
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
5-180 1.55e-16

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: 79.24  E-value: 1.55e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKvwLLFDYAEH-DLWHIIKFHRASKAnkkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14066    39 TELEMLGRLRHPNLVRLLGYCLESDEKL--LVYEYMPNgSLEDRLHCHKGSPP------LPWPQRLKIAKGIARGLEYLH 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANW---VLHRDLKPANILVmgegPERGRVKIADMGFARLFNsPLKPLADLDPVVVTFWYRAPELLLGARhYTKAIDIWAI 160
Cdd:cd14066   111 EECpppIIHGDIKSSNILL----DEDFEPKLTDFGLARLIP-PSESVSKTSAVKGTIGYLAPEYIRTGR-VSTKSDVYSF 184
                         170       180
                  ....*....|....*....|.
gi 1370507705 161 GCIFAELLTS-EPIFHCRQED 180
Cdd:cd14066   185 GVVLLELLTGkPAVDENRENA 205
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
35-274 1.57e-16

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: 80.19  E-value: 1.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  35 LLFDYAEHDLWHIIKfhraskaNKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADM 114
Cdd:cd14211    77 LVFEMLEQNLYDFLK-------QNKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDF 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 115 GFARLFNSPLKpladlDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDR 194
Cdd:cd14211   150 GSASHVSKAVC-----STYLQSRYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGSSE---------YDQIRY 214
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 195 IFSVMGFPA------------------DKDWEDIR-KMPE---YPTLQKDFRRTTYANSSL--IKYMEKHKVKPDSKVFL 250
Cdd:cd14211   215 ISQTQGLPAehllnaatktsrffnrdpDSPYPLWRlKTPEeheAETGIKSKEARKYIFNCLddMAQVNGPSDLEGSELLA 294
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370507705 251 ----------LLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14211   295 ekadrrefidLLKRMLTIDQERRITPGEALNHPF 328
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
5-179 1.58e-16

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: 79.44  E-value: 1.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKH---PNVIALQKVFLShsDRKVWLLFDYAEHDlwHIIKFHRASKANKKPMQLprsmvksLLYQILDGIHY 81
Cdd:cd06917    48 KEVALLSQLKLgqpKNIIKYYGSYLK--GPSLWIIMDYCEGG--SIRTLMRAGPIAERYIAV-------IMREVLVALKF 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPLADLdpvVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd06917   117 IHKDGIIHRDIKAANILVTNT----GNVKLCDFGVAASLNQNSSKRSTF---VGTPYWMAPEVITEGKYYDTKADIWSLG 189
                         170
                  ....*....|....*...
gi 1370507705 162 CIFAELLTSEPIfHCRQE 179
Cdd:cd06917   190 ITTYEMATGNPP-YSDVD 206
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
5-169 1.98e-16

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: 78.70  E-value: 1.98e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKFHRAskankkpMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd08218    48 KEVAVLSKMKHPNIVQYQESF--EENGNLYIVMDYCDGgDLYKRINAQRG-------VLFPEDQILDWFVQLCLALKHVH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKpLAdlDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCI 163
Cdd:cd08218   119 DRKILHRDIKSQNIFLT----KDGIIKLGDFGIARVLNSTVE-LA--RTCIGTPYYLSPEICEN-KPYNNKSDIWALGCV 190

                  ....*.
gi 1370507705 164 FAELLT 169
Cdd:cd08218   191 LYEMCT 196
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
5-161 2.21e-16

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: 79.24  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVflshsdrkvwlLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLY--QILDGIHYL 82
Cdd:cd14199    74 QEIAILKKLDHPNVVKLVEV-----------LDDPSEDHLYMVFELVKQGPVMEVPTLKPLSEDQARFYfqDLIKGIEYL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplkPLADLDPVVVTFWYRAPELLLGARHY--TKAIDIWAI 160
Cdd:cd14199   143 HYQKIIHRDVKPSNLLV----GEDGHIKIADFGVSNEFEG---SDALLTNTVGTPAFMAPETLSETRKIfsGKALDVWAM 215

                  .
gi 1370507705 161 G 161
Cdd:cd14199   216 G 216
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
5-168 2.21e-16

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 78.46  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEH-DLWHIIKfhraskankKPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14161    51 REIEIMSSLNHPHIISVYEVFENSS--KIVIVMEYASRgDLYDYIS---------ERQRLSELEARHFFRQIVSAVHYCH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplkpladlDPVVVTF----WYRAPELLLGARHYTKAIDIWA 159
Cdd:cd14161   120 ANGIVHRDLKLENILL----DANGNIKIADFGLSNLYNQ--------DKFLQTYcgspLYASPEIVNGRPYIGPEVDSWS 187

                  ....*....
gi 1370507705 160 IGCIFAELL 168
Cdd:cd14161   188 LGVLLYILV 196
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
9-281 2.39e-16

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 79.68  E-value: 2.39e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   9 LLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHII---KFHRASKANkkpmqlprsmvkSLLYQILDGIHYLHA 84
Cdd:cd14176    66 LLRYGQHPNIITLKDVY--DDGKYVYVVTELMKGgELLDKIlrqKFFSEREAS------------AVLFTITKTVEYLHA 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLadLDPvVVTFWYRAPElLLGARHYTKAIDIWAIGCIF 164
Cdd:cd14176   132 QGVVHRDLKPSNILYVDESGNPESIRICDFGFAKQLRAENGLL--MTP-CYTANFVAPE-VLERQGYDAACDIWSLGVLL 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 165 AELLTSEPIFHCRQEDIKtsnpfhHDQLDRI----FSVMGfpadkdwedirkmpeyptlqkdfrrtTYANSslikymekh 240
Cdd:cd14176   208 YTMLTGYTPFANGPDDTP------EEILARIgsgkFSLSG--------------------------GYWNS--------- 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 241 kVKPDSKVflLLQKLLTMDPTKRITSEQALQDPYF-QEDPLP 281
Cdd:cd14176   247 -VSDTAKD--LVSKMLHVDPHQRLTAALVLRHPWIvHWDQLP 285
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
63-275 8.71e-16

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: 77.97  E-value: 8.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  63 LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANIL------VMGEGPERGR---------VKIADMGFARLFNSPLKPL 127
Cdd:cd14213   113 FPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILfvqsdyVVKYNPKMKRdertlknpdIKVVDFGSATYDDEHHSTL 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 128 adldpvVVTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIF--HCRQEDI------------------KTSNPF 187
Cdd:cd14213   193 ------VSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFqtHDSKEHLammerilgplpkhmiqktRKRKYF 265
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 188 HHDQLDrifsvmgfpadkdWEDIRKMPEYptlqkdFRRttyANSSLIKYMEKHKVKPDsKVFLLLQKLLTMDPTKRITSE 267
Cdd:cd14213   266 HHDQLD-------------WDEHSSAGRY------VRR---RCKPLKEFMLSQDVDHE-QLFDLIQKMLEYDPAKRITLD 322

                  ....*...
gi 1370507705 268 QALQDPYF 275
Cdd:cd14213   323 EALKHPFF 330
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
74-196 9.01e-16

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK2 is a MAPK kinase kinase (MAPKKK or MKKK), that phosphorylates and activates the MAPK kinase MEK5 (or MKK5), which in turn phosphorylates and activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK2 also activates ERK1/2, c-Jun N-terminal kinase (JNK) and p38 through their respective MAPKKs MEK1/2, JNK-activating kinase 2 (JNKK2), and MKK3/6. MEKK2 plays roles in T cell receptor signaling, immune synapse formation, cytokine gene expression, as well as in EGF and FGF receptor signaling. The MEKK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 77.01  E-value: 9.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILvmgeGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTK 153
Cdd:cd06652   114 QILEGVHYLHSNMIVHRDIKGANIL----RDSVGNVKLGDFGASKRLQTICLSGTGMKSVTGTPYWMSPEVISGEGYGRK 189
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370507705 154 AiDIWAIGCIFAELLTSEP----------IFHCRQEDIKTSNPFH-----HDQLDRIF 196
Cdd:cd06652   190 A-DIWSVGCTVVEMLTEKPpwaefeamaaIFKIATQPTNPQLPAHvsdhcRDFLKRIF 246
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
9-281 9.62e-16

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: 77.37  E-value: 9.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   9 LLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHII---KFHRASKANkkpmqlprsmvkSLLYQILDGIHYLHA 84
Cdd:cd14175    48 LLRYGQHPNIITLKDVY--DDGKHVYLVTELMRGgELLDKIlrqKFFSEREAS------------SVLHTICKTVEYLHS 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLadLDPvVVTFWYRAPElLLGARHYTKAIDIWAIGCIF 164
Cdd:cd14175   114 QGVVHRDLKPSNILYVDESGNPESLRICDFGFAKQLRAENGLL--MTP-CYTANFVAPE-VLKRQGYDEGCDIWSLGILL 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 165 AELLTSEPIFHCRQEDIKtsnpfhHDQLDRI----FSVMGfpadKDWEDIRKMpeyptlQKDfrrttyansslikymekh 240
Cdd:cd14175   190 YTMLAGYTPFANGPSDTP------EEILTRIgsgkFTLSG----GNWNTVSDA------AKD------------------ 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 241 kvkpdskvflLLQKLLTMDPTKRITSEQALQDPYF-QEDPLP 281
Cdd:cd14175   236 ----------LVSKMLHVDPHQRLTAKQVLQHPWItQKDKLP 267
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
5-274 1.13e-15

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: 76.50  E-value: 1.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAE-HDLwhiikFHRASKANkkpMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14103    39 NEIEIMNQLRHPRLLQLYDAF--ETPREMVLVMEYVAgGEL-----FERVVDDD---FELTERDCILFMRQICEGVQYMH 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgeGPERGRVKIADMGFARLFNsPLKPLAdldpvvVTFW---YRAPELLlgarHYTK---AIDI 157
Cdd:cd14103   109 KQGILHLDLKPENILCV--SRTGNQIKIIDFGLARKYD-PDKKLK------VLFGtpeFVAPEVV----NYEPisyATDM 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 158 WAIGCIFAELLTSEpifhcrqediktsNPFhhdqldrifsvMGfpaDKDWEdirkmpeyptlqkdfrrtTYANSSLIKY- 236
Cdd:cd14103   176 WSVGVICYVLLSGL-------------SPF-----------MG---DNDAE------------------TLANVTRAKWd 210
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1370507705 237 ---MEKHKVKPDSKVFllLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14103   211 fddEAFDDISDEAKDF--ISKLLVKDPRKRMSAAQCLQHPW 249
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
2-174 1.22e-15

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 76.31  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEHDLWHiikfhraSKANKKPMQL-PRSMVKSLLYQILDGIH 80
Cdd:cd08221    45 DALNEIDILSLLNHDNIITYYNHFLD--GESLFIEMEYCNGGNLH-------DKIAQQKNQLfPEEVVLWYLYQIVSAVS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKpLAdlDPVVVTFWYRAPELLLGARhYTKAIDIWAI 160
Cdd:cd08221   116 HIHKAGILHRDIKTLNIFLT----KADLVKLGDFGISKVLDSESS-MA--ESIVGTPYYMSPELVQGVK-YNFKSDIWAV 187
                         170
                  ....*....|....
gi 1370507705 161 GCIFAELLTSEPIF 174
Cdd:cd08221   188 GCVLYELLTLKRTF 201
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
4-169 1.24e-15

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: 76.92  E-value: 1.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELKHPNVIA-------LQKvfLSHSDRKVwLLFDYAEH-DLW-HIIKFHRASKANKKPmqlprsmVKSLLYQ 74
Cdd:cd14038    40 CLEIQIMKRLNHPNVVAardvpegLQK--LAPNDLPL-LAMEYCQGgDLRkYLNQFENCCGLREGA-------ILTLLSD 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANIlVMGEGPERGRVKIADMGFARlfnsplkplaDLD------PVVVTFWYRAPElLLGA 148
Cdd:cd14038   110 ISSALRYLHENRIIHRDLKPENI-VLQQGEQRLIHKIIDLGYAK----------ELDqgslctSFVGTLQYLAPE-LLEQ 177
                         170       180
                  ....*....|....*....|.
gi 1370507705 149 RHYTKAIDIWAIGCIFAELLT 169
Cdd:cd14038   178 QKYTVTVDYWSFGTLAFECIT 198
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
5-175 1.43e-15

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: 76.24  E-value: 1.43e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDR----KVWLLFDYAE----HDLWHIIKFhraskankkpmqLPRSMVKSLLYQIL 76
Cdd:cd14012    47 KELESLKKLRHPNLVSYLAFSIERRGRsdgwKVYLLTEYAPggslSELLDSVGS------------VPLDTARRWTLQLL 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  77 DGIHYLHANWVLHRDLKPANILVmGEGPERGRVKIADMGFARLFNSPLKPLAdLDPVVVTFWyRAPELLLGARHYTKAID 156
Cdd:cd14012   115 EALEYLHRNGVVHKSLHAGNVLL-DRDAGTGIVKLTDYSLGKTLLDMCSRGS-LDEFKQTYW-LPPELAQGSKSPTRKTD 191
                         170
                  ....*....|....*....
gi 1370507705 157 IWAIGCIFAELLTSEPIFH 175
Cdd:cd14012   192 VWDLGLLFLQMLFGLDVLE 210
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
6-172 1.44e-15

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: 76.22  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDRKVWLLFDY-AEHDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd06653    54 EIQLLKNLRHDRIVQYYGCLRDPEEKKLSIFVEYmPGGSVKDQLKAYGA---------LTENVTRRYTRQILQGVSYLHS 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILvmgeGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAiDIWAIGCIF 164
Cdd:cd06653   125 NMIVHRDIKGANIL----RDSAGNVKLGDFGASKRIQTICMSGTGIKSVTGTPYWMSPEVISGEGYGRKA-DVWSVACTV 199

                  ....*...
gi 1370507705 165 AELLTSEP 172
Cdd:cd06653   200 VEMLTEKP 207
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
2-277 1.58e-15

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: 76.49  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELK-HPNVIALQKVFLSHSdrKVWLLFDyaehdlwhIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd14182    55 ATLKEIDILRKVSgHPNIIQLKDTYETNT--FFFLVFD--------LMKKGELFDYLTEKVTLSEKETRKIMRALLEVIC 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFArlfnSPLKPLADLDPVVVTFWYRAPELL---LGARH--YTKAI 155
Cdd:cd14182   125 ALHKLNIVHRDLKPENILL----DDDMNIKLTDFGFS----CQLDPGEKLREVCGTPGYLAPEIIecsMDDNHpgYGKEV 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 156 DIWAIGCIFAELLTSEPIFhcrqediktsnpFHHDQLDRIFSVM------GFPadkDWEDirkmpeYPTLQKDfrrttya 229
Cdd:cd14182   197 DMWSTGVIMYTLLAGSPPF------------WHRKQMLMLRMIMsgnyqfGSP---EWDD------RSDTVKD------- 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1370507705 230 nsslikymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYFQE 277
Cdd:cd14182   249 ---------------------LISRFLVVQPQKRYTAEEALAHPFFQQ 275
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
5-169 1.58e-15

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: 76.02  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKFHRASKANKkpmqlprsmVKSLLYQILDGIHYLH 83
Cdd:cd14072    48 REVRIMKILNHPNIVKLFEVI--ETEKTLYLVMEYASGgEVFDYLVAHGRMKEKE---------ARAKFRQIVSAVQYCH 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCI 163
Cdd:cd14072   117 QKRIVHRDLKAENLLLDAD----MNIKIADFGFSNEFTPGNK----LDTFCGSPPYAAPELFQGKKYDGPEVDVWSLGVI 188

                  ....*.
gi 1370507705 164 FAELLT 169
Cdd:cd14072   189 LYTLVS 194
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-174 1.99e-15

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: 75.92  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAE-HDLWHIIKFHRasKANKKPMQlprSMVKSLLYQILDGIHY 81
Cdd:cd08222    49 ANREAKLLSKLDHPAIVKFHDSFVE--KESFCIVTEYCEgGDLDDKISEYK--KSGTTIDE---NQILDWFIQLLLAVQY 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegpERGRVKIADMGFARLfnspLKPLADLdpvVVTF----WYRAPELLLGARHYTKAiDI 157
Cdd:cd08222   122 MHERRILHRDLKAKNIFL-----KNNVIKVGDFGISRI----LMGTSDL---ATTFtgtpYYMSPEVLKHEGYNSKS-DI 188
                         170
                  ....*....|....*..
gi 1370507705 158 WAIGCIFAELLTSEPIF 174
Cdd:cd08222   189 WSLGCILYEMCCLKHAF 205
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
5-274 2.01e-15

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: 76.05  E-value: 2.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIKFHRAskankkpmQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd14097    49 REVDILKHVNHAHIIHLEEVF--ETPKRMYLVMELCEDGELKELLLRKG--------FFSENETRHIIQSLASAVAYLHK 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMG---EGPERGRVKIADMGFARLFNSplKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIG 161
Cdd:cd14097   119 NDIVHRDLKLENILVKSsiiDNNDKLNIKVTDFGLSVQKYG--LGEDMLQETCGTPIYMAPE-VISAHGYSQQCDIWSIG 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFHCRQEdiktsnpfhhdqldrifsvmgfpaDKDWEDIRKmpeyptlqKDFRRTTYANSSLIKYMEKhk 241
Cdd:cd14097   196 VIMYMLLCGEPPFVAKSE------------------------EKLFEEIRK--------GDLTFTQSVWQSVSDAAKN-- 241
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370507705 242 vkpdskvflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14097   242 ---------VLQQLLKVDPAHRMTASELLDNPW 265
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
5-274 2.01e-15

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: 76.15  E-value: 2.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWL-------LFDYAehdlwhiikfhraskANKKpmQLPRSMVKSLLYQILD 77
Cdd:cd14196    57 REVSILRQVLHPNIITLHDVYENRTDVVLILelvsggeLFDFL---------------AQKE--SLSEEEATSFIKQILD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFARlfnsPLKPLADLDPVVVTFWYRAPELL----LGArhytk 153
Cdd:cd14196   120 GVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIKLIDFGLAH----EIEDGVEFKNIFGTPEFVAPEIVnyepLGL----- 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIF--HCRQEDIKTSNPFHHDQLDRIFSvmgfpadkdwedirkmpEYPTLQKDFrrttyans 231
Cdd:cd14196   191 EADMWSIGVITYILLSGASPFlgDTKQETLANITAVSYDFDEEFFS-----------------HTSELAKDF-------- 245
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1370507705 232 slikymekhkvkpdskvfllLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14196   246 --------------------IRKLLVKETRKRLTIQEALRHPW 268
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
6-163 2.12e-15

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: 75.91  E-value: 2.12e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIKFHRASKankkpmqLPRSMVKSLLYQILDGIHYLHAN 85
Cdd:cd14082    52 EVAILQQLSHPGVVNLECMF--ETPERVFVVMEKLHGDMLEMILSSEKGR-------LPERITKFLVTQILVALRYLHSK 122
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370507705  86 WVLHRDLKPANILVMGEGPeRGRVKIADMGFARLFnsPLKPLAdlDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCI 163
Cdd:cd14082   123 NIVHCDLKPENVLLASAEP-FPQVKLCDFGFARII--GEKSFR--RSVVGTPAYLAPEVLRNKG-YNRSLDMWSVGVI 194
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
6-171 2.15e-15

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: 75.88  E-value: 2.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIalQKVFLSHSDRKVWLLFDY-AEHDLWHIIKFHRaskankkpmQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd06629    58 EIDTLKDLDHPNIV--QYLGFEETEDYFSIFLEYvPGGSIGSCLRKYG---------KFEEDLVRFFTRQILDGLAYLHS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYrAPELL-LGARHYTKAIDIWAIGCI 163
Cdd:cd06629   127 KGILHRDLKADNILVDLE----GICKISDFGISKKSDDIYGNNGATSMQGSVFWM-APEVIhSQGQGYSAKVDIWSLGCV 201

                  ....*...
gi 1370507705 164 FAELLTSE 171
Cdd:cd06629   202 VLEMLAGR 209
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
4-161 2.24e-15

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 77.17  E-value: 2.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELKHPNVIALQKVFLSHSDRKVWLLF-DYAEHDLWHIIKFHRASkankkpmqlprsmvkSLLYQILDGIHYL 82
Cdd:PLN00034  120 CREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFmDGGSLEGTHIADEQFLA---------------DVARQILSGIAYL 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPladLDPVVVTFWYRAPEL----LLGARHYTKAIDIW 158
Cdd:PLN00034  185 HRRHIVHRDIKPSNLLI----NSAKNVKIADFGVSRILAQTMDP---CNSSVGTIAYMSPERintdLNHGAYDGYAGDIW 257

                  ...
gi 1370507705 159 AIG 161
Cdd:PLN00034  258 SLG 260
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
5-172 2.32e-15

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 75.74  E-value: 2.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdrKVWLLFDY----AEHDLWhiikfhraskankKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd06609    48 QEIQFLSQCDSPYITKYYGSFLKGS--KLWIIMEYcgggSVLDLL-------------KPGPLDETYIAFILREVLLGLE 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMgegpERGRVKIADMGFA-RLFNSPLKpladLDPVVVT-FWYrAPELLLGARHYTKAiDIW 158
Cdd:cd06609   113 YLHSEGKIHRDIKAANILLS----EEGDVKLADFGVSgQLTSTMSK----RNTFVGTpFWM-APEVIKQSGYDEKA-DIW 182
                         170
                  ....*....|....
gi 1370507705 159 AIGCIFAELLTSEP 172
Cdd:cd06609   183 SLGITAIELAKGEP 196
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
4-171 2.41e-15

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 75.79  E-value: 2.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAEHDlwhiiKFHRASKANKKPmqlPRSMVKSLLyQILDGIHYLH 83
Cdd:cd14148    41 RQEARLFWMLQHPNIIALRGVCLNPPH--LCLVMEYARGG-----ALNRALAGKKVP---PHVLVNWAV-QIARGMNYLH 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANW---VLHRDLKPANILVMgEGPERGRV-----KIADMGFARLFNSPLKPLAdldpvVVTFWYRAPELLlgaRH--YTK 153
Cdd:cd14148   110 NEAivpIIHRDLKSSNILIL-EPIENDDLsgktlKITDFGLAREWHKTTKMSA-----AGTYAWMAPEVI---RLslFSK 180
                         170
                  ....*....|....*...
gi 1370507705 154 AIDIWAIGCIFAELLTSE 171
Cdd:cd14148   181 SSDVWSFGVLLWELLTGE 198
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
35-274 2.50e-15

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


Pssm-ID: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 77.05  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  35 LLFDYAEHDLWHIIKFHRASKankkpmqLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADM 114
Cdd:cd14227    93 LVFEMLEQNLYDFLKQNKFSP-------LPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRQPYRVKVIDF 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 115 GFARLFNSplkplADLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDR 194
Cdd:cd14227   166 GSASHVSK-----AVCSTYLQSRYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGASE---------YDQIRY 230
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 195 IFSVMGFPA----------------DKD-----WEdiRKMP-----EYPTLQKDFRRTTY------ANSSLIKYMEKHKV 242
Cdd:cd14227   231 ISQTQGLPAeyllsagtkttrffnrDTDspyplWR--LKTPedheaETGIKSKEARKYIFnclddmAQVNMTTDLEGSDM 308
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1370507705 243 ---KPDSKVFL-LLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14227   309 lveKADRREFIdLLKKMLTIDADKRITPIETLNHPF 344
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
6-296 3.31e-15

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: 75.79  E-value: 3.31e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLShsDRKVWLLFDY----AEHDLWHIIKFHRASKANKKPMQLPRSMvksllyqildgihY 81
Cdd:cd06659    68 EVVIMRDYQHPNVVEMYKSYLV--GEELWVLMEYlqggALTDIVSQTRLNEEQIATVCEAVLQALA-------------Y 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEGpergRVKIADMGFARLFNsplKPLADLDPVVVTFWYRAPELLLGARhYTKAIDIWAIG 161
Cdd:cd06659   133 LHSQGVIHRDIKSDSILLTLDG----RVKLSDFGFCAQIS---KDVPKRKSLVGTPYWMAPEVISRCP-YGTEVDIWSLG 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPifhcrqediktsnPFhhdqldriFSVMGFPADKdweDIRKMPEyPTLQkdfrrttyaNSslikymekHK 241
Cdd:cd06659   205 IMVIEMVDGEP-------------PY--------FSDSPVQAMK---RLRDSPP-PKLK---------NS--------HK 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370507705 242 VKPDSKVFllLQKLLTMDPTKRITSEQALQDPYFQEDPLPTldvfagCQIP----YPKR 296
Cdd:cd06659   243 ASPVLRDF--LERMLVRDPQERATAQELLDHPFLLQTGLPE------CLVPliqqYRKR 293
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
68-169 3.39e-15

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: 75.36  E-value: 3.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  68 VKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPeRGRVKIADMGFARLFNSPlkplADLDPVVVTFWYRAPElLLG 147
Cdd:cd14197   113 VKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESP-LGDIKIVDFGLSRILKNS----EELREIMGTPEYVAPE-ILS 186
                          90       100
                  ....*....|....*....|..
gi 1370507705 148 ARHYTKAIDIWAIGCIFAELLT 169
Cdd:cd14197   187 YEPISTATDMWSIGVLAYVMLT 208
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
6-278 3.41e-15

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


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 75.85  E-value: 3.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLShSDRKVWLLFDYAEHDLWHII---KFHRASKANkkpmqlprsmvkSLLYQILDGIHYL 82
Cdd:cd14168    58 EIAVLRKIKHENIVALEDIYES-PNHLYLVMQLVSGGELFDRIvekGFYTEKDAS------------TLIRQVLDAVYYL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMGEgPERGRVKIADMGFARLFNSplkplAD-LDPVVVTFWYRAPElLLGARHYTKAIDIWAIG 161
Cdd:cd14168   125 HRMGIVHRDLKPENLLYFSQ-DEESKIMISDFGLSKMEGK-----GDvMSTACGTPGYVAPE-VLAQKPYSKAVDCWSIG 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPifhcrqediktsnPFHHDQLDRIFSVMgFPADKD-----WEDIRKMpeyptlQKDFrrttyanssliky 236
Cdd:cd14168   198 VIAYILLCGYP-------------PFYDENDSKLFEQI-LKADYEfdspyWDDISDS------AKDF------------- 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 237 mekhkvkpdskvfllLQKLLTMDPTKRITSEQALQDPYFQED 278
Cdd:cd14168   245 ---------------IRNLMEKDPNKRYTCEQALRHPWIAGD 271
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
6-172 3.81e-15

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: 75.12  E-value: 3.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYaehdlwhiIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHAN 85
Cdd:cd06651    59 EIQLLKNLQHERIVQYYGCLRDRAEKTLTIFMEY--------MPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILvmgeGPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAiDIWAIGCIFA 165
Cdd:cd06651   131 MIVHRDIKGANIL----RDSAGNVKLGDFGASKRLQTICMSGTGIRSVTGTPYWMSPEVISGEGYGRKA-DVWSLGCTVV 205

                  ....*..
gi 1370507705 166 ELLTSEP 172
Cdd:cd06651   206 EMLTEKP 212
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
6-179 4.27e-15

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: 74.97  E-value: 4.27e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDlwHIIKFHRASKANKKPMqlprsmVKSLLYQILDGIHYLHAN 85
Cdd:cd14187    57 EIAIHRSLAHQHVVGFHGFF--EDNDFVYVVLELCRRR--SLLELHKRRKALTEPE------ARYYLRQIILGCQYLHRN 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLdpvVVTFWYRAPElLLGARHYTKAIDIWAIGCIFA 165
Cdd:cd14187   127 RVIHRDLKLGNLFL----NDDMEVKIGDFGLATKVEYDGERKKTL---CGTPNYIAPE-VLSKKGHSFEVDIWSIGCIMY 198
                         170
                  ....*....|....*.
gi 1370507705 166 ELLTSEPIFH--CRQE 179
Cdd:cd14187   199 TLLVGKPPFEtsCLKE 214
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
5-271 4.41e-15

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: 75.10  E-value: 4.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAE-HDLWHIIKfhraskankKPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14046    53 REVMLLSRLNHQHVVRYYQAWIE--RANLYIQMEYCEkSTLRDLID---------SGLFQDTDRLWRLFRQILEGLAYIH 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFA----RLFNSPLKPLADLDPV-----------VVTFWYRAPELLLGA 148
Cdd:cd14046   122 SQGIIHRDLKPVNIFL----DSNGNVKIGDFGLAtsnkLNVELATQDINKSTSAalgssgdltgnVGTALYVAPEVQSGT 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 149 -RHYTKAIDIWAIGCIFAELltsepifhcrqediktSNPFhHDQLDRIFSVMgfpadkdweDIRKMPeyPTLQKDFRRTT 227
Cdd:cd14046   198 kSTYNEKVDMYSLGIIFFEM----------------CYPF-STGMERVQILT---------ALRSVS--IEFPPDFDDNK 249
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1370507705 228 YansslikymekhkvkpdSKVFLLLQKLLTMDPTKRITSEQALQ 271
Cdd:cd14046   250 H-----------------SKQAKLIRWLLNHDPAKRPSAQELLK 276
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
2-171 4.55e-15

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: 75.07  E-value: 4.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAEH-DLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd14146    39 SVRQEAKLFSMLRHPNIIKLEGVCLEEPN--LCLVMEFARGgTLNRALAAANAAPGPRRARRIPPHILVNWAVQIARGML 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWV---LHRDLKPANILVMgEGPE-----RGRVKIADMGFARLFNSPLKPLAdldpvVVTFWYRAPELLLGARhYT 152
Cdd:cd14146   117 YLHEEAVvpiLHRDLKSSNILLL-EKIEhddicNKTLKITDFGLAREWHRTTKMSA-----AGTYAWMAPEVIKSSL-FS 189
                         170
                  ....*....|....*....
gi 1370507705 153 KAIDIWAIGCIFAELLTSE 171
Cdd:cd14146   190 KGSDIWSYGVLLWELLTGE 208
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
6-175 4.64e-15

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: 75.45  E-value: 4.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlshsdrkvwllfdYAEHDLWHIIKFHRASKANKKPMQLPRSM----VKSLLYQILDGIHY 81
Cdd:cd06644    59 EIEILATCNHPYIVKLLGAF-------------YWDGKLWIMIEFCPGGAVDAIMLELDRGLtepqIQVICRQMLEALQY 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEgperGRVKIADMGFARlfnSPLKPLADLDPVVVTFWYRAPELLLGARH----YTKAIDI 157
Cdd:cd06644   126 LHSMKIIHRDLKAGNVLLTLD----GDIKLADFGVSA---KNVKTLQRRDSFIGTPYWMAPEVVMCETMkdtpYDYKADI 198
                         170
                  ....*....|....*...
gi 1370507705 158 WAIGCIFAELLTSEPIFH 175
Cdd:cd06644   199 WSLGITLIEMAQIEPPHH 216
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
6-210 9.23e-15

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: 73.91  E-value: 9.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAE-HDLWHIIkfhraSKANKKPMQLPRSMVksllYQILDGIHYLHA 84
Cdd:cd14184    49 EVSILRRVKHPNIIMLIEEMDTPAE--LYLVMELVKgGDLFDAI-----TSSTKYTERDASAMV----YNLASALKYLHG 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMgEGPERGR-VKIADMGFARLFNSPLKpladldPVVVTFWYRAPElLLGARHYTKAIDIWAIGCI 163
Cdd:cd14184   118 LCIVHRDIKPENLLVC-EYPDGTKsLKLGDFGLATVVEGPLY------TVCGTPTYVAPE-IIAETGYGLKVDIWAAGVI 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1370507705 164 FAELLTSEPIFhcrqediKTSNPFHHDQLDRIF-SVMGFPADKdWEDI 210
Cdd:cd14184   190 TYILLCGFPPF-------RSENNLQEDLFDQILlGKLEFPSPY-WDNI 229
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
5-172 1.04e-14

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 74.70  E-value: 1.04e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEHDLWHIIKFHraskanKKPMQlpRSMVKSLLYQILDGIHYLHA 84
Cdd:cd06635    74 KEVKFLQRIKHPNSIEYKGCYLR--EHTAWLVMEYCLGSASDLLEVH------KKPLQ--EIEIAAITHGALQGLAYLHS 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMgegpERGRVKIADMGFARLFnSPlkpladLDPVVVTFWYRAPELLLGAR--HYTKAIDIWAIGC 162
Cdd:cd06635   144 HNMIHRDIKAGNILLT----EPGQVKLADFGSASIA-SP------ANSFVGTPYWMAPEVILAMDegQYDGKVDVWSLGI 212
                         170
                  ....*....|
gi 1370507705 163 IFAELLTSEP 172
Cdd:cd06635   213 TCIELAERKP 222
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
6-171 1.31e-14

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: 73.41  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIAlqkvFLSH--SDRKVWLLFdyaehdlwhI--------IKFHRaskanKKPMQLPRSMVKSLLYQI 75
Cdd:cd13983    50 EIEILKSLKHPNIIK----FYDSweSKSKKEVIF---------ItelmtsgtLKQYL-----KRFKRLKLKVIKSWCRQI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  76 LDGIHYLHANW--VLHRDLKPANILVMGegpERGRVKIADMGFARLFNSPLKpladlDPVVVTFWYRAPELLLGarHYTK 153
Cdd:cd13983   112 LEGLNYLHTRDppIIHRDLKCDNIFING---NTGEVKIGDLGLATLLRQSFA-----KSVIGTPEFMAPEMYEE--HYDE 181
                         170
                  ....*....|....*...
gi 1370507705 154 AIDIWAIGCIFAELLTSE 171
Cdd:cd13983   182 KVDIYAFGMCLLEMATGE 199
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
2-210 1.38e-14

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: 73.52  E-value: 1.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFLSHSDRKVWL-------LFD-------YAEHDLWHIIKfhraskankkpmqlprsm 67
Cdd:cd14088    45 AAKNEINILKMVKHPNILQLVDVFETRKEYFIFLelatgreVFDwildqgyYSERDTSNVIR------------------ 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  68 vksllyQILDGIHYLHANWVLHRDLKPANILVMGEgPERGRVKIADMGFARLFNSPLKpladlDPVVvTFWYRAPELLlG 147
Cdd:cd14088   107 ------QVLEAVAYLHSLKIVHRNLKLENLVYYNR-LKNSKIVISDFHLAKLENGLIK-----EPCG-TPEYLAPEVV-G 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370507705 148 ARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNpfHHDQLDRIFSVMGFPADKD-WEDI 210
Cdd:cd14088   173 RQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYEN--HDKNLFRKILAGDYEFDSPyWDDI 234
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
1-168 1.46e-14

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: 73.70  E-value: 1.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHII-------KFHRASKANKKPMQLprSMVKSLLY 73
Cdd:cd14049    50 MKVLREVKVLAGLQHPNIVGYHTAWMEHVQLMLYIQMQLCELSLWDWIvernkrpCEEEFKSAPYTPVDV--DVTTKILQ 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEGPErgrVKIADMGFA-RLFNSPLKPLADLDPV--------VVTFWYRAPEL 144
Cdd:cd14049   128 QLLEGVTYIHSMGIVHRDLKPRNIFLHGSDIH---VRIGDFGLAcPDILQDGNDSTTMSRLnglthtsgVGTCLYAAPEQ 204
                         170       180
                  ....*....|....*....|....
gi 1370507705 145 LLGArHYTKAIDIWAIGCIFAELL 168
Cdd:cd14049   205 LEGS-HYDFKSDMYSIGVILLELF 227
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
5-203 1.55e-14

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: 73.36  E-value: 1.55e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHiikfhrasKANKKPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd14117    55 REIEIQSHLRHPNILRLYNYF--HDRKRIYLILEYAPRGELY--------KELQKHGRFDEQRTATFMEELADALHYCHE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILvMGegpERGRVKIADMGFarlfnSPLKPLADLDPVVVTFWYRAPELLLGARHYTKaIDIWAIGCIF 164
Cdd:cd14117   125 KKVIHRDIKPENLL-MG---YKGELKIADFGW-----SVHAPSLRRRTMCGTLDYLPPEMIEGRTHDEK-VDLWCIGVLC 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370507705 165 AELLTSEPIFhcrqediktSNPFHHDQLDRIFSV-MGFPA 203
Cdd:cd14117   195 YELLVGMPPF---------ESASHTETYRRIVKVdLKFPP 225
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
6-175 1.57e-14

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 75.93  E-value: 1.57e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705    6 EIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEH-DLWHIIKfhrasKANKKPMQLPRSMVKSLLYQILDGIHYLH- 83
Cdd:PTZ00266    62 EVNVMRELKHKNIVRYIDRFLNKANQKLYILMEFCDAgDLSRNIQ-----KCYKMFGKIEEHAIVDITRQLLHALAYCHn 136
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   84 ------ANWVLHRDLKPANILVMGEGPERGRV-------------KIADMGFARlfNSPLKPLAdlDPVVVTFWYRAPEL 144
Cdd:PTZ00266   137 lkdgpnGERVLHRDLKPQNIFLSTGIRHIGKItaqannlngrpiaKIGDFGLSK--NIGIESMA--HSCVGTPYYWSPEL 212
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1370507705  145 LLG-ARHYTKAIDIWAIGCIFAELLTSEPIFH 175
Cdd:PTZ00266   213 LLHeTKSYDDKSDMWALGCIIYELCSGKTPFH 244
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
4-263 1.59e-14

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: 73.77  E-value: 1.59e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAE-HDLwhiikFHRASKANKkpmqLPRSMVKSLLYQILDGIHYL 82
Cdd:cd05580    49 LNEKRILSEVRHPFIVNLLGSF--QDDRNLYMVMEYVPgGEL-----FSLLRRSGR----FPNDVAKFYAAEVVLALEYL 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMGEgperGRVKIADMGFArlfnsplKPLADLDPVVV-TFWYRAPELLLGaRHYTKAIDIWAIG 161
Cdd:cd05580   118 HSLDIVYRDLKPENLLLDSD----GHIKITDFGFA-------KRVKDRTYTLCgTPEYLAPEIILS-KGHGKAVDWWALG 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPifhcrqediktsnPFHHDQLDRIFsvmgfpaDKDWEDIRKMPEYptlqkdfrrttyansslikymekhk 241
Cdd:cd05580   186 ILIYEMLAGYP-------------PFFDENPMKIY-------EKILEGKIRFPSF------------------------- 220
                         250       260
                  ....*....|....*....|..
gi 1370507705 242 VKPDSKvfLLLQKLLTMDPTKR 263
Cdd:cd05580   221 FDPDAK--DLIKRLLVVDLTKR 240
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
66-182 1.78e-14

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: 73.33  E-value: 1.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  66 SMVKSLLY--QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldpvVVTFWYRAPE 143
Cdd:cd05577    93 SEARAIFYaaEIICGLEHLHNRFIVYRDLKPENILL----DDHGHVRISDLGLAVEFKGGKKIKGR----VGTHGYMAPE 164
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370507705 144 LLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIK 182
Cdd:cd05577   165 VLQKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVD 203
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
5-161 1.78e-14

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: 73.44  E-value: 1.78e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVflshsdrkvwlLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLY--QILDGIHYL 82
Cdd:cd14200    72 QEIAILKKLDHVNIVKLIEV-----------LDDPAEDNLYMVFDLLRKGPVMEVPSDKPFSEDQARLYfrDIVLGIEYL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplkPLADLDPVVVTFWYRAPELLL--GARHYTKAIDIWAI 160
Cdd:cd14200   141 HYQKIVHRDIKPSNLLL----GDDGHVKIADFGVSNQFEG---NDALLSSTAGTPAFMAPETLSdsGQSFSGKALDVWAM 213

                  .
gi 1370507705 161 G 161
Cdd:cd14200   214 G 214
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
9-276 1.80e-14

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: 73.51  E-value: 1.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   9 LLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHII---KFHRASKANkkpmqlprsmvkSLLYQILDGIHYLHA 84
Cdd:cd14177    51 LMRYGQHPNIITLKDVY--DDGRYVYLVTELMKGgELLDRIlrqKFFSEREAS------------AVLYTITKTVDYLHC 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLadLDPvVVTFWYRAPELLLgARHYTKAIDIWAIGCIF 164
Cdd:cd14177   117 QGVVHRDLKPSNILYMDDSANADSIRICDFGFAKQLRGENGLL--LTP-CYTANFVAPEVLM-RQGYDAACDIWSLGVLL 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 165 AELLTSEPIFhcrqedIKTSNPFHHDQLDRI----FSVMGfpadKDWEDIRKMpeyptlQKDfrrttyansslikymekh 240
Cdd:cd14177   193 YTMLAGYTPF------ANGPNDTPEEILLRIgsgkFSLSG----GNWDTVSDA------AKD------------------ 238
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1370507705 241 kvkpdskvflLLQKLLTMDPTKRITSEQAL---------QDPYFQ 276
Cdd:cd14177   239 ----------LLSHMLHVDPHQRYTAEQVLkhswiacrdQLPHYQ 273
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
6-275 1.89e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 74.14  E-value: 1.89e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEHDLWhiikfhraSKANKKPMQLPRSMVKSLLYQILDGIHYLHAN 85
Cdd:PHA03209  107 EAMLLQNVNHPSVIRMKDTLVSGA--ITCMVLPHYSSDLY--------TYLTKRSRPLPIDQALIIEKQILEGLRYLHAQ 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVMGEgperGRVKIADMGFARLfnsPLKPLADLDpVVVTFWYRAPELLLGARHYTKAiDIWAIGCIFA 165
Cdd:PHA03209  177 RIIHRDVKTENIFINDV----DQVCIGDLGAAQF---PVVAPAFLG-LAGTVETNAPEVLARDKYNSKA-DIWSAGIVLF 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 166 ELLT-SEPIFHCRQEDIKTSNPFHHDQLDRIFSVMG-----FPADKDWEDIRKMPEYPTLQKDfRRTTYANsslikyMEK 239
Cdd:PHA03209  248 EMLAyPSTIFEDPPSTPEEYVKSCHSHLLKIISTLKvhpeeFPRDPGSRLVRGFIEYASLERQ-PYTRYPC------FQR 320
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1370507705 240 HKVKPDSKvfLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:PHA03209  321 VNLPIDGE--FLVHKMLTFDAAMRPSAEEILNYPMF 354
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
5-161 2.23e-14

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: 72.53  E-value: 2.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKFHRASkankkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:pfam07714  50 EEASIMKKLDHPNIVKLLGVCTQ--GEPLYIVTEYMPGgDLLDFLRKHKRK--------LTLKDLLSMALQIAKGMEYLE 119
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYrAPELLLgARHYTKAIDIWAIG 161
Cdd:pfam07714 120 SKNFVHRDLAARNCLV----SENLVVKISDFGLSRDIYDDDYYRKRGGGKLPIKWM-APESLK-DGKFTSKSDVWSFG 191
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
6-277 2.38e-14

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: 72.85  E-value: 2.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlshsdrkvwllfdYAEHDLWHIIKFHRASKANKKPMQLPRSM----VKSLLYQILDGIHY 81
Cdd:cd06611    52 EIDILSECKHPNIVGLYEAY-------------FYENKLWILIEFCDGGALDSIMLELERGLtepqIRYVCRQMLEALNF 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKplaDLDPVVVTFWYRAPELLL----GARHYTKAIDI 157
Cdd:cd06611   119 LHSHKVIHRDLKAGNILLTLD----GDVKLADFGVSAKNKSTLQ---KRDTFIGTPYWMAPEVVAcetfKDNPYDYKADI 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 158 WAIGCIFAELLTSEPifhcrqediktsnPfHHDqldriFSVMGFpadkdwedIRKMP--EYPTLQKDFRRTTYANSSLIK 235
Cdd:cd06611   192 WSLGITLIELAQMEP-------------P-HHE-----LNPMRV--------LLKILksEPPTLDQPSKWSSSFNDFLKS 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 236 YMEKhkvkpdskvflllqklltmDPTKRITSEQALQDPYFQE 277
Cdd:cd06611   245 CLVK-------------------DPDDRPTAAELLKHPFVSD 267
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
2-169 2.58e-14

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: 72.47  E-value: 2.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFLSHsDRKVWLLFDYAEH-DLWHIIKfhraskaNKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd08223    45 AAEQEAKLLSKLKHPNIVSYKESFEGE-DGFLYIVMGFCEGgDLYTRLK-------EQKGVLLEERQVVEWFVQIAMALQ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPlkplADLDPVVV-TFWYRAPElLLGARHYTKAIDIWA 159
Cdd:cd08223   117 YMHERNILHRDLKTQNIFLT----KSNIIKVGDLGIARVLESS----SDMATTLIgTPYYMSPE-LFSNKPYNHKSDVWA 187
                         170
                  ....*....|
gi 1370507705 160 IGCIFAELLT 169
Cdd:cd08223   188 LGCCVYEMAT 197
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
74-172 2.64e-14

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: 72.85  E-value: 2.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFAR---LFNSPLKPLADLDPVVVTFWYRAPELLLGARH 150
Cdd:cd06631   111 QILEGVAYLHNNNVIHRDIKGNNIMLM----PNGVIKLIDFGCAKrlcINLSSGSQSQLLKSMRGTPYWMAPEVINETGH 186
                          90       100
                  ....*....|....*....|..
gi 1370507705 151 YTKAiDIWAIGCIFAELLTSEP 172
Cdd:cd06631   187 GRKS-DIWSIGCTVFEMATGKP 207
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
5-174 3.20e-14

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: 72.38  E-value: 3.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsdrkvwllfdyaEHDLWHIIKFHRASKANK--KPMQLPRSMVKSLLYQILDGIHYL 82
Cdd:cd14145    54 QEAKLFAMLKHPNIIALRGVCLK-------------EPNLCLVMEFARGGPLNRvlSGKRIPPDILVNWAVQIARGMNYL 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANW---VLHRDLKPANILVMgEGPERGRV-----KIADMGFARLFNSPLKPLAdldpvVVTFWYRAPELLLgARHYTKA 154
Cdd:cd14145   121 HCEAivpVIHRDLKSSNILIL-EKVENGDLsnkilKITDFGLAREWHRTTKMSA-----AGTYAWMAPEVIR-SSMFSKG 193
                         170       180
                  ....*....|....*....|
gi 1370507705 155 IDIWAIGCIFAELLTSEPIF 174
Cdd:cd14145   194 SDVWSYGVLLWELLTGEVPF 213
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
5-174 3.49e-14

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: 72.30  E-value: 3.49e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAE-----HDLWHIIKFHRASKAnkkpmqlprsmvkSLLYQILDGI 79
Cdd:cd14116    54 REVEIQSHLRHPNILRLYGYF--HDATRVYLILEYAPlgtvyRELQKLSKFDEQRTA-------------TYITELANAL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFArlFNSPLKPLADLdpvVVTFWYRAPELLLGARHYTKaIDIWA 159
Cdd:cd14116   119 SYCHSKRVIHRDIKPENLLL----GSAGELKIADFGWS--VHAPSSRRTTL---CGTLDYLPPEMIEGRMHDEK-VDLWS 188
                         170
                  ....*....|....*
gi 1370507705 160 IGCIFAELLTSEPIF 174
Cdd:cd14116   189 LGVLCYEFLVGKPPF 203
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
5-275 3.71e-14

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: 71.90  E-value: 3.71e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDY-AEHDL-WHIIKFHRASKAnkkpmqlprsMVKSLLYQILDGIHYL 82
Cdd:cd05578    49 NELEILQELEHPFLVNLWYSF--QDEEDMYMVVDLlLGGDLrYHLQQKVKFSEE----------TVKFYICEIVLALDYL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFARLfnspLKPLADLDPVVVTFWYRAPELLLGArHYTKAIDIWAIGC 162
Cdd:cd05578   117 HSKNIIHRDIKPDNILL----DEQGHVHITDFNIATK----LTDGTLATSTSGTKPYMAPEVFMRA-GYSFAVDWWSLGV 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLTSEPIFHcrqedIKTSNPfhHDQLDRIFSvmgfpadkdwediRKMPEYPTLQkdfrrttyaNSSLIKymekhkv 242
Cdd:cd05578   188 TAYEMLRGKRPYE-----IHSRTS--IEEIRAKFE-------------TASVLYPAGW---------SEEAID------- 231
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370507705 243 kpdskvflLLQKLLTMDPTKRITSEQALQD-PYF 275
Cdd:cd05578   232 --------LINKLLERDPQKRLGDLSDLKNhPYF 257
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
5-175 4.16e-14

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: 72.37  E-value: 4.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAeHDLWHIIKFHRaskanKKPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd08229    73 KEIDLLKQLNHPNVIKYYASFIEDNELNIVLELADA-GDLSRMIKHFK-----KQKRLIPEKTVWKYFVQLCSALEHMHS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEGPergrVKIADMGFARLFNSPLKPLADLdpvVVTFWYRAPElLLGARHYTKAIDIWAIGCIF 164
Cdd:cd08229   147 RRVMHRDIKPANVFITATGV----VKLGDLGLGRFFSSKTTAAHSL---VGTPYYMSPE-RIHENGYNFKSDIWSLGCLL 218
                         170
                  ....*....|.
gi 1370507705 165 AELLTSEPIFH 175
Cdd:cd08229   219 YEMAALQSPFY 229
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
5-172 4.31e-14

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: 72.75  E-value: 4.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEHDLWHIIKFHraskanKKPMQlpRSMVKSLLYQILDGIHYLHA 84
Cdd:cd06634    64 KEVKFLQKLRHPNTIEYRGCYLR--EHTAWLVMEYCLGSASDLLEVH------KKPLQ--EVEIAAITHGALQGLAYLHS 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMgegpERGRVKIADMGFARLfnsplkpLADLDPVVVTFWYRAPELLLGAR--HYTKAIDIWAIGC 162
Cdd:cd06634   134 HNMIHRDVKAGNILLT----EPGLVKLGDFGSASI-------MAPANSFVGTPYWMAPEVILAMDegQYDGKVDVWSLGI 202
                         170
                  ....*....|
gi 1370507705 163 IFAELLTSEP 172
Cdd:cd06634   203 TCIELAERKP 212
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
5-189 4.47e-14

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: 71.91  E-value: 4.47e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKFHRAskankkpMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd08225    48 KEVILLAKMKHPNIVTFFASF--QENGRLFIVMEYCDGgDLMKRINRQRG-------VLFSEDQILSWFVQISLGLKHIH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRV-KIADMGFARLFNSPLKpLAdlDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGC 162
Cdd:cd08225   119 DRKILHRDIKSQNIFL----SKNGMVaKLGDFGIARQLNDSME-LA--YTCVGTPYYLSPEICQN-RPYNNKTDIWSLGC 190
                         170       180
                  ....*....|....*....|....*..
gi 1370507705 163 IFAELLTSEPIFHcrqediktSNPFHH 189
Cdd:cd08225   191 VLYELCTLKHPFE--------GNNLHQ 209
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
1-174 9.00e-14

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


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 71.21  E-value: 9.00e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLREL-KHPNVIA-LQKVFLSHSDRK-VWLLFDYAEHDLWHIIKfhraskaNKKPMQLPRSMVKSLLYQILD 77
Cdd:cd13985    42 RVAIKEIEIMKRLcGHPNIVQyYDSAILSSEGRKeVLLLMEYCPGSLVDILE-------KSPPSPLSEEEVLRIFYQICQ 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANW--VLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLDPVV------VTFWYRAPELL---L 146
Cdd:cd13985   115 AVGHLHSQSppIIHRDIKIENILF----SNTGRFKLCDFGSATTEHYPLERAEEVNIIEeeiqknTTPMYRAPEMIdlyS 190
                         170       180
                  ....*....|....*....|....*...
gi 1370507705 147 GARHYTKAiDIWAIGCIFAELLTSEPIF 174
Cdd:cd13985   191 KKPIGEKA-DIWALGCLLYKLCFFKLPF 217
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
35-204 9.05e-14

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: 72.43  E-value: 9.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  35 LLFDYAEHDLWHIIKFHRASKankkpmqLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERGRVKIADM 114
Cdd:cd14228    93 LVFEMLEQNLYDFLKQNKFSP-------LPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPVRQPYRVKVIDF 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 115 GFARLFNSplkplADLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLDR 194
Cdd:cd14228   166 GSASHVSK-----AVCSTYLQSRYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGASE---------YDQIRY 230
                         170
                  ....*....|
gi 1370507705 195 IFSVMGFPAD 204
Cdd:cd14228   231 ISQTQGLPAE 240
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
70-274 9.26e-14

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: 71.17  E-value: 9.26e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  70 SLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPErGRVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPElLLGAR 149
Cdd:cd14089   104 EIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGPN-AILKLTDFGFAKETTTKKS----LQTPCYTPYYVAPE-VLGPE 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 150 HYTKAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFSVM---------GFPaDKDWEDIRKMpeyptlQ 220
Cdd:cd14089   178 KYDKSCDMWSLGVIMYILLCGYP-------------PFYSNHGLAISPGMkkrirngqyEFP-NPEWSNVSEE------A 237
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370507705 221 KDfrrttyanssLIKymekhkvkpdskvflllqKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14089   238 KD----------LIR------------------GLLKTDPSERLTIEEVMNHPW 263
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
2-169 1.07e-13

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: 70.70  E-value: 1.07e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIKfhraskanKKPMQLpRSMVKSLLYQILDGIHY 81
Cdd:cd14108    44 SARRELALLAELDHKSIVRFHDAF--EKRRVVIIVTELCHEELLERIT--------KRPTVC-ESEVRSYMRQLLEGIEY 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEGPErgRVKIADMGFARlfnsPLKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIG 161
Cdd:cd14108   113 LHQNDVLHLDLKPENLLMADQKTD--QVRICDFGNAQ----ELTPNEPQYCKYGTPEFVAPE-IVNQSPVSKVTDIWPVG 185

                  ....*...
gi 1370507705 162 CIFAELLT 169
Cdd:cd14108   186 VIAYLCLT 193
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
6-275 1.37e-13

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 70.55  E-value: 1.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEHDLWHIIKFHraskankkpMQLPRSMVKSLLYQILDGIHYLHAN 85
Cdd:cd06648    54 EVVIMRDYQHPNIVEMYSSYLV--GDELWVVMEFLEGGALTDIVTH---------TRMNEEQIATVCRAVLKALSFLHSQ 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPLADLdpvVVTFWYRAPELLlgARH-YTKAIDIWAIGCIF 164
Cdd:cd06648   123 GVIHRDIKSDSILLTSD----GRVKLSDFGFCAQVSKEVPRRKSL---VGTPYWMAPEVI--SRLpYGTEVDIWSLGIMV 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 165 AELLTSEPifhcrqediktsnPFhhdqldriFSVMGFPADKdweDIRKMPEyPTLQkdfrrttyansslikymEKHKVKP 244
Cdd:cd06648   194 IEMVDGEP-------------PY--------FNEPPLQAMK---RIRDNEP-PKLK-----------------NLHKVSP 231
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370507705 245 DSKVFllLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd06648   232 RLRSF--LDRMLVRDPAQRATAAELLNHPFL 260
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
5-171 1.50e-13

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: 70.44  E-value: 1.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAEHDlwhiiKFHRASKANKKPmqlPRSMVKSLLyQILDGIHYLHA 84
Cdd:cd14147    51 QEARLFAMLAHPNIIALKAVCLEEPN--LCLVMEYAAGG-----PLSRALAGRRVP---PHVLVNWAV-QIARGMHYLHC 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NW---VLHRDLKPANILVM----GEGPERGRVKIADMGFARLFNSPLKPLAdldpvVVTFWYRAPElLLGARHYTKAIDI 157
Cdd:cd14147   120 EAlvpVIHRDLKSNNILLLqpieNDDMEHKTLKITDFGLAREWHKTTQMSA-----AGTYAWMAPE-VIKASTFSKGSDV 193
                         170
                  ....*....|....
gi 1370507705 158 WAIGCIFAELLTSE 171
Cdd:cd14147   194 WSFGVLLWELLTGE 207
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
6-180 1.74e-13

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: 70.41  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAEH-DLWHIIkfhraSKANKKPMQLPRSMvkslLYQILDGIHYLHA 84
Cdd:cd14183    54 EVSILRRVKHPNIVLLIEEMDMPTE--LYLVMELVKGgDLFDAI-----TSTNKYTERDASGM----LYNLASAIKYLHS 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKpladldPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIF 164
Cdd:cd14183   123 LNIVHRDIKPENLLVYEHQDGSKSLKLGDFGLATVVDGPLY------TVCGTPTYVAPE-IIAETGYGLKVDIWAAGVIT 195
                         170
                  ....*....|....*.
gi 1370507705 165 AELLTSEPIFHCRQED 180
Cdd:cd14183   196 YILLCGFPPFRGSGDD 211
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
50-275 2.42e-13

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: 70.81  E-value: 2.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  50 FHRASKANKKPMQLPRsmVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPE---------------RGRVKIADM 114
Cdd:cd14214   103 FEFLKENNFQPYPLPH--IRHMAYQLCHALKFLHENQLTHTDLKPENILFVNSEFDtlynesksceeksvkNTSIRVADF 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 115 GFARlFNSPLKpladlDPVVVTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIFHCRQediktsNPFHHDQLDR 194
Cdd:cd14214   181 GSAT-FDHEHH-----TTIVATRHYRPPEVIL-ELGWAQPCDVWSLGCILFEYYRGFTLFQTHE------NREHLVMMEK 247
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 195 IFSVMGfpadkdwediRKMPEYPTLQKDFRRTTYA---NSSLIKYMEKHkVKP-------DS----KVFLLLQKLLTMDP 260
Cdd:cd14214   248 ILGPIP----------SHMIHRTRKQKYFYKGSLVwdeNSSDGRYVSEN-CKPlmsymlgDSlehtQLFDLLRRMLEFDP 316
                         250
                  ....*....|....*
gi 1370507705 261 TKRITSEQALQDPYF 275
Cdd:cd14214   317 ALRITLKEALLHPFF 331
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
6-171 2.51e-13

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: 69.45  E-value: 2.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlshSDRKVW-LLFDYAEH-DLWHIIKFHRaskankkpmQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14059    31 DIKHLRKLNHPNIIKFKGVC---TQAPCYcILMEYCPYgQLYEVLRAGR---------EITPSLLVDWSKQIASGMNYLH 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEGPergrVKIADMGFARLFNSPLKPLAdldpVVVTFWYRAPELLLGARHYTKaIDIWAIGCI 163
Cdd:cd14059    99 LHKIIHRDLKSPNVLVTYNDV----LKISDFGTSKELSEKSTKMS----FAGTVAWMAPEVIRNEPCSEK-VDIWSFGVV 169

                  ....*...
gi 1370507705 164 FAELLTSE 171
Cdd:cd14059   170 LWELLTGE 177
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
3-164 3.02e-13

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: 69.63  E-value: 3.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIAL---QKVFLSHSDRKVWLLFDYAEH-DLWHIIkfhRASKANKKPMQLPRsmVKSLLYQILDG 78
Cdd:cd13986    44 AMREIENYRLFNHPNILRLldsQIVKEAGGKKEVYLLLPYYKRgSLQDEI---ERRLVKGTFFPEDR--ILHIFLGICRG 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANW---VLHRDLKPANILVmgegPERGRVKIADMGF---ARLF---NSPLKPLADLDPVVVTFWYRAPELL---L 146
Cdd:cd13986   119 LKAMHEPElvpYAHRDIKPGNVLL----SEDDEPILMDLGSmnpARIEiegRREALALQDWAAEHCTMPYRAPELFdvkS 194
                         170
                  ....*....|....*...
gi 1370507705 147 GARHYTKAiDIWAIGCIF 164
Cdd:cd13986   195 HCTIDEKT-DIWSLGCTL 211
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
5-274 3.25e-13

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: 69.44  E-value: 3.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKFHRaskankkpmQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14076    55 REINILKGLTHPNIVRLLDVL--KTKKYIGIVLEFVSGgELFDYILARR---------RLKDSVACRLFAQLISGVAYLH 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegpERGR-VKIADMGFARLF---NSPLKPLADLDPVvvtfwYRAPELLLGARHYT-KAIDIW 158
Cdd:cd14076   124 KKGVVHRDLKLENLLL-----DKNRnLVITDFGFANTFdhfNGDLMSTSCGSPC-----YAAPELVVSDSMYAgRKADIW 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 159 AIGCIFAELLTSEpifhcrqediktsnpfhhdqldrifsvmgFPADKDwedirkmPEYPTLQKDFRRTTYANSSLIKYME 238
Cdd:cd14076   194 SCGVILYAMLAGY-----------------------------LPFDDD-------PHNPNGDNVPRLYRYICNTPLIFPE 237
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1370507705 239 KHKVKPDSkvflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14076   238 YVTPKARD----LLRRILVPNPRKRIRLSAIMRHAW 269
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
5-169 3.30e-13

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: 69.66  E-value: 3.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEH-DLWHIIKFHRASKANKKPMQLPRsmvksllyQILDGIHYLH 83
Cdd:cd14205    54 REIEILKSLQHDNIVKYKGVCYSAGRRNLRLIMEYLPYgSLRDYLQKHKERIDHIKLLQYTS--------QICKGMEYLG 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPLADLDP-VVVTFWYrAPELLLGARhYTKAIDIWAIGC 162
Cdd:cd14205   126 TKRYIHRDLATRNILVENE----NRVKIGDFGLTKVLPQDKEYYKVKEPgESPIFWY-APESLTESK-FSVASDVWSFGV 199

                  ....*..
gi 1370507705 163 IFAELLT 169
Cdd:cd14205   200 VLYELFT 206
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
74-184 3.67e-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: 69.69  E-value: 3.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFArlfnsplKPLADLDPV---VVTFWYRAPELLLGARh 150
Cdd:cd05605   110 EITCGLEHLHSERIVYRDLKPENILL----DDHGHVRISDLGLA-------VEIPEGETIrgrVGTVGYMAPEVVKNER- 177
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1370507705 151 YTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTS 184
Cdd:cd05605   178 YTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKRE 211
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
3-275 3.69e-13

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: 70.09  E-value: 3.69e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLSHSDRKVWLLfDYAE-HDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHY 81
Cdd:cd14041    57 ACREYRIHKELDHPRIVKLYDYFSLDTDSFCTVL-EYCEgNDLDFYLKQHKL---------MSEKEARSIIMQIVNALKY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHA--NWVLHRDLKPANILVMgEGPERGRVKIADMGFARLFNSPLKPLADLDPVVV----TFWYRAPELLLGARHYTK-- 153
Cdd:cd14041   127 LNEikPPIIHYDLKPGNILLV-NGTACGEIKITDFGLSKIMDDDSYNSVDGMELTSqgagTYWYLPPECFVVGKEPPKis 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 154 -AIDIWAIGCIFAELLTSEpifhcrqediktsNPFHHDQldrifsvmgfpadkdwedirkmpeypTLQKDFRRTTYANSS 232
Cdd:cd14041   206 nKVDVWSVGVIFYQCLYGR-------------KPFGHNQ--------------------------SQQDILQENTILKAT 246
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1370507705 233 LIKYMEKHKVKPDSKVFllLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14041   247 EVQFPPKPVVTPEAKAF--IRRCLAYRKEDRIDVQQLACDPYL 287
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
3-174 3.96e-13

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 69.15  E-value: 3.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFlshSDRKVWLL---FDYAEHDLWHIIKFHRASKANkkpmqlprsmVKSLLYQILDGI 79
Cdd:cd14107    45 AFQERDILARLSHRRLTCLLDQF---ETRKTLILileLCSSEELLDRLFLKGVVTEAE----------VKLYIQQVLEGI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILVMgeGPERGRVKIADMGFARlfnsplkplaDLDPVVVTF-WYRAPEL----LLGARHYTKA 154
Cdd:cd14107   112 GYLHGMNILHLDIKPDNILMV--SPTREDIKICDFGFAQ----------EITPSEHQFsKYGSPEFvapeIVHQEPVSAA 179
                         170       180
                  ....*....|....*....|.
gi 1370507705 155 IDIWAIGCI-FAELLTSEPIF 174
Cdd:cd14107   180 TDIWALGVIaYLSLTCHSPFA 200
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
3-185 4.31e-13

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: 69.70  E-value: 4.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLSHSDRKVWLLfDYAE-HDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHY 81
Cdd:cd14040    57 ACREYRIHKELDHPRIVKLYDYFSLDTDTFCTVL-EYCEgNDLDFYLKQHKL---------MSEKEARSIVMQIVNALRY 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LH--ANWVLHRDLKPANILVMgEGPERGRVKIADMGFARLFNSPLKPLADLDPV---VVTFWYRAPELLLGARHYTK--- 153
Cdd:cd14040   127 LNeiKPPIIHYDLKPGNILLV-DGTACGEIKITDFGLSKIMDDDSYGVDGMDLTsqgAGTYWYLPPECFVVGKEPPKisn 205
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370507705 154 AIDIWAIGCIFAELLTS-EPIFHCR-QEDIKTSN 185
Cdd:cd14040   206 KVDVWSVGVIFFQCLYGrKPFGHNQsQQDILQEN 239
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
5-169 4.94e-13

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: 69.19  E-value: 4.94e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYaehdlwhiikFHRASKANKKPMQLPRSMVKSLL---YQILDGIHY 81
Cdd:cd05079    55 KEIEILRNLYHENIVKYKGICTEDGGNGIKLIMEF----------LPSGSLKEYLPRNKNKINLKQQLkyaVQICKGMDY 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPLA---DLDPVVvtFWYrAPELLLGARHYtKAIDIW 158
Cdd:cd05079   125 LGSRQYVHRDLAARNVLVESE----HQVKIGDFGLTKAIETDKEYYTvkdDLDSPV--FWY-APECLIQSKFY-IASDVW 196
                         170
                  ....*....|.
gi 1370507705 159 AIGCIFAELLT 169
Cdd:cd05079   197 SFGVTLYELLT 207
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
63-273 5.03e-13

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: 68.56  E-value: 5.03e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  63 LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFA-RLFNSPlkPLADLDPVvvtfwYRA 141
Cdd:cd13997   100 LSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFI----SNKGTCKIGDFGLAtRLETSG--DVEEGDSR-----YLA 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 142 PELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhhdqldrifsvmgfpadkdWEDIR--KMPEYPT- 218
Cdd:cd13997   169 PELLNENYTHLPKADIFSLGVTVYEAATGEPLPRNGQQ---------------------------WQQLRqgKLPLPPGl 221
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507705 219 -LQKDFRRttyanssLIKYMekhkvkpdskvflllqklLTMDPTKRITSEQALQDP 273
Cdd:cd13997   222 vLSQELTR-------LLKVM------------------LDPDPTRRPTADQLLAHD 252
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
5-174 7.78e-13

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: 68.11  E-value: 7.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDY-AEHDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14188    50 KEIELHRILHHKHVVQFYHYF--EDKENIYILLEYcSRRSMAHILKARKV---------LTEPEVRYYLRQIVSGLKYLH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFArlfnSPLKPLADLDPVVV-TFWYRAPELLLGARHYTKAiDIWAIGC 162
Cdd:cd14188   119 EQEILHRDLKLGNFFI----NENMELKVGDFGLA----ARLEPLEHRRRTICgTPNYLSPEVLNKQGHGCES-DIWALGC 189
                         170
                  ....*....|..
gi 1370507705 163 IFAELLTSEPIF 174
Cdd:cd14188   190 VMYTMLLGRPPF 201
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
61-275 8.04e-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: 69.28  E-value: 8.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  61 MQLPRSMVKSLLYQILDGIHYLHANW-VLHRDLKPANILV-MGEG------------------PERGrvKIADMGFARLF 120
Cdd:cd14218   114 QGLPLPCVKSILRQVLQGLDYLHTKCkIIHTDIKPENILMcVDEGyvrrlaaeatiwqqagapPPSG--SSVSFGASDFL 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 121 NSPLKP---------LADLDPV----------VVTFWYRAPELLLGARHYTKAiDIWAIGCIFAELLTSEPIFHCRQEDI 181
Cdd:cd14218   192 VNPLEPqnadkirvkIADLGNAcwvhkhftedIQTRQYRALEVLIGAEYGTPA-DIWSTACMAFELATGDYLFEPHSGED 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 182 KTSNpfhHDQLDRIFSVMGfpadkdwedirKMPEYPTLQKDFRRTTYANSSLIKYMekHKVKPDSKVFLLLQK------- 254
Cdd:cd14218   271 YTRD---EDHIAHIVELLG-----------DIPPHFALSGRYSREYFNRRGELRHI--KNLKHWGLYEVLVEKyewpleq 334
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370507705 255 -------LLTMD---PTKRITSEQALQDPYF 275
Cdd:cd14218   335 aaqftdfLLPMMeflPEKRATAAQCLQHPWL 365
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
74-301 8.40e-13

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: 68.82  E-value: 8.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFAR--LFNsplkpladlDPVVVTFW----YRAPELLLG 147
Cdd:cd05620   104 EIVCGLQFLHSKGIIYRDLKLDNVMLDRD----GHIKIADFGMCKenVFG---------DNRASTFCgtpdYIAPEILQG 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 148 ARhYTKAIDIWAIGCIFAELLTSEpifhcrqediktsNPFHHDQLDRIFsvmgfpadkdwEDIR-KMPEYPtlqkdfrrt 226
Cdd:cd05620   171 LK-YTFSVDWWSFGVLLYEMLIGQ-------------SPFHGDDEDELF-----------ESIRvDTPHYP--------- 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 227 tyanssliKYMEKhkvkpDSKVflLLQKLLTMDPTKRITSEQALQD-PYFQE-----------DPLPTLDVFAGCQIPYP 294
Cdd:cd05620   217 --------RWITK-----ESKD--ILEKLFERDPTRRLGVVGNIRGhPFFKTinwtalekrelDPPFKPKVKSPSDYSNF 281

                  ....*..
gi 1370507705 295 KREFLNE 301
Cdd:cd05620   282 DREFLSE 288
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
6-172 8.75e-13

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: 68.03  E-value: 8.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDrkVWLLFDY-AEHDLWHIIKfhraskankkPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd06647    54 EILVMRENKNPNIVNYLDSYLVGDE--LWVVMEYlAGGSLTDVVT----------ETCMDEGQIAAVCRECLQALEFLHS 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEgperGRVKIADMGFArlfnsplkplADLDP-------VVVTFWYRAPELLLgARHYTKAIDI 157
Cdd:cd06647   122 NQVIHRDIKSDNILLGMD----GSVKLTDFGFC----------AQITPeqskrstMVGTPYWMAPEVVT-RKAYGPKVDI 186
                         170
                  ....*....|....*
gi 1370507705 158 WAIGCIFAELLTSEP 172
Cdd:cd06647   187 WSLGIMAIEMVEGEP 201
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
5-274 9.63e-13

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: 68.09  E-value: 9.63e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEH-DLwhiikFHRASKANKkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14665    45 REIINHRSLRHPNIVRFKEVILTPT--HLAIVMEYAAGgEL-----FERICNAGR----FSEDEARFFFQQLISGVSYCH 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgEGPERGRVKIADMGFAR--LFNSPLKpladldPVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd14665   114 SMQICHRDLKLENTLL--DGSPAPRLKICDFGYSKssVLHSQPK------STVGTPAYIAPEVLLKKEYDGKIADVWSCG 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLtsepifhcrqediktsnpfhhdqldrifsVMGFPadkdWEDirkmPEYPtlqKDFRRTTYANSSlIKYMEKHK 241
Cdd:cd14665   186 VTLYVML-----------------------------VGAYP----FED----PEEP---RNFRKTIQRILS-VQYSIPDY 224
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370507705 242 VKPDSKVFLLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14665   225 VHISPECRHLISRIFVADPATRITIPEIRNHEW 257
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
5-172 9.74e-13

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: 68.18  E-value: 9.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDY----AEHDLWhiikfhraskankKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd06641    51 QEITVLSQCDSPYVTKYYGSYLK--DTKLWIIMEYlgggSALDLL-------------EPGPLDETQIATILREILKGLD 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFA-RLFNSPLKPladlDPVVVTFWYRAPELLLGARHYTKAiDIWA 159
Cdd:cd06641   116 YLHSEKKIHRDIKAANVLL----SEHGEVKLADFGVAgQLTDTQIKR----N*FVGTPFWMAPEVIKQSAYDSKA-DIWS 186
                         170
                  ....*....|...
gi 1370507705 160 IGCIFAELLTSEP 172
Cdd:cd06641   187 LGITAIELARGEP 199
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
5-277 1.08e-12

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: 68.34  E-value: 1.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAE-HDL-WHIIKfhRASKAnkkpMQLPRSMVKSLLYQILDGIHYL 82
Cdd:cd14094    54 REASICHMLKHPHIVELLETY--SSDGMLYMVFEFMDgADLcFEIVK--RADAG----FVYSEAVASHYMRQILEALRYC 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILvMGEGPERGRVKIADMGFArlfnsplKPLADLDPV----VVTFWYRAPElLLGARHYTKAIDIW 158
Cdd:cd14094   126 HDNNIIHRDVKPHCVL-LASKENSAPVKLGGFGVA-------IQLGESGLVaggrVGTPHFMAPE-VVKREPYGKPVDVW 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 159 AIGCIFAELLTSEPIFHCRQEDI-----KTSNPFHHDQLDRIFSvmgfpADKDwedirkmpeyptlqkdfrrttyanssl 233
Cdd:cd14094   197 GCGVILFILLSGCLPFYGTKERLfegiiKGKYKMNPRQWSHISE-----SAKD--------------------------- 244
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1370507705 234 ikymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYFQE 277
Cdd:cd14094   245 -----------------LVRRMLMLDPAERITVYEALNHPWIKE 271
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
5-173 1.09e-12

TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, in multiple species of Burkholderia, in Acidovorax avenae subsp. citrulli AAC00-1 and Delftia acidovorans SPH-1, and in multiple copies in Sorangium cellulosum, in genomic neighborhoods that include a cyclodehydratase/docking scaffold fusion protein (TIGR03882) and a member of the thiazole/oxazole modified metabolite (TOMM) precursor family TIGR03795. It has a kinase domain in the N-terminal 300 amino acids, followed by a cyclase homology domain, followed by regions without named domain definitions. It is a probable bacteriocin-like metabolite biosynthesis protein. [Cellular processes, Toxin production and resistance]


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 70.26  E-value: 1.09e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705    5 REIALLRELKHPNVIALqkvfLSHSDRKVWLLFDYAEHDLWHIIkfhRASKANKKPmqLPRSMVKSLLYQILDGIHYLHA 84
Cdd:TIGR03903   27 RETALCARLYHPNIVAL----LDSGEAPPGLLFAVFEYVPGRTL---REVLAADGA--LPAGETGRLMLQVLDALACAHN 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   85 NWVLHRDLKPANILVMGEGPERgRVKIADMGFARLfnspLKPLADLD--------PVVVTFWYRAPELLLGaRHYTKAID 156
Cdd:TIGR03903   98 QGIVHRDLKPQNIMVSQTGVRP-HAKVLDFGIGTL----LPGVRDADvatltrttEVLGTPTYCAPEQLRG-EPVTPNSD 171
                          170
                   ....*....|....*..
gi 1370507705  157 IWAIGCIFAELLTSEPI 173
Cdd:TIGR03903  172 LYAWGLIFLECLTGQRV 188
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
5-169 1.26e-12

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: 67.73  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELK-HPNVIALQKVFLSHSDRKVWLLfDYAEH-DLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYL 82
Cdd:cd13987    38 REYNISLELSvHPHIIKTYDVAFETEDYYVFAQ-EYAPYgDLFSIIPPQVG---------LPEERVKRCAAQLASALDFM 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMgeGPERGRVKIADMGFARLFNSPLKPLADLDPvvvtfwYRAPELLLGARH----YTKAIDIW 158
Cdd:cd13987   108 HSKNLVHRDIKPENVLLF--DKDCRRVKLCDFGLTRRVGSTVKRVSGTIP------YTAPEVCEAKKNegfvVDPSIDVW 179
                         170
                  ....*....|.
gi 1370507705 159 AIGCIFAELLT 169
Cdd:cd13987   180 AFGVLLFCCLT 190
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
56-168 1.29e-12

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: 67.52  E-value: 1.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  56 ANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKpladLDPVVV 135
Cdd:cd14047   107 EKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLV----DTGKVKIGDFGLVTSLKNDGK----RTKSKG 178
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1370507705 136 TFWYRAPElLLGARHYTKAIDIWAIGCIFAELL 168
Cdd:cd14047   179 TLSYMSPE-QISSQDYGKEVDIYALGLILFELL 210
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
5-186 1.31e-12

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: 67.79  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEH-DLWHIIKFHRASKANKKpmqlprsmvkSLLY--QILDGIHY 81
Cdd:cd05038    55 REIEILRTLDHEYIVKYKGVCESPGRRSLRLIMEYLPSgSLRDYLQRHRDQIDLKR----------LLLFasQICKGMEY 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSP-----LKPLADLdPVvvtFWYrAPELLLGARHYTKAiD 156
Cdd:cd05038   125 LGSQRYIHRDLAARNILVESE----DLVKISDFGLAKVLPEDkeyyyVKEPGES-PI---FWY-APECLRESRFSSAS-D 194
                         170       180       190
                  ....*....|....*....|....*....|
gi 1370507705 157 IWAIGCIFAELLTsepifHCRqediKTSNP 186
Cdd:cd05038   195 VWSFGVTLYELFT-----YGD----PSQSP 215
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
5-172 1.47e-12

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


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 67.76  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdrKVWLLFDY----AEHDLWHIIKfhraskankkpmQLPRSMVKSLLYQILDGIH 80
Cdd:cd06645    57 QEIIMMKDCKHSNIVAYFGSYLRRD--KLWICMEFcgggSLQDIYHVTG------------PLSESQIAYVSRETLQGLY 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSplkPLADLDPVVVTFWYRAPELLLGARH--YTKAIDIW 158
Cdd:cd06645   123 YLHSKGKMHRDIKGANILLT----DNGHVKLADFGVSAQITA---TIAKRKSFIGTPYWMAPEVAAVERKggYNQLCDIW 195
                         170
                  ....*....|....
gi 1370507705 159 AIGCIFAELLTSEP 172
Cdd:cd06645   196 AVGITAIELAELQP 209
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
2-172 1.47e-12

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: 67.42  E-value: 1.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFLshsdrkvwllfdyAEHDLWHIIKFHRASKANK--KPMQLPRSMVKSLLYQILDGI 79
Cdd:cd14061    39 NVRQEARLFWMLRHPNIIALRGVCL-------------QPPNLCLVMEYARGGALNRvlAGRKIPPHVLVDWAIQIARGM 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANW---VLHRDLKPANILVM----GEGPERGRVKIADMGFAR-LFNSPLKPLADldpvvvTFWYRAPELLLGARhY 151
Cdd:cd14061   106 NYLHNEApvpIIHRDLKSSNILILeaieNEDLENKTLKITDFGLAReWHKTTRMSAAG------TYAWMAPEVIKSST-F 178
                         170       180
                  ....*....|....*....|.
gi 1370507705 152 TKAIDIWAIGCIFAELLTSEP 172
Cdd:cd14061   179 SKASDVWSYGVLLWELLTGEV 199
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
5-172 1.85e-12

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 67.36  E-value: 1.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHsdRKVWLLFDY----AEHDLWHIIKfhraskankkpmQLPRSMVKSLLYQILDGIH 80
Cdd:cd06646    55 QEIFMVKECKHCNIVAYFGSYLSR--EKLWICMEYcgggSLQDIYHVTG------------PLSELQIAYVCRETLQGLA 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSplkPLADLDPVVVTFWYRAPELLLGARH--YTKAIDIW 158
Cdd:cd06646   121 YLHSKGKMHRDIKGANILLT----DNGDVKLADFGVAAKITA---TIAKRKSFIGTPYWMAPEVAAVEKNggYNQLCDIW 193
                         170
                  ....*....|....
gi 1370507705 159 AIGCIFAELLTSEP 172
Cdd:cd06646   194 AVGITAIELAELQP 207
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
5-171 1.91e-12

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: 67.46  E-value: 1.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDrKVWLLFDYAEHDlwhiiKFHRASKANKkpmQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd06620    52 RELQILHECHSPYIVSFYGAFLNENN-NIIICMEYMDCG-----SLDKILKKKG---PFPEEVLGKIAVAVLEGLTYLYN 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NW-VLHRDLKPANILVMGegpeRGRVKIADMGFAR-LFNSplkpLAdlDPVVVTFWYRAPELLLGARhYTKAIDIWAIGC 162
Cdd:cd06620   123 VHrIIHRDIKPSNILVNS----KGQIKLCDFGVSGeLINS----IA--DTFVGTSTYMSPERIQGGK-YSVKSDVWSLGL 191

                  ....*....
gi 1370507705 163 IFAELLTSE 171
Cdd:cd06620   192 SIIELALGE 200
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
6-174 2.27e-12

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: 66.81  E-value: 2.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAehdlwHIIKFHRASKANKKPMQlpRSMVKSLLYQILDGIHYLHAN 85
Cdd:cd14186    51 EVEIHCQLKHPSILELYNYF--EDSNYVYLVLEMC-----HNGEMSRYLKNRKKPFT--EDEARHFMHQIVTGMLYLHSH 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPLADLdpvVVTFWYRAPELLLGARHYTKAiDIWAIGCIFA 165
Cdd:cd14186   122 GILHRDLTLSNLLLTRN----MNIKIADFGLATQLKMPHEKHFTM---CGTPNYISPEIATRSAHGLES-DVWSLGCMFY 193

                  ....*....
gi 1370507705 166 ELLTSEPIF 174
Cdd:cd14186   194 TLLVGRPPF 202
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
75-175 2.33e-12

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: 67.02  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKA 154
Cdd:cd13979   112 IARALRFCHSHGIVHLDVKPANILI----SEQGVCKLCDFGCSVKLGEGNEVGTPRSHIGGTYTYRAPELLKGERVTPKA 187
                          90       100
                  ....*....|....*....|.
gi 1370507705 155 iDIWAIGCIFAELLTSEPIFH 175
Cdd:cd13979   188 -DIYSFGITLWQMLTRELPYA 207
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
5-169 2.63e-12

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: 66.87  E-value: 2.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALqkvfLSHSDRKVWLLFDYA-EHDLWHIIKFHRASKANkkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14000    59 QELTVLSHLHHPSIVYL----LGIGIHPLMLVLELApLGSLDHLLQQDSRSFAS-----LGRTLQQRIALQVADGLRYLH 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMG-EGPERGRVKIADMGFAR-LFNSPLKPLADldpvvvTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd14000   130 SAMIIYRDLKSHNVLVWTlYPNSAIIIKIADYGISRqCCRMGAKGSEG------TPGFRAPEIARGNVIYNEKVDVFSFG 203

                  ....*...
gi 1370507705 162 CIFAELLT 169
Cdd:cd14000   204 MLLYEILS 211
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
2-275 2.78e-12

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: 67.75  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKH--PNVIALQKVFLSHSDRK--------VWLLFDYAEHdlwHIIKFhrASKANKKPMQLPrsMVKSL 71
Cdd:cd14216    52 TALDEIKLLKSVRNsdPNDPNREMVVQLLDDFKisgvngthICMVFEVLGH---HLLKW--IIKSNYQGLPLP--CVKKI 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  72 LYQILDGIHYLHAN-WVLHRDLKPANILVMGE--------------------------GPERGRVKIADMGFA----RLF 120
Cdd:cd14216   125 IRQVLQGLDYLHTKcRIIHTDIKPENILLSVNeqyirrlaaeatewqrnflvnplepkNAEKLKVKIADLGNAcwvhKHF 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 121 NSPLKpladldpvvvTFWYRAPELLLGARHYTKAiDIWAIGCIFAELLTSEPIFHCRQEDIKTSNpfhHDQLDRIFSVMG 200
Cdd:cd14216   205 TEDIQ----------TRQYRSLEVLIGSGYNTPA-DIWSTACMAFELATGDYLFEPHSGEDYSRD---EDHIALIIELLG 270
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370507705 201 FPADKDWEDIRKMPEYPTLQKDFRRTTYANS-SLIK-YMEKHK-VKPDSKVFL-LLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14216   271 KVPRKLIVAGKYSKEFFTKKGDLKHITKLKPwGLFEvLVEKYEwSQEEAAGFTdFLLPMLELIPEKRATAAECLRHPWL 349
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
6-174 2.87e-12

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: 66.94  E-value: 2.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLREL-KHPNVIALQKVFLSHSDR----KVWLLFDYAEH----DLwhiikfhrASKANKKPMQLPRSMVKSLLYQIL 76
Cdd:cd06608    52 EINILRKFsNHPNIATFYGAFIKKDPPggddQLWLVMEYCGGgsvtDL--------VKGLRKKGKRLKEEWIAYILRETL 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  77 DGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSplkPLADLDPVVVTFWYRAPELLLG----ARHYT 152
Cdd:cd06608   124 RGLAYLHENKVIHRDIKGQNILLT----EEAEVKLVDFGVSAQLDS---TLGRRNTFIGTPYWMAPEVIACdqqpDASYD 196
                         170       180
                  ....*....|....*....|..
gi 1370507705 153 KAIDIWAIGCIFAELLTSEPIF 174
Cdd:cd06608   197 ARCDVWSLGITAIELADGKPPL 218
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
6-196 2.87e-12

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: 67.08  E-value: 2.87e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALqkVFLSHSDRKVWLLFDYAEHDlwHIIKFHRASKANKKPMqlprsmvkSLLY--QILDGIHYLH 83
Cdd:cd05612    51 EKRVLKEVSHPFIIRL--FWTEHDQRFLYMLMEYVPGG--ELFSYLRNSGRFSNST--------GLFYasEIVCALEYLH 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEgperGRVKIADMGFArlfnsplKPLADLDPVVV-TFWYRAPElLLGARHYTKAIDIWAIGC 162
Cdd:cd05612   119 SKEIVYRDLKPENILLDKE----GHIKLTDFGFA-------KKLRDRTWTLCgTPEYLAPE-VIQSKGHNKAVDWWALGI 186
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370507705 163 IFAELLTSEPifhcrqediktsnPFHHDQLDRIF 196
Cdd:cd05612   187 LIYEMLVGYP-------------PFFDDNPFGIY 207
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
9-274 4.14e-12

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: 66.58  E-value: 4.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   9 LLRELKHPNVIALQKVFlshSDRKVWLLfdyaehdlwhIIKFHRASKANKKPMQ---LPRSMVKSLLYQILDGIHYLHAN 85
Cdd:cd14178    50 LLRYGQHPNIITLKDVY---DDGKFVYL----------VMELMRGGELLDRILRqkcFSEREASAVLCTITKTVEYLHSQ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVMGEGPERGRVKIADMGFARLFNSPLKPLadLDPvVVTFWYRAPElLLGARHYTKAIDIWAIGCIFA 165
Cdd:cd14178   117 GVVHRDLKPSNILYMDESGNPESIRICDFGFAKQLRAENGLL--MTP-CYTANFVAPE-VLKRQGYDAACDIWSLGILLY 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 166 ELLTSEPIFHCRQEDIKtsnpfhHDQLDRIFSVMGFPADKDWEDIRKMpeyptlQKDfrrttyansslikymekhkvkpd 245
Cdd:cd14178   193 TMLAGFTPFANGPDDTP------EEILARIGSGKYALSGGNWDSISDA------AKD----------------------- 237
                         250       260
                  ....*....|....*....|....*....
gi 1370507705 246 skvflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14178   238 -----IVSKMLHVDPHQRLTAPQVLRHPW 261
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
6-174 5.12e-12

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: 65.72  E-value: 5.12e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQK---------VFLSHSDRKvwllfdyaehDLWHIIKFHRAskankkpmqLPRSMVKSLLYQIL 76
Cdd:cd14189    51 EIELHRDLHHKHVVKFSHhfedaeniyIFLELCSRK----------SLAHIWKARHT---------LLEPEVRYYLKQII 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  77 DGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKplaDLDPVVVTFWYRAPELLLGARHYTKAiD 156
Cdd:cd14189   112 SGLKYLHLKGILHRDLKLGNFFIN----ENMELKVGDFGLAARLEPPEQ---RKKTICGTPNYLAPEVLLRQGHGPES-D 183
                         170
                  ....*....|....*...
gi 1370507705 157 IWAIGCIFAELLTSEPIF 174
Cdd:cd14189   184 VWSLGCVMYTLLCGNPPF 201
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
74-174 5.81e-12

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 67.51  E-value: 5.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPlkPLADLDPVVVTFWYRAPELllgARH--Y 151
Cdd:NF033483  115 QILSALEHAHRNGIVHRDIKPQNILIT----KDGRVKVTDFGIARALSST--TMTQTNSVLGTVHYLSPEQ---ARGgtV 185
                          90       100
                  ....*....|....*....|...
gi 1370507705 152 TKAIDIWAIGCIFAELLTSEPIF 174
Cdd:NF033483  186 DARSDIYSLGIVLYEMLTGRPPF 208
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
6-177 6.29e-12

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: 65.41  E-value: 6.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALqkvflshsdrkvwllfdyaeHDLWH-IIKFHR---------ASKANKKPMQLPRSMVKSLL--- 72
Cdd:cd14033    50 EVEMLKGLQHPNIVRF--------------------YDSWKsTVRGHKciilvtelmTSGTLKTYLKRFREMKLKLLqrw 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  73 -YQILDGIHYLHANW--VLHRDLKPANILVMGEgpeRGRVKIADMGFArlfnsPLKPLADLDPVVVTFWYRAPELLlgAR 149
Cdd:cd14033   110 sRQILKGLHFLHSRCppILHRDLKCDNIFITGP---TGSVKIGDLGLA-----TLKRASFAKSVIGTPEFMAPEMY--EE 179
                         170       180
                  ....*....|....*....|....*....
gi 1370507705 150 HYTKAIDIWAIGCIFAELLTSE-PIFHCR 177
Cdd:cd14033   180 KYDEAVDVYAFGMCILEMATSEyPYSECQ 208
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
3-164 6.50e-12

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: 66.43  E-value: 6.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELK--HPNVIALQKVFL---------SHSDRKVWL-------------LFDYAE-HDLWHIIKFHRASKAN 57
Cdd:cd13977    44 ALREFWALSSIQrqHPNVIQLEECVLqrdglaqrmSHGSSKSDLylllvetslkgerCFDPRSaCYLWFVMEFCDGGDMN 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  58 -----KKPmqlPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPERgRVKIADMGFARLFNSplKPLADLDP 132
Cdd:cd13977   124 eyllsRRP---DRQTNTSFMLQLSSALAFLHRNQIVHRDLKPDNILISHKRGEP-ILKVADFGLSKVCSG--SGLNPEEP 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 133 VVV----------TFWYRAPELLLGarHYTKAIDIWAIGCIF 164
Cdd:cd13977   198 ANVnkhflssacgSDFYMAPEVWEG--HYTAKADIFALGIII 237
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
5-161 7.23e-12

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: 65.55  E-value: 7.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALqKVFLSHSDRkVWLLFDYAE-HDLWHIIKFHRaskankkpmQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14077    62 REAALSSLLNHPHICRL-RDFLRTPNH-YYMLFEYVDgGQLLDYIISHG---------KLKEKQARKFARQIASALDYLH 130
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd14077   131 RNSIVHRDLKIENILI----SKSGNIKIIDFGLSNLYDPRRL----LRTFCGSLYFAAPELLQAQPYTGPEVDVWSFG 200
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
6-169 7.69e-12

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: 65.32  E-value: 7.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAEH-DLwhiikFHRASKANKKPMQLPrsmVKSLLYQILDGIHYLHA 84
Cdd:cd14193    51 EIEVMNQLNHANLIQLYDAFESRND--IVLVMEYVDGgEL-----FDRIIDENYNLTELD---TILFIKQICEGIQYMHQ 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEgpERGRVKIADMGFARLFnsplKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIF 164
Cdd:cd14193   121 MYILHLDLKPENILCVSR--EANQVKIIDFGLARRY----KPREKLRVNFGTPEFLAPE-VVNYEFVSFPTDMWSLGVIA 193

                  ....*
gi 1370507705 165 AELLT 169
Cdd:cd14193   194 YMLLS 198
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
5-274 8.33e-12

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: 65.43  E-value: 8.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELK-HPNVIALQKVFlsHSDRKVWLLFDYAEHD--LWHIikfHRASKANKKPMQLprsmvksLLYQILDGIHY 81
Cdd:cd14173    48 REVEMLYQCQgHRNVLELIEFF--EEEDKFYLVFEKMRGGsiLSHI---HRRRHFNELEASV-------VVQDIASALDF 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgEGPER-GRVKIA--DMGFARLFNSPLKPLAdlDPVVVT----FWYRAPELLLG----ARH 150
Cdd:cd14173   116 LHNKGIAHRDLKPENILC--EHPNQvSPVKICdfDLGSGIKLNSDCSPIS--TPELLTpcgsAEYMAPEVVEAfneeASI 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 151 YTKAIDIWAIGCIFAELLTSEPIF--HCRQE---DIKTSNPFHHDQLdrifsvmgfpadkdWEDIRKMP-EYPtlQKDFR 224
Cdd:cd14173   192 YDKRCDLWSLGVILYIMLSGYPPFvgRCGSDcgwDRGEACPACQNML--------------FESIQEGKyEFP--EKDWA 255
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370507705 225 RTTYANSSLIkymekhkvkpdskvflllQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14173   256 HISCAAKDLI------------------SKLLVRDAKQRLSAAQVLQHPW 287
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
34-283 8.74e-12

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: 65.79  E-value: 8.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  34 WLLF-DYAEHD---LWHIIKFHRA----SKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPE 105
Cdd:cd05601    62 WITKlQYAFQDsenLYLVMEYHPGgdllSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILI----DR 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 106 RGRVKIADMGFARLFNSPLKPLADLdPvVVTFWYRAPELLLGARHYTKA-----IDIWAIGCIFAELLTSEPifhcrqed 180
Cdd:cd05601   138 TGHIKLADFGSAAKLSSDKTVTSKM-P-VGTPDYIAPEVLTSMNGGSKGtygveCDWWSLGIVAYEMLYGKT-------- 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 181 iktsnPFHHDQLDRIFS-VMGFpadkdwEDIRKMPEYPTLQKDFRRttyansslikymekhkvkpdskvflLLQKLLTmD 259
Cdd:cd05601   208 -----PFTEDTVIKTYSnIMNF------KKFLKFPEDPKVSESAVD-------------------------LIKGLLT-D 250
                         250       260
                  ....*....|....*....|....
gi 1370507705 260 PTKRITSEQALQDPYFQEDPLPTL 283
Cdd:cd05601   251 AKERLGYEGLCCHPFFSGIDWNNL 274
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
5-175 8.81e-12

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 64.94  E-value: 8.81e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSH----------SDRKvwLLFDYAEHDLWhiikfhraskankkpmqlPRSMVKSLLYQ 74
Cdd:cd14110    48 REYQVLRRLSHPRIAQLHSAYLSPrhlvlieelcSGPE--LLYNLAERNSY------------------SEAEVTDYLWQ 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNsPLKPLAdLDPVVVTFWYRAPELLLGaRHYTKA 154
Cdd:cd14110   108 ILSAVDYLHSRRILHLDLRSENMIIT----EKNLLKIVDLGNAQPFN-QGKVLM-TDKKGDYVETMAPELLEG-QGAGPQ 180
                         170       180
                  ....*....|....*....|.
gi 1370507705 155 IDIWAIGCIFAELLTSEPIFH 175
Cdd:cd14110   181 TDIWAIGVTAFIMLSADYPVS 201
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
2-168 9.26e-12

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: 64.82  E-value: 9.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKFHRAskankkpmQLPRSMVKSLLYQILDGIH 80
Cdd:cd14065    34 SFLKEVKLMRRLSHPNILRFIGVCVK--DNKLNFITEYVNGgTLEELLKSMDE--------QLPWSQRVSLAKDIASGMA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEGPERGRVkIADMGFARLFnsPLKPLADLD-----PVVVTFWYRAPELLLGaRHYTKAI 155
Cdd:cd14065   104 YLHSKNIIHRDLNSKNCLVREANRGRNAV-VADFGLAREM--PDEKTKKPDrkkrlTVVGSPYWMAPEMLRG-ESYDEKV 179
                         170
                  ....*....|...
gi 1370507705 156 DIWAIGCIFAELL 168
Cdd:cd14065   180 DVFSFGIVLCEII 192
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
5-169 9.52e-12

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: 65.43  E-value: 9.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNV---IALQKVFLSHSDrKVWLLFDYAEH-DLWHIIKFHRASKanKKPMQLPRSMVKSL--LYQILDG 78
Cdd:cd14053    38 REIYSLPGMKHENIlqfIGAEKHGESLEA-EYWLITEFHERgSLCDYLKGNVISW--NELCKIAESMARGLayLHEDIPA 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFnSPLKPLADLDPVVVTFWYRAPELLLGARHYTK----A 154
Cdd:cd14053   115 TNGGHKPSIAHRDFKSKNVLLKSD----LTACIADFGLALKF-EPGKSCGDTHGQVGTRRYMAPEVLEGAINFTRdaflR 189
                         170
                  ....*....|....*
gi 1370507705 155 IDIWAIGCIFAELLT 169
Cdd:cd14053   190 IDMYAMGLVLWELLS 204
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
6-169 9.84e-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: 64.98  E-value: 9.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLwhiikFHRASKANKKPMQLprsmvKSLLY--QILDGIHYL 82
Cdd:cd14192    51 EINIMNQLNHVNLIQLYDAF--ESKTNLTLIMEYVDGgEL-----FDRITDESYQLTEL-----DAILFtrQICEGVHYL 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMGEGPErgRVKIADMGFARLFnsplKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGC 162
Cdd:cd14192   119 HQHYILHLDLKPENILCVNSTGN--QIKIIDFGLARRY----KPREKLKVNFGTPEFLAPE-VVNYDFVSFPTDMWSVGV 191

                  ....*..
gi 1370507705 163 IFAELLT 169
Cdd:cd14192   192 ITYMLLS 198
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
5-180 1.15e-11

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: 64.84  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHD-LWHIIKfhraskanKKPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14154    39 KEVKVMRSLDHPNVLKFIGVL--YKDKKLNLITEYIPGGtLKDVLK--------DMARPLPWAQRVRFAKDIASGMAYLH 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKPLADLDP-----------------VVVTFWYRAPELLL 146
Cdd:cd14154   109 SMNIIHRDLNSHNCLVR----EDKTVVVADFGLARLIVEERLPSGNMSPsetlrhlkspdrkkrytVVGNPYWMAPEMLN 184
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1370507705 147 GaRHYTKAIDIWAIGCIFAELL---TSEPIFHCRQED 180
Cdd:cd14154   185 G-RSYDEKVDIFSFGIVLCEIIgrvEADPDYLPRTKD 220
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
5-172 1.18e-11

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: 65.08  E-value: 1.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdrKVWLLFDY----AEHDLWhiikfhraskankKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd06642    51 QEITVLSQCDSPYITRYYGSYLKGT--KLWIIMEYlgggSALDLL-------------KPGPLEETYIATILREILKGLD 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFA-RLFNSPLKPladlDPVVVTFWYRAPELLLGARHYTKAiDIWA 159
Cdd:cd06642   116 YLHSERKIHRDIKAANVLL----SEQGDVKLADFGVAgQLTDTQIKR----NTFVGTPFWMAPEVIKQSAYDFKA-DIWS 186
                         170
                  ....*....|...
gi 1370507705 160 IGCIFAELLTSEP 172
Cdd:cd06642   187 LGITAIELAKGEP 199
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
29-169 1.19e-11

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 66.19  E-value: 1.19e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  29 SDRKVWLLFDYAEH-DLWHIIKfhrasKANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERG 107
Cdd:PTZ00267  136 SDDKLLLIMEYGSGgDLNKQIK-----QRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLM----PTG 206
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507705 108 RVKIADMGFARLFNSPLKpladLDpVVVTF----WYRAPELLLGARhYTKAIDIWAIGCIFAELLT 169
Cdd:PTZ00267  207 IIKLGDFGFSKQYSDSVS----LD-VASSFcgtpYYLAPELWERKR-YSKKADMWSLGVILYELLT 266
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
6-174 1.40e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 65.22  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLShsDRKVWLLFDY---AEhdlwhiiKFHRASKANKkpmqLPRSMVKSLLYQILDGIHYL 82
Cdd:PTZ00263   68 EKSILMELSHPFIVNMMCSFQD--ENRVYFLLEFvvgGE-------LFTHLRKAGR----FPNDVAKFYHAELVLAFEYL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPLADldpvvvTFWYRAPELLLGARHyTKAIDIWAIGC 162
Cdd:PTZ00263  135 HSKDIIYRDLKPENLLLDNK----GHVKVTDFGFAKKVPDRTFTLCG------TPEYLAPEVIQSKGH-GKAVDWWTMGV 203
                         170
                  ....*....|..
gi 1370507705 163 IFAELLTSEPIF 174
Cdd:PTZ00263  204 LLYEFIAGYPPF 215
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
44-194 1.49e-11

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: 65.33  E-value: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  44 LWHIIKFHRaskankkpMQLPRSMVKSLlyQILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARlfnSP 123
Cdd:cd05619    94 MFHIQSCHK--------FDLPRATFYAA--EIICGLQFLHSKGIVYRDLKLDNILLDKD----GHIKIADFGMCK---EN 156
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507705 124 LKPLADLDPVVVTFWYRAPELLLGARhYTKAIDIWAIGCIFAELLTSEPIFHCRQED-----IKTSNPFHHDQLDR 194
Cdd:cd05619   157 MLGDAKTSTFCGTPDYIAPEILLGQK-YNTSVDWWSFGVLLYEMLIGQSPFHGQDEEelfqsIRMDNPFYPRWLEK 231
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
5-161 1.52e-11

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: 64.75  E-value: 1.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAE-HDLWHIIKfhrasKANKKPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd06621    48 RELEINKSCASPYIVKYYGAFLDEQDSSIGIAMEYCEgGSLDSIYK-----KVKKKGGRIGEKVLGKIAESVLKGLSYLH 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgegpERGRVKIADMGFA-RLFNSplkpladldpVVVTF----WYRAPELLLGaRHYTKAIDIW 158
Cdd:cd06621   123 SRKIIHRDIKPSNILLT----RKGQVKLCDFGVSgELVNS----------LAGTFtgtsYYMAPERIQG-GPYSITSDVW 187

                  ...
gi 1370507705 159 AIG 161
Cdd:cd06621   188 SLG 190
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
74-273 1.55e-11

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: 65.10  E-value: 1.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFArlfnsplKPLADLDPVVVTFW----YRAPELLLGaR 149
Cdd:cd05592   104 EIICGLQFLHSRGIIYRDLKLDNVLLDRE----GHIKIADFGMC-------KENIYGENKASTFCgtpdYIAPEILKG-Q 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 150 HYTKAIDIWAIGCIFAELLTSEpifhcrqediktsNPFHHDQLDRIFsvmgfpadkdWEDIRKMPEYPtlqkdfrrttya 229
Cdd:cd05592   172 KYNQSVDWWSFGVLLYEMLIGQ-------------SPFHGEDEDELF----------WSICNDTPHYP------------ 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1370507705 230 nssliKYMEKHKVKpdskvflLLQKLLTMDPTKRITSEQALQDP 273
Cdd:cd05592   217 -----RWLTKEAAS-------CLSLLLERNPEKRLGVPECPAGD 248
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
5-274 1.66e-11

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: 64.33  E-value: 1.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWL---------LFDYaehdlwhIIKFHRaskankkpmqLPRSMVKSLLYQI 75
Cdd:cd14078    50 TEIEALKNLSHQHICRLYHVI--ETDNKIFMvleycpggeLFDY-------IVAKDR----------LSEDEARVFFRQI 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  76 LDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARlfnsplKPLADLDPVVVTFW----YRAPELLLGARHY 151
Cdd:cd14078   111 VSAVAYVHSQGYAHRDLKPENLLL----DEDQNLKLIDFGLCA------KPKGGMDHHLETCCgspaYAAPELIQGKPYI 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 152 TKAIDIWAIGCIFAELLtsepifhCrqediktsnpfhhdqldrifsvmGF-PADKDweDIRKMpeYPTLQKDfrrttyan 230
Cdd:cd14078   181 GSEADVWSMGVLLYALL-------C-----------------------GFlPFDDD--NVMAL--YRKIQSG-------- 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1370507705 231 ssliKYMEKHKVKPDSKvfLLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14078   219 ----KYEEPEWLSPSSK--LLLDQMLQVDPKKRITVKELLNHPW 256
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
75-277 1.69e-11

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: 64.93  E-value: 1.69e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPlkpladlDPVVVTFW----YRAPELLLGaRH 150
Cdd:cd05570   105 ICLALQFLHERGIIYRDLKLDNVLLDAE----GHIKIADFGMCKEGIWG-------GNTTSTFCgtpdYIAPEILRE-QD 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 151 YTKAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFsvmgfpadkdwEDIR-KMPEYPtlqkdfrrttya 229
Cdd:cd05570   173 YGFSVDWWALGVLLYEMLAGQS-------------PFEGDDEDELF-----------EAILnDEVLYP------------ 216
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370507705 230 nssliKYMEKHKVKpdskvflLLQKLLTMDPTKRI----TSEQALQD-PYFQE 277
Cdd:cd05570   217 -----RWLSREAVS-------ILKGLLTKDPARRLgcgpKGEADIKAhPFFRN 257
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
5-169 1.97e-11

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 63.82  E-value: 1.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALqkvfLSHSDRKVWLLFDYAEH-DLWHIIKFHRASkankkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14068    36 QELVVLSHLHHPSLVAL----LAAGTAPRMLVMELAPKgSLDALLQQDNAS--------LTRTLQHRIALHVADGLRYLH 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEGPERGRV-KIADMGFARLFNSplkplADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGC 162
Cdd:cd14068   104 SAMIIYRDLKPHNVLLFTLYPNCAIIaKIADYGIAQYCCR-----MGIKTSEGTPGFRAPEVARGNVIYNQQADVYSFGL 178

                  ....*..
gi 1370507705 163 IFAELLT 169
Cdd:cd14068   179 LLYDILT 185
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
5-163 2.15e-11

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 64.03  E-value: 2.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShSDRKVWLLFDYAEH-DLWHIIKfhraskankKPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14165    50 RELEILARLNHKSIIKTYEIFET-SDGKVYIVMELGVQgDLLEFIK---------LRGALPEDVARKMFHQLSSAIKYCH 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSplkplaDLDPVVV---TFW----YRAPELLLGARHYTKAID 156
Cdd:cd14165   120 ELDIVHRDLKCENLLLDKD----FNIKLTDFGFSKRCLR------DENGRIVlskTFCgsaaYAAPEVLQGIPYDPRIYD 189

                  ....*..
gi 1370507705 157 IWAIGCI 163
Cdd:cd14165   190 IWSLGVI 196
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
74-276 2.31e-11

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: 63.90  E-value: 2.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANW-VLHRDLKPANILVmgegPERGRVKIADMGFA-RLFNSplkpLADLDpvVVTFWYRAPELLLGArHY 151
Cdd:cd06605   107 AVVKGLIYLHEKHkIIHRDVKPSNILV----NSRGQVKLCDFGVSgQLVDS----LAKTF--VGTRSYMAPERISGG-KY 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 152 TKAIDIWAIGCIFAELLTSE-PIFHCRQEDIKTsnPFhhDQLDRIfsVMGFPadkdwedirkmPEYPTlqkdfrrttyan 230
Cdd:cd06605   176 TVKSDIWSLGLSLVELATGRfPYPPPNAKPSMM--IF--ELLSYI--VDEPP-----------PLLPS------------ 226
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1370507705 231 sslikymekHKVKPDSKVFllLQKLLTMDPTKRITSEQALQDPYFQ 276
Cdd:cd06605   227 ---------GKFSPDFQDF--VSQCLQKDPTERPSYKELMEHPFIK 261
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
37-275 2.38e-11

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: 64.65  E-value: 2.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  37 FDYAEH-----DLWHIIKFHRASKANKKPMqlPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGE------GPE 105
Cdd:cd14215    84 FDYHGHmcisfELLGLSTFDFLKENNYLPY--PIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSdyeltyNLE 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 106 RGR---------VKIADMGFARLFNSplkplaDLDPVVVTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIFHC 176
Cdd:cd14215   162 KKRdersvkstaIRVVDFGSATFDHE------HHSTIVSTRHYRAPEVIL-ELGWSQPCDVWSIGCIIFEYYVGFTLFQT 234
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 177 RqediktSNPFHHDQLDRIfsvMGFPADKDWEDIRKMPEYPTLQKDFRRTTYAN-------SSLIKYMEKhKVKPDSKVF 249
Cdd:cd14215   235 H------DNREHLAMMERI---LGPIPSRMIRKTRKQKYFYHGRLDWDENTSAGryvrencKPLRRYLTS-EAEEHHQLF 304
                         250       260
                  ....*....|....*....|....*.
gi 1370507705 250 LLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14215   305 DLIESMLEYEPSKRLTLAAALKHPFF 330
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
5-193 3.25e-11

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 63.30  E-value: 3.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDY--AEHDLWHIIKFHRASKANkkpmqlprsmVKSLLYQILDGIHYL 82
Cdd:cd14111    48 QEYEILKSLHHERIMALHEAYIT--PRYLVLIAEFcsGKELLHSLIDRFRYSEDD----------VVGYLVQILQGLEYL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMGEGPergrVKIADMGFARLFNsPLKpLADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGC 162
Cdd:cd14111   116 HGRRVLHLDIKPDNIMVTNLNA----IKIVDFGSAQSFN-PLS-LRQLGRRTGTLEYMAPEMVKG-EPVGPPADIWSIGV 188
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1370507705 163 IFAELLTSEPIFHcRQEDIKTSNPFHHDQLD 193
Cdd:cd14111   189 LTYIMLSGRSPFE-DQDPQETEAKILVAKFD 218
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
74-182 3.64e-11

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: 63.61  E-value: 3.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFnSPLKPLADldpvVVTFWYRAPELLLGARHYTK 153
Cdd:cd05606   106 EVILGLEHMHNRFIVYRDLKPANILL----DEHGHVRISDLGLACDF-SKKKPHAS----VGTHGYMAPEVLQKGVAYDS 176
                          90       100
                  ....*....|....*....|....*....
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFhcRQEDIK 182
Cdd:cd05606   177 SADWFSLGCMLYKLLKGHSPF--RQHKTK 203
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
9-174 3.75e-11

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: 63.96  E-value: 3.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   9 LLRELKHPNVIALQKVFlsHSDRKVWLLFDY-AEHDLWhiikfhraskankkpMQLPR------SMVKSLLYQILDGIHY 81
Cdd:cd05584    53 ILEAVKHPFIVDLHYAF--QTGGKLYLILEYlSGGELF---------------MHLERegifmeDTACFYLAEITLALGH 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEgperGRVKIADMGFArlfnsplKPLADLDPVVVTFW----YRAPELLLGARHyTKAIDI 157
Cdd:cd05584   116 LHSLGIIYRDLKPENILLDAQ----GHVKLTDFGLC-------KESIHDGTVTHTFCgtieYMAPEILTRSGH-GKAVDW 183
                         170
                  ....*....|....*..
gi 1370507705 158 WAIGCIFAELLTSEPIF 174
Cdd:cd05584   184 WSLGALMYDMLTGAPPF 200
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
79-274 3.75e-11

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: 63.47  E-value: 3.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVMGEgPERGRVKIADMGFAR---LFNSPLKPladldpvVVTFWYRAPElLLGARHYTKAI 155
Cdd:cd14172   116 IQYLHSMNIAHRDVKPENLLYTSK-EKDAVLKLTDFGFAKettVQNALQTP-------CYTPYYVAPE-VLGPEKYDKSC 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 156 DIWAIGCIFAELLTSEPIFHCrqediKTSNPFHHDQLDRI-FSVMGFPAdkdwedirkmPEYPTLQKDFRRttyanssli 234
Cdd:cd14172   187 DMWSLGVIMYILLCGFPPFYS-----NTGQAISPGMKRRIrMGQYGFPN----------PEWAEVSEEAKQ--------- 242
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370507705 235 kymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14172   243 ----------------LIRHLLKTDPTERMTITQFMNHPW 266
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
2-276 4.08e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 64.53  E-value: 4.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVflshsdRKV----WLLFDYAEHDLWHIIkfhraskaNKKPMQLPRSMVKSLLYQILD 77
Cdd:PHA03211  206 SSVHEARLLRRLSHPAVLALLDV------RVVggltCLVLPKYRSDLYTYL--------GARLRPLGLAQVTAVARQLLS 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANWVLHRDLKPANILVmgEGPErgRVKIADMG---FARLFNSPLKPLAdldpVVVTFWYRAPELLLGaRHYTKA 154
Cdd:PHA03211  272 AIDYIHGEGIIHRDIKTENVLV--NGPE--DICLGDFGaacFARGSWSTPFHYG----IAGTVDTNAPEVLAG-DPYTPS 342
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 155 IDIWAIG-CIFAELLTSEPIFHCRQEDIKTSnpfHHDQLDRIFS-----VMGFPADKdweDIRKMPEYPTLQKDFRRTTY 228
Cdd:PHA03211  343 VDIWSAGlVIFEAAVHTASLFSASRGDERRP---YDAQILRIIRqaqvhVDEFPQHA---GSRLVSQYRHRAARNRRPAY 416
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1370507705 229 ANSSLIKYMekhkvKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQ 276
Cdd:PHA03211  417 TRPAWTRYY-----KLDLDVEYLVCRALTFDGARRPSAAELLRLPLFQ 459
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
6-275 4.55e-11

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: 63.02  E-value: 4.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLR---ELKHPNVIALQKVFlSHSDRKVwLLFDYAE--HDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIH 80
Cdd:cd14005    53 EIALLLkasKPGVPGVIRLLDWY-ERPDGFL-LIMERPEpcQDLFDFITERGA---------LSENLARIIFRQVVEAVR 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLfnspLKpladlDPVVVTF----WYRAPELLLGARHYTKAID 156
Cdd:cd14005   122 HCHQRGVLHRDIKDENLLI---NLRTGEVKLIDFGCGAL----LK-----DSVYTDFdgtrVYSPPEWIRHGRYHGRPAT 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 157 IWAIGCIFAELLTSEPIFHcRQEDIKTSNPFHHdqldrifsvmgfpadkdwedirkmpeyPTLQKDFRRttyanssliky 236
Cdd:cd14005   190 VWSLGILLYDMLCGDIPFE-NDEQILRGNVLFR---------------------------PRLSKECCD----------- 230
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370507705 237 mekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14005   231 --------------LISRCLQFDPSKRPSLEQILSHPWF 255
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
6-282 5.17e-11

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: 63.12  E-value: 5.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAEHDLWHIIKFHraskankkpMQLPRSMVKSLLYQILDGIHYLHAN 85
Cdd:cd06657    67 EVVIMRDYQHENVVEMYNSYLVGDE--LWVVMEFLEGGALTDIVTH---------TRMNEEQIAAVCLAVLKALSVLHAQ 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVMGEgperGRVKIADMGFARLFNsplKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFA 165
Cdd:cd06657   136 GVIHRDIKSDSILLTHD----GRVKLSDFGFCAQVS---KEVPRRKSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVI 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 166 ELLTSEPifhcrqediktsnPFHHDqldrifsvmgfPADKDWEDIR-KMPeyPTLQKdfrrttyansslikymeKHKVKP 244
Cdd:cd06657   208 EMVDGEP-------------PYFNE-----------PPLKAMKMIRdNLP--PKLKN-----------------LHKVSP 244
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370507705 245 DSKVFllLQKLLTMDPTKRITSEQALQDPYFQEDPLPT 282
Cdd:cd06657   245 SLKGF--LDRLLVRDPAQRATAAELLKHPFLAKAGPPS 280
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
5-274 5.68e-11

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: 62.48  E-value: 5.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLshSDRKVWLLFDYAE-HDLwhiikFHRASKANKkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14662    45 REIINHRSLRHPNIIRFKEVVL--TPTHLAIVMEYAAgGEL-----FERICNAGR----FSEDEARYFFQQLISGVSYCH 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgEGPERGRVKIADMGFAR--LFNSPLKpladldPVVVTFWYRAPELLLGARHYTKAIDIWAIG 161
Cdd:cd14662   114 SMQICHRDLKLENTLL--DGSPAPRLKICDFGYSKssVLHSQPK------STVGTPAYIAPEVLSRKEYDGKVADVWSCG 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 C-IFAELLTSEPIfhcrqEDIKTSNPFhHDQLDRIFSVMgfpadkdwediRKMPEYPTLQKDFRRttyansslikymekh 240
Cdd:cd14662   186 VtLYVMLVGAYPF-----EDPDDPKNF-RKTIQRIMSVQ-----------YKIPDYVRVSQDCRH--------------- 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370507705 241 kvkpdskvflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14662   234 ----------LLSRIFVANPAKRITIPEIKNHPW 257
pknD PRK13184
serine/threonine-protein kinase PknD;
5-279 6.43e-11

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 64.41  E-value: 6.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIAlqkVFLSHSDRK-VWLLFDYAE-HDLWHIIKFHRASKANKKPMQLPRSmVKSLL---YQILDGI 79
Cdd:PRK13184   51 REAKIAADLIHPGIVP---VYSICSDGDpVYYTMPYIEgYTLKSLLKSVWQKESLSKELAEKTS-VGAFLsifHKICATI 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILV--MGEgpergrVKIADMGFARLFNSPLKPLADLD---------------PVVVTFWYRAP 142
Cdd:PRK13184  127 EYVHSKGVLHRDLKPDNILLglFGE------VVILDWGAAIFKKLEEEDLLDIDvdernicyssmtipgKIVGTPDYMAP 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 143 ELLLGARHyTKAIDIWAIGCIFAELLTsepifhcrqedikTSNPFHHdqldrifsvmgfpadkdwEDIRKMPeyptlqkd 222
Cdd:PRK13184  201 ERLLGVPA-SESTDIYALGVILYQMLT-------------LSFPYRR------------------KKGRKIS-------- 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370507705 223 FRRTTYANSSLIKYMEkhkVKPD-SKVFLllqKLLTMDPTKRITSEQALQD---PYFQEDP 279
Cdd:PRK13184  241 YRDVILSPIEVAPYRE---IPPFlSQIAM---KALAVDPAERYSSVQELKQdlePHLQGSP 295
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
6-180 6.58e-11

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: 62.52  E-value: 6.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKfhraskankkPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd14027    41 EGKMMNRLRHSRVVKLLGVILE--EGKYSLVMEYMEKgNLMHVLK----------KVSVPLSVKGRIILEIIEGMAYLHG 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmgegPERGRVKIADMGFA------RLFNSPLKPLADLDPVVV----TFWYRAPELL--LGARH-- 150
Cdd:cd14027   109 KGVIHKDLKPENILV----DNDFHIKIADLGLAsfkmwsKLTKEEHNEQREVDGTAKknagTLYYMAPEHLndVNAKPte 184
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370507705 151 ----YTKAIDIWAIgcifaeLLTSEPIFHCRQED 180
Cdd:cd14027   185 ksdvYSFAIVLWAI------FANKEPYENAINED 212
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
6-169 8.43e-11

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: 62.24  E-value: 8.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLwhiikFHRASKANKkPMQLPRSMVksLLYQILDGIHYLHA 84
Cdd:cd14190    51 EIQVMNQLNHRNLIQLYEAI--ETPNEIVLFMEYVEGgEL-----FERIVDEDY-HLTEVDAMV--FVRQICEGIQFMHQ 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEGPErgRVKIADMGFARLFNsplkPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIF 164
Cdd:cd14190   121 MRVLHLDLKPENILCVNRTGH--QVKIIDFGLARRYN----PREKLKVNFGTPEFLSPE-VVNYDQVSFPTDMWSMGVIT 193

                  ....*
gi 1370507705 165 AELLT 169
Cdd:cd14190   194 YMLLS 198
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
6-283 8.81e-11

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: 62.43  E-value: 8.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDrkVWLLFDY-AEHDLWHIIKfhraskankkPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd06655    66 EILVMKELKNPNIVNFLDSFLVGDE--LFVVMEYlAGGSLTDVVT----------ETCMDEAQIAAVCRECLQALEFLHA 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEgperGRVKIADMGFArlfnSPLKP-LADLDPVVVTFWYRAPELLLgARHYTKAIDIWAIGCI 163
Cdd:cd06655   134 NQVIHRDIKSDNVLLGMD----GSVKLTDFGFC----AQITPeQSKRSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIM 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 164 FAELLTSEPifhcrqediktsnpfhhdqldrifsvmgfpadkdwedirkmpeyPTLQKDFRRTTY--ANSSLIKYMEKHK 241
Cdd:cd06655   205 AIEMVEGEP--------------------------------------------PYLNENPLRALYliATNGTPELQNPEK 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1370507705 242 VKPDSKVFllLQKLLTMDPTKRITSEQALQDPYFQ-EDPLPTL 283
Cdd:cd06655   241 LSPIFRDF--LNRCLEMDVEKRGSAKELLQHPFLKlAKPLSSL 281
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
58-186 8.82e-11

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: 62.84  E-value: 8.82e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  58 KKPMQLPRSMVKSLLYQILDGIHYLHANW-VLHRDLKPANILVmgegPERGRVKIADMGFA-RLFNSplkpLAdlDPVVV 135
Cdd:cd06615    91 KKAGRIPENILGKISIAVLRGLTYLREKHkIMHRDVKPSNILV----NSRGEIKLCDFGVSgQLIDS----MA--NSFVG 160
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370507705 136 TFWYRAPELLLGArHYTKAIDIWAIGCIFAELLTS------------EPIFHCRQEDIKTSNP 186
Cdd:cd06615   161 TRSYMSPERLQGT-HYTVQSDIWSLGLSLVEMAIGrypipppdakelEAMFGRPVSEGEAKES 222
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
5-169 9.38e-11

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: 62.07  E-value: 9.38e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHsdRKVWLLFDYAE----HDLWHiikfhraSKANKKPMQLPRSMvkSLLYQILDGIH 80
Cdd:cd14058    35 VEVRQLSRVDHPNIIKLYGACSNQ--KPVCLVMEYAEggslYNVLH-------GKEPKPIYTAAHAM--SWALQCAKGVA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHA---NWVLHRDLKPANILVMGEGPErgrVKIADMGFArlfnsplkplADLDPVVV----TFWYRAPELLLGaRHYTK 153
Cdd:cd14058   104 YLHSmkpKALIHRDLKPPNLLLTNGGTV---LKICDFGTA----------CDISTHMTnnkgSAAWMAPEVFEG-SKYSE 169
                         170
                  ....*....|....*.
gi 1370507705 154 AIDIWAIGCIFAELLT 169
Cdd:cd14058   170 KCDVFSWGIILWEVIT 185
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
35-169 9.63e-11

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 63.73  E-value: 9.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  35 LLFDYAEH-DLWHIIKfhRASKANKkPMqlpRSMVKSLLY-QILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIA 112
Cdd:PTZ00283  116 LVLDYANAgDLRQEIK--SRAKTNR-TF---REHEAGLLFiQVLLAVHHVHSKHMIHRDIKSANILLCSN----GLVKLG 185
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370507705 113 DMGFARLFNSPLKpladlDPVVVTF----WYRAPELLLgARHYTKAIDIWAIGCIFAELLT 169
Cdd:PTZ00283  186 DFGFSKMYAATVS-----DDVGRTFcgtpYYVAPEIWR-RKPYSKKADMFSLGVLLYELLT 240
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
74-182 9.68e-11

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: 62.35  E-value: 9.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFArlFNSPLKplADLDPVVVTFWYRAPELLLGARhYTK 153
Cdd:cd05630   110 EICCGLEDLHRERIVYRDLKPENILL----DDHGHIRISDLGLA--VHVPEG--QTIKGRVGTVGYMAPEVVKNER-YTF 180
                          90       100
                  ....*....|....*....|....*....
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFHCRQEDIK 182
Cdd:cd05630   181 SPDWWALGCLLYEMIAGQSPFQQRKKKIK 209
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
5-168 9.88e-11

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: 62.28  E-value: 9.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWHIIKfhraskanKKPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14221    39 KEVKVMRCLEHPNVLKFIGVL--YKDKRLNFITEYIKGgTLRGIIK--------SMDSHYPWSQRVSFAKDIASGMAYLH 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgegpERGRVKIADMGFARLF----NSPLKPLADLDP-------VVVTFWYRAPELLLGaRHYT 152
Cdd:cd14221   109 SMNIIHRDLNSHNCLVR----ENKSVVVADFGLARLMvdekTQPEGLRSLKKPdrkkrytVVGNPYWMAPEMING-RSYD 183
                         170
                  ....*....|....*.
gi 1370507705 153 KAIDIWAIGCIFAELL 168
Cdd:cd14221   184 EKVDVFSFGIVLCEII 199
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
6-174 1.16e-10

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 62.43  E-value: 1.16e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDrkVWLLFDY-AEHDLWHIIKfhraskankkPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd06654    67 EILVMRENKNPNIVNYLDSYLVGDE--LWVVMEYlAGGSLTDVVT----------ETCMDEGQIAAVCRECLQALEFLHS 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEgperGRVKIADMGFArlfnSPLKP-LADLDPVVVTFWYRAPELLLgARHYTKAIDIWAIGCI 163
Cdd:cd06654   135 NQVIHRDIKSDNILLGMD----GSVKLTDFGFC----AQITPeQSKRSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIM 205
                         170
                  ....*....|.
gi 1370507705 164 FAELLTSEPIF 174
Cdd:cd06654   206 AIEMIEGEPPY 216
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
6-276 1.20e-10

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: 61.98  E-value: 1.20e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAEHDLWHIIKFHraskankkpMQLPRSMVKSLLYQILDGIHYLHAN 85
Cdd:cd06658    69 EVVIMRDYHHENVVDMYNSYLVGDE--LWVVMEFLEGGALTDIVTH---------TRMNEEQIATVCLSVLRALSYLHNQ 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVMGEgperGRVKIADMGFARLFNsplKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFA 165
Cdd:cd06658   138 GVIHRDIKSDSILLTSD----GRIKLSDFGFCAQVS---KEVPKRKSLVGTPYWMAPE-VISRLPYGTEVDIWSLGIMVI 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 166 ELLTSEPifhcrqediktsnPFHHDqldrifsvmgfpadkdwedirkmpeyPTLQKdFRRTTYANSSLIKymEKHKVKPD 245
Cdd:cd06658   210 EMIDGEP-------------PYFNE--------------------------PPLQA-MRRIRDNLPPRVK--DSHKVSSV 247
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370507705 246 SKVFLLLqkLLTMDPTKRITSEQALQDPYFQ 276
Cdd:cd06658   248 LRGFLDL--MLVREPSQRATAQELLQHPFLK 276
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
75-276 1.24e-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: 61.97  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVmgEGPER-GRVKIA--DMGFARLFNSPLKPLA--DLDPVVVTFWYRAPELLL--- 146
Cdd:cd14174   109 IASALDFLHTKGIAHRDLKPENILC--ESPDKvSPVKICdfDLGSGVKLNSACTPITtpELTTPCGSAEYMAPEVVEvft 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 147 -GARHYTKAIDIWAIGCIFAELLTSEPIF--HC-------RQEDIKT--SNPFHHDQLDRifsvMGFPaDKDWEDIRkmp 214
Cdd:cd14174   187 dEATFYDKRCDLWSLGVILYIMLSGYPPFvgHCgtdcgwdRGEVCRVcqNKLFESIQEGK----YEFP-DKDWSHIS--- 258
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370507705 215 eypTLQKDfrrttyansslikymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPYFQ 276
Cdd:cd14174   259 ---SEAKD----------------------------LISKLLVRDAKERLSAAQVLQHPWVQ 289
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
49-169 1.41e-10

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 61.67  E-value: 1.41e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  49 KFHRasKANKKPMQLPRSMVKSLLYQILDGIHYLHANW-VLHRDLKPANILVmgegPERGRVKIADMGFA-RLFNSPLKP 126
Cdd:cd06617    88 KFYK--KVYDKGLTIPEDILGKIAVSIVKALEYLHSKLsVIHRDVKPSNVLI----NRNGQVKLCDFGISgYLVDSVAKT 161
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370507705 127 L-ADLDPvvvtfwYRAPELL---LGARHYTKAIDIWAIGCIFAELLT 169
Cdd:cd06617   162 IdAGCKP------YMAPERInpeLNQKGYDVKSDVWSLGITMIELAT 202
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
6-172 1.57e-10

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: 61.93  E-value: 1.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLREL-KHPNVIALQKVFLShSDRkvwllfdYAEHDLWHIIKFHRASKAN-------KKPMQLPRSMVKSLLYQILD 77
Cdd:cd06639    68 EYNILRSLpNHPNVVKFYGMFYK-ADQ-------YVGGQLWLVLELCNGGSVTelvkgllKCGQRLDEAMISYILYGALL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANWVLHRDLKPANILVMGEGPergrVKIADMGF-ARLFNSPLKPLADldpVVVTFWYrAPELLLGARHYTKA-- 154
Cdd:cd06639   140 GLQHLHNNRIIHRDVKGNNILLTTEGG----VKLVDFGVsAQLTSARLRRNTS---VGTPFWM-APEVIACEQQYDYSyd 211
                         170       180
                  ....*....|....*....|
gi 1370507705 155 --IDIWAIGCIFAELLTSEP 172
Cdd:cd06639   212 arCDVWSLGITAIELADGDP 231
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
68-172 1.71e-10

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: 61.61  E-value: 1.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  68 VKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFA-RLFNSPLKPladlDPVVVTFWYRAPELLL 146
Cdd:cd06640   103 IATMLKEILKGLDYLHSEKKIHRDIKAANVLL----SEQGDVKLADFGVAgQLTDTQIKR----NTFVGTPFWMAPEVIQ 174
                          90       100
                  ....*....|....*....|....*.
gi 1370507705 147 GARHYTKAiDIWAIGCIFAELLTSEP 172
Cdd:cd06640   175 QSAYDSKA-DIWSLGITAIELAKGEP 199
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
69-182 1.82e-10

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: 61.91  E-value: 1.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  69 KSLLY--QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFnsplkPLADL-DPVVVTFWYRAPELL 145
Cdd:cd05632   105 RALFYaaEILCGLEDLHRENTVYRDLKPENILL----DDYGHIRISDLGLAVKI-----PEGESiRGRVGTVGYMAPEVL 175
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1370507705 146 LGARhYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIK 182
Cdd:cd05632   176 NNQR-YTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVK 211
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
6-275 2.03e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 62.40  E-value: 2.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLWHIIkFHRASKANKKPMQlprSMVKSLLYQILDGIHYLHAN 85
Cdd:PHA03210  213 EILALGRLNHENILKIEEIL--RSEANTYMITQKYDFDLYSFM-YDEAFDWKDRPLL---KQTRAIMKQLLCAVEYIHDK 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPLAdlDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCIFA 165
Cdd:PHA03210  287 KLIHRDIKLENIFLNCD----GKIVLGDFGTAMPFEKEREAFD--YGWVGTVATNSPEILAG-DGYCEITDIWSCGLILL 359
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 166 ELLTSE--PIfhcrqeDIKTSNPfhHDQLDRIFSVMGFpADKDWEDIR-KMPEYpTLQKDFRRTTYANSSLIKYMEKhkv 242
Cdd:PHA03210  360 DMLSHDfcPI------GDGGGKP--GKQLLKIIDSLSV-CDEEFPDPPcKLFDY-IDSAEIDHAGHSVPPLIRNLGL--- 426
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1370507705 243 kpDSKVFLLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:PHA03210  427 --PADFEYPLVKMLTFDWHLRPGAAELLALPLF 457
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
63-169 2.18e-10

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: 60.79  E-value: 2.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  63 LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGF-ARLFNSPLKPLADLDPVvvtfwYRA 141
Cdd:cd14050    97 LPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFL----SKDGVCKLGDFGLvVELDKEDIHDAQEGDPR-----YMA 167
                          90       100
                  ....*....|....*....|....*...
gi 1370507705 142 PELLLGarHYTKAIDIWAIGCIFAELLT 169
Cdd:cd14050   168 PELLQG--SFTKAADIFSLGITILELAC 193
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
5-169 2.31e-10

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: 61.06  E-value: 2.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLwhIIKFHRASKANKKPMQLprsmvksLLY--QILDGIHYL 82
Cdd:cd05081    54 REIQILKALHSDFIVKYRGVSYGPGRRSLRLVMEYLPSGC--LRDFLQRHRARLDASRL-------LLYssQICKGMEYL 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFnsPLkplaDLDPVVV-------TFWYrAPElLLGARHYTKAI 155
Cdd:cd05081   125 GSRRCVHRDLAARNILV----ESEAHVKIADFGLAKLL--PL----DKDYYVVrepgqspIFWY-APE-SLSDNIFSRQS 192
                         170
                  ....*....|....
gi 1370507705 156 DIWAIGCIFAELLT 169
Cdd:cd05081   193 DVWSFGVVLYELFT 206
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
6-177 2.36e-10

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 60.89  E-value: 2.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDRKVWLLFdYAEHDLWHIIKFHRASKANKKPmqlprSMVKSLLYQILDGIHYLHAN 85
Cdd:cd14031    59 EAEMLKGLQHPNIVRFYDSWESVLKGKKCIVL-VTELMTSGTLKTYLKRFKVMKP-----KVLRSWCRQILKGLQFLHTR 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 W--VLHRDLKPANILVMGEgpeRGRVKIADMGFARLFNSPLKpladlDPVVVTFWYRAPELLlgARHYTKAIDIWAIGCI 163
Cdd:cd14031   133 TppIIHRDLKCDNIFITGP---TGSVKIGDLGLATLMRTSFA-----KSVIGTPEFMAPEMY--EEHYDESVDVYAFGMC 202
                         170
                  ....*....|....*
gi 1370507705 164 FAELLTSE-PIFHCR 177
Cdd:cd14031   203 MLEMATSEyPYSECQ 217
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
71-277 2.51e-10

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: 61.20  E-value: 2.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  71 LLYQILDGIHYLHANWVLHRDLKPANILVMGEGPErGRVKIADMGFAR---LFNSPLKPladldpvVVTFWYRAPElLLG 147
Cdd:cd14170   106 IMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPN-AILKLTDFGFAKettSHNSLTTP-------CYTPYYVAPE-VLG 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 148 ARHYTKAIDIWAIGCIFAELLTSEPIFhcrqediktsnpfhhdqldriFSVMGFPADKDWEDIRKMPEYptlqkDFRRTT 227
Cdd:cd14170   177 PEKYDKSCDMWSLGVIMYILLCGYPPF---------------------YSNHGLAISPGMKTRIRMGQY-----EFPNPE 230
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370507705 228 YANSSlikymekhkvkpdSKVFLLLQKLLTMDPTKRITSEQALQDPYFQE 277
Cdd:cd14170   231 WSEVS-------------EEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQ 267
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
5-274 2.62e-10

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: 60.89  E-value: 2.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELK-HPNVIALQKVFlsHSDRKVWLLFD--YAEHDLWHIIK---F--HRASKANKkpmqlprsmvksllyQIL 76
Cdd:cd14090    48 REVETLHQCQgHPNILQLIEYF--EDDERFYLVFEkmRGGPLLSHIEKrvhFteQEASLVVR---------------DIA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  77 DGIHYLHANWVLHRDLKPANILVMGEGpERGRVKIADMGFA---RLFNSPLKPLA--DLDPVVVTFWYRAPELLLG---- 147
Cdd:cd14090   111 SALDFLHDKGIAHRDLKPENILCESMD-KVSPVKICDFDLGsgiKLSSTSMTPVTtpELLTPVGSAEYMAPEVVDAfvge 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 148 ARHYTKAIDIWAIGCIFAELLTSEPIF--HC-------RQEDIKT--SNPFHHDQlDRIFSvmgFPaDKDWEDIRKMpey 216
Cdd:cd14090   190 ALSYDKRCDLWSLGVILYIMLCGYPPFygRCgedcgwdRGEACQDcqELLFHSIQ-EGEYE---FP-EKEWSHISAE--- 261
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370507705 217 ptlQKDfrrttyansslikymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14090   262 ---AKD----------------------------LISHLLVRDASQRYTAEQVLQHPW 288
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
9-177 2.82e-10

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: 61.14  E-value: 2.82e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   9 LLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHD--LWHIIKFHRASKankkpmqlPRSMVKSLlyQILDGIHYLHANW 86
Cdd:cd05603    49 LLKNLKHPFLVGLHYSF--QTSEKLYFVLDYVNGGelFFHLQRERCFLE--------PRARFYAA--EVASAIGYLHSLN 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  87 VLHRDLKPANILVmgegPERGRVKIADMGFARlfnSPLKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFAE 166
Cdd:cd05603   117 IIYRDLKPENILL----DCQGHVVLTDFGLCK---EGMEPEETTSTFCGTPEYLAPE-VLRKEPYDRTVDWWCLGAVLYE 188
                         170
                  ....*....|.
gi 1370507705 167 LLTSEPIFHCR 177
Cdd:cd05603   189 MLYGLPPFYSR 199
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
5-169 3.13e-10

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 60.85  E-value: 3.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKFHR-------ASKANKKPMQLPRSMVKSLLYQIL 76
Cdd:cd05048    57 REAELMSDLQHPNIVCLLGVCTK--EQPQCMLFEYMAHgDLHEFLVRHSphsdvgvSSDDDGTASSLDQSDFLHIAIQIA 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  77 DGIHYLHANWVLHRDLKPANILVmGEGPErgrVKIADMGFARLFNSplkplADldpvvvtfWYR------------APEL 144
Cdd:cd05048   135 AGMEYLSSHHYVHRDLAARNCLV-GDGLT---VKISDFGLSRDIYS-----SD--------YYRvqsksllpvrwmPPEA 197
                         170       180
                  ....*....|....*....|....*
gi 1370507705 145 LLGARhYTKAIDIWAIGCIFAELLT 169
Cdd:cd05048   198 ILYGK-FTTESDVWSFGVVLWEIFS 221
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
6-174 3.51e-10

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: 60.89  E-value: 3.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDrkVWLLFDY-AEHDLWHIIKfhraskankkPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd06656    66 EILVMRENKNPNIVNYLDSYLVGDE--LWVVMEYlAGGSLTDVVT----------ETCMDEGQIAAVCRECLQALDFLHS 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEgperGRVKIADMGFArlfnSPLKP-LADLDPVVVTFWYRAPELLLgARHYTKAIDIWAIGCI 163
Cdd:cd06656   134 NQVIHRDIKSDNILLGMD----GSVKLTDFGFC----AQITPeQSKRSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIM 204
                         170
                  ....*....|.
gi 1370507705 164 FAELLTSEPIF 174
Cdd:cd06656   205 AIEMVEGEPPY 215
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
74-225 3.70e-10

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: 60.83  E-value: 3.70e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFnSPLKPLADldpvVVTFWYRAPELLLGARHYTK 153
Cdd:cd14223   111 EIILGLEHMHSRFVVYRDLKPANILL----DEFGHVRISDLGLACDF-SKKKPHAS----VGTHGYMAPEVLQKGVAYDS 181
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFhcRQEDIKTSNpfhhdQLDRIFSVMGFP-ADKDWEDIRKMPEyPTLQKDFRR 225
Cdd:cd14223   182 SADWFSLGCMLFKLLRGHSPF--RQHKTKDKH-----EIDRMTLTMAVElPDSFSPELRSLLE-GLLQRDVNR 246
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
5-169 3.93e-10

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


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 60.14  E-value: 3.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVflSHSDRKVWLLFDYAEHDLWHIikFHRASKANKKPMQlprsmvkSLLY---QILDGIHY 81
Cdd:cd05148    51 KEVQALKRLRHKHLISLFAV--CSVGEPVYIITELMEKGSLLA--FLRSPEGQVLPVA-------SLIDmacQVAEGMAY 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmGEGPErgrVKIADMGFARLFNSPLKPLADLD-PVVVTfwyrAPElLLGARHYTKAIDIWAI 160
Cdd:cd05148   120 LEEQNSIHRDLAARNILV-GEDLV---CKVADFGLARLIKEDVYLSSDKKiPYKWT----APE-AASHGTFSTKSDVWSF 190

                  ....*....
gi 1370507705 161 GCIFAELLT 169
Cdd:cd05148   191 GILLYEMFT 199
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
6-180 4.09e-10

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


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 60.59  E-value: 4.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALqkVFLSHSDRKVWLLFDYAEHDLWhiikFHRASKANKKPmQLPRSMVKSLLYQILDGIHYLHAN 85
Cdd:cd14158    64 EIQVMAKCQHENLVEL--LGYSCDGPQLCLVYTYMPNGSL----LDRLACLNDTP-PLSWHMRCKIAQGTANGINYLHEN 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVmgegPERGRVKIADMGFARlfNSPLKPLADLDPVVV-TFWYRAPELLLGarHYTKAIDIWAIGCIF 164
Cdd:cd14158   137 NHIHRDIKSANILL----DETFVPKISDFGLAR--ASEKFSQTIMTERIVgTTAYMAPEALRG--EITPKSDIFSFGVVL 208
                         170
                  ....*....|....*.
gi 1370507705 165 AELLTSEPIFHCRQED 180
Cdd:cd14158   209 LEIITGLPPVDENRDP 224
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
55-183 4.11e-10

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 60.27  E-value: 4.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  55 KANKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGPergrVKIADMGFARLFN---------SPLK 125
Cdd:cd14048   107 NRRCTMESRELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDV----VKVGDFGLVTAMDqgepeqtvlTPMP 182
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370507705 126 PLADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCIFAELLTSepiFHCRQEDIKT 183
Cdd:cd14048   183 AYAKHTGQVGTRLYMSPEQIHG-NQYSEKVDIFALGLILFELIYS---FSTQMERIRT 236
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
74-197 4.13e-10

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: 60.50  E-value: 4.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldpvvvTFWYRAPELLLgARHYTK 153
Cdd:cd14209   109 QIVLAFEYLHSLDLIYRDLKPENLLI----DQQGYIKVTDFGFAKRVKGRTWTLCG------TPEYLAPEIIL-SKGYNK 177
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370507705 154 AIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFS 197
Cdd:cd14209   178 AVDWWALGVLIYEMAAGYP-------------PFFADQPIQIYE 208
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
6-169 4.68e-10

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: 59.99  E-value: 4.68e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDRKvwLLFDYAEHD--LWHIIKFHraskankkpmQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14113    53 ELGVLQSLQHPQLVGLLDTFETPTSYI--LVLEMADQGrlLDYVVRWG----------NLTEEKIRFYLREILEALQYLH 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmGEGPERGRVKIADMGFARLFNSPLKpladLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCI 163
Cdd:cd14113   121 NCRIAHLDLKPENILV-DQSLSKPTIKLADFGDAVQLNTTYY----IHQLLGSPEFAAPEIILG-NPVSLTSDLWSIGVL 194

                  ....*.
gi 1370507705 164 FAELLT 169
Cdd:cd14113   195 TYVLLS 200
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
6-177 6.03e-10

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 59.71  E-value: 6.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDRKVWLLFdYAEHDLWHIIKFHRASKANKKPmqlprSMVKSLLYQILDGIHYLHAN 85
Cdd:cd14032    50 EAEMLKGLQHPNIVRFYDFWESCAKGKRCIVL-VTELMTSGTLKTYLKRFKVMKP-----KVLRSWCRQILKGLLFLHTR 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 W--VLHRDLKPANILVMGEgpeRGRVKIADMGFArlfnsPLKPLADLDPVVVTFWYRAPELLlgARHYTKAIDIWAIGCI 163
Cdd:cd14032   124 TppIIHRDLKCDNIFITGP---TGSVKIGDLGLA-----TLKRASFAKSVIGTPEFMAPEMY--EEHYDESVDVYAFGMC 193
                         170
                  ....*....|....*
gi 1370507705 164 FAELLTSE-PIFHCR 177
Cdd:cd14032   194 MLEMATSEyPYSECQ 208
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
74-182 6.55e-10

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: 59.90  E-value: 6.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFA---RLFNSPLKPLADldpvvvTFWYRAPELLLGaRH 150
Cdd:cd05608   113 QIISGLEHLHQRRIIYRDLKPENVLLDDD----GNVRISDLGLAvelKDGQTKTKGYAG------TPGFMAPELLLG-EE 181
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370507705 151 YTKAIDIWAIGCIFAELLTSEPIFHCRQEDIK 182
Cdd:cd05608   182 YDYSVDYFTLGVTLYEMIAARGPFRARGEKVE 213
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
5-288 6.98e-10

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: 60.07  E-value: 6.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDlwhiikfhRASKANKKPMQLPRSMVKSLLYQILDGIHYL-H 83
Cdd:cd06650    52 RELQVLHECNSPYIVGFYGAF--YSDGEISICMEHMDGG--------SLDQVLKKAGRIPEQILGKVSIAVIKGLTYLrE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFA-RLFNSplkpLAdlDPVVVTFWYRAPELLLGArHYTKAIDIWAIGC 162
Cdd:cd06650   122 KHKIMHRDVKPSNILV----NSRGEIKLCDFGVSgQLIDS----MA--NSFVGTRSYMSPERLQGT-HYSVQSDIWSMGL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 163 IFAELLTSE-PIfhcrqediktsNPFHHDQLDRIFsvmGFPADKDWEDIRKMPEYP----TLQKDFRRTTYANSSLIKYM 237
Cdd:cd06650   191 SLVEMAVGRyPI-----------PPPDAKELELMF---GCQVEGDAAETPPRPRTPgrplSSYGMDSRPPMAIFELLDYI 256
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370507705 238 -EKHKVKPDSKVFLL-----LQKLLTMDPTKRITSEQALQDPYFQEDPLPTLDvFAG 288
Cdd:cd06650   257 vNEPPPKLPSGVFSLefqdfVNKCLIKNPAERADLKQLMVHAFIKRSDAEEVD-FAG 312
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
3-276 7.04e-10

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: 59.94  E-value: 7.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAE-HDLWHIIKfhraskanKKPMQ-LPRSMVKSLLYQILDGIH 80
Cdd:cd05574    48 VLTEREILATLDHPFLPTLYASF--QTSTHLCFVMDYCPgGELFRLLQ--------KQPGKrLPEEVARFYAAEVLLALE 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEG-------------PERGRVKIADMGFAR---LFNSPLKPLADLDPV------VVTFW 138
Cdd:cd05574   118 YLHLLGFVYRDLKPENILLHESGhimltdfdlskqsSVTPPPVRKSLRKGSrrsSVKSIEKETFVAEPSarsnsfVGTEE 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 139 YRAPELLLGARHyTKAIDIWAIGCIFAELLTSEpifhcrqediktsNPFHHDQLDRIFS-VMGFPAdkdwedirKMPEYP 217
Cdd:cd05574   198 YIAPEVIKGDGH-GSAVDWWTLGILLYEMLYGT-------------TPFKGSNRDETFSnILKKEL--------TFPESP 255
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370507705 218 TLQKDFRrttyansSLIKymekhkvkpdskvflllqKLLTMDPTKRITSEQALQD----PYFQ 276
Cdd:cd05574   256 PVSSEAK-------DLIR------------------KLLVKDPSKRLGSKRGASEikrhPFFR 293
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
5-169 7.98e-10

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: 59.22  E-value: 7.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKV------------FLSHSDrkvwlLFDYAEHDLWHIIKFHRaskankkpmqlprsmvksLL 72
Cdd:cd05034    39 QEAQIMKKLRHDKLVQLYAVcsdeepiyivteLMSKGS-----LLDYLRTGEGRALRLPQ------------------LI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  73 Y---QILDGIHYLHANWVLHRDLKPANILVmGEGPErgrVKIADMGFARLFNS-----------PLKpladldpvvvtfW 138
Cdd:cd05034    96 DmaaQIASGMAYLESRNYIHRDLAARNILV-GENNV---CKVADFGLARLIEDdeytaregakfPIK------------W 159
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1370507705 139 yRAPELLLGARHYTKAiDIWAIGCIFAELLT 169
Cdd:cd05034   160 -TAPEAALYGRFTIKS-DVWSFGILLYEIVT 188
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
14-171 1.39e-09

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 58.71  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  14 KHPNVIALQkvFLSHSDRKVWLLFDY-AEHDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHYLHANWVLHRDL 92
Cdd:PHA03390   67 DNPNFIKLY--YSVTTLKGHVLIMDYiKDGDLFDLLKKEGK---------LSEAEVKKIIRQLVEALNDLHKHNIIHNDI 135
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370507705  93 KPANILVMGegpERGRVKIADMGFARLFNSPLKpladLDPVVVtfwYRAPELLLGaRHYTKAIDIWAIGCIFAELLTSE 171
Cdd:PHA03390  136 KLENVLYDR---AKDRIYLCDYGLCKIIGTPSC----YDGTLD---YFSPEKIKG-HNYDVSFDWWAVGVLTYELLTGK 203
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
1-172 1.54e-09

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: 58.62  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKfhraskanKKPMQLPRSMVKSLLYQILDGI 79
Cdd:cd13978    37 KALLKEAEKMERARHSYVLPLLGVCVE--RRSLGLVMEYMENgSLKSLLE--------REIQDVPWSLRFRIIHEIALGM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLH--ANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLK--PLADLDPVVVTFWYRAPELL-LGARHYTKA 154
Cdd:cd13978   107 NFLHnmDPPLLHHDLKPENILLDNH----FHVKISDFGLSKLGMKSISanRRRGTENLGGTPIYMAPEAFdDFNKKPTSK 182
                         170
                  ....*....|....*....
gi 1370507705 155 IDIWAIG-CIFAELLTSEP 172
Cdd:cd13978   183 SDVYSFAiVIWAVLTRKEP 201
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
5-169 1.54e-09

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 58.69  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKV------------FLSHSDRKVWLLFD--YAEHDLWHIIKFHRASKANKKPMQLPRSMVKS 70
Cdd:cd05050    57 REAALMAEFDHPNIVKLLGVcavgkpmcllfeYMAYGDLNEFLRHRspRAQCSLSHSTSSARKCGLNPLPLSCTEQLCIA 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  71 LlyQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYrAPELLLGARh 150
Cdd:cd05050   137 K--QVAAGMAYLSERKFVHRDLATRNCLV----GENMVVKIADFGLSRNIYSADYYKASENDAIPIRWM-PPESIFYNR- 208
                         170
                  ....*....|....*....
gi 1370507705 151 YTKAIDIWAIGCIFAELLT 169
Cdd:cd05050   209 YTTESDVWAYGVVLWEIFS 227
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
74-182 1.65e-09

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: 59.30  E-value: 1.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFnSPLKPLADldpvVVTFWYRAPELLLGARHYTK 153
Cdd:cd05633   116 EIILGLEHMHNRFVVYRDLKPANILL----DEHGHVRISDLGLACDF-SKKKPHAS----VGTHGYMAPEVLQKGTAYDS 186
                          90       100
                  ....*....|....*....|....*....
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFhcRQEDIK 182
Cdd:cd05633   187 SADWFSLGCMLFKLLRGHSPF--RQHKTK 213
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
78-194 1.78e-09

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: 58.47  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFArlfnSPLKPLADLDPVVVTFWYRAPELLLGARhYTKAIDI 157
Cdd:cd05631   114 GLEDLQRERIVYRDLKPENILL----DDRGHIRISDLGLA----VQIPEGETVRGRVGTVGYMAPEVINNEK-YTFSPDW 184
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1370507705 158 WAIGCIFAELLTSEPIFHCRQEDIKtsnpfhHDQLDR 194
Cdd:cd05631   185 WGLGCLIYEMIQGQSPFRKRKERVK------REEVDR 215
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
5-169 1.78e-09

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: 58.20  E-value: 1.78e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKFHRASKankkpMQLPRSMVKSLLYQILD---GIH 80
Cdd:cd05044    48 KEAHLMSNFKHPNILKLLGVCLD--NDPQYIILELMEGgDLLSYLRAARPTA-----FTPPLLTLKDLLSICVDvakGCV 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFAR-LFNSPL--KPLADLDPVVvtfWYrAPELLLGARhYTKAIDI 157
Cdd:cd05044   121 YLEDMHFVHRDLAARNCLVSSKDYRERVVKIGDFGLARdIYKNDYyrKEGEGLLPVR---WM-APESLVDGV-FTTQSDV 195
                         170
                  ....*....|..
gi 1370507705 158 WAIGCIFAELLT 169
Cdd:cd05044   196 WAFGVLMWEILT 207
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
5-196 1.91e-09

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: 58.47  E-value: 1.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLshSDRKVWLLFDYAEH-DLWHIIKFHRASKANKKP---MQLPRSMVKSLLYQILDGIH 80
Cdd:cd05095    68 KEIKIMSRLKDPNIIRLLAVCI--TDDPLCMITEYMENgDLNQFLSRQQPEGQLALPsnaLTVSYSDLRFMAAQIASGMK 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegperGR---VKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGarHYTKAIDI 157
Cdd:cd05095   146 YLSSLNFVHRDLATRNCLV-------GKnytIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMSWESILLG--KFTTASDV 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370507705 158 WAIGCIFAELLT---SEPIFHCRQED-IKTSNPFHHDQLDRIF 196
Cdd:cd05095   217 WAFGVTLWETLTfcrEQPYSQLSDEQvIENTGEFFRDQGRQTY 259
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
5-226 2.01e-09

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: 58.10  E-value: 2.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVW----LLFDYAEHDLWHiiKFHRASKANKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd05075    50 SEAVCMKEFDHPNVMRLIGVCLQNTESEGYpspvVILPFMKHGDLH--SFLLYSRLGDCPVYLPTQMLVKFMTDIASGME 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFA-RLFNSPLKPLADLDPVVVTfWYRAPEllLGARHYTKAIDIWA 159
Cdd:cd05075   128 YLSSKNFIHRDLAARNCML----NENMNVCVADFGLSkKIYNGDYYRQGRISKMPVK-WIAIES--LADRVYTTKSDVWS 200
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370507705 160 IGCIFAELLT-----------SEPIFHCRQEDIKTSNPfhhDQLDRIFSVMGfpadKDWE-DIRKMPEYPTLQKDFRRT 226
Cdd:cd05075   201 FGVTMWEIATrgqtpypgvenSEIYDYLRQGNRLKQPP---DCLDGLYELMS----SCWLlNPKDRPSFETLRCELEKI 272
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
9-188 2.49e-09

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: 58.44  E-value: 2.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   9 LLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWhiikFHRaskanKKPMQLPRSMVKSLLYQILDGIHYLHANWV 87
Cdd:cd05604    50 LLKNVKHPFLVGLHYSF--QTTDKLYFVLDFVNGgELF----FHL-----QRERSFPEPRARFYAAEIASALGYLHSINI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  88 LHRDLKPANILVmgegPERGRVKIADMGFARlfnsplKPLADLDpVVVTFW----YRAPELLLgARHYTKAIDIWAIGCI 163
Cdd:cd05604   119 VYRDLKPENILL----DSQGHIVLTDFGLCK------EGISNSD-TTTTFCgtpeYLAPEVIR-KQPYDNTVDWWCLGSV 186
                         170       180
                  ....*....|....*....|....*
gi 1370507705 164 FAELLTSEPIFHCRQEDIKTSNPFH 188
Cdd:cd05604   187 LYEMLYGLPPFYCRDTAEMYENILH 211
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
6-169 2.58e-09

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


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 57.84  E-value: 2.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHsdRKVWLLFDYAEHDLwhIIKFHRASKaNKKPMQLPRSMVKsllyQILDGIHYLHAN 85
Cdd:cd05059    49 EAKVMMKLSHPKLVQLYGVCTKQ--RPIFIVTEYMANGC--LLNYLRERR-GKFQTEQLLEMCK----DVCEAMEYLESN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVmgegPERGRVKIADMGFARL-----FNS------PLKpladldpvvvtfwYRAPELLLGARHYTKA 154
Cdd:cd05059   120 GFIHRDLAARNCLV----GEQNVVKVSDFGLARYvlddeYTSsvgtkfPVK-------------WSPPEVFMYSKFSSKS 182
                         170
                  ....*....|....*
gi 1370507705 155 iDIWAIGCIFAELLT 169
Cdd:cd05059   183 -DVWSFGVLMWEVFS 196
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
4-172 2.90e-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: 57.79  E-value: 2.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELKHPNVIALqKVFLSHSDRKVWLLFDYAEHDLWHIIKfhRASKANKKPmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14001    53 KEEAKILKSLNHPNIVGF-RAFTKSEDGSLCLAMEYGGKSLNDLIE--ERYEAGLGP--FPAATILKVALSIARALEYLH 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 AN-WVLHRDLKPANILVMGEGPErgrVKIADMGFARLFNSPLKplADLDP---VVVTFWYRAPELLLGARHYTKAIDIWA 159
Cdd:cd14001   128 NEkKILHGDIKSGNVLIKGDFES---VKLCDFGVSLPLTENLE--VDSDPkaqYVGTEPWKAKEALEEGGVITDKADIFA 202
                         170
                  ....*....|...
gi 1370507705 160 IGCIFAELLTSEP 172
Cdd:cd14001   203 YGLVLWEMMTLSV 215
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
5-196 3.29e-09

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 57.68  E-value: 3.29e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLshSDRKVWLLFDYAEH-DLWHIIKFHRASKANKKPMQLPRSMVKSLLY---QILDGIH 80
Cdd:cd05097    66 KEIKIMSRLKNPNIIRLLGVCV--SDDPLCMITEYMENgDLNQFLSQREIESTFTHANNIPSVSIANLLYmavQIASGMK 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegperGR---VKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGarHYTKAIDI 157
Cdd:cd05097   144 YLASLNFVHRDLATRNCLV-------GNhytIKIADFGMSRNLYSGDYYRIQGRAVLPIRWMAWESILLG--KFTTASDV 214
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370507705 158 WAIGCIFAELLT---SEPIFHCRQED-IKTSNPFHHDQLDRIF 196
Cdd:cd05097   215 WAFGVTLWEMFTlckEQPYSLLSDEQvIENTGEFFRNQGRQIY 257
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
14-169 3.81e-09

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: 57.43  E-value: 3.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  14 KHPNVIALQKVflSHSDRKVWLLFDYAEH-DLWHIIKFHR--ASKANKKPMQLPRSMVK-----SLLYQILDGIHYLHAN 85
Cdd:cd05053    75 KHKNIINLLGA--CTQDGPLYVVVEYASKgNLREFLRARRppGEEASPDDPRVPEEQLTqkdlvSFAYQVARGMEYLASK 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVmGEGPErgrVKIADMGFARLFNS------------PLKpladldpvvvtfWYrAPELLLgARHYTK 153
Cdd:cd05053   153 KCIHRDLAARNVLV-TEDNV---MKIADFGLARDIHHidyyrkttngrlPVK------------WM-APEALF-DRVYTH 214
                         170
                  ....*....|....*.
gi 1370507705 154 AIDIWAIGCIFAELLT 169
Cdd:cd05053   215 QSDVWSFGVLLWEIFT 230
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
27-164 3.88e-09

Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Dusty protein kinase is also called Receptor-interacting protein kinase 5 (RIPK5 or RIP5) or RIP-homologous kinase. It is widely distributed in the central nervous system, and may be involved in inducing both caspase-dependent and caspase-independent cell death. The Dusty subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 57.12  E-value: 3.88e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  27 SHSDRKVWLLFDYAEHDLwhiikfHRASKANkkpMQLPRSMVKSLlyQILDGIHYLHANWVLHRDLKPANILVmgegPER 106
Cdd:cd13975    74 GGSSIAVLLIMERLHRDL------YTGIKAG---LSLEERLQIAL--DVVEGIRFLHSQGLVHRDIKLKNVLL----DKK 138
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370507705 107 GRVKIADMGFArlfnsplKPLADLDPVVV-TFWYRAPELLLGarHYTKAIDIWAIGCIF 164
Cdd:cd13975   139 NRAKITDLGFC-------KPEAMMSGSIVgTPIHMAPELFSG--KYDNSVDVYAFGILF 188
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
5-168 3.97e-09

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: 57.28  E-value: 3.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNViaLQKV----FLSHSDRKVWLLFDYAEH-DLWHIIKFHRASKAnkkpmqlprSMVKsLLYQILDGI 79
Cdd:cd14056    38 TEIYQTVMLRHENI--LGFIaadiKSTGSWTQLWLITEYHEHgSLYDYLQRNTLDTE---------EALR-LAYSAASGL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANW--------VLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPL-ADLDPVVVTFWYRAPELLLGARH 150
Cdd:cd14056   106 AHLHTEIvgtqgkpaIAHRDLKSKNILVKRD----GTCCIADLGLAVRYDSDTNTIdIPPNPRVGTKRYMAPEVLDDSIN 181
                         170       180
                  ....*....|....*....|...
gi 1370507705 151 YT-----KAIDIWAIGCIFAELL 168
Cdd:cd14056   182 PKsfesfKMADIYSFGLVLWEIA 204
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
63-191 4.05e-09

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: 56.90  E-value: 4.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  63 LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLFNSPLkpLADLDPVVVtfwYRAP 142
Cdd:cd14100   103 LPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILI---DLNTGELKLIDFGSGALLKDTV--YTDFDGTRV---YSPP 174
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1370507705 143 ELLLGARHYTKAIDIWAIGCIFAELLTSepifhcrqeDIktsnPFHHDQ 191
Cdd:cd14100   175 EWIRFHRYHGRSAAVWSLGILLYDMVCG---------DI----PFEHDE 210
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
62-276 4.66e-09

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: 57.68  E-value: 4.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  62 QLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNS---------PLKPLADLDP 132
Cdd:cd05573    97 VFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILL----DADGHIKLADFGLCTKMNKsgdresylnDSVNTLFQDN 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 133 VVVTFW-----------------YRAPELLLGaRHYTKAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRI 195
Cdd:cd05573   173 VLARRRphkqrrvraysavgtpdYIAPEVLRG-TGYGPECDWWSLGVILYEMLYGFP-------------PFYSDSLVET 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 196 FS-VMgfpadkDWEDIRKMPEYPTLQKDFRrttyansslikymekhkvkpdskvfLLLQKLLTmDPTKRITS-EQALQDP 273
Cdd:cd05573   239 YSkIM------NWKESLVFPDDPDVSPEAI-------------------------DLIRRLLC-DPEDRLGSaEEIKAHP 286

                  ...
gi 1370507705 274 YFQ 276
Cdd:cd05573   287 FFK 289
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
5-168 4.86e-09

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: 56.88  E-value: 4.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDLwhIIKFHRASkaNKKPMQLPRSMVKSllyqILDGIHYLHA 84
Cdd:cd14222    39 TEVKVMRSLDHPNVLKFIGVL--YKDKRLNLLTEFIEGGT--LKDFLRAD--DPFPWQQKVSFAKG----IASGMAYLHS 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEGPergrVKIADMGFARLFNSPlKPLADLD------------------PVVVTFWYRAPELLL 146
Cdd:cd14222   109 MSIIHRDLNSHNCLIKLDKT----VVVADFGLSRLIVEE-KKKPPPDkpttkkrtlrkndrkkryTVVGNPYWMAPEMLN 183
                         170       180
                  ....*....|....*....|..
gi 1370507705 147 GARhYTKAIDIWAIGCIFAELL 168
Cdd:cd14222   184 GKS-YDEKVDIFSFGIVLCEII 204
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
74-175 7.05e-09

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: 56.81  E-value: 7.05e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLfnsPLKPLADLDPVVVTFWYRAPELLLGaRHYTK 153
Cdd:cd05585   102 ELLCALECLHKFNVIYRDLKPENILL----DYTGHIALCDFGLCKL---NMKDDDKTNTFCGTPEYLAPELLLG-HGYTK 173
                          90       100
                  ....*....|....*....|..
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFH 175
Cdd:cd05585   174 AVDWWTLGVLLYEMLTGLPPFY 195
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
5-194 7.36e-09

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: 56.36  E-value: 7.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHD--LWHIIKFHRaskankkpmqLPRSMVKSLLYQILDGIHYL 82
Cdd:cd14070    52 REGRIQQMIRHPNITQLLDIL--ETENSYYLVMELCPGGnlMHRIYDKKR----------LEEREARRYIRQLVSAVEHL 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPlkplADLDPVVV---TFWYRAPElLLGARHYTKAIDIWA 159
Cdd:cd14070   120 HRAGVVHRDLKIENLLL----DENDNIKLIDFGLSNCAGIL----GYSDPFSTqcgSPAYAAPE-LLARKKYGPKVDVWS 190
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1370507705 160 IGCIFAELLTSEPIFhcrqedikTSNPFHHDQLDR 194
Cdd:cd14070   191 IGVNMYAMLTGTLPF--------TVEPFSLRALHQ 217
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
5-275 7.67e-09

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: 56.44  E-value: 7.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDY-AEHDLWHIIkfhrASKANKkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14114    48 KEIQIMNQLHHPKLINLHDAF--EDDNEMVLILEFlSGGELFERI----AAEHYK----MSEAEVINYMRQVCEGLCHMH 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANIlvMGEGPERGRVKIADMGFArlfnSPLKPLADLDPVVVTFWYRAPELLLG--ARHYTkaiDIWAIG 161
Cdd:cd14114   118 ENNIVHLDIKPENI--MCTTKRSNEVKLIDFGLA----THLDPKESVKVTTGTAEFAAPEIVERepVGFYT---DMWAVG 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 162 CIFAELLTSEPIFHCRQEDiktsnpfhhDQLDRIFSVmgfpadkDWEdirkmpeyptlqkdfrrttYANSSLikymekHK 241
Cdd:cd14114   189 VLSYVLLSGLSPFAGENDD---------ETLRNVKSC-------DWN-------------------FDDSAF------SG 227
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1370507705 242 VKPDSKVFllLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14114   228 ISEEAKDF--IRKLLLADPNKRMTIHQALEHPWL 259
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
16-183 8.23e-09

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 56.40  E-value: 8.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  16 PNVIALQKVFLShsDRKVWLLFDYAEH-DLW-HIIKFHRASKANKKPMQL------------PRSMVKSLLYQILDGIHY 81
Cdd:cd05576    51 PNMVCLRKYIIS--EESVFLVLQHAEGgKLWsYLSKFLNDKEIHQLFADLderlaaasrfyiPEECIQRWAAEMVVALDA 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIAdmGFARLfnSPLKPLADLDpvVVTFWYRAPELLlGARHYTKAIDIWAIG 161
Cdd:cd05576   129 LHREGIVCRDLNPNNILL----NDRGHIQLT--YFSRW--SEVEDSCDSD--AIENMYCAPEVG-GISEETEACDWWSLG 197
                         170       180
                  ....*....|....*....|..
gi 1370507705 162 CIFAELLTSEPIFHCRQEDIKT 183
Cdd:cd05576   198 ALLFELLTGKALVECHPAGINT 219
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
62-167 9.95e-09

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: 56.04  E-value: 9.95e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  62 QLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFAR-LFNSPLKPLadldpvVVTFWYR 140
Cdd:cd06619    91 KIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLV----NTRGQVKLCDFGVSTqLVNSIAKTY------VGTNAYM 160
                          90       100
                  ....*....|....*....|....*..
gi 1370507705 141 APELLLGaRHYTKAIDIWAIGCIFAEL 167
Cdd:cd06619   161 APERISG-EQYGIHSDVWSLGISFMEL 186
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
5-186 1.01e-08

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: 56.06  E-value: 1.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEhdLWHIIKFhraskankkpmqLPR---SMVKSLLY--QILDGI 79
Cdd:cd05080    55 QEIDILKTLYHENIVKYKGCCSEQGGKSLQLIMEYVP--LGSLRDY------------LPKhsiGLAQLLLFaqQICEGM 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILVmgegpERGR-VKIADMGFARLFnsplkPLADL---------DPVvvtFWYrAPELLLGAR 149
Cdd:cd05080   121 AYLHSQHYIHRDLAARNVLL-----DNDRlVKIGDFGLAKAV-----PEGHEyyrvredgdSPV---FWY-APECLKEYK 186
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1370507705 150 HYTkAIDIWAIGCIFAELLTsepifHCrqeDIKTSNP 186
Cdd:cd05080   187 FYY-ASDVWSFGVTLYELLT-----HC---DSSQSPP 214
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
5-169 1.03e-08

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: 56.02  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDrkVWLLFDY-AEHDLWHIIKFHRaskankkpMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14104    45 KEISILNIARHRNILRLHESFESHEE--LVMIFEFiSGVDIFERITTAR--------FELNEREIVSYVRQVCEALEFLH 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgegPERGR-VKIADMGFARlfnsPLKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGC 162
Cdd:cd14104   115 SKNIGHFDIRPENIIYC---TRRGSyIKIIEFGQSR----QLKPGDKFRLQYTSAEFYAPE-VHQHESVSTATDMWSLGC 186

                  ....*..
gi 1370507705 163 IFAELLT 169
Cdd:cd14104   187 LVYVLLS 193
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
6-169 1.11e-08

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 56.12  E-value: 1.11e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVflSHSDRKVWLLFDYAEH-DLWHIIKFHR-------ASKANKKPMQ--------LPRSMVK 69
Cdd:cd05045    53 EFNLLKQVNHPHVIKLYGA--CSQDGPLLLIVEYAKYgSLRSFLRESRkvgpsylGSDGNRNSSYldnpderaLTMGDLI 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  70 SLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLF---NSPLKPLADLDPVVvtfwYRAPELLl 146
Cdd:cd05045   131 SFAWQISRGMQYLAEMKLVHRDLAARNVLV----AEGRKMKISDFGLSRDVyeeDSYVKRSKGRIPVK----WMAIESL- 201
                         170       180
                  ....*....|....*....|....
gi 1370507705 147 gARH-YTKAIDIWAIGCIFAELLT 169
Cdd:cd05045   202 -FDHiYTTQSDVWSFGVLLWEIVT 224
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
5-166 1.30e-08

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: 55.89  E-value: 1.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELK---HPNVIALQKVFLSHSdrKVWLLFDYAEH-DLwhiiKFHRASKANKKPMQLPRsmVKSLLYQILDGIH 80
Cdd:cd14052    49 EEVSILRELTldgHDNIVQLIDSWEYHG--HLYIQTELCENgSL----DVFLSELGLLGRLDEFR--VWKILVELSLGLR 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFnsPLKPLADLDPVVVtfwYRAPELLLGaRHYTKAIDIWAI 160
Cdd:cd14052   121 FIHDHHFVHLDLKPANVLITFE----GTLKIGDFGMATVW--PLIRGIEREGDRE---YIAPEILSE-HMYDKPADIFSL 190

                  ....*.
gi 1370507705 161 GCIFAE 166
Cdd:cd14052   191 GLILLE 196
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
6-177 1.38e-08

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: 55.83  E-value: 1.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRASKANKKpmqlprSMVKSLLYQILDGIHYLHAN 85
Cdd:cd14030    74 EAGMLKGLQHPNIVRFYDSWESTVKGKKCIVLVTELMTSGTLKTYLKRFKVMKI------KVLRSWCRQILKGLQFLHTR 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 W--VLHRDLKPANILVMGegpERGRVKIADMGFARLFNSPLKpladlDPVVVTFWYRAPELLlgARHYTKAIDIWAIGCI 163
Cdd:cd14030   148 TppIIHRDLKCDNIFITG---PTGSVKIGDLGLATLKRASFA-----KSVIGTPEFMAPEMY--EEKYDESVDVYAFGMC 217
                         170
                  ....*....|....*
gi 1370507705 164 FAELLTSE-PIFHCR 177
Cdd:cd14030   218 MLEMATSEyPYSECQ 232
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
6-281 1.59e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 56.16  E-value: 1.59e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEHDLWHIIKFHRaskankkpmQLPRSMVKSLLYQILDGIHYLHAN 85
Cdd:PHA03212  133 EAHILRAINHPSIIQLKGTFTYNK--FTCLILPRYKTDLYCYLAAKR---------NIAICDILAIERSVLRAIQYLHEN 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVmgegPERGRVKIADMGFARLfnsplkpladldPVVV----------TFWYRAPELLlgARH-YTKA 154
Cdd:PHA03212  202 RIIHRDIKAENIFI----NHPGDVCLGDFGAACF------------PVDInankyygwagTIATNAPELL--ARDpYGPA 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 155 IDIWAIGCIFAELLTSEpifhcrqediktsnpfhhdqlDRIFSVMGFPADKDWED-----IRKMPEYPTlQKDFRRTTYA 229
Cdd:PHA03212  264 VDIWSAGIVLFEMATCH---------------------DSLFEKDGLDGDCDSDRqikliIRRSGTHPN-EFPIDAQANL 321
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507705 230 NSSLIKYMEKHKVKPDSK------------VFLLLQKLLTMDPTKRITSEQALQDPYFQE--DPLP 281
Cdd:PHA03212  322 DEIYIGLAKKSSRKPGSRplwtnlyelpidLEYLICKMLAFDAHHRPSAEALLDFAAFQDipDPYP 387
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
5-169 2.07e-08

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 55.40  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLL---------YQI 75
Cdd:cd05090    56 QEASLMTELHHPNIVCLLGVVTQ--EQPVCMLFEFMNQGDLHEFLIMRSPHSDVGCSSDEDGTVKSSLdhgdflhiaIQI 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  76 LDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYrAPELLLGARhYTKAI 155
Cdd:cd05090   134 AAGMEYLSSHFFVHKDLAARNILV----GEQLHVKISDLGLSREIYSSDYYRVQNKSLLPIRWM-PPEAIMYGK-FSSDS 207
                         170
                  ....*....|....
gi 1370507705 156 DIWAIGCIFAELLT 169
Cdd:cd05090   208 DIWSFGVVLWEIFS 221
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
74-274 2.07e-08

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 55.16  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMgEGPERGRVKIADMGFARLFNsplkplADLDPVVVTFWYRAPELLLGARH--- 150
Cdd:cd14171   117 QIALAVQHCHSLNIAHRDLKPENLLLK-DNSEDAPIKLCDFGFAKVDQ------GDLMTPQFTPYYVAPQVLEAQRRhrk 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 151 -------------YTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNpfhhDQLDRIFS-VMGFPADkDWEDIRKMpey 216
Cdd:cd14171   190 ersgiptsptpytYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTITK----DMKRKIMTgSYEFPEE-EWSQISEM--- 261
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370507705 217 ptlQKDfrrttyansslikymekhkvkpdskvflLLQKLLTMDPTKRITSEQALQDPY 274
Cdd:cd14171   262 ---AKD----------------------------IVRKLLCVDPEERMTIEEVLHHPW 288
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
74-176 2.22e-08

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: 55.05  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgegpERGRVKIADMGfarLFNsplkpLADLDP--------VVVTFW--YRAPE 143
Cdd:cd14063   105 QICQGMGYLHAKGIIHKDLKSKNIFL-----ENGRVVITDFG---LFS-----LSGLLQpgrredtlVIPNGWlcYLAPE 171
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 144 LL---------LGARHYTKAIDIWAIGCIFAELLTSEPIFHC 176
Cdd:cd14063   172 IIralspdldfEESLPFTKASDVYAFGTVWYELLAGRWPFKE 213
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
6-172 2.53e-08

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: 55.02  E-value: 2.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELK-HPNVIALQKVFLSHSDR---KVWLLFDYAE----HDLwhiikfhrASKANKKPMQLPRSMVKSLLYQILD 77
Cdd:cd06638    64 EYNILKALSdHPNVVKFYGMYYKKDVKngdQLWLVLELCNggsvTDL--------VKGFLKRGERMEEPIIAYILHEALM 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANWVLHRDLKPANILVMGEGPergrVKIADMGF-ARLFNSPLKPLADldpVVVTFWYrAPELLLGARH----YT 152
Cdd:cd06638   136 GLQHLHVNKTIHRDVKGNNILLTTEGG----VKLVDFGVsAQLTSTRLRRNTS---VGTPFWM-APEVIACEQQldstYD 207
                         170       180
                  ....*....|....*....|
gi 1370507705 153 KAIDIWAIGCIFAELLTSEP 172
Cdd:cd06638   208 ARCDVWSLGITAIELGDGDP 227
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
16-167 3.03e-08

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: 55.27  E-value: 3.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  16 PNVIALQKVFLSHSDrkVWLLFDYAEHD--LWHIikfhraskanKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLK 93
Cdd:cd05586    56 PFIVGLKFSFQTPTD--LYLVTDYMSGGelFWHL----------QKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLK 123
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370507705  94 PANILVMGEGpergRVKIADMGFARlfnSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAEL 167
Cdd:cd05586   124 PENILLDANG----HIALCDFGLSK---ADLTDNKTTNTFCGTTEYLAPEVLLDEKGYTKMVDFWSLGVLVFEM 190
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
1-276 3.67e-08

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: 54.08  E-value: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLREL----KHPNVIALQKVFlsHSDRKVWLLFDYAEH--DLWHIIkfhraskANKKPmqLPRSMVKSLLYQ 74
Cdd:cd14101    48 NPVPNEVALLQSVgggpGHRGVIRLLDWF--EIPEGFLLVLERPQHcqDLFDYI-------TERGA--LDESLARRFFKQ 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFARLFNSplKPLADLDPVVVtfwYRAPELLLGARHYTKA 154
Cdd:cd14101   117 VVEAVQHCHSKGVVHRDIKDENILV---DLRTGDIKLIDFGSGATLKD--SMYTDFDGTRV---YSPPEWILYHQYHALP 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 155 IDIWAIGCIFAELLTSepifhcrqeDIktsnPFHHDQldrifsvmgfpadkdwEDIRKMPEYPTlqkdfrrttyanssli 234
Cdd:cd14101   189 ATVWSLGILLYDMVCG---------DI----PFERDT----------------DILKAKPSFNK---------------- 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 235 kymekhKVKPDSKVflLLQKLLTMDPTKRITSEQALQDPYFQ 276
Cdd:cd14101   224 ------RVSNDCRS--LIRSCLAYNPSDRPSLEQILLHPWMM 257
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
3-169 3.76e-08

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 54.07  E-value: 3.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEHDLwhiikFHRASKANKKPMQlprsMVKSLLYQILDGIHYL 82
Cdd:cd14112    47 AVREFESLRTLQHENVQRLIAAFKPSN--FAYLVMEKLQEDV-----FTRFSSNDYYSEE----QVATTVRQILDALHYL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANIlvMGEGPERGRVKIADMGFARlfnsPLKPLADLDPVVVTFWyRAPELLLGARHYTKAIDIWAIGC 162
Cdd:cd14112   116 HFKGIAHLDVQPDNI--MFQSVRSWQVKLVDFGRAQ----KVSKLGKVPVDGDTDW-ASPEFHNPETPITVQSDIWGLGV 188

                  ....*..
gi 1370507705 163 IFAELLT 169
Cdd:cd14112   189 LTFCLLS 195
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
5-169 4.06e-08

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


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 54.25  E-value: 4.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLR-ELKHPNVIALQKVFLShsDRKVWLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSmVKS---------LLYQ 74
Cdd:cd05091    57 RHEAMLRsRLQHPNIVCLLGVVTK--EQPMSMIFSYCSHGDLHEFLVMRSPHSDVGSTDDDKT-VKStlepadflhIVTQ 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMG-FARLFNSPLKPLADLDPVVVTfwYRAPELLLGARHYTK 153
Cdd:cd05091   134 IAAGMEYLSSHHVVHKDLATRNVLVF----DKLNVKISDLGlFREVYAADYYKLMGNSLLPIR--WMSPEAIMYGKFSID 207
                         170
                  ....*....|....*.
gi 1370507705 154 AiDIWAIGCIFAELLT 169
Cdd:cd05091   208 S-DIWSYGVVLWEVFS 222
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
5-167 4.24e-08

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: 54.67  E-value: 4.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEHDlwhiikfhRASKANKKPMQLPRSMVKSLLYQILDGIHYL-H 83
Cdd:cd06649    52 RELQVLHECNSPYIVGFYGAF--YSDGEISICMEHMDGG--------SLDQVLKEAKRIPEEILGKVSIAVLRGLAYLrE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFA-RLFNSPlkpladLDPVVVTFWYRAPELLLGArHYTKAIDIWAIGC 162
Cdd:cd06649   122 KHQIMHRDVKPSNILV----NSRGEIKLCDFGVSgQLIDSM------ANSFVGTRSYMSPERLQGT-HYSVQSDIWSMGL 190

                  ....*
gi 1370507705 163 IFAEL 167
Cdd:cd06649   191 SLVEL 195
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
13-188 4.55e-08

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


Pssm-ID: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 54.37  E-value: 4.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  13 LKHPNVIAlqkvFL------SHSDRKVWLLFDYAEH-DLWHIIKFHRASKankkpmqlpRSMVKsLLYQILDGIHYLHAN 85
Cdd:cd13998    46 LKHENILQ----FIaaderdTALRTELWLVTAFHPNgSL*DYLSLHTIDW---------VSLCR-LALSVARGLAHLHSE 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WV---------LHRDLKPANILVMGEgperGRVKIADMGFA-RLFNSPLKPLADLDPVVVTFWYRAPELLLGA---RHYT 152
Cdd:cd13998   112 IPgctqgkpaiAHRDLKSKNILVKND----GTCCIADFGLAvRLSPSTGEEDNANNGQVGTKRYMAPEVLEGAinlRDFE 187
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1370507705 153 --KAIDIWAIGCIFAELLTSEPIFHCRQEDIKTsnPFH 188
Cdd:cd13998   188 sfKRVDIYAMGLVLWEMASRCTDLFGIVEEYKP--PFY 223
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
68-277 4.61e-08

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: 54.25  E-value: 4.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  68 VKSLLYQILDGIHYLHANW-VLHRDLKPANILVMgegpERGRVKIADMGFA-------------RLFNSPLKPLADLDPV 133
Cdd:cd14011   116 IKYGLLQISEALSFLHNDVkLVHGNICPESVVIN----SNGEWKLAGFDFCisseqatdqfpyfREYDPNLPPLAQPNLN 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 134 vvtfwYRAPELLLGARHYTKAiDIWAIGCIFAELLTS-EPIFHCrqEDIKTSnpfhhdqldrifsvmgfpADKDWEDIRK 212
Cdd:cd14011   192 -----YLAPEYILSKTCDPAS-DMFSLGVLIYAIYNKgKPLFDC--VNNLLS------------------YKKNSNQLRQ 245
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370507705 213 MPeyptlqkdfrrttyansslikymEKHKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQE 277
Cdd:cd14011   246 LS-----------------------LSLLEKVPEELRDHVKTLLNVTPEVRPDAEQLSKIPFFDD 287
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
5-196 4.66e-08

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


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 54.56  E-value: 4.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLWHIIKFHR-------ASKANKKPMQLPRSMVKSLLY--- 73
Cdd:cd05096    68 KEVKILSRLKDPNIIRLLGVCVD--EDPLCMITEYMENgDLNQFLSSHHlddkeenGNDAVPPAHCLPAISYSSLLHval 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgeGPERgRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLLGArhYTK 153
Cdd:cd05096   146 QIASGMKYLSSLNFVHRDLATRNCLV---GENL-TIKIADFGMSRNLYAGDYYRIQGRAVLPIRWMAWECILMGK--FTT 219
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1370507705 154 AIDIWAIGCIFAELLT---SEPIFHCRQED-IKTSNPFHHDQLDRIF 196
Cdd:cd05096   220 ASDVWAFGVTLWEILMlckEQPYGELTDEQvIENAGEFFRDQGRQVY 266
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
9-177 5.76e-08

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: 54.25  E-value: 5.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   9 LLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEH-DLWHIIKFHRAskankkpMQLPRSMVKSLlyQILDGIHYLHANWV 87
Cdd:cd05602    61 LLKNVKHPFLVGLHFSFQTTD--KLYFVLDYINGgELFYHLQRERC-------FLEPRARFYAA--EIASALGYLHSLNI 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  88 LHRDLKPANILVmgegPERGRVKIADMGFARlfnSPLKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFAEL 167
Cdd:cd05602   130 VYRDLKPENILL----DSQGHIVLTDFGLCK---ENIEPNGTTSTFCGTPEYLAPE-VLHKQPYDRTVDWWCLGAVLYEM 201
                         170
                  ....*....|
gi 1370507705 168 LTSEPIFHCR 177
Cdd:cd05602   202 LYGLPPFYSR 211
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
63-275 6.30e-08

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


Pssm-ID: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 54.27  E-value: 6.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  63 LPRSMVKSLLYQILDGIHYLHANW-VLHRDLKPANILV-------------------MGEGPERG--------------- 107
Cdd:cd14217   118 LPIRCVKSIIRQVLQGLDYLHSKCkIIHTDIKPENILMcvddayvrrmaaeatewqkAGAPPPSGsavstapdllvnpld 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 108 -------RVKIADMGFARLFNSplkplaDLDPVVVTFWYRAPELLLGARHYTKAiDIWAIGCIFAELLTSEPIFHCRQED 180
Cdd:cd14217   198 prnadkiRVKIADLGNACWVHK------HFTEDIQTRQYRSIEVLIGAGYSTPA-DIWSTACMAFELATGDYLFEPHSGE 270
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 181 IKTSNpfhHDQLDRIFSVMGfpadkdwedirKMPEYPTLQKDFRRTTYANSSLIKYMEkhKVKPDSKVFLLLQK------ 254
Cdd:cd14217   271 DYSRD---EDHIAHIIELLG-----------CIPRHFALSGKYSREFFNRRGELRHIT--KLKPWSLFDVLVEKygwphe 334
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1370507705 255 -----------LLTMDPTKRITSEQALQDPYF 275
Cdd:cd14217   335 daaqftdflipMLEMVPEKRASAGECLRHPWL 366
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
5-172 6.30e-08

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 53.68  E-value: 6.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEHD-LWHIIKfhraskanKKPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14156    37 REISLLQKLSHPNIVRYLGICVK--DEKLHPILEYVSGGcLEELLA--------REELPLSWREKVELACDISRGMVYLH 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgEGPERGRVKI-ADMGFAR-LFNSPLK-PLADLDPVVVTFWYrAPELLLGaRHYTKAIDIWAI 160
Cdd:cd14156   107 SKNIYHRDLNSKNCLI--RVTPRGREAVvTDFGLAReVGEMPANdPERKLSLVGSAFWM-APEMLRG-EPYDRKVDVFSF 182
                         170
                  ....*....|..
gi 1370507705 161 GCIFAELLTSEP 172
Cdd:cd14156   183 GIVLCEILARIP 194
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
6-169 6.56e-08

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


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 53.38  E-value: 6.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlshSDRKVWLLFDYAEH-DLWHIIKfhrasKANKKPMQLPRsmVKSLLYQILDGIHYLHA 84
Cdd:cd14203    40 EAQIMKKLRHDKLVQLYAVV---SEEPIYIVTEFMSKgSLLDFLK-----DGEGKYLKLPQ--LVDMAAQIASGMAYIER 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNS-----------PLKpladldpvvvtfwYRAPELLLGARHYTK 153
Cdd:cd14203   110 MNYIHRDLRAANILV----GDNLVCKIADFGLARLIEDneytarqgakfPIK-------------WTAPEAALYGRFTIK 172
                         170
                  ....*....|....*.
gi 1370507705 154 AiDIWAIGCIFAELLT 169
Cdd:cd14203   173 S-DVWSFGILLTELVT 187
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
74-180 8.56e-08

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: 53.55  E-value: 8.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPlkpladlDPVVVTFW----YRAPELLLgAR 149
Cdd:cd05587   105 EIAVGLFFLHSKGIIYRDLKLDNVMLDAE----GHIKIADFGMCKEGIFG-------GKTTRTFCgtpdYIAPEIIA-YQ 172
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1370507705 150 HYTKAIDIWAIGCIFAELLTSEPIFHCRQED 180
Cdd:cd05587   173 PYGKSVDWWAYGVLLYEMLAGQPPFDGEDED 203
PK_STRAD_beta cd08226
Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain ...
6-103 8.63e-08

Pseudokinase domain of STE20-related kinase adapter protein beta; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity.STRAD-beta is also referred to as ALS2CR2 (Amyotrophic lateral sclerosis 2 chromosomal region candidate gene 2 protein), since the human gene encoding it is located within the juvenile ALS2 critical region on chromosome 2q33-q34. It is not linked to the development of ALS2. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. The STRAD-beta subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270864 [Multi-domain]  Cd Length: 328  Bit Score: 53.72  E-value: 8.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDrkvwllfdyaehdLWHIIKFHRASKANKK-----PMQLPRSMVKSLLYQILDGIH 80
Cdd:cd08226    49 EVVLSHFFRHPNIMTHWTVFTEGSW-------------LWVISPFMAYGSARGLlktyfPEGMNEALIGNILYGAIKALN 115
                          90       100
                  ....*....|....*....|...
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEG 103
Cdd:cd08226   116 YLHQNGCIHRSVKASHILISGDG 138
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
74-171 9.14e-08

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: 53.17  E-value: 9.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFA----RLFNSPLKPladlDPVVVTFWYrAPEL--LLG 147
Cdd:cd14062    97 QTAQGMDYLHAKNIIHRDLKSNNIFLH----EDLTVKIGDFGLAtvktRWSGSQQFE----QPTGSILWM-APEVirMQD 167
                          90       100
                  ....*....|....*....|....
gi 1370507705 148 ARHYTKAIDIWAIGCIFAELLTSE 171
Cdd:cd14062   168 ENPYSFQSDVYAFGIVLYELLTGQ 191
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
5-169 1.14e-07

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


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 52.76  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHsdRKVWLLFDYAEHDlwHIIKFHRASKANKKPMQLPRsmvksLLYQILDGIHYLHA 84
Cdd:cd05033    54 TEASIMGQFDHPNVIRLEGVVTKS--RPVMIVTEYMENG--SLDKFLRENDGKFTVTQLVG-----MLRGIASGMKYLSE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEgperGRVKIADMGFARLfnsplkpLADLDPVVVT-------FWyRAPElLLGARHYTKAIDI 157
Cdd:cd05033   125 MNYVHRDLAARNILVNSD----LVCKVSDFGLSRR-------LEDSEATYTTkggkipiRW-TAPE-AIAYRKFTSASDV 191
                         170
                  ....*....|..
gi 1370507705 158 WAIGCIFAELLT 169
Cdd:cd05033   192 WSFGIVMWEVMS 203
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
5-174 1.20e-07

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: 52.65  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVwlLFDYAEH-DLWHIIkfhraskANKKPMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd14060    31 KEAEILSVLSHRNIIQFYGAILEAPNYGI--VTEYASYgSLFDYL-------NSNESEEMDMDQIMTWATDIAKGMHYLH 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANW---VLHRDLKPANILVMGEGPergrVKIADMGFARLFNSPLKPladldPVVVTFWYRAPELLLGARhYTKAIDIWAI 160
Cdd:cd14060   102 MEApvkVIHRDLKSRNVVIAADGV----LKICDFGASRFHSHTTHM-----SLVGTFPWMAPEVIQSLP-VSETCDTYSY 171
                         170
                  ....*....|....
gi 1370507705 161 GCIFAELLTSEPIF 174
Cdd:cd14060   172 GVVLWEMLTREVPF 185
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
9-177 1.41e-07

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: 53.09  E-value: 1.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   9 LLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLWhiikFHraskankkpMQLPRSM--VKSLLY--QILDGIHYLH 83
Cdd:cd05575    49 LLKNVKHPFLVGLHYSF--QTKDKLYFVLDYVNGgELF----FH---------LQRERHFpePRARFYaaEIASALGYLH 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMGEgperGRVKIADMGfarLFNSPLKPLADLDPVVVTFWYRAPELLLgARHYTKAIDIWAIGCI 163
Cdd:cd05575   114 SLNIIYRDLKPENILLDSQ----GHVVLTDFG---LCKEGIEPSDTTSTFCGTPEYLAPEVLR-KQPYDRTVDWWCLGAV 185
                         170
                  ....*....|....
gi 1370507705 164 FAELLTSEPIFHCR 177
Cdd:cd05575   186 LYEMLYGLPPFYSR 199
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
6-264 1.48e-07

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: 53.09  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHsDRKVWLLfDYAEH-DLWhiikFHraskankkpmqLPRSMV----KSLLY--QILDG 78
Cdd:cd05595    45 ESRVLQNTRHPFLTALKYAFQTH-DRLCFVM-EYANGgELF----FH-----------LSRERVftedRARFYgaEIVSA 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARlfnSPLKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIW 158
Cdd:cd05595   108 LEYLHSRDVVYRDIKLENLML----DKDGHIKITDFGLCK---EGITDGATMKTFCGTPEYLAPE-VLEDNDYGRAVDWW 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 159 AIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFSVMGFpadkdwEDIRkmpeyptlqkdFRRTtyansslikyme 238
Cdd:cd05595   180 GLGVVMYEMMCGRL-------------PFYNQDHERLFELILM------EEIR-----------FPRT------------ 217
                         250       260
                  ....*....|....*....|....*.
gi 1370507705 239 khkVKPDSKVflLLQKLLTMDPTKRI 264
Cdd:cd05595   218 ---LSPEAKS--LLAGLLKKDPKQRL 238
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
63-174 1.48e-07

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: 52.79  E-value: 1.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  63 LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGegpeRGRVKIADMGFARLfnsPLKPLA--------DLDP-- 132
Cdd:cd05609    97 LPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITS----MGHIKLTDFGLSKI---GLMSLTtnlyeghiEKDTre 169
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370507705 133 -----VVVTFWYRAPELLLgARHYTKAIDIWAIGCIFAELLTSEPIF 174
Cdd:cd05609   170 fldkqVCGTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEFLVGCVPF 215
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
6-169 1.61e-07

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: 52.20  E-value: 1.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlshSDRKVWLLFDYAEHDlwHIIKFHRASKANKkpmqLPRSMVKSLLYQILDGIHYLHAN 85
Cdd:cd05067    52 EANLMKQLQHQRLVRLYAVV---TQEPIYIITEYMENG--SLVDFLKTPSGIK----LTINKLLDMAAQIAEGMAFIEER 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVmgegPERGRVKIADMGFARLFNS-----------PLKpladldpvvvtfwYRAPELL-LGArhYTK 153
Cdd:cd05067   123 NYIHRDLRAANILV----SDTLSCKIADFGLARLIEDneytaregakfPIK-------------WTAPEAInYGT--FTI 183
                         170
                  ....*....|....*.
gi 1370507705 154 AIDIWAIGCIFAELLT 169
Cdd:cd05067   184 KSDVWSFGILLTEIVT 199
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
9-175 1.87e-07

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: 52.40  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   9 LLRELKHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLwhiikFHRASKAnkkpMQLPRSMVKSLLYQILDGIHYLHANWV 87
Cdd:cd05582    50 ILADVNHPFIVKLHYAF--QTEGKLYLILDFLRGgDL-----FTRLSKE----VMFTEEDVKFYLAELALALDHLHSLGI 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  88 LHRDLKPANILVmgegPERGRVKIADMGFARlfnsplKPLADLDPVVV---TFWYRAPElLLGARHYTKAIDIWAIGCIF 164
Cdd:cd05582   119 IYRDLKPENILL----DEDGHIKLTDFGLSK------ESIDHEKKAYSfcgTVEYMAPE-VVNRRGHTQSADWWSFGVLM 187
                         170
                  ....*....|.
gi 1370507705 165 AELLTSEPIFH 175
Cdd:cd05582   188 FEMLTGSLPFQ 198
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
6-169 1.87e-07

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: 52.26  E-value: 1.87e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEHDLwhIIKFHRASKAnkkpmQLPRSMVKSLLYQILDGIHYLHAN 85
Cdd:cd05112    49 EAEVMMKLSHPKLVQLYGVCLEQA--PICLVFEFMEHGC--LSDYLRTQRG-----LFSAETLLGMCLDVCEGMAYLEEA 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVmgegPERGRVKIADMGFAR--LFNSPLKPLADLDPVVvtfwYRAPELLLGARHYTKAiDIWAIGCI 163
Cdd:cd05112   120 SVIHRDLAARNCLV----GENQVVKVSDFGMTRfvLDDQYTSSTGTKFPVK----WSSPEVFSFSRYSSKS-DVWSFGVL 190

                  ....*.
gi 1370507705 164 FAELLT 169
Cdd:cd05112   191 MWEVFS 196
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
4-168 1.93e-07

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: 52.29  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELK-HPNVIalqKVFLSHSDR------KVWLLFDYAEHDlwHIIKFHRASKANKkpmqLPRSMVKSLLYQIL 76
Cdd:cd14037    48 KREIEIMKRLSgHKNIV---GYIDSSANRsgngvyEVLLLMEYCKGG--GVIDLMNQRLQTG----LTESEILKIFCDVC 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  77 DGIHYLHA--NWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLDPVV------VTFWYRAPEL--LL 146
Cdd:cd14037   119 EAVAAMHYlkPPLIHRDLKVENVLI----SDSGNYKLCDFGSATTKILPPQTKQGVTYVEedikkyTTLQYRAPEMidLY 194
                         170       180
                  ....*....|....*....|..
gi 1370507705 147 GARHYTKAIDIWAIGCIFAELL 168
Cdd:cd14037   195 RGKPITEKSDIWALGCLLYKLC 216
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
74-180 2.05e-07

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: 52.69  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARlfnsplkpLADLDPVVV-TFW----YRAPElLLGA 148
Cdd:cd05616   109 EIAIGLFFLQSKGIIYRDLKLDNVMLDSE----GHIKIADFGMCK--------ENIWDGVTTkTFCgtpdYIAPE-IIAY 175
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370507705 149 RHYTKAIDIWAIGCIFAELLTSEPIFHCRQED 180
Cdd:cd05616   176 QPYGKSVDWWAFGVLLYEMLAGQAPFEGEDED 207
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
6-169 2.42e-07

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: 51.97  E-value: 2.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLShsDRKVWLLFDY-AEHDLWHIIKFHRASKankkpMQLPRSMVKSLlyQILDGIHYLHA 84
Cdd:cd05072    52 EANLMKTLQHDKLVRLYAVVTK--EEPIYIITEYmAKGSLLDFLKSDEGGK-----VLLPKLIDFSA--QIAEGMAYIER 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNS-----------PLKpladldpvvvtfwYRAPELL-LGArhYT 152
Cdd:cd05072   123 KNYIHRDLRAANVLV----SESLMCKIADFGLARVIEDneytaregakfPIK-------------WTAPEAInFGS--FT 183
                         170
                  ....*....|....*..
gi 1370507705 153 KAIDIWAIGCIFAELLT 169
Cdd:cd05072   184 IKSDVWSFGILLYEIVT 200
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
5-169 2.48e-07

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: 52.00  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlshSDRKVWLLFDY-AEHDLWHIIKfhrasKANKKPMQLPRsmVKSLLYQILDGIHYLH 83
Cdd:cd05069    56 QEAQIMKKLRHDKLVPLYAVV---SEEPIYIVTEFmGKGSLLDFLK-----EGDGKYLKLPQ--LVDMAAQIADGMAYIE 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFARLF--NSPLKPLADLDPVVVTfwyrAPELLLGARHYTKAiDIWAIG 161
Cdd:cd05069   126 RMNYIHRDLRAANILV----GDNLVCKIADFGLARLIedNEYTARQGAKFPIKWT----APEAALYGRFTIKS-DVWSFG 196

                  ....*...
gi 1370507705 162 CIFAELLT 169
Cdd:cd05069   197 ILLTELVT 204
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
5-169 2.51e-07

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: 51.64  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKV------------FLSHSDrkvwlLFDYAEHDlwhiikfhraskanKKPMQLPRSMvkSLL 72
Cdd:cd05068    52 REAQIMKKLRHPKLIQLYAVctleepiyiiteLMKHGS-----LLEYLQGK--------------GRSLQLPQLI--DMA 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  73 YQILDGIHYLHANWVLHRDLKPANILVmGEGperGRVKIADMGFARLFNS------------PLKpladldpvvvtfWyR 140
Cdd:cd05068   111 AQVASGMAYLESQNYIHRDLAARNVLV-GEN---NICKVADFGLARVIKVedeyearegakfPIK------------W-T 173
                         170       180
                  ....*....|....*....|....*....
gi 1370507705 141 APELLLGARHYTKAiDIWAIGCIFAELLT 169
Cdd:cd05068   174 APEAANYNRFSIKS-DVWSFGILLTEIVT 201
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
15-275 2.66e-07

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 51.58  E-value: 2.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  15 HPNVIALQKVFLShsDRKVWLLFDYAEHDLwhiikfHRASKANKKpmqLPRSMVKSLLYQILDGIHYLHANWVLHRDLKP 94
Cdd:cd14022    44 HSNINQITEIILG--ETKAYVFFERSYGDM------HSFVRTCKK---LREEEAARLFYQIASAVAHCHDGGLVLRDLKL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  95 ANILVMGEgpERGRVKIADMGFARLFNSPLKPLADLDPVVVtfwYRAPELLLGARHYT-KAIDIWAIGCIFAELLTSEPI 173
Cdd:cd14022   113 RKFVFKDE--ERTRVKLESLEDAYILRGHDDSLSDKHGCPA---YVSPEILNTSGSYSgKAADVWSLGVMLYTMLVGRYP 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 174 FHcrqeDIKTSNPFhhdqldrifsvmgfpadkdwEDIRK----MPEyptlqkdfrrttyansslikymekhKVKPDSKVf 249
Cdd:cd14022   188 FH----DIEPSSLF--------------------SKIRRgqfnIPE-------------------------TLSPKAKC- 217
                         250       260
                  ....*....|....*....|....*.
gi 1370507705 250 lLLQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14022   218 -LIRSILRREPSERLTSQEILDHPWF 242
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
14-169 3.36e-07

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: 51.89  E-value: 3.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  14 KHPNVIALQKVflSHSDRKVWLLFDYAEH-DLWHIIKFHR---------ASKANKKPMQLPrSMVkSLLYQILDGIHYLH 83
Cdd:cd05099    76 KHKNIINLLGV--CTQEGPLYVIVEYAAKgNLREFLRARRppgpdytfdITKVPEEQLSFK-DLV-SCAYQVARGMEYLE 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgegpERGRVKIADMGFARlfnsplkPLADLD----------PVVvtfwYRAPELLLGaRHYTK 153
Cdd:cd05099   152 SRRCIHRDLAARNVLVT----EDNVMKIADFGLAR-------GVHDIDyykktsngrlPVK----WMAPEALFD-RVYTH 215
                         170
                  ....*....|....*.
gi 1370507705 154 AIDIWAIGCIFAELLT 169
Cdd:cd05099   216 QSDVWSFGILMWEIFT 231
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
74-172 4.21e-07

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: 51.16  E-value: 4.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGegperGRVKIADMGFARLFNSPLKPLADLDPvvvTFWYRAPELLLGARHYTK 153
Cdd:cd13995   104 HVLKGLDFLHSKNIIHHDIKPSNIVFMS-----TKAVLVDFGLSVQMTEDVYVPKDLRG---TEIYMSPEVILCRGHNTK 175
                          90
                  ....*....|....*....
gi 1370507705 154 AiDIWAIGCIFAELLTSEP 172
Cdd:cd13995   176 A-DIYSLGATIIHMQTGSP 193
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
5-169 4.40e-07

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: 50.96  E-value: 4.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRkvWLLFDY-AEHDLWHIIkfhRASKANKKPMQLPRSMVKSLlyQILDGIHYLH 83
Cdd:cd14664    39 AEIQTLGMIRHRNIVRLRGYCSNPTTN--LLVYEYmPNGSLGELL---HSRPESQPPLDWETRQRIAL--GSARGLAYLH 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 AN---WVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplKPLADLDPVVVTFWYRAPELLLGARHYTKAiDIWAI 160
Cdd:cd14664   112 HDcspLIIHRDVKSNNILL----DEEFEAHVADFGLAKLMDD--KDSHVMSSVAGSYGYIAPEYAYTGKVSEKS-DVYSY 184

                  ....*....
gi 1370507705 161 GCIFAELLT 169
Cdd:cd14664   185 GVVLLELIT 193
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
57-120 4.50e-07

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


Pssm-ID: 270919 [Multi-domain]  Cd Length: 263  Bit Score: 51.10  E-value: 4.50e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370507705  57 NKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANIlVMGEGPERGR-VKIADMGFARLF 120
Cdd:cd14017    88 SQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNF-AIGRGPSDERtVYILDFGLARQY 151
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
71-120 4.53e-07

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: 50.92  E-value: 4.53e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370507705  71 LLYQILDGIHYLHANWVLHRDLKPANILvMGEGPERGRVKIADMGFARLF 120
Cdd:cd14016   101 LADQMISRLEYLHSKGYIHRDIKPENFL-MGLGKNSNKVYLIDFGLAKKY 149
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
5-169 4.66e-07

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: 51.18  E-value: 4.66e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEH-DLW-----HIIKFHRASKANKKPmqLPRSMvksLLY---QI 75
Cdd:cd05051    68 KEVKIMSQLKDPNIVRLLGVCTR--DEPLCMIVEYMENgDLNqflqkHEAETQGASATNSKT--LSYGT---LLYmatQI 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  76 LDGIHYLHA-NWVlHRDLKPANILVmgeGPeRGRVKIADMGFAR-LFNS-----------PLKPLAdldpvvvtfWyrap 142
Cdd:cd05051   141 ASGMKYLESlNFV-HRDLATRNCLV---GP-NYTIKIADFGMSRnLYSGdyyriegravlPIRWMA---------W---- 202
                         170       180
                  ....*....|....*....|....*..
gi 1370507705 143 ELLLGARhYTKAIDIWAIGCIFAELLT 169
Cdd:cd05051   203 ESILLGK-FTTKSDVWAFGVTLWEILT 228
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
6-163 5.43e-07

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: 50.77  E-value: 5.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDrKVWLLFDYAEHDLwhiikFHRASKANKKPMQlpRSMVKSLLyQILDGIHYLHAN 85
Cdd:cd14191    49 EISIMNCLHHPKLVQCVDAFEEKAN-IVMVLEMVSGGEL-----FERIIDEDFELTE--RECIKYMR-QISEGVEYIHKQ 119
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370507705  86 WVLHRDLKPANILVMGEgpERGRVKIADMGFARLFNSPlkplADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCI 163
Cdd:cd14191   120 GIVHLDLKPENIMCVNK--TGTKIKLIDFGLARRLENA----GSLKVLFGTPEFVAPE-VINYEPIGYATDMWSIGVI 190
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
78-183 7.33e-07

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: 50.69  E-value: 7.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARlfnsPLKPLADLDPVVVTFWYRAPELLLgARHYTKAIDI 157
Cdd:cd05599   113 AIESIHKLGYIHRDIKPDNLLL----DARGHIKLSDFGLCT----GLKKSHLAYSTVGTPDYIAPEVFL-QKGYGKECDW 183
                          90       100
                  ....*....|....*....|....*.
gi 1370507705 158 WAIGCIFAELLTSEPIFhCRQEDIKT 183
Cdd:cd05599   184 WSLGVIMYEMLIGYPPF-CSDDPQET 208
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
74-169 7.43e-07

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: 50.49  E-value: 7.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgEGPErgRVKIADMGFARLFNSPLKPLADLDPVVVTFWYrAPELLLgARHYTK 153
Cdd:cd05057   117 QIAKGMSYLEEKRLVHRDLAARNVLV--KTPN--HVKITDFGLAKLLDVDEKEYHAEGGKVPIKWM-ALESIQ-YRIYTH 190
                          90
                  ....*....|....*.
gi 1370507705 154 AIDIWAIGCIFAELLT 169
Cdd:cd05057   191 KSDVWSYGVTVWELMT 206
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
70-169 7.58e-07

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: 50.78  E-value: 7.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  70 SLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYrAPELLLGaR 149
Cdd:cd05101   150 SCTYQLARGMEYLASQKCIHRDLAARNVLVT----ENNVMKIADFGLARDINNIDYYKKTTNGRLPVKWM-APEALFD-R 223
                          90       100
                  ....*....|....*....|
gi 1370507705 150 HYTKAIDIWAIGCIFAELLT 169
Cdd:cd05101   224 VYTHQSDVWSFGVLMWEIFT 243
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
2-169 7.85e-07

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: 50.45  E-value: 7.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   2 SACREIALLRELKHPNVIALQKVFlshSDRKVWLLFDYAEHDlwHIIKFHRASKAnkKPMQLPRsmVKSLLYQILDGIHY 81
Cdd:cd05070    50 SFLEEAQIMKKLKHDKLVQLYAVV---SEEPIYIVTEYMSKG--SLLDFLKDGEG--RALKLPN--LVDMAAQVAAGMAY 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmGEGPergRVKIADMGFARLF--NSPLKPLADLDPVVVTfwyrAPELLLGARHYTKAiDIWA 159
Cdd:cd05070   121 IERMNYIHRDLRSANILV-GNGL---ICKIADFGLARLIedNEYTARQGAKFPIKWT----APEAALYGRFTIKS-DVWS 191
                         170
                  ....*....|
gi 1370507705 160 IGCIFAELLT 169
Cdd:cd05070   192 FGILLTELVT 201
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
6-169 8.04e-07

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: 50.41  E-value: 8.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlshSDRKVWLLFDYAEHDlwHIIKFHRASKANKKPmqLPRSMVKSLlyQILDGIHYLHAN 85
Cdd:cd05073    56 EANVMKTLQHDKLVKLHAVV---TKEPIYIITEFMAKG--SLLDFLKSDEGSKQP--LPKLIDFSA--QIAEGMAFIEQR 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFA 165
Cdd:cd05073   127 NYIHRDLRAANILV----SASLVCKIADFGLARVIED--NEYTAREGAKFPIKWTAPE-AINFGSFTIKSDVWSFGILLM 199

                  ....
gi 1370507705 166 ELLT 169
Cdd:cd05073   200 EIVT 203
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
5-169 8.12e-07

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: 50.11  E-value: 8.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKV------------FLSHSDrkvwlLFDYaehdlwhiikFHRASKANKKPMqlprsmvkSLL 72
Cdd:cd05052    51 KEAAVMKEIKHPNLVQLLGVctreppfyiiteFMPYGN-----LLDY----------LRECNREELNAV--------VLL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  73 Y---QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNS-----------PLKpladldpvvvtfw 138
Cdd:cd05052   108 YmatQIASAMEYLEKKNFIHRDLAARNCLV----GENHLVKVADFGLSRLMTGdtytahagakfPIK------------- 170
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1370507705 139 YRAPELLLGARHYTKAiDIWAIGCIFAELLT 169
Cdd:cd05052   171 WTAPESLAYNKFSIKS-DVWAFGVLLWEIAT 200
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
5-169 8.38e-07

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: 50.30  E-value: 8.38e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLsHSDRKVWL-----LFDYAEHDLWHiiKFHRASKANKKPMQLPRSMVKSLLYQILDGI 79
Cdd:cd05074    60 REAACMKEFDHPNVIKLIGVSL-RSRAKGRLpipmvILPFMKHGDLH--TFLLMSRIGEEPFTLPLQTLVRFMIDIASGM 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNS------------PLKPLAdLDPvvvtfwyrapellLG 147
Cdd:cd05074   137 EYLSSKNFIHRDLAARNCML----NENMTVCVADFGLSKKIYSgdyyrqgcasklPVKWLA-LES-------------LA 198
                         170       180
                  ....*....|....*....|..
gi 1370507705 148 ARHYTKAIDIWAIGCIFAELLT 169
Cdd:cd05074   199 DNVYTTHSDVWAFGVTMWEIMT 220
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
74-169 8.86e-07

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


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 50.41  E-value: 8.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgEGPErgRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPELLlgARHYTK 153
Cdd:cd05108   117 QIAKGMNYLEDRRLVHRDLAARNVLV--KTPQ--HVKITDFGLAKLLGAEEKEYHAEGGKVPIKWMALESIL--HRIYTH 190
                          90
                  ....*....|....*.
gi 1370507705 154 AIDIWAIGCIFAELLT 169
Cdd:cd05108   191 QSDVWSYGVTVWELMT 206
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
63-168 8.89e-07

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: 50.20  E-value: 8.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  63 LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEGperGRVKIADMGFA-RLFNSPLKPLADLDPVVV-TFWYR 140
Cdd:cd13991    95 LPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDG---SDAFLCDFGHAeCLDPDGLGKSLFTGDYIPgTETHM 171
                          90       100
                  ....*....|....*....|....*...
gi 1370507705 141 APELLLGARHYTKAiDIWAIGCIFAELL 168
Cdd:cd13991   172 APEVVLGKPCDAKV-DVWSSCCMMLHML 198
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
1-192 9.61e-07

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: 50.57  E-value: 9.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   1 MSACREIALLRelKHPNVIALQKVFLShSDRkvwlLFDYAEH----DLwhIIKFHRASKANKkpmqlPRSMVKSLlyQIL 76
Cdd:cd05591    43 MTEKRILALAA--KHPFLTALHSCFQT-KDR----LFFVMEYvnggDL--MFQIQRARKFDE-----PRARFYAA--EVT 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  77 DGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARlfnsplKPLADlDPVVVTFW----YRAPElLLGARHYT 152
Cdd:cd05591   107 LALMFLHRHGVIYRDLKLDNILLDAE----GHCKLADFGMCK------EGILN-GKTTTTFCgtpdYIAPE-ILQELEYG 174
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370507705 153 KAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPFHHDQL 192
Cdd:cd05591   175 PSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVL 214
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
4-189 9.79e-07

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: 49.84  E-value: 9.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRELKHPNVIALQKVFLSHSDrKVWLLFDYAEHDlwhiiKFHRASKANKKPMQLPRSMVKSLlyQILDGIHYLH 83
Cdd:cd14064    39 CREVSILCRLNHPCVIQFVGACLDDPS-QFAIVTQYVSGG-----SLFSLLHEQKRVIDLQSKLIIAV--DVAKGMEYLH 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 --ANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSplkpladLDPVVVT-----FWYRAPELLLGARHYTKAID 156
Cdd:cd14064   111 nlTQPIIHRDLNSHNILLY----EDGHAVVADFGESRFLQS-------LDEDNMTkqpgnLRWMAPEVFTQCTRYSIKAD 179
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370507705 157 IWAIGCIFAELLTSE-PIFHCRQEDIKTSNPFHH 189
Cdd:cd14064   180 VFSYALCLWELLTGEiPFAHLKPAAAAADMAYHH 213
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
5-180 1.10e-06

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 50.03  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIAlqkvFLSHSDRKVWLlfdyaEHDLWHIIKFH-RAS-----KAN----KKPMQLPRSMVKsllyq 74
Cdd:cd14140    38 REIFSTPGMKHENLLQ----FIAAEKRGSNL-----EMELWLITAFHdKGSltdylKGNivswNELCHIAETMAR----- 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ildGIHYLHAN--W---------VLHRDLKPANILVMGEGPergrVKIADMGFARLFnSPLKPLADLDPVVVTFWYRAPE 143
Cdd:cd14140   104 ---GLSYLHEDvpRckgeghkpaIAHRDFKSKNVLLKNDLT----AVLADFGLAVRF-EPGKPPGDTHGQVGTRRYMAPE 175
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1370507705 144 LLLGARHYTK----AIDIWAIGCIFAELLTsepifHCRQED 180
Cdd:cd14140   176 VLEGAINFQRdsflRIDMYAMGLVLWELVS-----RCKAAD 211
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
6-172 1.32e-06

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: 49.62  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKH-PNVIALQKVFLSHS----DRKVWLLFDY-AEHDLWHIIKfhraskaNKKPMQLPRSMVKSLLYQILDGI 79
Cdd:cd06636    62 EINMLKKYSHhRNIATYYGAFIKKSppghDDQLWLVMEFcGAGSVTDLVK-------NTKGNALKEDWIAYICREILRGL 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNsplKPLADLDPVVVTFWYRAPELLLGARH----YTKAI 155
Cdd:cd06636   135 AHLHAHKVIHRDIKGQNVLLT----ENAEVKLVDFGVSAQLD---RTVGRRNTFIGTPYWMAPEVIACDENpdatYDYRS 207
                         170
                  ....*....|....*..
gi 1370507705 156 DIWAIGCIFAELLTSEP 172
Cdd:cd06636   208 DIWSLGITAIEMAEGAP 224
PLN03225 PLN03225
Serine/threonine-protein kinase SNT7; Provisional
58-149 1.39e-06

Serine/threonine-protein kinase SNT7; Provisional


Pssm-ID: 215638 [Multi-domain]  Cd Length: 566  Bit Score: 50.56  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  58 KKPMQLPRS------MVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFArlfnsplkplADLD 131
Cdd:PLN03225  241 GKVQDLPKGlerenkIIQTIMRQILFALDGLHSTGIVHRDVKPQNIIF---SEGSGSFKIIDLGAA----------ADLR 307
                          90
                  ....*....|....*...
gi 1370507705 132 pvvVTFWYRAPELLLGAR 149
Cdd:PLN03225  308 ---VGINYIPKEFLLDPR 322
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
5-169 1.40e-06

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: 49.26  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdrkVWLLFDYAE-HDLWHIIKFHRASkankkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd05040    47 KEVNAMHSLDHPNLIRLYGVVLSSP---LMMVTELAPlGSLLDRLRKDQGH--------FLISTLCDYAVQIANGMAYLE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgegpERGRVKIADMGFAR---------LFNSPLKpladldpvvVTFWYRAPElLLGARHYTKA 154
Cdd:cd05040   116 SKRFIHRDLAARNILLA----SKDKVKIGDFGLMRalpqnedhyVMQEHRK---------VPFAWCAPE-SLKTRKFSHA 181
                         170
                  ....*....|....*
gi 1370507705 155 IDIWAIGCIFAELLT 169
Cdd:cd05040   182 SDVWMFGVTLWEMFT 196
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
4-174 1.57e-06

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


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 49.56  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   4 CREIALLRE--LKHPNVIALQKVFLShsDRKVWLLFDYAEHDLwhiikFHRASKankKPMQlprSMV--KSLLYQILDGI 79
Cdd:cd13980    44 KQRLEEIRDrlLELPNVLPFQKVIET--DKAAYLIRQYVKYNL-----YDRIST---RPFL---NLIekKWIAFQLLHAL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  80 HYLHANWVLHRDLKPANILVMGEGpergRVKIADmgFArlfnsPLKP--LADLDPVVVTFW---------YRAPELLLGA 148
Cdd:cd13980   111 NQCHKRGVCHGDIKTENVLVTSWN----WVYLTD--FA-----SFKPtyLPEDNPADFSYFfdtsrrrtcYIAPERFVDA 179
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1370507705 149 RHY-----------TKAIDIWAIGCIFAELLTSE-PIF 174
Cdd:cd13980   180 LTLdaeserrdgelTPAMDIFSLGCVIAELFTEGrPLF 217
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
50-225 1.59e-06

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: 49.68  E-value: 1.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  50 FHRASKANKKPMqlPRSMVKSLLYQILDGIHYLHANW-VLHRDLKPANILVmgegPERGRVKIADMGFA-RLFNSPLKPL 127
Cdd:cd06618   100 LDKLLKRIQGPI--PEDILGKMTVSIVKALHYLKEKHgVIHRDVKPSNILL----DESGNVKLCDFGISgRLVDSKAKTR 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 128 ADLDPVvvtfwYRAPELLLGARH--YTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPFHHDQLDRIFSVMGFPAD- 204
Cdd:cd06618   174 SAGCAA-----YMAPERIDPPDNpkYDIRADVWSLGISLVELATGQFPYRNCKTEFEVLTKILNEEPPSLPPNEGFSPDf 248
                         170       180
                  ....*....|....*....|....*...
gi 1370507705 205 KDW------EDIRKMPEYPTL-QKDFRR 225
Cdd:cd06618   249 CSFvdlcltKDHRYRPKYRELlQHPFIR 276
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
78-174 1.64e-06

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: 49.61  E-value: 1.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANWVLHRDLKPANILVMGEgperGRVKIAD-------MGFARLFNsplkpladldpvvvTFW----YRAPELLL 146
Cdd:cd05589   113 GLQFLHEHKIVYRDLKLDNLLLDTE----GYVKIADfglckegMGFGDRTS--------------TFCgtpeFLAPEVLT 174
                          90       100
                  ....*....|....*....|....*...
gi 1370507705 147 gARHYTKAIDIWAIGCIFAELLTSEPIF 174
Cdd:cd05589   175 -DTSYTRAVDWWGLGVLIYEMLVGESPF 201
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
32-167 1.82e-06

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: 49.40  E-value: 1.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  32 KVWLLFDYaeHDLWHIIKFHRASKANKKPMQLprsmvksLLYQILDGIHYLHAN--------WVLHRDLKPANILVmgeg 103
Cdd:cd14144    67 QLYLITDY--HENGSLYDFLRGNTLDTQSMLK-------LAYSAACGLAHLHTEifgtqgkpAIAHRDIKSKNILV---- 133
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370507705 104 PERGRVKIADMGFARLFNSPLKPLaDL--DPVVVTFWYRAPELL---LGARHYT--KAIDIWAIGCIFAEL 167
Cdd:cd14144   134 KKNGTCCIADLGLAVKFISETNEV-DLppNTRVGTKRYMAPEVLdesLNRNHFDayKMADMYSFGLVLWEI 203
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
62-175 1.85e-06

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: 50.01  E-value: 1.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  62 QLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADmgfarlFNSPLKPLAD----LDPVVVTF 137
Cdd:cd05624   169 KLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLL----DMNGHIRLAD------FGSCLKMNDDgtvqSSVAVGTP 238
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370507705 138 WYRAPELLL----GARHYTKAIDIWAIGCIFAELLTSEPIFH 175
Cdd:cd05624   239 DYISPEILQamedGMGKYGPECDWWSLGVCMYEMLYGETPFY 280
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
74-181 1.89e-06

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: 49.13  E-value: 1.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFArlfnSPLKPLADLDPVVVTFWYRAPELLLgARHYTK 153
Cdd:cd05607   112 QITCGILHLHSLKIVYRDMKPENVLL----DDNGNCRLSDLGLA----VEVKEGKPITQRAGTNGYMAPEILK-EESYSY 182
                          90       100
                  ....*....|....*....|....*...
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFHCRQEDI 181
Cdd:cd05607   183 PVDWFAMGCSIYEMVAGRTPFRDHKEKV 210
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
5-180 2.08e-06

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: 49.01  E-value: 2.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRkvwllfdyaeHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd14155    37 REVQLMNRLSHPNILRFMGVCVHQGQL----------HALTEYINGGNLEQLLDSNEPLSWTVRVKLALDIARGLSYLHS 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEgpERGRVKI-ADMGFARLF------NSPLkpladldPVVVTFWYRAPELLLGARHYTKAiDI 157
Cdd:cd14155   107 KGIFHRDLTSKNCLIKRD--ENGYTAVvGDFGLAEKIpdysdgKEKL-------AVVGSPYWMAPEVLRGEPYNEKA-DV 176
                         170       180
                  ....*....|....*....|....*.
gi 1370507705 158 WAIGCIFAEL---LTSEPIFHCRQED 180
Cdd:cd14155   177 FSYGIILCEIiarIQADPDYLPRTED 202
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
5-275 2.23e-06

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: 48.66  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdRKVWLLFDYAEHDLWHIIKFHRASKANKKpmqlprSMVKSLLYQILDGIHYLHA 84
Cdd:cd14109    45 REVDIHNSLDHPNIVQMHDAYDDEK-LAVTVIDNLASTIELVRDNLLPGKDYYTE------RQVAVFVRQLLLALKHMHD 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMGEgpergRVKIADMGFARLFNsplkpladlDPVVVTFWYRAPEL----LLGARHYTKAIDIWAI 160
Cdd:cd14109   118 LGIAHLDLRPEDILLQDD-----KLKLADFGQSRRLL---------RGKLTTLIYGSPEFvspeIVNSYPVTLATDMWSV 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 161 GCIFAELLTSepifhcrqediktSNPFHhdqldrifsvmgfpADKDWEDIRKMPEYptlQKDFRRTTYANSSlikymekh 240
Cdd:cd14109   184 GVLTYVLLGG-------------ISPFL--------------GDNDRETLTNVRSG---KWSFDSSPLGNIS-------- 225
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1370507705 241 kvkPDSKVFLllQKLLTMDPTKRITSEQALQDPYF 275
Cdd:cd14109   226 ---DDARDFI--KKLLVYIPESRLTVDEALNHPWF 255
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
58-275 2.33e-06

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: 49.36  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  58 KKPMQLPRS------MVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgeGPERGRVKIADMGFA---RL-FN-SPLKP 126
Cdd:cd14013   106 GRVLIPPRGpkrenvIIKSIMRQILVALRKLHSTGIVHRDVKPQNIIV---SEGDGQFKIIDLGAAadlRIgINyIPKEF 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 127 LadLDPVvvtfwYRAPELLLGARHYTKAIDIwaigcIFAELLTsePIFHcrqediKTSNPfhhDQLDrIFSV------MG 200
Cdd:cd14013   183 L--LDPR-----YAPPEQYIMSTQTPSAPPA-----PVAAALS--PVLW------QMNLP---DRFD-MYSAgvillqMA 238
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 201 FPADKDWEDIRKmpeyptLQKDFRRTTYansSLIKYMEKHKVKPDSKV--------------FLLLQKLLTMDPTKRITS 266
Cdd:cd14013   239 FPNLRSDSNLIA------FNRQLKQCDY---DLNAWRMLVEPRASADLregfeildlddgagWDLVTKLIRYKPRGRLSA 309

                  ....*....
gi 1370507705 267 EQALQDPYF 275
Cdd:cd14013   310 SAALAHPYF 318
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
5-180 2.42e-06

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: 49.00  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALqkVFLSHSDRKVWLLFDYAehDLWHIIKFHRASKA---NKKPMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd05046    57 RELDMFRKLSHKNVVRL--LGLCREAEPHYMILEYT--DLGDLKQFLRATKSkdeKLKPPPLSTKQKVALCTQIALGMDH 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEgperGRVKIADMGFAR--------LFNSPLKPLAdldpvvvtfWYrAPELLLGARHYTK 153
Cdd:cd05046   133 LSNARFVHRDLAARNCLVSSQ----REVKVSLLSLSKdvynseyyKLRNALIPLR---------WL-APEAVQEDDFSTK 198
                         170       180
                  ....*....|....*....|....*..
gi 1370507705 154 AiDIWAIGCIFAELLTSEPIFHCRQED 180
Cdd:cd05046   199 S-DVWSFGVLMWEVFTQGELPFYGLSD 224
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
79-175 2.56e-06

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: 49.11  E-value: 2.56e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARL--------------------------------------- 119
Cdd:cd05610   117 LDYLHRHGIIHRDLKPDNMLISNE----GHIKLTDFGLSKVtlnrelnmmdilttpsmakpkndysrtpgqvlslisslg 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370507705 120 FNSPLK-----------PLADLDPVVVTFWYRAPELLLGARHyTKAIDIWAIGCIFAELLTSEPIFH 175
Cdd:cd05610   193 FNTPTPyrtpksvrrgaARVEGERILGTPDYLAPELLLGKPH-GPAVDWWALGVCLFEFLTGIPPFN 258
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
74-169 2.59e-06

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: 48.88  E-value: 2.59e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEGPergrVKIADMGFARLFNSplkpladldpvvvTFWYR------------A 141
Cdd:cd05032   127 EIADGMAYLAAKKFVHRDLAARNCMVAEDLT----VKIGDFGMTRDIYE-------------TDYYRkggkgllpvrwmA 189
                          90       100
                  ....*....|....*....|....*...
gi 1370507705 142 PELLLGARhYTKAIDIWAIGCIFAELLT 169
Cdd:cd05032   190 PESLKDGV-FTTKSDVWSFGVVLWEMAT 216
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
15-174 2.62e-06

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: 49.26  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  15 HPNVIALQKVFLSHSdrKVWLLFDYAEH-DLwhiiKFHRaskanKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLK 93
Cdd:cd05618    80 HPFLVGLHSCFQTES--RLFFVIEYVNGgDL----MFHM-----QRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLK 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  94 PANILVMGEgperGRVKIADMGFARlfnSPLKPLADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCIFAELLTSEPI 173
Cdd:cd05618   149 LDNVLLDSE----GHIKLTDYGMCK---EGLRPGDTTSTFCGTPNYIAPEILRG-EDYGFSVDWWALGVLMFEMMAGRSP 220

                  .
gi 1370507705 174 F 174
Cdd:cd05618   221 F 221
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
14-294 2.67e-06

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: 48.84  E-value: 2.67e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  14 KHPNVIALQKVFlsHSDRKVWLLFDYAEH-DLW-HIIKFHRASKANkkpmqlprsmVKSLLYQILDGIHYLHANWVLHRD 91
Cdd:cd05613    63 QSPFLVTLHYAF--QTDTKLHLILDYINGgELFtHLSQRERFTENE----------VQIYIGEIVLALEHLHKLGIIYRD 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  92 LKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldPVVVTFWYRAPELLLGARH-YTKAIDIWAIGCIFAELLTS 170
Cdd:cd05613   131 IKLENILL----DSSGHVVLTDFGLSKEFLLDENERAY--SFCGTIEYMAPEIVRGGDSgHDKAVDWWSLGVLMYELLTG 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 171 EPIFhcrqeDIKTSNPFHHDQLDRIfsvmgfpadkdwedIRKMPEYP----TLQKDfrrttyansslikymekhkvkpds 246
Cdd:cd05613   205 ASPF-----TVDGEKNSQAEISRRI--------------LKSEPPYPqemsALAKD------------------------ 241
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370507705 247 kvflLLQKLLTMDPTKRITS-----EQALQDPYFQEdplPTLDVFAGCQIPYP 294
Cdd:cd05613   242 ----IIQRLLMKDPKKRLGCgpngaDEIKKHPFFQK---INWDDLAAKKVPAP 287
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
74-174 2.77e-06

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: 48.54  E-value: 2.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFnsplkpLADLDPVVVTFW----YRAPELLLGAR 149
Cdd:cd05583   107 EIVLALEHLHKLGIIYRDIKLENILLDSE----GHVVLTDFGLSKEF------LPGENDRAYSFCgtieYMAPEVVRGGS 176
                          90       100
                  ....*....|....*....|....*.
gi 1370507705 150 H-YTKAIDIWAIGCIFAELLTSEPIF 174
Cdd:cd05583   177 DgHDKAVDWWSLGVLTYELLTGASPF 202
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
6-168 2.93e-06

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: 48.57  E-value: 2.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFlshSDRKVWLLFDYAEH-DLWHIIKFHRASkankkpmqLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd05056    57 EAYIMRQFDHPHIVKLIGVI---TENPVWIVMELAPLgELRSYLQVNKYS--------LDLASLILYAYQLSTALAYLES 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMgeGPErgRVKIADMGFARLFNS-----------PLKPLAdldPVVVTFwyrapelllgaRHYTK 153
Cdd:cd05056   126 KRFVHRDIAARNVLVS--SPD--CVKLGDFGLSRYMEDesyykaskgklPIKWMA---PESINF-----------RRFTS 187
                         170
                  ....*....|....*
gi 1370507705 154 AIDIWAIGCIFAELL 168
Cdd:cd05056   188 ASDVWMFGVCMWEIL 202
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
6-167 3.03e-06

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


Pssm-ID: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 48.83  E-value: 3.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAEH----DLwhiIKFHRaskankkPMQLPRSMVKSLLYQILDGIHY 81
Cdd:cd08216    49 EILTSRQLQHPNILPYVTSFVVDND--LYVVTPLMAYgscrDL---LKTHF-------PEGLPELAIAFILRDVLNALEY 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVMGEgperGRVKIADMGFARLFNS---PLKPLADLDP--VVVTFWYrAPELL----LGarhYT 152
Cdd:cd08216   117 IHSKGYIHRSVKASHILISGD----GKVVLSGLRYAYSMVKhgkRQRVVHDFPKssEKNLPWL-SPEVLqqnlLG---YN 188
                         170
                  ....*....|....*
gi 1370507705 153 KAIDIWAIGCIFAEL 167
Cdd:cd08216   189 EKSDIYSVGITACEL 203
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
13-169 3.19e-06

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


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 48.53  E-value: 3.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  13 LKHPNVIAlqkvFLSHSDRKV------WLLFDYAEH-DLWHIIKFHRASKAnkkpmQLpRSMVKSLLyqilDGIHYLHAN 85
Cdd:cd14055    52 LKHENILQ----FLTAEERGVgldrqyWLITAYHENgSLQDYLTRHILSWE-----DL-CKMAGSLA----RGLAHLHSD 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 W---------VLHRDLKPANILVMGEgperGRVKIADMGFARLfnspLKPLADLDPV-----VVTFWYRAPELL-----L 146
Cdd:cd14055   118 RtpcgrpkipIAHRDLKSSNILVKND----GTCVLADFGLALR----LDPSLSVDELansgqVGTARYMAPEALesrvnL 189
                         170       180
                  ....*....|....*....|...
gi 1370507705 147 GARHYTKAIDIWAIGCIFAELLT 169
Cdd:cd14055   190 EDLESFKQIDVYSMALVLWEMAS 212
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
6-169 3.25e-06

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


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 48.60  E-value: 3.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDRKVWLlfdYAEHDLWHIIKFHRASKANKK--PMQLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd05043    57 ESSLLYGLSHQNLLPILHVCIEDGEKPMVL---YPYMNWGNLKLFLQQCRLSEAnnPQALSTQQLVHMALQIACGMSYLH 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVmgegPERGRVKIADMGFAR-LF-----------NSPLKpladldpvvvtfWYrAPELLLGaRHY 151
Cdd:cd05043   134 RRGVIHKDIAARNCVI----DDELQVKITDNALSRdLFpmdyhclgdneNRPIK------------WM-SLESLVN-KEY 195
                         170
                  ....*....|....*...
gi 1370507705 152 TKAIDIWAIGCIFAELLT 169
Cdd:cd05043   196 SSASDVWSFGVLLWELMT 213
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
14-169 3.51e-06

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


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 48.47  E-value: 3.51e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  14 KHPNVIALqkVFLSHSDRKVWLLFDYAEH-DLWHIIKFHR--ASKANKKPMQLPRSMVK-----SLLYQILDGIHYLHAN 85
Cdd:cd05098    77 KHKNIINL--LGACTQDGPLYVIVEYASKgNLREYLQARRppGMEYCYNPSHNPEEQLSskdlvSCAYQVARGMEYLASK 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYrAPELLLGaRHYTKAIDIWAIGCIFA 165
Cdd:cd05098   155 KCIHRDLAARNVLVT----EDNVMKIADFGLARDIHHIDYYKKTTNGRLPVKWM-APEALFD-RIYTHQSDVWSFGVLLW 228

                  ....
gi 1370507705 166 ELLT 169
Cdd:cd05098   229 EIFT 232
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
6-167 3.92e-06

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


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 48.50  E-value: 3.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIAlqkvFLSHSDRKVWLlfdyaEHDLWHIIKFHRAS------KAN----KKPMQLPRSMVKSL--LY 73
Cdd:cd14141    39 EIYSLPGMKHENILQ----FIGAEKRGTNL-----DVDLWLITAFHEKGsltdylKANvvswNELCHIAQTMARGLayLH 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPlKPLADLDPVVVTFWYRAPELLLGARHYTK 153
Cdd:cd14141   110 EDIPGLKDGHKPAIAHRDIKSKNVLL----KNNLTACIADFGLALKFEAG-KSAGDTHGQVGTRRYMAPEVLEGAINFQR 184
                         170
                  ....*....|....*...
gi 1370507705 154 ----AIDIWAIGCIFAEL 167
Cdd:cd14141   185 daflRIDMYAMGLVLWEL 202
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
74-178 3.95e-06

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 48.44  E-value: 3.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADldpvvvTFWYRAPELLLGARHyTK 153
Cdd:PTZ00426  139 QIVLIFEYLQSLNIVYRDLKPENLLL----DKDGFIKMTDFGFAKVVDTRTYTLCG------TPEYIAPEILLNVGH-GK 207
                          90       100
                  ....*....|....*....|....*
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFHCRQ 178
Cdd:PTZ00426  208 AADWWTLGIFIYEILVGCPPFYANE 232
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
74-174 4.09e-06

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: 48.38  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEGpergRVKIADMGFARLFNSPLKPLADldPVVVTFWYRAPELLLGARHYTK 153
Cdd:cd05614   113 EIILALEHLHKLGIVYRDIKLENILLDSEG----HVVLTDFGLSKEFLTEEKERTY--SFCGTIEYMAPEIIRGKSGHGK 186
                          90       100
                  ....*....|....*....|.
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIF 174
Cdd:cd05614   187 AVDWWSLGILMFELLTGASPF 207
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
32-167 4.38e-06

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: 48.21  E-value: 4.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  32 KVWLLFDYAEH-DLWHIIKFHRASkankkpmqlPRSMVKsLLYQILDGIHYLHANWV--------LHRDLKPANILVmge 102
Cdd:cd14143    67 QLWLVSDYHEHgSLFDYLNRYTVT---------VEGMIK-LALSIASGLAHLHMEIVgtqgkpaiAHRDLKSKNILV--- 133
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370507705 103 gPERGRVKIADMGFARLFNSPLKPLaDLDP--VVVTFWYRAPELL---LGARHYT--KAIDIWAIGCIFAEL 167
Cdd:cd14143   134 -KKNGTCCIADLGLAVRHDSATDTI-DIAPnhRVGTKRYMAPEVLddtINMKHFEsfKRADIYALGLVFWEI 203
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
15-186 5.17e-06

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: 48.48  E-value: 5.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  15 HPNVIALQKVFLSHSdrKVWLLFDYAEH-DLwhiiKFHRaskanKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLK 93
Cdd:cd05617    75 NPFLVGLHSCFQTTS--RLFLVIEYVNGgDL----MFHM-----QRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLK 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  94 PANILVMGEgperGRVKIADMGFARlfnSPLKPLADLDPVVVTFWYRAPELLLGaRHYTKAIDIWAIGCIFAELLTSEPI 173
Cdd:cd05617   144 LDNVLLDAD----GHIKLTDYGMCK---EGLGPGDTTSTFCGTPNYIAPEILRG-EEYGFSVDWWALGVLMFEMMAGRSP 215
                         170
                  ....*....|...
gi 1370507705 174 FhcrqeDIKTSNP 186
Cdd:cd05617   216 F-----DIITDNP 223
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
36-115 5.79e-06

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: 45.51  E-value: 5.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  36 LFDYAEHDLWHIIKFHRASKAN----KKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKI 111
Cdd:cd13968    57 VLVTEDVDGPNILLMELVKGGTliayTQEEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLS----EDGNVKL 132

                  ....
gi 1370507705 112 ADMG 115
Cdd:cd13968   133 IDFG 136
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
79-277 6.30e-06

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: 48.10  E-value: 6.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFA-----------------RLFNSPL-------------KPLA 128
Cdd:cd05600   124 ISSLHQLGYIHRDLKPENFLI----DSSGHIKLTDFGLAsgtlspkkiesmkirleEVKNTAFleltakerrniyrAMRK 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 129 DLDP----VVVTFWYRAPELLLGaRHYTKAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQLDRIFSVMgfpad 204
Cdd:cd05600   200 EDQNyansVVGSPDYMAPEVLRG-EGYDLTVDYWSLGCILFECLVGFP-------------PFSGSTPNETWANL----- 260
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370507705 205 KDWEDIRKMPEY--PTLQKDFRRTTYansSLIkymekhkvkpdskvflllqKLLTMDPTKRITS-EQALQDPYFQE 277
Cdd:cd05600   261 YHWKKTLQRPVYtdPDLEFNLSDEAW---DLI-------------------TKLITDPQDRLQSpEQIKNHPFFKN 314
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
74-180 6.74e-06

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: 48.07  E-value: 6.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARlfnSPLKPLADLDPVVVTFWYRAPElLLGARHYTK 153
Cdd:cd05615   119 EISVGLFFLHKKGIIYRDLKLDNVMLDSE----GHIKIADFGMCK---EHMVEGVTTRTFCGTPDYIAPE-IIAYQPYGR 190
                          90       100
                  ....*....|....*....|....*..
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFHCRQED 180
Cdd:cd05615   191 SVDWWAYGVLLYEMLAGQPPFDGEDED 217
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
6-171 6.80e-06

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 47.36  E-value: 6.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIalqkVFLSHSDR-KVWLLFDYAE-HDLWHIIKFHRASKANKKPMQLPRsmvksllyQILDGIHYLH 83
Cdd:cd14151    54 EVGVLRKTRHVNIL----LFMGYSTKpQLAIVTQWCEgSSLYHHLHIIETKFEMIKLIDIAR--------QTAQGMDYLH 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANILVMgegpERGRVKIADMGFARLfNSPLKPLADLDPVVVTFWYRAPEL--LLGARHYTKAIDIWAIG 161
Cdd:cd14151   122 AKSIIHRDLKSNNIFLH----EDLTVKIGDFGLATV-KSRWSGSHQFEQLSGSILWMAPEVirMQDKNPYSFQSDVYAFG 196
                         170
                  ....*....|
gi 1370507705 162 CIFAELLTSE 171
Cdd:cd14151   197 IVLYELMTGQ 206
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
6-169 7.80e-06

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: 47.16  E-value: 7.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHsdRKVWLLFDYAEHDLwhIIKFHRASKAnkkpmQLPRSMVKSLLYQILDGIHYLHAN 85
Cdd:cd05114    49 EAKVMMKLTHPKLVQLYGVCTQQ--KPIYIVTEFMENGC--LLNYLRQRRG-----KLSRDMLLSMCQDVCEGMEYLERN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVmgegPERGRVKIADMGFAR--LFNSPLKPLADLDPVVvtfwYRAPELLLGARHYTKAiDIWAIGCI 163
Cdd:cd05114   120 NFIHRDLAARNCLV----NDTGVVKVSDFGMTRyvLDDQYTSSSGAKFPVK----WSPPEVFNYSKFSSKS-DVWSFGVL 190

                  ....*.
gi 1370507705 164 FAELLT 169
Cdd:cd05114   191 MWEVFT 196
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
6-118 8.37e-06

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: 47.38  E-value: 8.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDRKVwLLFDYAEHDLWHIIKFHRAskankKPMQLPRSMVKSLLYQILD---GIHYL 82
Cdd:cd05036    59 EALIMSKFNHPNIVRCIGVCFQRLPRFI-LLELMAGGDLKSFLRENRP-----RPEQPSSLTMLDLLQLAQDvakGCRYL 132
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1370507705  83 HANWVLHRDLKPANILVMGEGPERgRVKIADMGFAR 118
Cdd:cd05036   133 EENHFIHRDIAARNCLLTCKGPGR-VAKIGDFGMAR 167
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
5-169 8.52e-06

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: 47.37  E-value: 8.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFlshSDRKVWLLFDYAehDLWHIIKFHRASKAnkKPMQLPRsmVKSLLYQILDGIHYLHA 84
Cdd:cd05071    53 QEAQVMKKLRHEKLVQLYAVV---SEEPIYIVTEYM--SKGSLLDFLKGEMG--KYLRLPQ--LVDMAAQIASGMAYVER 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmgegPERGRVKIADMGFARLF--NSPLKPLADLDPVVVTfwyrAPELLLGARHYTKAiDIWAIGC 162
Cdd:cd05071   124 MNYVHRDLRAANILV----GENLVCKVADFGLARLIedNEYTARQGAKFPIKWT----APEAALYGRFTIKS-DVWSFGI 194

                  ....*..
gi 1370507705 163 IFAELLT 169
Cdd:cd05071   195 LLTELTT 201
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
5-169 8.64e-06

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: 47.49  E-value: 8.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAEH-DLWHIIKFHRASKAnkkpmqLPRSMVKSLLYQILDGIHYLH 83
Cdd:cd13988    40 REFEVLKKLNHKNIVKLFAIEEELTTRHKVLVMELCPCgSLYTVLEEPSNAYG------LPESEFLIVLRDVVAGMNHLR 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  84 ANWVLHRDLKPANIlvMGEGPERGRV--KIADMGFARlfnsplkPLADLDPVVV---TFWYRAPELLLGA-------RHY 151
Cdd:cd13988   114 ENGIVHRDIKPGNI--MRVIGEDGQSvyKLTDFGAAR-------ELEDDEQFVSlygTEEYLHPDMYERAvlrkdhqKKY 184
                         170
                  ....*....|....*...
gi 1370507705 152 TKAIDIWAIGCIFAELLT 169
Cdd:cd13988   185 GATVDLWSIGVTFYHAAT 202
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
5-163 9.12e-06

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: 47.12  E-value: 9.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELK-HPNVIA------LQKVFLSHSDRKVWLLFDYAEHDLWHIIKFHRAskanKKPMQLprSMVKSLLYQILD 77
Cdd:cd14036    46 QEINFMKKLSgHPNIVQfcsaasIGKEESDQGQAEYLLLTELCKGQLVDFVKKVEA----PGPFSP--DTVLKIFYQTCR 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANW--VLHRDLKPANILVMGEGpergRVKIADMGFARlfNSPLKP-----------LADLDPVVVTFWYRAPEL 144
Cdd:cd14036   120 AVQHMHKQSppIIHRDLKIENLLIGNQG----QIKLCDFGSAT--TEAHYPdyswsaqkrslVEDEITRNTTPMYRTPEM 193
                         170       180
                  ....*....|....*....|.
gi 1370507705 145 LLGARHY--TKAIDIWAIGCI 163
Cdd:cd14036   194 IDLYSNYpiGEKQDIWALGCI 214
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
5-169 1.01e-05

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: 47.14  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSDR----KVWLLFDYAEHDLWHiiKFHRASKANKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd05035    50 SEAACMKDFDHPNVMRLIGVCFTASDLnkppSPMVILPFMKHGDLH--SYLLYSRLGGLPEKLPLQTLLKFMVDIAKGME 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNS------------PLKPLAdLDPvvvtfwyrapellLGA 148
Cdd:cd05035   128 YLSNRNFIHRDLAARNCML----DENMTVCVADFGLSRKIYSgdyyrqgriskmPVKWIA-LES-------------LAD 189
                         170       180
                  ....*....|....*....|.
gi 1370507705 149 RHYTKAIDIWAIGCIFAELLT 169
Cdd:cd05035   190 NVYTSKSDVWSFGVTMWEIAT 210
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
5-171 1.05e-05

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: 46.88  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLsHSdrkvwLLFDYAEHDLWHIIKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd14067    59 QEASMLHSLQHPCIVYLIGISI-HP-----LCFALELAPLGSLNTVLEENHKGSSFMPLGHMLTFKIAYQIAAGLAYLHK 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMG-EGPERGRVKIADMGFAR--LFNSPLKpladldpVVVTFWYRAPELLLGARhYTKAIDIWAIG 161
Cdd:cd14067   133 KNIIFCDLKSDNILVWSlDVQEHINIKLSDYGISRqsFHEGALG-------VEGTPGYQAPEIRPRIV-YDEKVDMFSYG 204
                         170
                  ....*....|
gi 1370507705 162 CIFAELLTSE 171
Cdd:cd14067   205 MVLYELLSGQ 214
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
79-175 1.22e-05

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: 46.93  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVmgegpER-GRVKIADMGFARLF----NSPLKPLADLdpvVVTFWYRAPELLLgARHYTK 153
Cdd:cd05598   114 IESVHKMGFIHRDIKPDNILI-----DRdGHIKLTDFGLCTGFrwthDSKYYLAHSL---VGTPNYIAPEVLL-RTGYTQ 184
                          90       100
                  ....*....|....*....|..
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFH 175
Cdd:cd05598   185 LCDWWSVGVILYEMLVGQPPFL 206
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
70-172 1.24e-05

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


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 46.63  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  70 SLLYQILDGIHYLHANWVLHRDLKPANILVMGegpeRGRVKIADMGFARLFNSPLKPLADLDPVVVtFWyRAPELL---L 146
Cdd:cd14043   101 SLLLDLIKGMRYLHHRGIVHGRLKSRNCVVDG----RFVLKITDYGYNEILEAQNLPLPEPAPEEL-LW-TAPELLrdpR 174
                          90       100
                  ....*....|....*....|....*.
gi 1370507705 147 GARHYTKAIDIWAIGCIFAELLTSEP 172
Cdd:cd14043   175 LERRGTFPGDVFSFAIIMQEVIVRGA 200
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
76-206 1.30e-05

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: 47.31  E-value: 1.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  76 LDGIHYLHanwVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplKPLADLDPVVVTFWYRAPELLL---GARHYT 152
Cdd:cd05622   185 LDAIHSMG---FIHRDVKPDNMLL----DKSGHLKLADFGTCMKMNK--EGMVRCDTAVGTPDYISPEVLKsqgGDGYYG 255
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370507705 153 KAIDIWAIGCIFAELLTSEpifhcrqediktsNPFHHDQLDRIFS-------VMGFPADKD 206
Cdd:cd05622   256 RECDWWSVGVFLYEMLVGD-------------TPFYADSLVGTYSkimnhknSLTFPDDND 303
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
70-172 1.37e-05

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


Pssm-ID: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 46.94  E-value: 1.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  70 SLLYQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYrAPELLLGaR 149
Cdd:cd05100   138 SCAYQVARGMEYLASQKCIHRDLAARNVLVT----EDNVMKIADFGLARDVHNIDYYKKTTNGRLPVKWM-APEALFD-R 211
                          90       100
                  ....*....|....*....|...
gi 1370507705 150 HYTKAIDIWAIGCIFAELLTSEP 172
Cdd:cd05100   212 VYTHQSDVWSFGVLLWEIFTLGG 234
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
5-275 1.43e-05

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: 46.47  E-value: 1.43e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELK-HPNVIALQKVFLSHSDRKV---WLLFDYAEHDLWHIIkfhraskANKKPMQLPRSMVKSLLYQILDGIH 80
Cdd:cd14020    52 KERAALEQLQgHRNIVTLYGVFTNHYSANVpsrCLLLELLDVSVSELL-------LRSSNQGCSMWMIQHCARDVLEALA 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVMGEGPergRVKIADMGFA-RLFNSPLKpladldpVVVTFWYRAPELLL----------GAR 149
Cdd:cd14020   125 FLHHEGYVHADLKPRNILWSAEDE---CFKLIDFGLSfKEGNQDVK-------YIQTDGYRAPEAELqnclaqaglqSET 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 150 HYTKAIDIWAIGCIFAELLTSEPIFH-CRQEDIKTSNPfhhDQLDRIFSvmgfpadkdwediRKMPEYPTLqkdfrrTTY 228
Cdd:cd14020   195 ECTSAVDLWSLGIVLLEMFSGMKLKHtVRSQEWKDNSS---AIIDHIFA-------------SNAVVNPAI------PAY 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1370507705 229 ANSSLIKYMekhkvkpdskvflllqklLTMDPTKRITSEQALQDPYF 275
Cdd:cd14020   253 HLRDLIKSM------------------LHNDPGKRATAEAALCSPFF 281
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
5-285 1.51e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 47.15  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdrKVWLLFDYAEHDLWHIIKfhraskaNKKPMQLPRSMVksLLYQILDGIHYLHA 84
Cdd:PHA03207  135 REIDILKTISHRAIINLIHAYRWKS--TVCMVMPKYKCDLFTYVD-------RSGPLPLEQAIT--IQRRLLEALAYLHG 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmgegPERGRVKIADMGFA-RLFNSPLKPlaDLDPVVVTFWYRAPELLLGARHYTKAiDIWAIGCI 163
Cdd:PHA03207  204 RGIIHRDVKTENIFL----DEPENAVLGDFGAAcKLDAHPDTP--QCYGWSGTLETNSPELLALDPYCAKT-DIWSAGLV 276
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 164 FAELLTSEPIFHCRQedIKTSNpfhhDQLDRIFSVMG-----FPADKDWEDIRKMPEYPTLqkdfRRTTYANSSLIKyme 238
Cdd:PHA03207  277 LFEMSVKNVTLFGKQ--VKSSS----SQLRSIIRCMQvhpleFPQNGSTNLCKHFKQYAIV----LRPPYTIPPVIR--- 343
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1370507705 239 khKVKPDSKVFLLLQKLLTMDPTKRITSEQALQDPYFQEDPLPTLDV 285
Cdd:PHA03207  344 --KYGMHMDVEYLIAKMLTFDQEFRPSAQDILSLPLFTKEPINLLNI 388
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
6-169 1.57e-05

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: 46.40  E-value: 1.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEHDlwHIIKFHRASKANKKPMQLprsmvKSLLYQILDGIHYLHAN 85
Cdd:cd05065    55 EASIMGQFDHPNIIHLEGVVTK--SRPVMIITEFMENG--ALDSFLRQNDGQFTVIQL-----VGMLRGIAAGMKYLSEM 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVMGEGPergrVKIADMGFAR-LFNSPLKP-----LADLDPVVVTfwyrAPElLLGARHYTKAIDIWA 159
Cdd:cd05065   126 NYVHRDLAARNILVNSNLV----CKVSDFGLSRfLEDDTSDPtytssLGGKIPIRWT----APE-AIAYRKFTSASDVWS 196
                         170
                  ....*....|
gi 1370507705 160 IGCIFAELLT 169
Cdd:cd05065   197 YGIVMWEVMS 206
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
74-169 1.73e-05

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 46.17  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgEGPErgRVKIADMGFARLFNSPLKPL-ADLDPVVVTfWYRAPELLlgARHYT 152
Cdd:cd05109   117 QIAKGMSYLEEVRLVHRDLAARNVLV--KSPN--HVKITDFGLARLLDIDETEYhADGGKVPIK-WMALESIL--HRRFT 189
                          90
                  ....*....|....*..
gi 1370507705 153 KAIDIWAIGCIFAELLT 169
Cdd:cd05109   190 HQSDVWSYGVTVWELMT 206
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
5-172 1.81e-05

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: 46.25  E-value: 1.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKH-PNVIALQKVFLSHS----DRKVWLLFDY-AEHDLWHIIKfhraskaNKKPMQLPRSMVKSLLYQILDG 78
Cdd:cd06637    51 QEINMLKKYSHhRNIATYYGAFIKKNppgmDDQLWLVMEFcGAGSVTDLIK-------NTKGNTLKEEWIAYICREILRG 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNsplKPLADLDPVVVTFWYRAPELLLGARH----YTKA 154
Cdd:cd06637   124 LSHLHQHKVIHRDIKGQNVLLT----ENAEVKLVDFGVSAQLD---RTVGRRNTFIGTPYWMAPEVIACDENpdatYDFK 196
                         170
                  ....*....|....*...
gi 1370507705 155 IDIWAIGCIFAELLTSEP 172
Cdd:cd06637   197 SDLWSLGITAIEMAEGAP 214
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
3-169 1.93e-05

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: 45.72  E-value: 1.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   3 ACREIALLRELKHPNVIALQKVFLSHSDRKVWL-------LFDY-AEHDlwhiikfhraskankkpmQLPRSMVKSLLYQ 74
Cdd:cd14115    36 AAHEAALLQHLQHPQYITLHDTYESPTSYILVLelmddgrLLDYlMNHD------------------ELMEEKVAFYIRD 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVMGEGPErGRVKIADMGfarlfnsplkpladlDPVVVTFWYR-----------APE 143
Cdd:cd14115    98 IMEALQYLHNCRVAHLDIKPENLLIDLRIPV-PRVKLIDLE---------------DAVQISGHRHvhhllgnpefaAPE 161
                         170       180
                  ....*....|....*....|....*.
gi 1370507705 144 LLLGARhYTKAIDIWAIGCIFAELLT 169
Cdd:cd14115   162 VIQGTP-VSLATDIWSIGVLTYVMLS 186
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
76-192 2.04e-05

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: 46.60  E-value: 2.04e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  76 LDGIHYLHanwVLHRDLKPANILVMGegpeRGRVKIADMGFARLFNSplKPLADLDPVVVTFWYRAPELLL---GARHYT 152
Cdd:cd05596   138 LDAIHSMG---FVHRDVKPDNMLLDA----SGHLKLADFGTCMKMDK--DGLVRSDTAVGTPDYISPEVLKsqgGDGVYG 208
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1370507705 153 KAIDIWAIGCIFAELLTSEPifhcrqediktsnPFHHDQL 192
Cdd:cd05596   209 RECDWWSVGVFLYEMLVGDT-------------PFYADSL 235
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
73-219 2.17e-05

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: 46.54  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  73 YQILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYrAPELLLGARhYT 152
Cdd:cd05107   246 YQVANGMEFLASKNCVHRDLAARNVLIC----EGKLVKICDFGLARDIMRDSNYISKGSTFLPLKWM-APESIFNNL-YT 319
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370507705 153 KAIDIWAIGCIFAELLT-----------SEPIFHCRQEDIKTSNPFHHDqlDRIFSVMgfpaDKDWED-IRKMPEYPTL 219
Cdd:cd05107   320 TLSDVWSFGILLWEIFTlggtpypelpmNEQFYNAIKRGYRMAKPAHAS--DEIYEIM----QKCWEEkFEIRPDFSQL 392
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
5-169 2.22e-05

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 45.93  E-value: 2.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShSDRKVWLLFDYAEH-DLWHIIkfhraskanKKPMQLPrsMVKSLL---YQILDGIH 80
Cdd:cd05058    45 KEGIIMKDFSHPNVLSLLGICLP-SEGSPLVVLPYMKHgDLRNFI---------RSETHNP--TVKDLIgfgLQVAKGME 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  81 YLHANWVLHRDLKPANILVmgegPERGRVKIADMGFAR-LFNSPLKPLADLDPVVVTFWYRAPELLLGARHYTKAiDIWA 159
Cdd:cd05058   113 YLASKKFVHRDLAARNCML----DESFTVKVADFGLARdIYDKEYYSVHNHTGAKLPVKWMALESLQTQKFTTKS-DVWS 187
                         170
                  ....*....|
gi 1370507705 160 IGCIFAELLT 169
Cdd:cd05058   188 FGVLLWELMT 197
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
5-170 2.34e-05

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: 45.51  E-value: 2.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALqkVFLSHSDRKVWLLFDYAEHDlwHIIKFHRASKANKKPMQLprsmvkslLYQILD---GIHY 81
Cdd:cd05041    42 QEARILKQYDHPNIVKL--IGVCVQKQPIMIVMELVPGG--SLLTFLRKKGARLTVKQL--------LQMCLDaaaGMEY 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  82 LHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLDPVVVTFWyRAPELLLGARhYTKAIDIWAIG 161
Cdd:cd05041   110 LESKNCIHRDLAARNCLV----GENNVLKISDFGMSREEEDGEYTVSDGLKQIPIKW-TAPEALNYGR-YTSESDVWSFG 183

                  ....*....
gi 1370507705 162 CIFAELLTS 170
Cdd:cd05041   184 ILLWEIFSL 192
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
6-169 2.75e-05

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: 45.38  E-value: 2.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHsdRKVWLLFDYAEHDlwHIIKFHRASKANKKPMQLPRSMVKSLlyqilDGIHYLHAN 85
Cdd:cd05085    43 EARILKQYDHPNIVKLIGVCTQR--QPIYIVMELVPGG--DFLSFLRKKKDELKTKQLVKFSLDAA-----AGMAYLESK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLDPVVVTfwYRAPELLLGARhYTKAIDIWAIGCIFA 165
Cdd:cd05085   114 NCIHRDLAARNCLV----GENNALKISDFGMSRQEDDGVYSSSGLKQIPIK--WTAPEALNYGR-YSSESDVWSFGILLW 186

                  ....
gi 1370507705 166 ELLT 169
Cdd:cd05085   187 ETFS 190
PTZ00284 PTZ00284
protein kinase; Provisional
71-174 2.99e-05

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 46.11  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  71 LLYQILDGIHYLHANW-VLHRDLKPANILVMGEG------------PERGRVKIADMGfarlfnSPLKPLADLDPVVVTF 137
Cdd:PTZ00284  236 IIFQTGVALDYFHTELhLMHTDLKPENILMETSDtvvdpvtnralpPDPCRVRICDLG------GCCDERHSRTAIVSTR 309
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1370507705 138 WYRAPELLLGArHYTKAIDIWAIGCIFAELLTSEPIF 174
Cdd:PTZ00284  310 HYRSPEVVLGL-GWMYSTDMWSMGCIIYELYTGKLLY 345
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
74-180 3.10e-05

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: 45.67  E-value: 3.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFAR--LFNSPLkpladldpvVVTFW----YRAPElLLG 147
Cdd:cd05590   104 EITSALMFLHDKGIIYRDLKLDNVLLDHE----GHCKLADFGMCKegIFNGKT---------TSTFCgtpdYIAPE-ILQ 169
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1370507705 148 ARHYTKAIDIWAIGCIFAELLTSEPIFHCRQED 180
Cdd:cd05590   170 EMLYGPSVDWWAMGVLLYEMLCGHAPFEAENED 202
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
6-169 3.25e-05

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: 45.35  E-value: 3.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDrkVWLLFDYAEHDLwhIIKFHRASKANKKPMQLprsmvKSLLYQILDGIHYLHAN 85
Cdd:cd05063    56 EASIMGQFSHHNIIRLEGVVTKFKP--AMIITEYMENGA--LDKYLRDHDGEFSSYQL-----VGMLRGIAAGMKYLSDM 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFA 165
Cdd:cd05063   127 NYVHRDLAARNILVNSN----LECKVSDFGLSRVLEDDPEGTYTTSGGKIPIRWTAPE-AIAYRKFTSASDVWSFGIVMW 201

                  ....
gi 1370507705 166 ELLT 169
Cdd:cd05063   202 EVMS 205
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
62-175 3.26e-05

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: 45.78  E-value: 3.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  62 QLPRSMVKSLLYQI---LDGIHYLHanwVLHRDLKPANILVmgegPERGRVKIADmgfarlFNSPLKPLAD----LDPVV 134
Cdd:cd05623   169 RLPEDMARFYLAEMvlaIDSVHQLH---YVHRDIKPDNILM----DMNGHIRLAD------FGSCLKLMEDgtvqSSVAV 235
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370507705 135 VTFWYRAPELLL----GARHYTKAIDIWAIGCIFAELLTSEPIFH 175
Cdd:cd05623   236 GTPDYISPEILQamedGKGKYGPECDWWSLGVCMYEMLYGETPFY 280
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
63-175 3.37e-05

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 45.80  E-value: 3.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  63 LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADmgfarlFNSPLKPLAD---LDPVVV-TFW 138
Cdd:cd05597    99 LPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLL----DRNGHIRLAD------FGSCLKLREDgtvQSSVAVgTPD 168
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1370507705 139 YRAPELLL----GARHYTKAIDIWAIGCIFAELLTSEPIFH 175
Cdd:cd05597   169 YISPEILQamedGKGRYGPECDWWSLGVCMYEMLYGETPFY 209
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
13-212 3.85e-05

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


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 45.51  E-value: 3.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  13 LKHPNVIAL--QKVFLSHSDRKVWLLFDYAEH-DLWHIIKFHRASkankkpmqlPRSMVKsLLYQILDGIHYLHAN---- 85
Cdd:cd14142    56 LRHENILGFiaSDMTSRNSCTQLWLITHYHENgSLYDYLQRTTLD---------HQEMLR-LALSAASGLVHLHTEifgt 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 ----WVLHRDLKPANILVMGEgperGRVKIADMGFARLFNSPLKPLaDL--DPVVVTFWYRAPELLLGARHYT-----KA 154
Cdd:cd14142   126 qgkpAIAHRDLKSKNILVKSN----GQCCIADLGLAVTHSQETNQL-DVgnNPRVGTKRYMAPEVLDETINTDcfesyKR 200
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370507705 155 IDIWAIGCIFAELltsepifhCRQ-------EDIKTsnPFhhdqldriFSVMgfPADKDWEDIRK 212
Cdd:cd14142   201 VDIYAFGLVLWEV--------ARRcvsggivEEYKP--PF--------YDVV--PSDPSFEDMRK 245
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
5-169 4.05e-05

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: 45.03  E-value: 4.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLSHSdrkVWLLFDYAEhdLWHIIKFHRaskanKKPmQLPRSMVKSLLYQILDGIHYLHA 84
Cdd:cd05060    45 REASVMAQLDHPCIVRLIGVCKGEP---LMLVMELAP--LGPLLKYLK-----KRR-EIPVSDLKELAHQVAMGMAYLES 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVMgegpERGRVKIADMGFARLFNS-------------PLKpladldpvvvtfWYrAPELLLGARHY 151
Cdd:cd05060   114 KHFVHRDLAARNVLLV----NRHQAKISDFGMSRALGAgsdyyrattagrwPLK------------WY-APECINYGKFS 176
                         170
                  ....*....|....*...
gi 1370507705 152 TKAiDIWAIGCIFAELLT 169
Cdd:cd05060   177 SKS-DVWSYGVTLWEAFS 193
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
43-117 4.18e-05

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


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 45.35  E-value: 4.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370507705  43 DLWHIIKfhraskANKKpmQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmGEGPERGRVKIADMGFA 117
Cdd:cd14015   112 DLQKIFE------KNGK--RFPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLL-GFGKNKDQVYLVDYGLA 177
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
58-218 4.19e-05

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 45.38  E-value: 4.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  58 KKPMQLPRSMVKSllYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFAR-LFNSPlKPLADLDPVVVT 136
Cdd:cd14207   174 KRPLTMEDLISYS--FQVARGMEFLSSRKCIHRDLAARNILL----SENNVVKICDFGLARdIYKNP-DYVRKGDARLPL 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705 137 FWYrAPELLLGARHYTKAiDIWAIGCIFAELLTsepifhcrqediKTSNPFHHDQLDRIFsvmgfpADKDWEDIR-KMPE 215
Cdd:cd14207   247 KWM-APESIFDKIYSTKS-DVWSYGVLLWEIFS------------LGASPYPGVQIDEDF------CSKLKEGIRmRAPE 306

                  ...
gi 1370507705 216 YPT 218
Cdd:cd14207   307 FAT 309
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
73-169 4.77e-05

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: 45.36  E-value: 4.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  73 YQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFAR-LFNSPlKPLADLDPVVVTFWYrAPELLLGaRHY 151
Cdd:cd05103   186 FQVAKGMEFLASRKCIHRDLAARNILL----SENNVVKICDFGLARdIYKDP-DYVRKGDARLPLKWM-APETIFD-RVY 258
                          90
                  ....*....|....*...
gi 1370507705 152 TKAIDIWAIGCIFAELLT 169
Cdd:cd05103   259 TIQSDVWSFGVLLWEIFS 276
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
6-169 4.87e-05

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: 44.86  E-value: 4.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLshsdrkvwllfdyaeHDLWHIIKFHrASKANKKPMQLPRSMVKSLLYQIL-------DG 78
Cdd:cd05083    49 ETAVMTKLQHKNLVRLLGVIL---------------HNGLYIVMEL-MSKGNLVNFLRSRGRALVPVIQLLqfsldvaEG 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLfnsplkPLADLDPVVVTFWYRAPELLLGARHYTKAiDIW 158
Cdd:cd05083   113 MEYLESKKLVHRDLAARNILV----SEDGVAKISDFGLAKV------GSMGVDNSRLPVKWTAPEALKNKKFSSKS-DVW 181
                         170
                  ....*....|.
gi 1370507705 159 AIGCIFAELLT 169
Cdd:cd05083   182 SYGVLLWEVFS 192
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
6-169 5.09e-05

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: 44.87  E-value: 5.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVflSHSDRKVWLLFDYAEHDLwhIIKFHRASKANKKPMQLprsmvKSLLYQILDGIHYLHAN 85
Cdd:cd05113    49 EAKVMMNLSHEKLVQLYGV--CTKQRPIFIITEYMANGC--LLNYLREMRKRFQTQQL-----LEMCKDVCEAMEYLESK 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVmgegPERGRVKIADMGFAR--LFNSPLKPLADLDPVVvtfwYRAPELLLGARHYTKAiDIWAIGCI 163
Cdd:cd05113   120 QFLHRDLAARNCLV----NDQGVVKVSDFGLSRyvLDDEYTSSVGSKFPVR----WSPPEVLMYSKFSSKS-DVWAFGVL 190

                  ....*.
gi 1370507705 164 FAELLT 169
Cdd:cd05113   191 MWEVYS 196
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
6-169 5.31e-05

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer 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 Mer 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: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 44.93  E-value: 5.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDR---KVWLLFDYAEHDLWHiiKFHRASKANKKPMQLPRSMVKSLLYQILDGIHYL 82
Cdd:cd14204    59 EAACMKDFNHPNVIRLLGVCLEVGSQripKPMVILPFMKYGDLH--SFLLRSRLGSGPQHVPLQTLLKFMIDIALGMEYL 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  83 HANWVLHRDLKPANILVMGEGPergrVKIADMGFA------------RLFNSPLKPLADLDpvvvtfwyrapellLGARH 150
Cdd:cd14204   137 SSRNFLHRDLAARNCMLRDDMT----VCVADFGLSkkiysgdyyrqgRIAKMPVKWIAVES--------------LADRV 198
                         170
                  ....*....|....*....
gi 1370507705 151 YTKAIDIWAIGCIFAELLT 169
Cdd:cd14204   199 YTVKSDVWAFGVTMWEIAT 217
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
13-167 6.31e-05

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: 44.65  E-value: 6.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  13 LKHPNVIALQKVFL--SHSDRKVWLLFDYAEH-DLWHIIKFHRASKankkpmqlpRSMVKsLLYQILDGIHYLHAN---- 85
Cdd:cd14220    46 MRHENILGFIAADIkgTGSWTQLYLITDYHENgSLYDFLKCTTLDT---------RALLK-LAYSAACGLCHLHTEiygt 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 ----WVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPL-ADLDPVVVTFWYRAPELL---LGARHYTKAI-- 155
Cdd:cd14220   116 qgkpAIAHRDLKSKNILI----KKNGTCCIADLGLAVKFNSDTNEVdVPLNTRVGTKRYMAPEVLdesLNKNHFQAYIma 191
                         170
                  ....*....|..
gi 1370507705 156 DIWAIGCIFAEL 167
Cdd:cd14220   192 DIYSFGLIIWEM 203
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
57-169 6.93e-05

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 44.66  E-value: 6.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  57 NKKPMQLPRSMVKSLLYQILDGIHYLHANW-VLHRDLKPANILVMGegpeRGRVKIADMGFA-RLFNSPLKPL-ADLDPv 133
Cdd:cd06616   100 EVLDSVIPEEILGKIAVATVKALNYLKEELkIIHRDVKPSNILLDR----NGNIKLCDFGISgQLVDSIAKTRdAGCRP- 174
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370507705 134 vvtfwYRAPELLLGARH---YTKAIDIWAIGCIFAELLT 169
Cdd:cd06616   175 -----YMAPERIDPSASrdgYDVRSDVWSLGITLYEVAT 208
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
74-175 7.27e-05

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: 44.69  E-value: 7.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARlfnSPLKPLADLDPVVVTFWYRAPElLLGARHYTK 153
Cdd:cd05593   123 EIVSALDYLHSGKIVYRDLKLENLML----DKDGHIKITDFGLCK---EGITDAATMKTFCGTPEYLAPE-VLEDNDYGR 194
                          90       100
                  ....*....|....*....|..
gi 1370507705 154 AIDIWAIGCIFAELLTSEPIFH 175
Cdd:cd05593   195 AVDWWGLGVVMYEMMCGRLPFY 216
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
74-169 7.79e-05

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: 44.24  E-value: 7.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMgegpERGRVKIADMGFARLFN--SPLKPLAdlDPVVVTFWYrAPEL--LLGAR 149
Cdd:cd14150   104 QTAQGMDYLHAKNIIHRDLKSNNIFLH----EGLTVKIGDFGLATVKTrwSGSQQVE--QPSGSILWM-APEVirMQDTN 176
                          90       100
                  ....*....|....*....|
gi 1370507705 150 HYTKAIDIWAIGCIFAELLT 169
Cdd:cd14150   177 PYSFQSDVYAYGVVLYELMS 196
PLN03224 PLN03224
probable serine/threonine protein kinase; Provisional
66-117 1.06e-04

probable serine/threonine protein kinase; Provisional


Pssm-ID: 178763 [Multi-domain]  Cd Length: 507  Bit Score: 44.68  E-value: 1.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370507705  66 SMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFA 117
Cdd:PLN03224  309 NVIKGVMRQVLTGLRKLHRIGIVHRDIKPENLLVTVD----GQVKIIDFGAA 356
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
5-169 1.06e-04

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: 43.70  E-value: 1.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   5 REIALLRELKHPNVIALQKVFLShsDRKVWLLFDYAEHDlwHIIKFHRASKANKKPMQLprsmvKSLLYQILDGIHYLHA 84
Cdd:cd05066    54 SEASIMGQFDHPNIIHLEGVVTR--SKPVMIVTEYMENG--SLDAFLRKHDGQFTVIQL-----VGMLRGIASGMKYLSD 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  85 NWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplkplaDLDPVVVT------FWYRAPElLLGARHYTKAIDIW 158
Cdd:cd05066   125 MGYVHRDLAARNILV----NSNLVCKVSDFGLSRVLED------DPEAAYTTrggkipIRWTAPE-AIAYRKFTSASDVW 193
                         170
                  ....*....|.
gi 1370507705 159 AIGCIFAELLT 169
Cdd:cd05066   194 SYGIVMWEVMS 204
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
74-181 1.08e-04

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: 43.88  E-value: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFAR---LFNSPLKpladldpvvvTFW----YRAPELLL 146
Cdd:cd05571   103 EIVLALGYLHSQGIVYRDLKLENLLLDKD----GHIKITDFGLCKeeiSYGATTK----------TFCgtpeYLAPEVLE 168
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1370507705 147 GArHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDI 181
Cdd:cd05571   169 DN-DYGRAVDWWGLGVVMYEMMCGRLPFYNRDHEV 202
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
14-192 1.21e-04

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 44.02  E-value: 1.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  14 KHPNVIALQKVFLS--------HSDRKVWLLFDYAEHDLWH------IIKFHRASKANKKPMQLPRSMVKSLLY-QILDG 78
Cdd:cd14018    71 PHPNIIRVQRAFTDsvpllpgaIEDYPDVLPARLNPSGLGHnrtlflVMKNYPCTLRQYLWVNTPSYRLARVMIlQLLEG 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANWVLHRDLKPANILVMGEGPERGRVKIADMGFArlfnsplkpLADLDP---VVVTFWY---------RAPELLL 146
Cdd:cd14018   151 VDHLVRHGIAHRDLKSDNILLELDFDGCPWLVIADFGCC---------LADDSIglqLPFSSWYvdrggnaclMAPEVST 221
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370507705 147 ---GAR---HYTKAiDIWAIGCIFAELLTSEPIFHCRQEDIKTSNPFHHDQL 192
Cdd:cd14018   222 avpGPGvviNYSKA-DAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQESQL 272
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
78-169 1.34e-04

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: 43.50  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  78 GIHYLHANW---------VLHRDLKPANILVMGEgperGRVKIADMGFA-RLFNS--PLKPLADLDPV----VVTFWYRA 141
Cdd:cd14054   105 GLAYLHTDLrrgdqykpaIAHRDLNSRNVLVKAD----GSCVICDFGLAmVLRGSslVRGRPGAAENAsiseVGTLRYMA 180
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1370507705 142 PELLLGA------RHYTKAIDIWAIGCIFAELLT 169
Cdd:cd14054   181 PEVLEGAvnlrdcESALKQVDVYALGLVLWEIAM 214
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
63-175 1.51e-04

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: 43.83  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  63 LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSplKPLADLDPVVVTFWYRAP 142
Cdd:cd05621   148 VPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLL----DKYGHLKLADFGTCMKMDE--TGMVHCDTAVGTPDYISP 221
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1370507705 143 ELLL---GARHYTKAIDIWAIGCIFAELLTSEPIFH 175
Cdd:cd05621   222 EVLKsqgGDGYYGRECDWWSVGVFLFEMLVGDTPFY 257
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
18-182 1.51e-04

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: 43.41  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  18 VIALQKVflSHSDRKVWLLFDYAEHDLWHIIKFHRASKAN------KKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRD 91
Cdd:cd14102    53 IVLLKKV--GSGFRGVIKLLDWYERPDGFLIVMERPEPVKdlfdfiTEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRD 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  92 LKPANILVmgeGPERGRVKIADMGFARLFNSPLkpLADLDPVVVtfwYRAPELLLGARHYTKAIDIWAIGCIFAELLTSE 171
Cdd:cd14102   131 IKDENLLV---DLRTGELKLIDFGSGALLKDTV--YTDFDGTRV---YSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGD 202
                         170
                  ....*....|.
gi 1370507705 172 PIFHCRQEDIK 182
Cdd:cd14102   203 IPFEQDEEILR 213
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
74-123 1.76e-04

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


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 43.13  E-value: 1.76e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILvMGEGPERGRVKIADMGFARLFNSP 123
Cdd:cd14125   104 QMISRIEYVHSKNFIHRDIKPDNFL-MGLGKKGNLVYIIDFGLAKKYRDP 152
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
6-169 2.07e-04

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: 43.11  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLREL-KHPNVIALqkVFLSHSDRKVWLLFDYAEHDlwHIIKFHRAS----------KANKKPMQLPRSMVKSLLYQ 74
Cdd:cd05047    45 ELEVLCKLgHHPNIINL--LGACEHRGYLYLAIEYAPHG--NLLDFLRKSrvletdpafaIANSTASTLSSQQLLHFAAD 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSPLKPLADLDPVVvtfWYRAPELLLGArhYTKA 154
Cdd:cd05047   121 VARGMDYLSQKQFIHRDLAARNILV----GENYVAKIADFGLSRGQEVYVKKTMGRLPVR---WMAIESLNYSV--YTTN 191
                         170
                  ....*....|....*
gi 1370507705 155 IDIWAIGCIFAELLT 169
Cdd:cd05047   192 SDVWSYGVLLWEIVS 206
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
6-175 2.66e-04

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: 43.09  E-value: 2.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHsDRKVWLLfDYAEH-DLWhiikFHraskankkpmqLPRSMV----KSLLY--QILDG 78
Cdd:cd05594    75 ENRVLQNSRHPFLTALKYSFQTH-DRLCFVM-EYANGgELF----FH-----------LSRERVfsedRARFYgaEIVSA 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  79 IHYLHANW-VLHRDLKPANILVmgegPERGRVKIADMGFARlfnSPLKPLADLDPVVVTFWYRAPELLlGARHYTKAIDI 157
Cdd:cd05594   138 LDYLHSEKnVVYRDLKLENLML----DKDGHIKITDFGLCK---EGIKDGATMKTFCGTPEYLAPEVL-EDNDYGRAVDW 209
                         170
                  ....*....|....*...
gi 1370507705 158 WAIGCIFAELLTSEPIFH 175
Cdd:cd05594   210 WGLGVVMYEMMCGRLPFY 227
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
15-175 3.38e-04

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 42.03  E-value: 3.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  15 HPNVIALQKVFLShsDRKVWLLFDYAEHDLwhiikfHRASKANKKpmqLPRSMVKSLLYQILDGIHYLHANWVLHRDLKP 94
Cdd:cd13976    44 HPNISGVHEVIAG--ETKAYVFFERDHGDL------HSYVRSRKR---LREPEAARLFRQIASAVAHCHRNGIVLRDLKL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  95 ANILVMGEgpERGRVKIADMGFARLFNSPLKPLADLD--PVvvtfwYRAPELLLGARHYT-KAIDIWAIGCIFAELLTSE 171
Cdd:cd13976   113 RKFVFADE--ERTKLRLESLEDAVILEGEDDSLSDKHgcPA-----YVSPEILNSGATYSgKAADVWSLGVILYTMLVGR 185

                  ....
gi 1370507705 172 PIFH 175
Cdd:cd13976   186 YPFH 189
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
6-169 3.95e-04

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 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: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 42.36  E-value: 3.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705   6 EIALLRELKHPNVIALQKVFLSHSDRKVWLLFDYAehdlwHIIKFHRASKANkkpmqLPRSMVKSLLYQILDGIHYLHAN 85
Cdd:cd05110    59 EALIMASMDHPHLVRLLGVCLSPTIQLVTQLMPHG-----CLLDYVHEHKDN-----IGSQLLLNWCVQIAKGMMYLEER 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  86 WVLHRDLKPANILVmgEGPErgRVKIADMGFARLFNSPLKPLaDLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFA 165
Cdd:cd05110   129 RLVHRDLAARNVLV--KSPN--HVKITDFGLARLLEGDEKEY-NADGGKMPIKWMALE-CIHYRKFTHQSDVWSYGVTIW 202

                  ....
gi 1370507705 166 ELLT 169
Cdd:cd05110   203 ELMT 206
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
75-167 4.15e-04

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: 41.89  E-value: 4.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  75 ILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFARLFNSpLKPLADLdPVVVTfwyrAPELLLGARHYTKA 154
Cdd:cd05082   111 VCEAMEYLEGNNFVHRDLAARNVLV----SEDNVAKVSDFGLTKEASS-TQDTGKL-PVKWT----APEALREKKFSTKS 180
                          90
                  ....*....|...
gi 1370507705 155 iDIWAIGCIFAEL 167
Cdd:cd05082   181 -DVWSFGILLWEI 192
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
70-184 4.27e-04

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. 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-C 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: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 41.79  E-value: 4.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  70 SLLYQILDGIHYLHA-NWVLHRDLKPANILVMGegpeRGRVKIADMGfarlFNSPLKPLADLdpvvvtfwYRAPELLLGA 148
Cdd:cd14044   113 SVMYDIAKGMSYLHSsKTEVHGRLKSTNCVVDS----RMVVKITDFG----CNSILPPSKDL--------WTAPEHLRQA 176
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1370507705 149 RHYTKAiDIWAIGCIFAELLTSEPIF---HCRQEDIKTS 184
Cdd:cd14044   177 GTSQKG-DVYSYGIIAQEIILRKETFytaACSDRKEKIY 214
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
74-168 5.46e-04

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: 42.02  E-value: 5.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370507705  74 QILDGIHYLHANWVLHRDLKPANILVMGEgperGRVKIADMGFARlfnSPLKPLADLDPVVVTFWYRAPELLLGaRHYTK 153
Cdd:cd05588   104 EISLALNFLHEKGIIYRDLKLDNVLLDSE----GHIKLTDYGMCK---EGLRPGDTTSTFCGTPNYIAPEILRG-EDYGF 175
                          90
                  ....*....|....*
gi 1370507705 154 AIDIWAIGCIFAELL 168
Cdd:cd05588   176 SVDWWALGVLMFEML 190
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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