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Conserved domains on  [gi|525343631|ref|NP_001266614|]
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interferon-induced, double-stranded RNA-activated protein kinase [Gorilla gorilla gorilla]

Protein Classification

interferon-induced double-stranded RNA-activated protein kinase( domain architecture ID 14447364)

interferon-induced, double-stranded RNA-activated protein kinase plays an important role in the innate immune response to viral infection and is also involved in a wide variety of cellular processes such as regulation of signal transduction, apoptosis, proliferation and differentiation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
260-536 8.05e-161

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: 458.49  E-value: 8.05e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 260 DKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGVDYDPETSdd 339
Cdd:cd14047    1 DERFRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAEREVKALAKLDHPNIVRYNGCWDGFDYDPETS-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpenSKNSSRSKTKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14047   79 -----------SSNSSRSKTKCLFIQMEFCEKGTLESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLR 499
Cdd:cd14047  148 IFLVDTGKVKIGDFGLVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKSKFWTDLR 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 525343631 500 DGIISDIFDK---KEKTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd14047  228 NGILPDIFDKrykIEKTIIKKMLSKKPEDRPNASEILRTL 267
DSRM_EIF2AK2_rpt2 cd19904
second double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
99-165 3.35e-34

second double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


:

Pssm-ID: 380733  Cd Length: 69  Bit Score: 123.78  E-value: 3.35e-34
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631  99 GNYIGLINRIAQKKRLTVNYEQCAS-GVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQI 165
Cdd:cd19904    1 VNYISLLNQYAQKKRLTVNYEQCAStGVPGPPRFSCKCKIGQKEYGIGTGSTKQEAKQAAAKEAYEQL 68
DSRM_EIF2AK2_rpt1 cd19903
first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
8-59 2.35e-23

first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


:

Pssm-ID: 380732  Cd Length: 68  Bit Score: 93.22  E-value: 2.35e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631   8 GFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFRVIIDEREFPEGEGRS 59
Cdd:cd19903    1 GNYMGKLNEYCQKQKVVLDYVEVPTSGPSHDPRFTFQVVIDGKEYPEGEGKS 52
 
Name Accession Description Interval E-value
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
260-536 8.05e-161

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: 458.49  E-value: 8.05e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 260 DKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGVDYDPETSdd 339
Cdd:cd14047    1 DERFRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAEREVKALAKLDHPNIVRYNGCWDGFDYDPETS-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpenSKNSSRSKTKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14047   79 -----------SSNSSRSKTKCLFIQMEFCEKGTLESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLR 499
Cdd:cd14047  148 IFLVDTGKVKIGDFGLVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKSKFWTDLR 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 525343631 500 DGIISDIFDK---KEKTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd14047  228 NGILPDIFDKrykIEKTIIKKMLSKKPEDRPNASEILRTL 267
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
267-534 7.29e-65

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 212.00  E-value: 7.29e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN-----EKAEREVKALAKLDHVNIVHYngcwdgvdYDPETSDDYl 341
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKikkdrERILREIKILKKLKHPNIVRL--------YDVFEDEDK- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   342 essdydpensknssrsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:smart00220  72 --------------------LYLVMEYCEGGDLFDLLKKRG--RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   422 LVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL---HVCDTAFETSKFFTDL 498
Cdd:smart00220 130 LDEDGHVKLADFGLARQLDPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLtgkPPFPGDDQLLELFKKI 209
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 525343631   499 RDGIISDIFDKKE-----KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:smart00220 210 GKPKPPFPPPEWDispeaKDLIRKLLVKDPEKRLTAEEALQ 250
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
270-536 1.07e-53

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 189.45  E-value: 1.07e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIKRVKY---NNEKA----EREVKALAKLDHVNIVHYngcwdgvdYDPETSDDYLe 342
Cdd:COG0515   12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPelaADPEArerfRREARALARLNHPNIVRV--------YDVGEEDGRP- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssrsktkclFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:COG0515   83 --------------------YLVMEYVEGESLADLL--RRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLVTSLkNDGKRTRS---KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL-----HVCDTAFET--- 491
Cdd:COG0515  141 TPDGRVKLIDFGIARAL-GGATLTQTgtvVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLtgrppFDGDSPAELlra 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 525343631 492 --SKFFTDLRDGI--ISDIFDKkektLLQKLLSKKPEDRPNT-SEILRTL 536
Cdd:COG0515  220 hlREPPPPPSELRpdLPPALDA----IVLRALAKDPEERYQSaAELAAAL 265
Pkinase pfam00069
Protein kinase domain;
267-534 1.06e-34

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 130.06  E-value: 1.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631  267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE------REVKALAKLDHVNIVHYNGCWdgvdydpetsddy 340
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKkdknilREIKILKKLNHPNIVRLYDAF------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631  341 lESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWIENRrgekldkvlalelfeqitkgvdyihsKKLIHRDLKpsNI 420
Cdd:pfam00069  68 -EDKDN---------------LYLVLEYVEGGSLFDLLSEK--------------------------GAFSEREAK--FI 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631  421 FlvdtKQVkigdfglVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL---HVCDTAFETSKFFTD 497
Cdd:pfam00069 104 M----KQI-------LEGLESGSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLtgkPPFPGINGNEIYELI 172
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 525343631  498 LRDGIISDIFDK---KE-KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:pfam00069 173 IDQPYAFPELPSnlsEEaKDLLKKLLKKDPSKRLTATQALQ 213
DSRM_EIF2AK2_rpt2 cd19904
second double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
99-165 3.35e-34

second double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380733  Cd Length: 69  Bit Score: 123.78  E-value: 3.35e-34
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631  99 GNYIGLINRIAQKKRLTVNYEQCAS-GVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQI 165
Cdd:cd19904    1 VNYISLLNQYAQKKRLTVNYEQCAStGVPGPPRFSCKCKIGQKEYGIGTGSTKQEAKQAAAKEAYEQL 68
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
248-535 1.16e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 110.11  E-value: 1.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 248 DLPDMKETKYTVDKRFGMdFKEIELIGSGGFGQVFKAKHRIDGKTYVI-KRVKYNNEK----AEREVKALAKLDHVNIVH 322
Cdd:PTZ00267  51 DLPEGEEVPESNNPREHM-YVLTTLVGRNPTTAAFVATRGSDPKEKVVaKFVMLNDERqaayARSELHCLAACDHFGIVK 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 323 YngcwdgvdYDPETSDDylessdydpensknssrsktKCLFIqMEFCDKGTLEQWIENRRGEKL--DKVLALELFEQITK 400
Cdd:PTZ00267 130 H--------FDDFKSDD--------------------KLLLI-MEYGSGGDLNKQIKQRLKEHLpfQEYEVGLLFYQIVL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 401 GVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSK---GTLRYMSPEQISSQDYGKEVDLYALGLI 477
Cdd:PTZ00267 181 ALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASsfcGTPYYLAPELWERKRYSKKADMWSLGVI 260
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 478 LAELLHVCDTAFETSKffTDLRDGIISDIFD-------KKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:PTZ00267 261 LYELLTLHRPFKGPSQ--REIMQQVLYGKYDpfpcpvsSGMKALLDPLLSKNPALRPTTQQLLHT 323
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
270-482 4.07e-25

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 109.11  E-value: 4.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIK--RVKYNN-----EKAEREVKALAKLDHVNIVhyngcwdGVdYDPETSDDYLe 342
Cdd:NF033483  12 GERIGRGGMAEVYLAKDTRLDRDVAVKvlRPDLARdpefvARFRREAQSAASLSHPNIV-------SV-YDVGEDGGIP- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssrsktkclFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:NF033483  83 --------------------YIVMEYVDGRTLKDYI--REHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILI 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 423 VDTKQVKIGDFGLV-----TSLKNdgkrTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:NF033483 141 TKDGRVKVTDFGIAralssTTMTQ----TNSVlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEML 202
DSRM_EIF2AK2_rpt1 cd19903
first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
8-59 2.35e-23

first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380732  Cd Length: 68  Bit Score: 93.22  E-value: 2.35e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631   8 GFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFRVIIDEREFPEGEGRS 59
Cdd:cd19903    1 GNYMGKLNEYCQKQKVVLDYVEVPTSGPSHDPRFTFQVVIDGKEYPEGEGKS 52
DSRM smart00358
Double-stranded RNA binding motif;
101-165 7.41e-13

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 63.44  E-value: 7.41e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631   101 YIGLINRIAQKKRLTVNYEQCA-SGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQI 165
Cdd:smart00358   1 PKSLLQELAQKRKLPPEYELVKeEGPDHAPRFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSL 66
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
101-165 1.60e-12

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 62.63  E-value: 1.60e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631  101 YIGLINRIAQKKRLTVNYE--QCASGVHGPEgFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQI 165
Cdd:pfam00035   1 PKSLLQEYAQKNGKPPPYEyvSEEGPPHSPK-FTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
DSRM smart00358
Double-stranded RNA binding motif;
14-59 2.41e-10

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 56.50  E-value: 2.41e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 525343631    14 LNTYRQKQGVVLKYQELPNSGPPHDRRFTFRVIIDEREFPEGEGRS 59
Cdd:smart00358   5 LQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGKRTGEGEGSS 50
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
362-482 2.76e-09

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 60.24  E-value: 2.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   362 LFIQMEFCDKGTLEQWIENrrgeklDKVLALE----LFEQITKGVDYIHSKKLIHRDLKPSNIFLV---DTKQVKIGDFG 434
Cdd:TIGR03903   54 LFAVFEYVPGRTLREVLAA------DGALPAGetgrLMLQVLDALACAHNQGIVHRDLKPQNIMVSqtgVRPHAKVLDFG 127
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631   435 LVTSLKNDGKRTRSK--------GTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:TIGR03903  128 IGTLLPGVRDADVATltrttevlGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECL 183
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
13-64 2.09e-03

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 36.82  E-value: 2.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 525343631   13 ELNTYRQKQGVVLKYQELPNSGPPHDRRFTFRVIIDEREFPEGEGRSKKEAK 64
Cdd:pfam00035   4 LLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKLYGSGTGSSKKEAE 55
 
Name Accession Description Interval E-value
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
260-536 8.05e-161

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: 458.49  E-value: 8.05e-161
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 260 DKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGVDYDPETSdd 339
Cdd:cd14047    1 DERFRQDFKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEKAEREVKALAKLDHPNIVRYNGCWDGFDYDPETS-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpenSKNSSRSKTKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14047   79 -----------SSNSSRSKTKCLFIQMEFCEKGTLESWIEKRNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSN 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLR 499
Cdd:cd14047  148 IFLVDTGKVKIGDFGLVTSLKNDGKRTKSKGTLSYMSPEQISSQDYGKEVDIYALGLILFELLHVCDSAFEKSKFWTDLR 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 525343631 500 DGIISDIFDK---KEKTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd14047  228 NGILPDIFDKrykIEKTIIKKMLSKKPEDRPNASEILRTL 267
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
260-536 1.99e-117

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: 348.13  E-value: 1.99e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 260 DKRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN-----EKAEREVKALAKLDHVNIVHYNGCWDGVDydp 334
Cdd:cd13996    1 NSRYLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEkssasEKVLREVKALAKLNHPNIVRYYTAWVEEP--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 335 etsddylessdydpensknssrsktkCLFIQMEFCDKGTLEQWIENRRG-EKLDKVLALELFEQITKGVDYIHSKKLIHR 413
Cdd:cd13996   78 --------------------------PLYIQMELCEGGTLRDWIDRRNSsSKNDRKLALELFKQILKGVSYIHSKGIVHR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 414 DLKPSNIFLV-DTKQVKIGDFGLVTSL---------------KNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLI 477
Cdd:cd13996  132 DLKPSNIFLDnDDLQVKIGDFGLATSIgnqkrelnnlnnnnnGNTSNNSVGIGTPLYASPEQLDGENYNEKADIYSLGII 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 478 LAELLHVCDTAFETSKFFTDLRDGIISDIFDKK---EKTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd13996  212 LFEMLHPFKTAMERSTILTDLRNGILPESFKAKhpkEADLIQSLLSKNPEERPSAEQLLRSL 273
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
262-532 5.24e-70

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: 226.29  E-value: 5.24e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 262 RFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKY-NNEKAE----REVKALAKLDHVNIVHYNGCWDgvDYDPEt 336
Cdd:cd14048    3 RFLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLpNNELARekvlREVRALAKLDHPGIVRYFNAWL--ERPPE- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sdDYLESSD--YdpensknssrsktkcLFIQMEFCDKGTLEQWIENRRG-EKLDKVLALELFEQITKGVDYIHSKKLIHR 413
Cdd:cd14048   80 --GWQEKMDevY---------------LYIQMQLCRKENLKDWMNRRCTmESRELFVCLNIFKQIASAVEYLHSKGLIHR 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 414 DLKPSNIFLVDTKQVKIGDFGLVTSLKND-------------GKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAE 480
Cdd:cd14048  143 DLKPSNVFFSLDDVVKVGDFGLVTAMDQGepeqtvltpmpayAKHTGQVGTRLYMSPEQIHGNQYSEKVDIFALGLILFE 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 481 LLHVCDTAFETSKFFTDLRDGIISDIFDKK---EKTLLQKLLSKKPEDRPNTSEI 532
Cdd:cd14048  223 LIYSFSTQMERIRTLTDVRKLKFPALFTNKypeERDMVQQMLSPSPSERPEAHEV 277
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
262-533 5.68e-66

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: 215.70  E-value: 5.68e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 262 RFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK-----YNNEKAEREVKALAKLDHVNIVHYNGCWdgvdydpet 336
Cdd:cd14046    3 RYLTDFEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKlrsesKNNSRILREVMLLSRLNHQHVVRYYQAW--------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddyLESSDydpensknssrsktkcLFIQMEFCDKGTLEQWIENrrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd14046   74 ----IERAN----------------LYIQMEYCEKSTLRDLIDS--GLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLK 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLKN-------------------DGKRTRSKGTLRYMSPEQISSQD--YGKEVDLYALG 475
Cdd:cd14046  132 PVNIFLDSNGNVKIGDFGLATSNKLnvelatqdinkstsaalgsSGDLTGNVGTALYVAPEVQSGTKstYNEKVDMYSLG 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 476 LILAELLHVCDTAFETSKFFTDLRDGIIS--DIFDK----KEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14046  212 IIFFEMCYPFSTGMERVQILTALRSVSIEfpPDFDDnkhsKQAKLIRWLLNHDPAKRPSAQELL 275
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
267-534 7.29e-65

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 212.00  E-value: 7.29e-65
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN-----EKAEREVKALAKLDHVNIVHYngcwdgvdYDPETSDDYl 341
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKikkdrERILREIKILKKLKHPNIVRL--------YDVFEDEDK- 71
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   342 essdydpensknssrsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:smart00220  72 --------------------LYLVMEYCEGGDLFDLLKKRG--RLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENIL 129
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   422 LVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL---HVCDTAFETSKFFTDL 498
Cdd:smart00220 130 LDEDGHVKLADFGLARQLDPGEKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLtgkPPFPGDDQLLELFKKI 209
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 525343631   499 RDGIISDIFDKKE-----KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:smart00220 210 GKPKPPFPPPEWDispeaKDLIRKLLVKDPEKRLTAEEALQ 250
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
266-535 1.85e-63

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: 208.47  E-value: 1.85e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN------EKAEREVKALAKLDHVNIVHYNgcwdgvdydpetsDD 339
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNmsekerEEALNEVKLLSKLKHPNIVKYY-------------ES 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLESsdydpensknssrsktKCLFIQMEFCDKGTLEQWIENRR--GEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd08215   68 FEEN----------------GKLCIVMEYADGGDLAQKIKKQKkkGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKT 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAFETSKfFT 496
Cdd:cd08215  132 QNIFLTKDGVVKLGDFGISKVLESTTDLAKTVvGTPYYLSPELCENKPYNYKSDIWALGCVLYELC-TLKHPFEANN-LP 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 525343631 497 DLRDGI-------ISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:cd08215  210 ALVYKIvkgqyppIPSQYSSELRDLVNSMLQKDPEKRPSANEILSS 255
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
273-536 1.78e-60

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: 199.03  E-value: 1.78e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNN-----EKAEREVKALAKLDHVNIVHYNGCWDgvdydpetsddylessdyd 347
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKlkkllEELLREIEILKKLNHPNIVKLYDVFE------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 pensknssrsKTKCLFIQMEFCDKGTLEQWIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQ 427
Cdd:cd00180   62 ----------TENFLYLVMEYCEGGSLKDLLKENKG-PLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 428 VKIGDFGLVTSLKNDGKRTRSKGTL---RYMSPEQISSQDYGKEVDLYALGLILAELlhvcdtafetskffTDLRDgiis 504
Cdd:cd00180  131 VKLADFGLAKDLDSDDSLLKTTGGTtppYYAPPELLGGRYYGPKVDIWSLGVILYEL--------------EELKD---- 192
                        250       260       270
                 ....*....|....*....|....*....|..
gi 525343631 505 difdkkektLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd00180  193 ---------LIRRMLQYDPKKRPSAKELLEHL 215
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
270-534 1.92e-59

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: 197.81  E-value: 1.92e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN-------EKAEREVKALAKLDHVNIVHYngcwdgvdYDpetsddyle 342
Cdd:cd14014    5 VRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELaedeefrERFLREARALARLSHPNIVRV--------YD--------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 sSDYDPensknssrsktKCLFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd14014   68 -VGEDD-----------GRPYIVMEYVEGGSLADLL--RERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLVTSLkNDGKRTRS---KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL-----HVCDTAFETSKF 494
Cdd:cd14014  134 TEDGRVKLTDFGIARAL-GDSGLTQTgsvLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLtgrppFDGDSPAAVLAK 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 495 FTDLRDGIISDIFDKKEK---TLLQKLLSKKPEDRPNT-SEILR 534
Cdd:cd14014  213 HLQEAPPPPSPLNPDVPPaldAIILRALAKDPEERPQSaAELLA 256
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
270-536 1.07e-53

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 189.45  E-value: 1.07e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIKRVKY---NNEKA----EREVKALAKLDHVNIVHYngcwdgvdYDPETSDDYLe 342
Cdd:COG0515   12 LRLLGRGGMGVVYLARDLRLGRPVALKVLRPelaADPEArerfRREARALARLNHPNIVRV--------YDVGEEDGRP- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssrsktkclFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:COG0515   83 --------------------YLVMEYVEGESLADLL--RRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLVTSLkNDGKRTRS---KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL-----HVCDTAFET--- 491
Cdd:COG0515  141 TPDGRVKLIDFGIARAL-GGATLTQTgtvVGTPGYMAPEQARGEPVDPRSDVYSLGVTLYELLtgrppFDGDSPAELlra 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 525343631 492 --SKFFTDLRDGI--ISDIFDKkektLLQKLLSKKPEDRPNT-SEILRTL 536
Cdd:COG0515  220 hlREPPPPPSELRpdLPPALDA----IVLRALAKDPEERYQSaAELAAAL 265
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
266-534 4.67e-52

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: 178.17  E-value: 4.67e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE----REVKALAKLDHVNIVHYNGCWdgvdydpeTSDDYL 341
Cdd:cd05122    1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKesilNEIAILKKCKHPNIVKYYGSY--------LKKDEL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdydpensknssrsktkclFIQMEFCDKGTLEQWIENRRG---EKLDKVLALELFeqitKGVDYIHSKKLIHRDLKPS 418
Cdd:cd05122   73 ---------------------WIVMEFCSGGSLKDLLKNTNKtltEQQIAYVCKEVL----KGLEYLHSHGIIHRDIKAA 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAEL---------LHVCDTAF 489
Cdd:cd05122  128 NILLTSDGEVKLIDFGLSAQLSDGKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMaegkppyseLPPMKALF 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 525343631 490 ETSKF-FTDLRDG-IISDIFdkkeKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd05122  208 LIATNgPPGLRNPkKWSKEF----KDFLKKCLQKDPEKRPTAEQLLK 250
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
262-533 1.42e-50

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: 175.39  E-value: 1.42e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 262 RFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV------KYNNEKAEREVKALAKLDHVNIVHYNGCWdgvdydpe 335
Cdd:cd14049    3 RYLNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKIlikkvtKRDCMKVLREVKVLAGLQHPNIVGYHTAW-------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 336 tsddyLESSDYdpensknssrsktkCLFIQMEFCDKgTLEQWI--ENRRGEK----------LDKVLALELFEQITKGVD 403
Cdd:cd14049   75 -----MEHVQL--------------MLYIQMQLCEL-SLWDWIveRNKRPCEeefksapytpVDVDVTTKILQQLLEGVT 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 404 YIHSKKLIHRDLKPSNIFL-VDTKQVKIGDFGLV---------TSLKNDGKRTRSK----GTLRYMSPEQISSQDYGKEV 469
Cdd:cd14049  135 YIHSMGIVHRDLKPRNIFLhGSDIHVRIGDFGLAcpdilqdgnDSTTMSRLNGLTHtsgvGTCLYAAPEQLEGSHYDFKS 214
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 470 DLYALGLILAELLHVCDTAFETSKFFTDLRDGIISDIFDKK---EKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14049  215 DMYSIGVILLELFQPFGTEMERAEVLTQLRNGQIPKSLCKRwpvQAKYIKLLTSTEPSERPSASQLL 281
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
273-536 3.15e-49

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: 170.41  E-value: 3.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRidGKTYVIKRVKYNNEKAE------REVKALAKLDHVNIVHYNGcwdgvdydpetsddylessdy 346
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDEllkefrREVSILSKLRHPNIVQFIG--------------------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 dpensknsSRSKTKCLFIQMEFCDKGTLEQWIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK 426
Cdd:cd13999   58 --------ACLSPPPLCIVTEYMPGGSLYDLLHKKKI-PLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENF 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 427 QVKIGDFGLVTSL-KNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAFE--------TSKFFTD 497
Cdd:cd13999  129 TVKIADFGLSRIKnSTTEKMTGVVGTPRWMAPEVLRGEPYTEKADVYSFGIVLWELL-TGEVPFKelspiqiaAAVVQKG 207
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 525343631 498 LRDGIISDIfDKKEKTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd13999  208 LRPPIPPDC-PPELSKLIKRCWNEDPEKRPSFSEIVKRL 245
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
266-535 2.87e-45

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: 160.40  E-value: 2.87e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN--NEKaER-----EVKALAKLDHVNIVHYngcwdgvdYDPEtsd 338
Cdd:cd08217    1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGkmSEK-EKqqlvsEVNILRELKHPNIVRY--------YDRI--- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dylessdYDPENSKnssrsktkcLFIQMEFCDKGTLEQWIEN--RRGEKLDKVLALELFEQITKGVDYIH-----SKKLI 411
Cdd:cd08217   69 -------VDRANTT---------LYIVMEYCEGGDLAQLIKKckKENQYIPEEFIWKIFTQLLLALYECHnrsvgGGKIL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 412 HRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAEL--LHvcdTA 488
Cdd:cd08217  133 HRDLKPANIFLDSDNNVKLGDFGLARVLSHDSSFAKTYvGTPYYMSPELLNEQSYDEKSDIWSLGCLIYELcaLH---PP 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 525343631 489 FETSKFF---TDLRDGIISDI---FDKKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:cd08217  210 FQAANQLelaKKIKEGKFPRIpsrYSSELNEVIKSMLNVDPDKRPSVEELLQL 262
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
270-534 3.94e-45

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: 159.61  E-value: 3.94e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIK------RVKYNNEKAEREVKALAKLDHVNIVHYngcwdgvdYDpetsddYLES 343
Cdd:cd14003    5 GKTLGEGSFGKVKLARHKLTGEKVAIKiidkskLKEEIEEKIKREIEIMKLLNHPNIIKL--------YE------VIET 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 SDYdpensknssrsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd14003   71 ENK---------------IYLVMEYASGGELFDYIVNNG--RLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLD 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 424 DTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLIL---------------AELLH-VCD 486
Cdd:cd14003  134 KNGNLKIIDFGLSNEFRGGSLLKTFCGTPAYAAPEVLLGRKYdGPKADVWSLGVILyamltgylpfdddndSKLFRkILK 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 525343631 487 TAFETSKFFT-DLRDgiisdifdkkektLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14003  214 GKYPIPSHLSpDARD-------------LIRRMLVVDPSKRITIEEILN 249
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
266-535 8.92e-43

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: 153.34  E-value: 8.92e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN------EKAEREVKALAKLDHVNIVHYngcwdgvdydpetsdd 339
Cdd:cd08529    1 DFEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRmsrkmrEEAIDEARVLSKLNSPYVIKY---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdYDPENSKNSsrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd08529   65 ------YDSFVDKGK-------LNIVMEYAENGDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMN 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELL---HVCDTAFETSKFF 495
Cdd:cd08529  132 IFLDKGDNVKIGDLGVAKILSDTTNFAQTIvGTPYYLSPELCEDKPYNEKSDVWALGCVLYELCtgkHPFEAQNQGALIL 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 525343631 496 TDLRdGI---ISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:cd08529  212 KIVR-GKyppISASYSQDLSQLIDSCLTKDYRQRPDTTELLRN 253
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
266-534 1.72e-42

The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKI proteins are monomeric and they play pivotal roles in the nervous system, including long-term potentiation, dendritic arborization, neurite outgrowth, and the formation of spines, synapses, and axons. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. CAMKIV is implicated in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors, as well as in T-cell development and signaling. The CAMK family also consists of other related kinases including the Phosphorylase kinase Gamma subunit (PhKG), the C-terminal kinase domains of Ribosomal S6 kinase (RSK) and Mitogen and stress-activated kinase (MSK), Doublecortin-like kinase (DCKL), and the MAPK-activated protein kinases MK2, MK3, and MK5, among others. The CAMK family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 152.63  E-value: 1.72e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIK-----RVKYNNEKA-EREVKALAKLDHVNIVHYngcwdgvdYdpetsdD 339
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKiidkkKLKSEDEEMlRREIEILKRLDHPNIVKL--------Y------E 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd05117   67 VFEDDKN---------------LYLVMELCTGGELFDRIVKK--GSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPEN 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQ---VKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhvcdtaFETSKFFT 496
Cdd:cd05117  130 ILLASKDPdspIKIIDFGLAKIFEEGEKLKTVCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILL------CGYPPFYG 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631 497 DLRDGIISDI------FDKKE--------KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd05117  204 ETEQELFEKIlkgkysFDSPEwknvseeaKDLIKRLLVVDPKKRLTAAEALN 255
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
266-534 9.59e-42

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: 150.32  E-value: 9.59e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKR------VKYNNEKA-EREVKALAKLDHVNIVHYNGCWdgvdydpetsd 338
Cdd:cd14007    1 DFEIGKPLGKGKFGNVYLAREKKSGFIVALKVisksqlQKSGLEHQlRREIEIQSHLRHPNILRLYGYF----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dylessdYDPENsknssrsktkcLFIQMEFCDKGTLEQwIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd14007   70 -------EDKKR-----------IYLILEYAPNGELYK-ELKKQK-RFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPE 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSLKNDGKRTRSkGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCdTAFEtSKFFTDL 498
Cdd:cd14007  130 NILLGSNGELKLADFGWSVHAPSNRRKTFC-GTLDYLPPEMVEGKEYDYKVDIWSLGVLCYELLVGK-PPFE-SKSHQET 206
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 525343631 499 RDGIIS-DI-FDKK----EKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14007  207 YKRIQNvDIkFPSSvspeAKDLISKLLQKDPSKRLSLEQVLN 248
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
266-535 5.43e-41

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: 148.30  E-value: 5.43e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKY------NNEKAEREVKALAKL-DHVNIVHYNGCWDgvdydpetsd 338
Cdd:cd13997    1 HFHELEQIGSGSFSEVFKVRSKVDGCLYAVKKSKKpfrgpkERARALREVEAHAALgQHPNIVRYYSSWE---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dylessdydpENSKnssrsktkcLFIQMEFCDKGTLEQWIE-NRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd13997   71 ----------EGGH---------LYIQMELCENGSLQDALEeLSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKP 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSLKNDGKrtRSKGTLRYMSPEQIS-SQDYGKEVDLYALGLILAELlhVCDTAFETS-KFF 495
Cdd:cd13997  132 DNIFISNKGTCKIGDFGLATRLETSGD--VEEGDSRYLAPELLNeNYTHLPKADIFSLGVTVYEA--ATGEPLPRNgQQW 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 496 TDLRDGIISDIFDKKEKTLLQKL----LSKKPEDRPNTSEILRT 535
Cdd:cd13997  208 QQLRQGKLPLPPGLVLSQELTRLlkvmLDPDPTRRPTADQLLAH 251
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
266-534 9.61e-40

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPKKKs (MKKKs or MAP3Ks) are also called MAP/ERK kinase kinases (MEKKs) in some cases. They phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. This subfamily is composed of the Apoptosis Signal-regulating Kinases ASK1 (or MAPKKK5) and ASK2 (or MAPKKK6), MEKK1, MEKK2, MEKK3, MEKK4, as well as plant and fungal MAPKKKs. Also included in this subfamily are the cell division control proteins Schizosaccharomyces pombe Cdc7 and Saccharomyces cerevisiae Cdc15. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 145.36  E-value: 9.61e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE------REVKALAKLDHVNIVHYNGCwdgvdydpETSDD 339
Cdd:cd06606    1 RWKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEelealeREIRILSSLKHPNIVRYLGT--------ERTEN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLessdydpensknssrsktkCLFiqMEFCDKGTLEQWIENRRG--EKLDKVLAlelfEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd06606   73 TL-------------------NIF--LEYVPGGSLASLLKKFGKlpEPVVRKYT----RQILEGLEYLHSNGIVHRDIKG 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 418 SNIFLVDTKQVKIGDFG----LVTSLKNDGKRTRsKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhvcdTA----F 489
Cdd:cd06606  128 ANILVDSDGVVKLADFGcakrLAEIATGEGTKSL-RGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMA----TGkppwS 202
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631 490 ETSKFFTDL-RDGI------ISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06606  203 ELGNPVAALfKIGSsgepppIPEHLSEEAKDFLRKCLQRDPKKRPTADELLQ 254
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
266-534 1.80e-39

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: 144.50  E-value: 1.80e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN------EKAEREVKALAKLDHVNIVHYNGCWDGvdydpetsdd 339
Cdd:cd08223    1 EYQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNaskrerKAAEQEAKLLSKLKHPNIVSYKESFEG---------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknssrsKTKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd08223   71 ------------------EDGFLYIVMGFCEGGDLYTRLKEQKGVLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQN 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKN--DGKRTRSkGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVcDTAFeTSKFFTD 497
Cdd:cd08223  133 IFLTKSNIIKVGDLGIARVLESssDMATTLI-GTPYYMSPELFSNKPYNHKSDVWALGCCVYEMATL-KHAF-NAKDMNS 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 498 LRDGIIS-------DIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd08223  210 LVYKILEgklppmpKQYSPELGELIKAMLHQDPEKRPSVKRILR 253
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
267-534 1.29e-38

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: 142.26  E-value: 1.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN------EKAEREVKALAKLDHVNIVHYNgcwdgvdydpetsddy 340
Cdd:cd08218    2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKmspkerEESRKEVAVLSKMKHPNIVQYQ---------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpensknSSRSKTKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd08218   66 -------------ESFEENGNLYIVMDYCDGGDLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNI 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 421 FLVDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVcDTAFETSKfFTDLR 499
Cdd:cd08218  133 FLTKDGIIKLGDFGIARVLNSTVELARTcIGTPYYLSPEICENKPYNNKSDIWALGCVLYEMCTL-KHAFEAGN-MKNLV 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 525343631 500 DGII-------SDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd08218  211 LKIIrgsyppvPSRYSYDLRSLVSQLFKRNPRDRPSINSILE 252
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
273-534 6.43e-38

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: 140.38  E-value: 6.43e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIK----------RVKYN--------NEKAEREVKALAKLDHVNIVHYNGCWDgvdydp 334
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKifnksrlrkrREGKNdrgkiknaLDDVRREIAIMKKLDHPNIVRLYEVID------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 335 etsddylessdyDPENSKnssrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRD 414
Cdd:cd14008   75 ------------DPESDK---------LYLVLEYCEGGPVMELDSGDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRD 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFLVDTKQVKIGDFGLVTSLKNDGKR-TRSKGTLRYMSPE--QISSQDY-GKEVDLYALG-----LILAELLHVC 485
Cdd:cd14008  134 IKPENLLLTADGTVKISDFGVSEMFEDGNDTlQKTAGTPAFLAPElcDGDSKTYsGKAADIWALGvtlycLVFGRLPFNG 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 525343631 486 DTAFETSKFFTDLRDGIISDIFDKKE-KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14008  214 DNILELYEAIQNQNDEFPIPPELSPElKDLLRRMLEKDPEKRITLKEIKE 263
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
266-534 1.44e-37

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: 139.65  E-value: 1.44e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER-----EVKALAKLDHVNIVHYNGcwdgVDYDPETsddy 340
Cdd:cd06623    2 DLERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEEFRkqllrELKTLRSCESPYVVKCYG----AFYKEGE---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpensknssrsktkcLFIQMEFCDKGTLEQWIenRRGEKL-DKVLALeLFEQITKGVDYIHSK-KLIHRDLKPS 418
Cdd:cd06623   74 ---------------------ISIVLEYMDGGSLADLL--KKVGKIpEPVLAY-IARQILKGLDYLHTKrHIIHRDIKPS 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL--------------- 482
Cdd:cd06623  130 NLLINSKGEVKIADFGISKVLENTLDQCNTfVGTVTYMSPERIQGESYSYAADIWSLGLTLLECAlgkfpflppgqpsff 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 483 ----HVCDTAFEtskfftDLRDGIISDIFdkkeKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06623  210 elmqAICDGPPP------SLPAEEFSPEF----RDFISACLQKDPKKRPSAAELLQ 255
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
267-534 1.12e-36

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 137.01  E-value: 1.12e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN------EKAEREVKALAKLDHVNIVHYNGCWDgvdydpetsddy 340
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKmpvkekEASKKEVILLAKMKHPNIVTFFASFQ------------ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpENSKnssrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd08225   70 --------ENGR---------LFIVMEYCDGGDLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNI 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 421 FLVDTKQV-KIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVcDTAFETSKF---- 494
Cdd:cd08225  133 FLSKNGMVaKLGDFGIARQLNDSMELAYTcVGTPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTL-KHPFEGNNLhqlv 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 525343631 495 --FTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd08225  212 lkICQGYFAPISPNFSRDLRSLISQLFKVSPRDRPSITSILK 253
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
266-533 1.71e-36

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: 136.40  E-value: 1.71e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV------KYNNEKAEREVKALAKLDHVNIVHYngcwdgvdYDPETSDd 339
Cdd:cd08220    1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIpveqmtKEERQAALNEVKVLSMLHHPNIIEY--------YESFLED- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknssrsktKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd08220   72 --------------------KALMIVMEYAPGGTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQN 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQ-VKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVcDTAFETSKF---- 494
Cdd:cd08220  132 ILLNKKRTvVKIGDFGISKILSSKSKAYTVVGTPCYISPELCEGKPYNQKSDIWALGCVLYELASL-KRAFEAANLpalv 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 525343631 495 --FTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd08220  211 lkIMRGTFAPISDRYSEELRHLILSMLHLDPNKRPTLSEIM 251
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
266-535 2.70e-36

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: 135.60  E-value: 2.70e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN-EKAER-----EVKALAKLDHVNIVHYNgcwdgvdydpetsdd 339
Cdd:cd08530    1 DFKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLGSlSQKERedsvnEIRLLASVNHPNIIRYK--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpENSKNSSRsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALEL----FEQITKGVDYIHSKKLIHRDL 415
Cdd:cd08530   66 ---------EAFLDGNR-----LCIVMEYAPFGDLSKLISKRK--KKRRLFPEDDiwriFIQMLRGLKALHDQKILHRDL 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 416 KPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSkGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVcDTAFEtSKFF 495
Cdd:cd08530  130 KSANILLSAGDLVKIGDLGISKVLKKNLAKTQI-GTPLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATF-RPPFE-ARTM 206
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 525343631 496 TDLRDGI-------ISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:cd08530  207 QELRYKVcrgkfppIPPVYSQDLQQIIRSLLQVNPKKRPSCDKLLQS 253
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
267-533 7.02e-36

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: 134.36  E-value: 7.02e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK--YNNEKAE----REVKALAKL-DHVNIVHYNGCWDgvdydpetsdd 339
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRsrFRGEKDRkrklEEVERHEKLgEHPNCVRFIKAWE----------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknssrsKTKCLFIQMEFCDKgTLEQWIEnrRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14050   72 ------------------EKGILYIQTELCDT-SLQQYCE--ETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPAN 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSqDYGKEVDLYALGLILAELlhVCDtaFETSKFFTD-- 497
Cdd:cd14050  131 IFLSKDGVCKLGDFGLVVELDKEDIHDAQEGDPRYMAPELLQG-SFTKAADIFSLGITILEL--ACN--LELPSGGDGwh 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 525343631 498 -LRDGIISDIF----DKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14050  206 qLRQGYLPEEFtaglSPELRSIIKLMMDPDPERRPTAEDLL 246
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
267-534 5.75e-35

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: 131.95  E-value: 5.75e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER---EVKALAKLDHVNIVHYNGCwdgvdydpetsddYLES 343
Cdd:cd06614    2 YKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKELiinEILIMKECKHPNIVDYYDS-------------YLVG 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 sdydpensknssrsktKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALeLFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd06614   69 ----------------DELWVVMEYMDGGSLTDIITQNPVRMNESQIAY-VCREVLQGLEYLHSQNVIHRDIKSDNILLS 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 424 DTKQVKIGDFGLVTSL-KNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL-----HVCDTAFE-----TS 492
Cdd:cd06614  132 KDGSVKLADFGFAAQLtKEKSKRNSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAegeppYLEEPPLRalfliTT 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 525343631 493 KFFTDLRDgiiSDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06614  212 KGIPPLKN---PEKWSPEFKDFLNKCLVKDPEKRPSAEELLQ 250
Pkinase pfam00069
Protein kinase domain;
267-534 1.06e-34

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 130.06  E-value: 1.06e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631  267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE------REVKALAKLDHVNIVHYNGCWdgvdydpetsddy 340
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKkdknilREIKILKKLNHPNIVRLYDAF------------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631  341 lESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWIENRrgekldkvlalelfeqitkgvdyihsKKLIHRDLKpsNI 420
Cdd:pfam00069  68 -EDKDN---------------LYLVLEYVEGGSLFDLLSEK--------------------------GAFSEREAK--FI 103
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631  421 FlvdtKQVkigdfglVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL---HVCDTAFETSKFFTD 497
Cdd:pfam00069 104 M----KQI-------LEGLESGSSLTTFVGTPWYMAPEVLGGNPYGPKVDVWSLGCILYELLtgkPPFPGINGNEIYELI 172
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 525343631  498 LRDGIISDIFDK---KE-KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:pfam00069 173 IDQPYAFPELPSnlsEEaKDLLKKLLKKDPSKRLTATQALQ 213
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
267-482 1.78e-34

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: 131.45  E-value: 1.78e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK------AEREVKALAKLDHVNIVHYngcwdgvdydpetsddy 340
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEegipstALREISLLKELKHPNIVKL----------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdYDPENSKNSsrsktkcLFIQMEFCDKgTLEQWIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd07829   64 -----LDVIHTENK-------LYLVFEYCDQ-DLKKYLDKRPG-PLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNL 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 421 FLVDTKQVKIGDFGLVTSLKNDGKR-TRSKGTLRYMSPEQI-SSQDYGKEVDLYALGLILAELL 482
Cdd:cd07829  130 LINRDGVLKLADFGLARAFGIPLRTyTHEVVTLWYRAPEILlGSKHYSTAVDIWSVGCIFAELI 193
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
266-534 3.15e-34

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: 129.98  E-value: 3.15e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK-------YNNEKAEREVKALAKLDHVNIVHYNGCWdgvdydpetsd 338
Cdd:cd14099    2 RYRRGKFLGKGGFAKCYEVTDMSTGKVYAGKVVPkssltkpKQREKLKSEIKIHRSLKHPNIVKFHDCF----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dylessdydpENSKNssrsktkcLFIQMEFCDKGTLEQWIENRRgekldkvlALELFE------QITKGVDYIHSKKLIH 412
Cdd:cd14099   71 ----------EDEEN--------VYILLELCSNGSLMELLKRRK--------ALTEPEvryfmrQILSGVKYLHSNRIIH 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 413 RDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQIS-SQDYGKEVDLYALGLILAELLhVCDTAFE 490
Cdd:cd14099  125 RDLKLGNLFLDENMNVKIGDFGLAARLEYDGERKKTLcGTPNYIAPEVLEkKKGHSFEVDIWSLGVILYTLL-VGKPPFE 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 491 TSKFFTDLR-----------DGIISDIfdkkEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14099  204 TSDVKETYKrikkneysfpsHLSISDE----AKDLIRSMLQPDPTKRPSLDEILS 254
DSRM_EIF2AK2_rpt2 cd19904
second double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
99-165 3.35e-34

second double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the second motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380733  Cd Length: 69  Bit Score: 123.78  E-value: 3.35e-34
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631  99 GNYIGLINRIAQKKRLTVNYEQCAS-GVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQI 165
Cdd:cd19904    1 VNYISLLNQYAQKKRLTVNYEQCAStGVPGPPRFSCKCKIGQKEYGIGTGSTKQEAKQAAAKEAYEQL 68
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
273-526 4.00e-34

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: 129.65  E-value: 4.00e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRV------KYNNEKAEREVKALAKLDHVNIVHYNgcwdgvdydpetsdDYLESSDY 346
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEIsrkklnKKLQENLESEIAILKSIKHPNIVRLY--------------DVQKTEDF 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 dpensknssrsktkcLFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK 426
Cdd:cd14009   67 ---------------IYLVLEYCAGGDLSQYI--RKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSG 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 427 ---QVKIGDFGLVTSLKNDGKrtrsKGTLR----YMSPEQISSQDYGKEVDLYALGLILAELLHvCDTAFETSKFFtDLR 499
Cdd:cd14009  130 ddpVLKIADFGFARSLQPASM----AETLCgsplYMAPEILQFQKYDAKADLWSVGAILFEMLV-GKPPFRGSNHV-QLL 203
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 525343631 500 DGIISDIFDKKE----------KTLLQKLLSKKPEDR 526
Cdd:cd14009  204 RNIERSDAVIPFpiaaqlspdcKDLLRRLLRRDPAER 240
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
266-533 6.46e-34

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: 129.31  E-value: 6.46e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK-------YNNEKAEREVKALAKLDHVNIVHYngcwdgvdydpetsd 338
Cdd:cd08224    1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQifemmdaKARQDCLKEIDLLQQLNHPNIIKY--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dyLESSDYDPEnsknssrsktkcLFIQMEFCDKGTLEQWIENRRGEK--LDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd08224   66 --LASFIENNE------------LNIVLELADAGDLSRLIKHFKKQKrlIPERTIWKYFVQLCSALEHMHSKRIMHRDIK 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELlhvcdtAFETSKFF 495
Cdd:cd08224  132 PANVFITANGVVKLGDLGLGRFFSSKTTAAHSLvGTPYYMSPERIREQGYDFKSDIWSLGCLLYEM------AALQSPFY 205
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631 496 TD----------LRDG----IISDIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd08224  206 GEkmnlyslckkIEKCeyppLPADLYSQELRDLVAACIQPDPEKRPDISYVL 257
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
266-535 2.89e-33

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: 127.92  E-value: 2.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRID-GKTYVIKRVKYNNEKAE------REVKALAKLD---HVNIVHYNGCWdgvdydpe 335
Cdd:cd14052    1 RFANVELIGSGEFSQVYKVSERVPtGKVYAVKKLKPNYAGAKdrlrrlEEVSILRELTldgHDNIVQLIDSW-------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 336 tsddylESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWI-ENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRD 414
Cdd:cd14052   73 ------EYHGH---------------LYIQTELCENGSLDVFLsELGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLD 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRsKGTLRYMSPEQISSQDYGKEVDLYALGLILAE-------------- 480
Cdd:cd14052  132 LKPANVLITFEGTLKIGDFGMATVWPLIRGIER-EGDREYIAPEILSEHMYDKPADIFSLGLILLEaaanvvlpdngdaw 210
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 481 -----------------LLHVCDTaFETSKFFTDLRDGIISDIFDkkekTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:cd14052  211 qklrsgdlsdaprlsstDLHSASS-PSSNPPPDPPNMPILSGSLD----RVVRWMLSPEPDRRPTADDVLAT 277
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
268-536 3.74e-33

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: 127.28  E-value: 3.74e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   268 KEIELIGSGGFGQVFKAKHR-IDGKTYV---IKRVKYNNEKAE-----REVKALAKLDHVNIVHYNGCwdgvdydpetsd 338
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGTLKgKGDGKEVevaVKTLKEDASEQQieeflREARIMRKLDHPNIVKLLGV------------ 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   339 dyleSSDYDPensknssrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:smart00221  70 ----CTEEEP-------------LMIVMEYMPGGDLLDYLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAAR 132
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   419 NIFLVDTKQVKIGDFGLVTSLKNDG--KRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDT---AFETSK 493
Cdd:smart00221 133 NCLVGENLVVKISDFGLSRDLYDDDyyKVKGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEEpypGMSNAE 212
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 525343631   494 FFTDLRDGII--------SDIFDkkektLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:smart00221 213 VLEYLKKGYRlpkppncpPELYK-----LMLQCWAEDPEDRPTFSELVEIL 258
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
267-481 4.44e-33

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: 127.78  E-value: 4.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE------REVKALAKLD---HVNIVHYNGCWDGVDYDPETS 337
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEGiplstiREIALLKQLEsfeHPNVVRLLDVCHGPRTDRELK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 ddylessdydpensknssrsktkcLFIQMEFCDKgTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd07838   81 ------------------------LTLVFEHVDQ-DLATYLDKCPKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKP 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd07838  136 QNILVTSDGQVKLADFGLARIYSFEMALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAEL 199
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
266-533 5.44e-33

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: 126.65  E-value: 5.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN----EKAEREVKALAKLDHVNIVHYNGCWDGVDYdpetsddyl 341
Cdd:cd06613    1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPgddfEIIQQEISMLKECRHPNIVAYFGSYLRRDK--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdydpensknssrsktkcLFIQMEFCDKGTLeQWIENRRGEKLDKVLALELFEQItKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd06613   72 --------------------LWIVMEYCGGGSL-QDIYQVTGPLSELQIAYVCRETL-KGLAYLHSTGKIHRDIKGANIL 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFGLVTSLKND-GKRTRSKGTLRYMSPEQISSQD---YGKEVDLYALGLI---LAEL------LHVCDTA 488
Cdd:cd06613  130 LTEDGDVKLADFGVSAQLTATiAKRKSFIGTPYWMAPEVAAVERkggYDGKCDIWALGITaieLAELqppmfdLHPMRAL 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 525343631 489 FETSKFFTD---LRDgiiSDIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd06613  210 FLIPKSNFDppkLKD---KEKWSPDFHDFIKKCLTKNPKKRPTATKLL 254
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
266-526 1.21e-32

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: 125.44  E-value: 1.21e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV--KYNNEKA----EREVKALAKLDHVNIVHYngcwdgvdydpetsDD 339
Cdd:cd14002    2 NYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIpkRGKSEKElrnlRQEIEILRKLNHPNIIEM--------------LD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLESSdydpensknssrsktKCLFIQMEFCDkGTLEQWIENrrgeklDKVLALELF----EQITKGVDYIHSKKLIHRDL 415
Cdd:cd14002   68 SFETK---------------KEFVVVTEYAQ-GELFQILED------DGTLPEEEVrsiaKQLVSALHYLHSNRIIHRDM 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 416 KPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAFETSKF 494
Cdd:cd14002  126 KPQNILIGKGGVVKLCDFGFARAMSCNTLVLTSiKGTPLYMAPELVQEQPYDHTADLWSLGCILYELF-VGQPPFYTNSI 204
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 525343631 495 FTDLRDGIISDIFDKKE-----KTLLQKLLSKKPEDR 526
Cdd:cd14002  205 YQLVQMIVKDPVKWPSNmspefKSFLQGLLNKDPSKR 241
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
271-537 1.53e-32

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: 125.34  E-value: 1.53e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAK-HRIDGKTYV--IKRVKYNNEKAER-----EVKALAKLDHVNIVHYNGCwdgvdydpetsddyle 342
Cdd:cd00192    1 KKLGEGAFGEVYKGKlKGGDGKTVDvaVKTLKEDASESERkdflkEARVMKKLGHPNVVRLLGV---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 SSDYDPensknssrsktkcLFIQMEFCDKGTLEQWIENRRG----EKLDKVLALELFE---QITKGVDYIHSKKLIHRDL 415
Cdd:cd00192   65 CTEEEP-------------LYLVMEYMEGGDLLDFLRKSRPvfpsPEPSTLSLKDLLSfaiQIAKGMEYLASKKFVHRDL 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 416 KPSNIFLVDTKQVKIGDFGL-VTSLKNDGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFE-- 490
Cdd:cd00192  132 AARNCLVGEDLVVKISDFGLsRDIYDDDYYRKKTGGKLpiRWMAPESLKDGIFTSKSDVWSFGVLLWEIFTLGATPYPgl 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 491 -TSKFFTDLRDGII--------SDIFDkkektLLQKLLSKKPEDRPNTSEILRTLT 537
Cdd:cd00192  212 sNEEVLEYLRKGYRlpkpencpDELYE-----LMLSCWQLDPEDRPTFSELVERLE 262
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
273-526 1.68e-32

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: 124.94  E-value: 1.68e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIK-----RVKYNNE----KAEREVkaLAKLDHVNIVHyngcwdgvdydpetsddyLES 343
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKvlrkkEIIKRKEvehtLNERNI--LERVNHPFIVK------------------LHY 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 SDYDPENsknssrsktkcLFIQMEFCDKGTLEQWIENRR--GEKLDKVLALElfeqITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd05123   61 AFQTEEK-----------LYLVLDYVPGGELFSHLSKEGrfPEERARFYAAE----IVLALEYLHSLGIIYRDLKPENIL 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAFETSK----FFT 496
Cdd:cd05123  126 LDSDGHIKLTDFGLAKELSSDGDRTYTFcGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEML-TGKPPFYAENrkeiYEK 204
                        250       260       270
                 ....*....|....*....|....*....|.
gi 525343631 497 DLRDGI-ISDIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05123  205 ILKSPLkFPEYVSPEAKSLISGLLQKDPTKR 235
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
266-533 2.83e-32

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: 124.69  E-value: 2.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN--NEKAEREVKALAKLDHVNIVHYNGCwdgvdydpetsddYLES 343
Cdd:cd06612    4 VFDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEedLQEIIKEISILKQCDSPYIVKYYGS-------------YFKN 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 SDydpensknssrsktkcLFIQMEFCDKGTLEQwIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd06612   71 TD----------------LWIVMEYCGAGSVSD-IMKITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLN 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 424 DTKQVKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLilaellhvcdTAFETSKFFTDLRD-- 500
Cdd:cd06612  134 EEGQAKLADFGVSGQLTDTMAKRNTViGTPFWMAPEVIQEIGYNNKADIWSLGI----------TAIEMAEGKPPYSDih 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 525343631 501 --GIISDIFDKKEKTL-------------LQKLLSKKPEDRPNTSEIL 533
Cdd:cd06612  204 pmRAIFMIPNKPPPTLsdpekwspefndfVKKCLVKDPEERPSAIQLL 251
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
273-537 3.25e-32

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: 125.08  E-value: 3.25e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRiDGKTYVIKRVKYNNEKA-----EREVKALAKLDHVNIVHYNGCwdgvdydpetsddylessdyd 347
Cdd:cd14066    1 IGSGGFGTVYKGVLE-NGTVVAVKRLNEMNCAAskkefLTELEMLGRLRHPNLVRLLGY--------------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 pensknSSRSKTKCLFiqMEFCDKGTLEQWIENRRGEK-LDKVLALELFEQITKGVDYIHS---KKLIHRDLKPSNIFLV 423
Cdd:cd14066   59 ------CLESDEKLLV--YEYMPNGSLEDRLHCHKGSPpLPWPQRLKIAKGIARGLEYLHEecpPPIIHGDIKSSNILLD 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 424 DTKQVKIGDFGLVTSLKNDGKRTR---SKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL------HVCDTAFETS-- 492
Cdd:cd14066  131 EDFEPKLTDFGLARLIPPSESVSKtsaVKGTIGYLAPEYIRTGRVSTKSDVYSFGVVLLELLtgkpavDENRENASRKdl 210
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 493 -KFFTDLRDGIISDIFDKK--------EKTLLQKL------LSKKPEDRPNTSEILRTLT 537
Cdd:cd14066  211 vEWVESKGKEELEDILDKRlvdddgveEEEVEALLrlallcTRSDPSLRPSMKEVVQMLE 270
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
266-527 3.38e-32

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 125.02  E-value: 3.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV------KYNNEK-AEREVKALAKLDHVNIVHYNGCWDgvdydpetsd 338
Cdd:cd05581    2 DFKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLdkrhiiKEKKVKyVTIEKEVLSRLAHPGIVKLYYTFQ---------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dylessdyDPEnsknssrsktkCLFIQMEFCDKGTLEQWIeNRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd05581   72 --------DES-----------KLYFVLEYAPNGDLLEYI-RKYG-SLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPE 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTKQVKIGDFG-----------------LVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAE 480
Cdd:cd05581  131 NILLDEDMHIKITDFGtakvlgpdsspestkgdADSQIAYNQARAASfVGTAEYVSPELLNEKPAGKSSDLWALGCIIYQ 210
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631 481 LLH-----VCDTAFETSKFFTDLrDGIISDIFDKKEKTLLQKLLSKKPEDRP 527
Cdd:cd05581  211 MLTgkppfRGSNEYLTFQKIVKL-EYEFPENFPPDAKDLIQKLLVLDPSKRL 261
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
267-483 4.35e-32

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: 124.98  E-value: 4.35e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK------AEREVKALAKLDHVNIVHYngcwdgvdYDPETSddy 340
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKegfpitAIREIKLLQKLDHPNVVRL--------KEIVTS--- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdYDPENSKNSsrsktkcLFIQMEFCD---KGTLEqwienRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd07840   70 -----KGSAKYKGS-------IYMVFEYMDhdlTGLLD-----NPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKG 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKG--TLRYMSPEQI-SSQDYGKEVDLYALGLILAELLH 483
Cdd:cd07840  133 SNILINNDGVLKLADFGLARPYTKENNADYTNRviTLWYRPPELLlGATRYGPEVDMWSVGCILAELFT 201
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
268-536 4.98e-32

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 123.80  E-value: 4.98e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   268 KEIELIGSGGFGQVFKAKHR-IDGKTYV---IKRVKYNNEKAE-----REVKALAKLDHVNIVHYNGCwdgvdydpetsd 338
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKLKgKGGKKKVevaVKTLKEDASEQQieeflREARIMRKLDHPNVVKLLGV------------ 69
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   339 dyleSSDYDPensknssrsktkcLFIQMEFCDKGTLEQWIENRRGE-KLDKVLALELfeQITKGVDYIHSKKLIHRDLKP 417
Cdd:smart00219  70 ----CTEEEP-------------LYIVMEYMEGGDLLSYLRKNRPKlSLSDLLSFAL--QIARGMEYLESKNFIHRDLAA 130
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   418 SNIFLVDTKQVKIGDFGLVTSLKNDG--KRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFE---TS 492
Cdd:smart00219 131 RNCLVGENLVVKISDFGLSRDLYDDDyyRKRGGKLPIRWMAPESLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPgmsNE 210
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 525343631   493 KFFTDLRDGII--------SDIFDkkektLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:smart00219 211 EVLEYLKNGYRlpqppncpPELYD-----LMLQCWAEDPEDRPTFSELVEIL 257
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
267-535 5.38e-32

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: 124.07  E-value: 5.38e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVF-----KAKHriDGKTYVIKRVKYNNEK------AEREVKALAKLDHVNIVHYngcwdgvdYDPE 335
Cdd:cd08222    2 YRVVRKLGSGNFGTVYlvsdlKATA--DEELKVLKEISVGELQpdetvdANREAKLLSKLDHPAIVKF--------HDSF 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 336 TSDDYLessdydpensknssrsktkClfIQMEFCDKGTLEQWIEN--RRGEKLDKVLALELFEQITKGVDYIHSKKLIHR 413
Cdd:cd08222   72 VEKESF-------------------C--IVTEYCEGGDLDDKISEykKSGTTIDENQILDWFIQLLLAVQYMHERRILHR 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 414 DLKPSNIFLvDTKQVKIGDFGLVTSLKNDGK-RTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELlhvC--DTAFE 490
Cdd:cd08222  131 DLKAKNIFL-KNNVIKVGDFGISRILMGTSDlATTFTGTPYYMSPEVLKHEGYNSKSDIWSLGCILYEM---CclKHAFD 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 525343631 491 TSKFFTDLRDGI------ISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:cd08222  207 GQNLLSVMYKIVegetpsLPDKYSKELNAIYSRMLNKDPALRPSAAEILKI 257
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
266-534 6.83e-32

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: 123.59  E-value: 6.83e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE------REVKALAKLDHVNIVHYNGCwdgvdydpetsdd 339
Cdd:cd14069    2 DWDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDcpenikKEVCIQKMLSHKNVVRFYGH------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknssRSKTKCLFIQMEFCDKGTLEQWIENRRGekLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14069   69 ----------------RREGEFQYLFLEYASGGELFDKIEPDVG--MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPEN 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKR---TRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELLH---VCDTAFETS 492
Cdd:cd14069  131 LLLDENDNLKISDFGLATVFRYKGKErllNKMCGTLPYVAPELLAKKKYrAEPVDVWSCGIVLFAMLAgelPWDQPSDSC 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 525343631 493 KFFTDLRDGIIS--DIFDKKEKT---LLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14069  211 QEYSDWKENKKTylTPWKKIDTAalsLLRKILTENPNKRITIEDIKK 257
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
266-482 8.07e-32

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: 124.36  E-value: 8.07e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN------EKAEREVKALAKL-DHVNIVhyngcwdgvdydpETSD 338
Cdd:cd07832    1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKleggipNQALREIKALQACqGHPYVV-------------KLRD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 DYLESSdydpensknssrsktkCLFIQMEFCDkGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd07832   68 VFPHGT----------------GFVLVFEYML-SSLSEVLRDEE-RPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPA 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSLKNDGKRTRSK--GTLRYMSPEQI-SSQDYGKEVDLYALGLILAELL 482
Cdd:cd07832  130 NLLISSTGVLKIADFGLARLFSEEDPRLYSHqvATRWYRAPELLyGSRKYDEGVDLWAVGCIFAELL 196
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
271-534 1.76e-31

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: 122.51  E-value: 1.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNE---------KAEREVKALAKLDHVNIVHYNGCwdgvdydpETSDDYL 341
Cdd:cd06632    6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVDDdkksresvkQLEQEIALLSKLRHPNIVQYYGT--------EREEDNL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdydpensknssrsktkclFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIf 421
Cdd:cd06632   78 ---------------------YIFLEYVPGGSIHKLL--QRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANI- 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTK-QVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQD--YGKEVDLYALGLILAELlhvCDTAFETSKF---- 494
Cdd:cd06632  134 LVDTNgVVKLADFGMAKHVEAFSFAKSFKGSPYWMAPEVIMQKNsgYGLAVDIWSLGCTVLEM---ATGKPPWSQYegva 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 525343631 495 --FTDLRDG---IISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06632  211 aiFKIGNSGelpPIPDHLSPDAKDFIRLCLQRDPEDRPTASQLLE 255
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
270-535 9.56e-31

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: 120.23  E-value: 9.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN--NEKAER----EVKALAKLDHVNIV-HYNGCWDGvdydpetsddyle 342
Cdd:cd08221    5 VRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSrlSEKERRdalnEIDILSLLNHDNIItYYNHFLDG------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssrsktKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd08221   72 -----------------ESLFIEMEYCNGGNLHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETS--KFFTDLR 499
Cdd:cd08221  135 TKADLVKLGDFGISKVLDSESSMAESiVGTPYYMSPELVQGVKYNFKSDIWAVGCVLYELLTLKRTFDATNplRLAVKIV 214
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 525343631 500 DGIISDIFDKKEKTLLQ---KLLSKKPEDRPNTSEILRT 535
Cdd:cd08221  215 QGEYEDIDEQYSEEIIQlvhDCLHQDPEDRPTAEELLER 253
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
273-534 1.36e-30

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AMPK, also called SNF1 (sucrose non-fermenting1) in yeasts and SnRK1 (SNF1-related kinase1) in plants, is a heterotrimeric enzyme composed of a catalytic alpha subunit and two regulatory subunits, beta and gamma. It is a stress-activated kinase that serves as master regulator of glucose and lipid metabolism by monitoring carbon and energy supplies, via sensing the cell's AMP:ATP ratio. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 120.07  E-value: 1.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIK---RVKYNN----EKAEREVKALAKLDHVNIVHYngcwdgvdYDP-ETSDDyless 344
Cdd:cd14079   10 LGVGSFGKVKLAEHELTGHKVAVKilnRQKIKSldmeEKIRREIQILKLFRHPHIIRL--------YEViETPTD----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpensknssrsktkcLFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd14079   77 -----------------IFMVMEYVSGGELFDYIVQK--GRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDS 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLvTSLKNDGK--RTrSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELLhvCDT-AFE---TSKFFTD 497
Cdd:cd14079  138 NMNVKIADFGL-SNIMRDGEflKT-SCGSPNYAAPEVISGKLYaGPEVDVWSCGVILYALL--CGSlPFDdehIPNLFKK 213
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 525343631 498 LRDGI--ISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14079  214 IKSGIytIPSHLSPGARDLIKRMLVVDPLKRITIPEIRQ 252
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
266-533 1.68e-30

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: 119.69  E-value: 1.68e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK-----YNNEKAEREVKALAKLDHVNIVHYNgcwdgvdydpetsddy 340
Cdd:cd08219    1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRlpkssSAVEDSRKEAVLLAKMKHPNIVAFK---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lESSDYDPEnsknssrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd08219   65 -ESFEADGH------------LYIVMEYCDGGDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNI 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 421 FLVDTKQVKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAEL----------------LH 483
Cdd:cd08219  132 FLTQNGKVKLGDFGSARLLTSPGAYACTYvGTPYYVPPEIWENMPYNNKSDIWSLGCILYELctlkhpfqanswknliLK 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631 484 VCDTAFE--TSKFFTDLRdgiisdifdkkekTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd08219  212 VCQGSYKplPSHYSYELR-------------SLIKQMFKRNPRSRPSATTIL 250
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
267-481 1.72e-30

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: 120.33  E-value: 1.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK---YNNEK--AEREVKALAKL-DHVNIVHYngcwdgvdydpetsddy 340
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKkkfYSWEEcmNLREVKSLRKLnEHPNIVKL----------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdYDpensknsSRSKTKCLFIQMEFCDkGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd07830   64 -----KE-------VFRENDELYFVFEYME-GNLYQLMKDRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENL 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 421 FLVDTKQVKIGDFGLVtslkndgKRTRSK-------GTLRYMSPEQI-SSQDYGKEVDLYALGLILAEL 481
Cdd:cd07830  131 LVSGPEVVKIADFGLA-------REIRSRppytdyvSTRWYRAPEILlRSTSYSSPVDIWALGCIMAEL 192
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
262-534 1.81e-30

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


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 120.13  E-value: 1.81e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 262 RFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK------YNNEKAEREVKALAKL-DHVNIVHYNGCWdgvdydp 334
Cdd:cd14138    2 RYATEFHELEKIGSGEFGSVFKCVKRLDGCIYAIKRSKkplagsVDEQNALREVYAHAVLgQHSHVVRYYSAW------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 335 eTSDDYlessdydpensknssrsktkcLFIQMEFCDKGTLEQWI-ENRRGEKLDKVLAL-ELFEQITKGVDYIHSKKLIH 412
Cdd:cd14138   75 -AEDDH---------------------MLIQNEYCNGGSLADAIsENYRIMSYFTEPELkDLLLQVARGLKYIHSMSLVH 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 413 RDLKPSNIFLVDTKQ-------------------VKIGDFGLVTSLKNDgkrTRSKGTLRYMSPEqISSQDYG--KEVDL 471
Cdd:cd14138  133 MDIKPSNIFISRTSIpnaaseegdedewasnkviFKIGDLGHVTRVSSP---QVEEGDSRFLANE-VLQENYThlPKADI 208
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 472 YALGLILaellhVCDTAFE----TSKFFTDLRDGI---ISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14138  209 FALALTV-----VCAAGAEplptNGDQWHEIRQGKlprIPQVLSQEFLDLLKVMIHPDPERRPSAVALVK 273
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
266-534 1.91e-30

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: 120.04  E-value: 1.91e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVkyNNEKAE-------REVKALAKLDHVNIVHYNGCwdgvdydpetsd 338
Cdd:cd06609    2 LFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVI--DLEEAEdeiediqQEIQFLSQCDSPYITKYYGS------------ 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dYLEssdydpeNSKnssrsktkcLFIQMEFCDKGTLEQWIENRrgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd06609   68 -FLK-------GSK---------LWIIMEYCGGGSVLDLLKPG---PLDETYIAFILREVLLGLEYLHSEGKIHRDIKAA 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSLKNdgkrTRSK-----GTLRYMSPEQISSQDYGKEVDLYALGLILAEL---------LHV 484
Cdd:cd06609  128 NILLSEEGDVKLADFGVSGQLTS----TMSKrntfvGTPFWMAPEVIKQSGYDEKADIWSLGITAIELakgepplsdLHP 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 525343631 485 CDTAFETSKFFTD-LRDGIISDIFdkkeKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06609  204 MRVLFLIPKNNPPsLEGNKFSKPF----KDFVELCLNKDPKERPSAKELLK 250
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
267-481 4.08e-30

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: 120.17  E-value: 4.08e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK------AEREVKALAKLDHVNIVH-YNGCwdgvdydpetsdd 339
Cdd:cd07865   14 YEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKegfpitALREIKILQLLKHENVVNlIEIC------------- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 yleSSDYDPENSKNSSrsktkcLFIQMEFCD---KGTLeqwieNRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd07865   81 ---RTKATPYNRYKGS------IYLVFEFCEhdlAGLL-----SNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMK 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 417 PSNIFLVDTKQVKIGDFGL--VTSLKNDGKRTRSKG---TLRYMSPE-QISSQDYGKEVDLYALGLILAEL 481
Cdd:cd07865  147 AANILITKDGVLKLADFGLarAFSLAKNSQPNRYTNrvvTLWYRPPElLLGERDYGPPIDMWGAGCIMAEM 217
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
272-537 7.84e-30

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: 118.21  E-value: 7.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK----AEREVKALAKL-DHVNIVHYngcwdgvdydpetsddylessdY 346
Cdd:cd13985    7 QLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEqlrvAIKEIEIMKRLcGHPNIVQY----------------------Y 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 DPENSKNSSRSKtkCLfIQMEFCdKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKK--LIHRDLKPSNIFLVD 424
Cdd:cd13985   65 DSAILSSEGRKE--VL-LLMEYC-PGSLVDILEKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSN 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLVTSL--------------KNDGKRTrskgTLRYMSPEQISSQDY---GKEVDLYALGLILAELLHVcDT 487
Cdd:cd13985  141 TGRFKLCDFGSATTEhypleraeevniieEEIQKNT----TPMYRAPEMIDLYSKkpiGEKADIWALGCLLYKLCFF-KL 215
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 525343631 488 AFETSKFFTDLR---DGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLT 537
Cdd:cd13985  216 PFDESSKLAIVAgkySIPEQPRYSPELHDLIRHMLTPDPAERPDIFQVINIIT 268
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
273-537 1.55e-29

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: 116.77  E-value: 1.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRidGKTYVIKRVKYNNEK--AEREVKALAKLDHVNIVHYNGCwdgvdydpetsddylessdydpen 350
Cdd:cd14058    1 VGRGSFGVVCKARWR--NQIVAVKIIESESEKkaFEVEVRQLSRVDHPNIIKLYGA------------------------ 54
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 351 sknSSRSKTKCLFiqMEFCDKGTLEQWIENRRGEKLDKVL-ALELFEQITKGVDYIHS---KKLIHRDLKPSNIFLVDTK 426
Cdd:cd14058   55 ---CSNQKPVCLV--MEYAEGGSLYNVLHGKEPKPIYTAAhAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGG 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 427 QV-KIGDFGLVTSLKNdgKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL-------HVCDTAFETSKF-FTD 497
Cdd:cd14058  130 TVlKICDFGTACDIST--HMTNNKGSAAWMAPEVFEGSKYSEKCDVFSWGIILWEVItrrkpfdHIGGPAFRIMWAvHNG 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 525343631 498 LRDGIISDIfDKKEKTLLQKLLSKKPEDRPNTSEILRTLT 537
Cdd:cd14058  208 ERPPLIKNC-PKPIESLMTRCWSKDPEKRPSMKEIVKIMS 246
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
266-534 1.67e-29

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


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 117.50  E-value: 1.67e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK------YNNEKAEREVKALAKL-DHVNIVHYNGCWdgvdydpeTSD 338
Cdd:cd14051    1 EFHEVEKIGSGEFGSVYKCINRLDGCVYAIKKSKkpvagsVDEQNALNEVYAHAVLgKHPHVVRYYSAW--------AED 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 DYLessdydpensknssrsktkclFIQMEFCDKGTLEQWIE--NRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd14051   73 DHM---------------------IIQNEYCNGGSLADAISenEKAGERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIK 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQV------------------------KIGDFGLVTSLKNDgkrTRSKGTLRYMsPEQISSQDYGK--EVD 470
Cdd:cd14051  132 PGNIFISRTPNPvsseeeeedfegeednpesnevtyKIGDLGHVTSISNP---QVEEGDCRFL-ANEILQENYSHlpKAD 207
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 471 LYALGLilaellhvcdTAFETS---------KFFTDLRDGI------ISDIFDKkektLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14051  208 IFALAL----------TVYEAAgggplpkngDEWHEIRQGNlpplpqCSPEFNE----LLRSMIHPDPEKRPSAAALLQ 272
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
267-482 3.10e-29

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: 117.03  E-value: 3.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNE------KAEREVKALAKLDHVNIVhyngcwdgvdydpetsddy 340
Cdd:cd07833    3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDdedvkkTALREVKVLRQLRHENIV------------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpeNSKNSSRSKTKcLFIQMEFCDKGTLEQWIENRRGEKLDKVLALeLFeQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd07833   64 ---------NLKEAFRRKGR-LYLVFEYVERTLLELLEASPGGLPPDAVRSY-IW-QLLQAIAYCHSHNIIHRDIKPENI 131
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 421 FLVDTKQVKIGDFGLVTSLKNDGKR--TRSKGTLRYMSPE-QISSQDYGKEVDLYALGLILAELL 482
Cdd:cd07833  132 LVSESGVLKLCDFGFARALTARPASplTDYVATRWYRAPElLVGDTNYGKPVDVWAIGCIMAELL 196
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
267-534 4.58e-29

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: 115.41  E-value: 4.58e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK---YNNEKAEREVKALAKL----DHVNIVHYNgcwdgvdydpetsdd 339
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKndfRHPKAALREIKLLKHLndveGHPNIVKLL--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpeNSKNSSRSKTKCLFiqMEFCDKgTLEQWIENRRGEKLDKVLALELFeQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd05118   66 ----------DVFEHRGGNHLCLV--FELMGM-NLYELIKDYPRGLPLDLIKSYLY-QLLQALDFLHSNGIIHRDLKPEN 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLV-DTKQVKIGDFGLVTSLkNDGKRTRSKGTLRYMSPEQI-SSQDYGKEVDLYALGLILAELLhvcdtafeTSKFFTD 497
Cdd:cd05118  132 ILINlELGQLKLADFGLARSF-TSPPYTPYVATRWYRAPEVLlGAKPYGSSIDIWSLGCILAELL--------TGRPLFP 202
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 525343631 498 LRDGI-----ISDIFDKKE-KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd05118  203 GDSEVdqlakIVRLLGTPEaLDLLSKMLKYDPAKRITASQALA 245
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
267-536 1.11e-28

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: 114.75  E-value: 1.11e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV--KYNNEKAE---------REVKALAKL-DHVNIVHYngcwdgvdydp 334
Cdd:cd13993    2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLykSGPNSKDGndfqklpqlREIDLHRRVsRHPNIITL----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 335 etsDDYLESSDydpensknssrsktkCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRD 414
Cdd:cd13993   71 ---HDVFETEV---------------AIYIVLEYCPNGDLFEAITENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRD 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFL-VDTKQVKIGDFGLVTSlkNDGKRTRSKGTLRYMSPEQISSQDYGKE------VDLYALGLILAELL----- 482
Cdd:cd13993  133 IKPENILLsQDEGTVKLCDFGLATT--EKISMDFGVGSEFYMAPECFDEVGRSLKgypcaaGDIWSLGIILLNLTfgrnp 210
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 483 --HVCDTAFETSKFFTD---LRDGI--ISDIFDkkekTLLQKLLSKKPEDRpNTSEILRTL 536
Cdd:cd13993  211 wkIASESDPIFYDYYLNspnLFDVIlpMSDDFY----NLLRQIFTVNPNNR-ILLPELQLL 266
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
266-534 1.24e-28

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: 114.76  E-value: 1.24e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV---KYNNEKAE--REVKALAKLDHVNIVHYNGcwdgvdydpetsddy 340
Cdd:cd06610    2 DYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIdleKCQTSMDElrKEIQAMSQCNHPNVVSYYT--------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpensknsSRSKTKCLFIQMEFCDKGTLEQWIENRRGEK-LDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd06610   67 --------------SFVVGDELWLVMPLLSGGSLLDIMKSSYPRGgLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGN 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTRSK-----GTLRYMSPEQISSQD-YGKEVDLYALGLILAELLHvcdTAFETSK 493
Cdd:cd06610  133 ILLGEDGSVKIADFGVSASLATGGDRTRKVrktfvGTPCWMAPEVMEQVRgYDFKADIWSFGITAIELAT---GAAPYSK 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 525343631 494 F-------------FTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06610  210 YppmkvlmltlqndPPSLETGADYKKYSKSFRKMISLCLQKDPSKRPTAEELLK 263
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
266-533 1.50e-28

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: 114.36  E-value: 1.50e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE-----REVKALAKLDHVNIVHYNGCWdgvdydpetsddY 340
Cdd:cd06605    2 DLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEIDEALqkqilRELDVLHKCNSPYIVGFYGAF------------Y 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSdydpensknssrsktkcLFIQMEFCDKGTLEQwIENRRGEKLDKVLAlELFEQITKGVDYIHSK-KLIHRDLKPSN 419
Cdd:cd06605   70 SEGD-----------------ISICMEYMDGGSLDK-ILKEVGRIPERILG-KIAVAVVKGLIYLHEKhKIIHRDVKPSN 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IfLVDTK-QVKIGDFGLVTSLKNDGKRTrSKGTLRYMSPEQISSQDYGKEVDLYALGLILAEL------LHVCDTAFETS 492
Cdd:cd06605  131 I-LVNSRgQVKLCDFGVSGQLVDSLAKT-FVGTRSYMAPERISGGKYTVKSDIWSLGLSLVELatgrfpYPPPNAKPSMM 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 525343631 493 KFftDLRDGII--------SDIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd06605  209 IF--ELLSYIVdepppllpSGKFSPDFQDFVSQCLQKDPTERPSYKELM 255
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
271-526 2.42e-28

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: 113.54  E-value: 2.42e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYV-IKRVKYNN-EKAER-----EVKALAKLDHVNIVHyngcwdgvdydpetsddyLES 343
Cdd:cd14121    1 EKLGSGTYATVYKAYRKSGAREVVaVKCVSKSSlNKASTenlltEIELLKKLKHPHIVE------------------LKD 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 SDYDPENsknssrsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd14121   63 FQWDEEH-----------IYLIMEYCSGGDLSRFIRSRR--TLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLS 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 424 --DTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHvcDTAFETSKFFTDLRDG 501
Cdd:cd14121  130 srYNPVLKLADFGFAQHLKPNDEAHSLRGSPLYMAPEMILKKKYDARVDLWSVGVILYECLF--GRAPFASRSFEELEEK 207
                        250       260       270
                 ....*....|....*....|....*....|....
gi 525343631 502 IISD---------IFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd14121  208 IRSSkpieiptrpELSADCRDLLLRLLQRDPDRR 241
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
271-482 3.32e-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: 113.09  E-value: 3.32e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER------EVKALAKLDHVNIVHYNGCwdgvdydpetsddyLESS 344
Cdd:cd06627    6 DLIGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDlksvmgEIDLLKKLNHPNIVKYIGS--------------VKTK 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 DYdpensknssrsktkcLFIQMEFCDKGTLEQWIEN--RRGEKLdkvLALELFeQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd06627   72 DS---------------LYIILEYVENGSLASIIKKfgKFPESL---VAVYIY-QVLEGLAYLHEQGVIHRDIKGANILT 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 423 VDTKQVKIGDFGLVTSLK-NDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd06627  133 TKDGLVKLADFGVATKLNeVEKDENSVVGTPYWMAPEVIEMSGVTTASDIWSVGCTVIELL 193
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
271-534 4.14e-28

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: 112.80  E-value: 4.14e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIK-----RVK--YNNEKAEREVKALAKLDHVNIVHYNgcwdgvdydpetsdDYLEs 343
Cdd:cd14188    7 KVLGKGGFAKCYEMTDLTTNKVYAAKiiphsRVSkpHQREKIDKEIELHRILHHKHVVQFY--------------HYFE- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 sdyDPENsknssrsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd14188   72 ---DKEN-----------IYILLEYCSRRSMAHILKARK--VLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFIN 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 424 DTKQVKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAFETSKF------FT 496
Cdd:cd14188  136 ENMELKVGDFGLAARLEPLEHRRRTIcGTPNYLSPEVLNKQGHGCESDIWALGCVMYTML-LGRPPFETTNLketyrcIR 214
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 525343631 497 DLRDGIISDIFdKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14188  215 EARYSLPSSLL-APAKHLIASMLSKNPEDRPSLDEIIR 251
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
267-482 7.89e-28

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: 113.05  E-value: 7.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK---------AEREVKALAKLDHVNIVhyngcwdgvdydpETS 337
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKeakdginftALREIKLLQELKHPNII-------------GLL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 DDYlessdydpensknssrSKTKCLFIQMEFCDkGTLEQWIENRRgekldKVLAL----ELFEQITKGVDYIHSKKLIHR 413
Cdd:cd07841   69 DVF----------------GHKSNINLVFEFME-TDLEKVIKDKS-----IVLTPadikSYMLMTLRGLEYLHSNWILHR 126
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 414 DLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKG-TLRYMSPEQI-SSQDYGKEVDLYALGLILAELL 482
Cdd:cd07841  127 DLKPNNLLIASDGVLKLADFGLARSFGSPNRKMTHQVvTRWYRAPELLfGARHYGVGVDMWSVGCIFAELL 197
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
264-482 7.93e-28

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: 112.98  E-value: 7.93e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 264 GMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV----KYNNekaeREVKALAKLDHVNIVHyngcwdgvdydpetsdd 339
Cdd:cd14137    3 EISYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVlqdkRYKN----RELQIMRRLKHPNIVK----------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 yLESSDYDPENSKNSsrsktKCLFIQMEFCDKgTLEQWIE--NRRGEKLD----KVLALELFeqitKGVDYIHSKKLIHR 413
Cdd:cd14137   62 -LKYFFYSSGEKKDE-----VYLNLVMEYMPE-TLYRVIRhySKNKQTIPiiyvKLYSYQLF----RGLAYLHSLGICHR 130
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 414 DLKPSNIfLVD--TKQVKIGDFGLVTSLKNDGKR-----TRSkgtlrYMSPEQI-SSQDYGKEVDLYALGLILAELL 482
Cdd:cd14137  131 DIKPQNL-LVDpeTGVLKLCDFGSAKRLVPGEPNvsyicSRY-----YRAPELIfGATDYTTAIDIWSAGCVLAELL 201
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
273-535 1.08e-27

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


Pssm-ID: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 112.02  E-value: 1.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHR--IDGKTYVIK--RVKYNNEKAEREVKALAK-------LDHVNIVHYngcwdgVDYDPETSDDYl 341
Cdd:cd13994    1 IGKGATSVVRIVTKKnpRSGVLYAVKeyRRRDDESKRKDYVKRLTSeyiisskLHHPNIVKV------LDLCQDLHGKW- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdydpensknssrsktkCLFiqMEFCDKGTLEQWIEnrRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd13994   74 -------------------CLV--MEYCPGGDLFTLIE--KADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENIL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFGLVTSLKNDG-KRTRSK----GTLRYMSPEQISSQDY-GKEVDLYALGLILAELL-------HVCDT- 487
Cdd:cd13994  131 LDEDGVLKLTDFGTAEVFGMPAeKESPMSaglcGSEPYMAPEVFTSGSYdGRAVDVWSCGIVLFALFtgrfpwrSAKKSd 210
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 525343631 488 ----AFETS-KFFTDLRDGIISDIFdKKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:cd13994  211 saykAYEKSgDFTNGPYEPIENLLP-SECRRLIYRMLHPDPEKRITIDEALND 262
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
271-533 1.10e-27

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: 112.09  E-value: 1.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRidGKTYVIKRVK--------YNNEKAEREVkalAKLDHVNIVHYngcwdgvdydpetsddyle 342
Cdd:cd13979    9 EPLGSGGFGSVYKATYK--GETVAVKIVRrrrknrasRQSFWAELNA---ARLRHENIVRV------------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpenSKNSSRSKTKCL-FIQMEFCDKGTLEQWIeNRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd13979   65 --------LAAETGTDFASLgLIIMEYCGNGTLQQLI-YEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANIL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFG----LVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL---------HVCdTA 488
Cdd:cd13979  136 ISEQGVCKLCDFGcsvkLGEGNEVGTPRSHIGGTYTYRAPELLKGERVTPKADIYSFGITLWQMLtrelpyaglRQH-VL 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 525343631 489 FETSKFftDLR---DGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd13979  215 YAVVAK--DLRpdlSGLEDSEFGQRLRSLISRCWSAQPAERPNADESL 260
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
273-536 2.01e-27

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: 110.95  E-value: 2.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAK-HridgKTYVIKRVKYNNEKAER------EVKALAKLDHVNIVHYNGCwdgvdydpetsddylessd 345
Cdd:cd14062    1 IGSGSFGTVYKGRwH----GDVAVKKLNVTDPTPSQlqafknEVAVLRKTRHVNILLFMGY------------------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 ydpeNSKNSsrsktkcLFIQMEFCDKGTLEQWI---ENrrgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd14062   58 ----MTKPQ-------LAIVTQWCEGSSLYKHLhvlET----KFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFL 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLVT--SLKNDGKRTRS-KGTLRYMSPEQISSQD---YGKEVDLYALGLILAELLhvcdtafeTSKF-F 495
Cdd:cd14062  123 HEDLTVKIGDFGLATvkTRWSGSQQFEQpTGSILWMAPEVIRMQDenpYSFQSDVYAFGIVLYELL--------TGQLpY 194
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 496 TDL--RDGII----------------SDIfDKKEKTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd14062  195 SHInnRDQILfmvgrgylrpdlskvrSDT-PKALRRLMEDCIKFQRDERPLFPQILASL 252
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
267-536 2.22e-27

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: 111.05  E-value: 2.22e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631  267 FKEIELIGSGGFGQVFKAKHRIDGKTY----VIKRVKYNNEKAE-----REVKALAKLDHVNIVHYNGCwdgvdydpets 337
Cdd:pfam07714   1 LTLGEKLGEGAFGEVYKGTLKGEGENTkikvAVKTLKEGADEEEredflEEASIMKKLDHPNIVKLLGV----------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631  338 ddyleSSDYDPensknssrsktkcLFIQMEFCDKGTLEQWIEnRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:pfam07714  70 -----CTQGEP-------------LYIVTEYMPGGDLLDFLR-KHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAA 130
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631  418 SNIFLVDTKQVKIGDFGLVTSLKNDG---KRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFE---T 491
Cdd:pfam07714 131 RNCLVSENLVVKISDFGLSRDIYDDDyyrKRGGGKLPIKWMAPESLKDGKFTSKSDVWSFGVLLWEIFTLGEQPYPgmsN 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 525343631  492 SKFFTDLRDGII--------SDIFDkkektLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:pfam07714 211 EEVLEFLEDGYRlpqpencpDELYD-----LMKQCWAYDPEDRPTFSELVEDL 258
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
273-482 2.64e-27

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: 110.28  E-value: 2.64e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRidGKTYVIKRVKynnEKAEREVKALAKLDHVNIVHYNG-Cwdgvdydpetsddylessdydpens 351
Cdd:cd14059    1 LGSGAQGAVFLGKFR--GEEVAVKKVR---DEKETDIKHLRKLNHPNIIKFKGvC------------------------- 50
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 352 knssrSKTKCLFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIG 431
Cdd:cd14059   51 -----TQAPCYCILMEYCPYGQLYEVL--RAGREITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKIS 123
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 525343631 432 DFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14059  124 DFGTSKELSEKSTKMSFAGTVAWMAPEVIRNEPCSEKVDIWSFGVVLWELL 174
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
266-526 4.03e-27

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: 111.13  E-value: 4.03e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKynneKAE-----------REVKALAKLDHVNIVHYNGCWdgvdydp 334
Cdd:cd05580    2 DFEFLKTLGTGSFGRVRLVKHKDSGKYYALKILK----KAKiiklkqvehvlNEKRILSEVRHPFIVNLLGSF------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 335 etSDDylessdydpensknssrsktKCLFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRD 414
Cdd:cd05580   71 --QDD--------------------RNLYMVMEYVPGGELFSLL--RRSGRFPNDVAKFYAAEVVLALEYLHSLDIVYRD 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFLVDTKQVKIGDFGLVTSLKndgKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDtafetsK 493
Cdd:cd05580  127 LKPENLLLDSDGHIKITDFGFAKRVK---DRTYTLcGTPEYLAPEIILSKGHGKAVDWWALGILIYEMLAGYP------P 197
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 525343631 494 FFTDLRDGIISDI----------FDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05580  198 FFDENPMKIYEKIlegkirfpsfFDPDAKDLIKRLLVVDLTKR 240
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
266-481 5.16e-27

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: 110.47  E-value: 5.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER---EVKALAKL-DHVNIVHYNGCWdgVDYDPETSDDYL 341
Cdd:cd06608    7 IFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMDIIEDEEEEiklEINILRKFsNHPNIATFYGAF--IKKDPPGGDDQL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdydpensknssrsktkclFIQMEFCDKGTLEQWIEN--RRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd06608   85 ---------------------WLVMEYCGGGSVTDLVKGlrKKGKRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQN 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKND-GKRTRSKGTLRYMSPEQISS-----QDYGKEVDLYALGLILAEL 481
Cdd:cd06608  144 ILLTEEAEVKLVDFGVSAQLDSTlGRRNTFIGTPYWMAPEVIACdqqpdASYDARCDVWSLGITAIEL 211
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
266-534 1.24e-26

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 109.70  E-value: 1.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIelIGSGGFGQVFKAKHRIDGKTYVIKRVK----YNNEKAEREVKALAKLDHVNIVhyngcwdgvdydpeTSDDYL 341
Cdd:cd14166    6 IFMEV--LGSGAFSEVYLVKQRSTGKLYALKCIKksplSRDSSLENEIAVLKRIKHENIV--------------TLEDIY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWIENrRGEKLDKVlALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd14166   70 ESTTH---------------YYLVMQLVSGGELFDRILE-RGVYTEKD-ASRVINQVLSAVKYLHENGIVHRDLKPENLL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LV---DTKQVKIGDFGLvTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFE--TSKFFT 496
Cdd:cd14166  133 YLtpdENSKIMITDFGL-SKMEQNGIMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVITYILLCGYPPFYEetESRLFE 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 497 DLRDGIIS------DIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14166  212 KIKEGYYEfespfwDDISESAKDFIRHLLEKNPSKRYTCEKALS 255
DSRM_EIF2AK2 cd20314
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
99-165 1.51e-26

double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380746  Cd Length: 68  Bit Score: 102.47  E-value: 1.51e-26
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631  99 GNYIGLINRIAQKKRLTVNYEQCA-SGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQI 165
Cdd:cd20314    1 GNYVSLLNEYCQKERLTVKYEEEKrSGPTHKPRFFCKYIIDGKEYPEGEGKSKKEAKQAAARLAYEEL 68
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
273-527 2.82e-26

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: 108.07  E-value: 2.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVK---------YNNEKAEREVkaLAKLDHVNIVHYNGCWDGVDYdpetsddyles 343
Cdd:cd05579    1 ISRGAYGRVYLAKKKSTGDLYAIKVIKkrdmirknqVDSVLAERNI--LSQAQNPFVVKLYYSFQGKKN----------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 sdydpensknssrsktkcLFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd05579   68 ------------------LYLVMEYLPGGDLYSLLENV--GALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILID 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 424 DTKQVKIGDFGL----------------VTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVC-- 485
Cdd:cd05579  128 ANGHLKLTDFGLskvglvrrqiklsiqkKSNGAPEKEDRRIVGTPDYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIpp 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 525343631 486 ---DTAFETskfFTDLRDGIISDIFD----KKEKTLLQKLLSKKPEDRP 527
Cdd:cd05579  208 fhaETPEEI---FQNILNGKIEWPEDpevsDEAKDLISKLLTPDPEKRL 253
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
273-481 2.98e-26

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: 107.77  E-value: 2.98e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKY--NNEKA----EREVKALAKLDHVNIVHYNGcwdgvdydpetsddyLESSdy 346
Cdd:cd06626    8 IGEGTFGKVYTAVNLDTGELMAMKEIRFqdNDPKTikeiADEMKVLEGLDHPNLVRYYG---------------VEVH-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 dpensknssRSKtkcLFIQMEFCDKGTLEQWIENrrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK 426
Cdd:cd06626   71 ---------REE---VYIFMEYCQEGTLEELLRH--GRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNG 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 427 QVKIGDFGLVTSLKNDGKRTRSK------GTLRYMSPEQISSQD---YGKEVDLYALGLILAEL 481
Cdd:cd06626  137 LIKLGDFGSAVKLKNNTTTMAPGevnslvGTPAYMAPEVITGNKgegHGRAADIWSLGCVVLEM 200
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
266-533 3.25e-26

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: 107.64  E-value: 3.25e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN-------NEKAEREVKALAKLDHVNIVH-YNgcwdgvdydpets 337
Cdd:cd14186    2 DFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKamqkagmVQRVRNEVEIHCQLKHPSILElYN------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 ddYLESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd14186   69 --YFEDSNY---------------VYLVLEMCHNGEMSRYLKNRK-KPFTEDEARHFMHQIVTGMLYLHSHGILHRDLTL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSLKN-DGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAFETSKFFT 496
Cdd:cd14186  131 SNLLLTRNMNIKIADFGLATQLKMpHEKHFTMCGTPNYISPEIATRSAHGLESDVWSLGCMFYTLL-VGRPPFDTDTVKN 209
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 525343631 497 DLRDGIISD-----IFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14186  210 TLNKVVLADyempaFLSREAQDLIHQLLRKNPADRLSLSSVL 251
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
267-548 4.17e-26

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: 108.27  E-value: 4.17e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE---REVKALAKLDH-VNIVHYNGCWdgVDYDPETSDDYLe 342
Cdd:cd06637    8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEEeikQEINMLKKYSHhRNIATYYGAF--IKKNPPGMDDQL- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssrsktkclFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd06637   85 --------------------WLVMEFCGAGSVTDLIKNTKGNTLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLVTSL-KNDGKRTRSKGTLRYMSPEQISSQD-----YGKEVDLYALGLILAELLH----VCDTAFETS 492
Cdd:cd06637  145 TENAEVKLVDFGVSAQLdRTVGRRNTFIGTPYWMAPEVIACDEnpdatYDFKSDLWSLGITAIEMAEgappLCDMHPMRA 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 493 KFFTDLRDG--IISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNER 548
Cdd:cd06637  225 LFLIPRNPAprLKSKKWSKKFQSFIESCLVKNHSQRPSTEQLMKHPFIRDQPNERQVR 282
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
259-533 4.84e-26

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: 107.33  E-value: 4.84e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 259 VDKRFGMDFKEIELIGSGGFGQVFKAKH---------RIDGKTYVIKrvKYNNEKAEREVKALAKLDHVNIVHYNGcwdg 329
Cdd:cd14187    1 VDPRTRRRYVRGRFLGKGGFAKCYEITDadtkevfagKIVPKSLLLK--PHQKEKMSMEIAIHRSLAHQHVVGFHG---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 330 vdydpetsddYLESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWieNRRGEKLDKVLALELFEQITKGVDYIHSKK 409
Cdd:cd14187   75 ----------FFEDNDF---------------VYVVLELCRRRSLLEL--HKRRKALTEPEARYYLRQIILGCQYLHRNR 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 410 LIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTA 488
Cdd:cd14187  128 VIHRDLKLGNLFLNDDMEVKIGDFGLATKVEYDGERKKTLcGTPNYIAPEVLSKKGHSFEVDIWSIGCIMYTLL-VGKPP 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 525343631 489 FETSKFF-TDLR----DGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14187  207 FETSCLKeTYLRikknEYSIPKHINPVAASLIQKMLQTDPTARPTINELL 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
271-533 7.46e-26

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: 106.70  E-value: 7.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIK------------RVKynnekaeREVKALAKLDHVNIV---HYngcwdgvdydPE 335
Cdd:cd14078    9 ETIGSGGFAKVKLATHILTGEKVAIKimdkkalgddlpRVK-------TEIEALKNLSHQHICrlyHV----------IE 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 336 TSDDYlessdydpensknssrsktkclFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDL 415
Cdd:cd14078   72 TDNKI----------------------FMVLEYCPGGELFDYIVAK--DRLSEDEARVFFRQIVSAVAYVHSQGYAHRDL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 416 KPSNIFLVDTKQVKIGDFGLVTSLKNdGKRTRSK---GTLRYMSPEQISSQDY-GKEVDLYALGLILAELLhvCD-TAFE 490
Cdd:cd14078  128 KPENLLLDEDQNLKLIDFGLCAKPKG-GMDHHLEtccGSPAYAAPELIQGKPYiGSEADVWSMGVLLYALL--CGfLPFD 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 525343631 491 TSKFFTdLRDGIISDIFDKKE------KTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14078  205 DDNVMA-LYRKIQSGKYEEPEwlspssKLLLDQMLQVDPKKRITVKELL 252
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
268-486 9.33e-26

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: 107.08  E-value: 9.33e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 268 KEIELIGSGGFGQVFKAKHRI-DGKTY---VIKRVKYNNEKA-----EREVKALAKLDHVNIVHYNGCwdgvdydpetsd 338
Cdd:cd05038    7 KFIKQLGEGHFGSVELCRYDPlGDNTGeqvAVKSLQPSGEEQhmsdfKREIEILRTLDHEYIVKYKGV------------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dylesSDYDPENSknssrsktkcLFIQMEFCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd05038   75 -----CESPGRRS----------LRLIMEYLPSGSLRDYLQRHR-DQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAAR 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 419 NIFLVDTKQVKIGDFGL--VTSLKNDGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAELLHVCD 486
Cdd:cd05038  139 NILVESEDLVKISDFGLakVLPEDKEYYYVKEPGESpiFWYAPECLRESRFSSASDVWSFGVTLYELFTYGD 210
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
248-535 1.16e-25

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 110.11  E-value: 1.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 248 DLPDMKETKYTVDKRFGMdFKEIELIGSGGFGQVFKAKHRIDGKTYVI-KRVKYNNEK----AEREVKALAKLDHVNIVH 322
Cdd:PTZ00267  51 DLPEGEEVPESNNPREHM-YVLTTLVGRNPTTAAFVATRGSDPKEKVVaKFVMLNDERqaayARSELHCLAACDHFGIVK 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 323 YngcwdgvdYDPETSDDylessdydpensknssrsktKCLFIqMEFCDKGTLEQWIENRRGEKL--DKVLALELFEQITK 400
Cdd:PTZ00267 130 H--------FDDFKSDD--------------------KLLLI-MEYGSGGDLNKQIKQRLKEHLpfQEYEVGLLFYQIVL 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 401 GVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSK---GTLRYMSPEQISSQDYGKEVDLYALGLI 477
Cdd:PTZ00267 181 ALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASsfcGTPYYLAPELWERKRYSKKADMWSLGVI 260
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 478 LAELLHVCDTAFETSKffTDLRDGIISDIFD-------KKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:PTZ00267 261 LYELLTLHRPFKGPSQ--REIMQQVLYGKYDpfpcpvsSGMKALLDPLLSKNPALRPTTQQLLHT 323
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
262-533 1.88e-25

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: 105.39  E-value: 1.88e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 262 RFGmdfKEIELIGSGGFGQVFKAKHRIDGKTY---VIKRVKYNNEKAER---EVKALAKLDHVNIVHYNGCWdgvdydpe 335
Cdd:cd13983    1 RYL---KFNEVLGRGSFKTVYRAFDTEEGIEVawnEIKLRKLPKAERQRfkqEIEILKSLKHPNIIKFYDSW-------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 336 tsddylessdydpensknSSRSKTKCLFIQmEFCDKGTLEQWIenRRGEKLD-KVLAlELFEQITKGVDYIHSKK--LIH 412
Cdd:cd13983   70 ------------------ESKSKKEVIFIT-ELMTSGTLKQYL--KRFKRLKlKVIK-SWCRQILEGLNYLHTRDppIIH 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 413 RDLKPSNIFlVD--TKQVKIGDFGLVTsLKNDGKRTRSKGTLRYMSPEqISSQDYGKEVDLYALGLILAELL------HV 484
Cdd:cd13983  128 RDLKCDNIF-INgnTGEVKIGDLGLAT-LLRQSFAKSVIGTPEFMAPE-MYEEHYDEKVDIYAFGMCLLEMAtgeypySE 204
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 525343631 485 CDTAFETSKFFTdlrDGI----ISDIFDKKEKTLLQKLLsKKPEDRPNTSEIL 533
Cdd:cd13983  205 CTNAAQIYKKVT---SGIkpesLSKVKDPELKDFIEKCL-KPPDERPSARELL 253
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
266-482 2.30e-25

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: 106.30  E-value: 2.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK------AEREVKALAKLDHVNIVHYNGCWDGvdydpetsdD 339
Cdd:cd07845    8 EFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDNERdgipisSLREITLLLNLRHPNIVELKEVVVG---------K 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLESsdydpensknssrsktkcLFIQMEFCDKgTLEQWIENRR---GEKLDKVLALELFeqitKGVDYIHSKKLIHRDLK 416
Cdd:cd07845   79 HLDS------------------IFLVMEYCEQ-DLASLLDNMPtpfSESQVKCLMLQLL----RGLQYLHENFIIHRDLK 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLKN-DGKRTRSKGTLRYMSPEQI-SSQDYGKEVDLYALGLILAELL 482
Cdd:cd07845  136 VSNLLLTDKGCLKIADFGLARTYGLpAKPMTPKVVTLWYRAPELLlGCTTYTTAIDMWAVGCILAELL 203
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
267-533 2.60e-25

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: 105.97  E-value: 2.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE-----REVKALAKLDHVNIVHYNGCWdgvdYDPETSDdyl 341
Cdd:cd06621    3 IVELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVqkqilRELEINKSCASPYIVKYYGAF----LDEQDSS--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdydpensknssrsktkcLFIQMEFCDKGTLEQWIE------NRRGEK-LDKVLalelfEQITKGVDYIHSKKLIHRD 414
Cdd:cd06621   76 --------------------IGIAMEYCEGGSLDSIYKkvkkkgGRIGEKvLGKIA-----ESVLKGLSYLHSRKIIHRD 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSkGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCdTAFETSK- 493
Cdd:cd06621  131 IKPSNILLTRKGQVKLCDFGVSGELVNSLAGTFT-GTSYYMAPERIQGGPYSITSDVWSLGLTLLEVAQNR-FPFPPEGe 208
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 494 ---------------FFTDLRDGIISDIFDKKE-KTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd06621  209 pplgpiellsyivnmPNPELKDEPENGIKWSESfKDFIEKCLEKDGTRRPGPWQML 264
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
273-534 3.13e-25

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: 104.64  E-value: 3.13e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNE-------KAEREVkALAKL-DHVNIVHYNGCWdgvdydpetsddyless 344
Cdd:cd14081    9 LGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLskesvlmKVEREI-AIMKLiEHPNVLKLYDVY----------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpENSKNssrsktkcLFIQMEFCDKGTLEQWIeNRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd14081   71 ----ENKKY--------LYLVLEYVSGGELFDYL-VKKG-RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDE 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELLhVCDTAFE---TSKFFTDLRD 500
Cdd:cd14081  137 KNNIKIADFGMASLQPEGSLLETSCGSPHYACPEVIKGEKYdGRKADIWSCGVILYALL-VGALPFDddnLRQLLEKVKR 215
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 525343631 501 GI--ISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14081  216 GVfhIPHFISPDAQDLLRRMLEVNPEKRITIEEIKK 251
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
273-480 3.38e-25

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: 105.61  E-value: 3.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER-------EVKALAKLDHVNIVHYngcwdgVDYDPETSddylessd 345
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSPSDKnrerwclEVQIMKKLNHPNVVSA------RDVPPELE-------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 ydpensknsSRSKTKCLFIQMEFCDKGTLEQWI---ENRRGEKLDKVLalELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd13989   67 ---------KLSPNDLPLLAMEYCSGGDLRKVLnqpENCCGLKESEVR--TLLSDISSAISYLHENRIIHRDLKPENIVL 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 423 VDTKQ---VKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAE 480
Cdd:cd13989  136 QQGGGrviYKLIDLGYAKELDQGSLCTSFVGTLQYLAPELFESKKYTCTVDYWSFGTLAFE 196
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
266-534 3.95e-25

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: 104.86  E-value: 3.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV--------KYNNEKAEREVKALAKLDHVNIVHYNGCWDgvdydpets 337
Cdd:cd14098    1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIvkrkvagnDKNLQLFQREINILKSLEHPGIVRLIDWYE--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 ddylessdyDPEnsknssrsktkCLFIQMEFCDKGTLEQWIENRRGekLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd14098   72 ---------DDQ-----------HIYLVMEYVEGGDLMDFIMAWGA--IPEQHARELTKQILEAMAYTHSMGITHRDLKP 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 418 SNIFLV--DTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQD------YGKEVDLYALGLILAELLhvcdTAF 489
Cdd:cd14098  130 ENILITqdDPVIVKISDFGLAKVIHTGTFLVTFCGTMAYLAPEILMSKEqnlqggYSNLVDMWSVGCLVYVML----TGA 205
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 490 etSKFFTDLRDGIISDI--------------FDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14098  206 --LPFDGSSQLPVEKRIrkgrytqpplvdfnISEEAIDFILRLLDVDPEKRMTAAQALD 262
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
270-482 4.07e-25

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 109.11  E-value: 4.07e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIK--RVKYNN-----EKAEREVKALAKLDHVNIVhyngcwdGVdYDPETSDDYLe 342
Cdd:NF033483  12 GERIGRGGMAEVYLAKDTRLDRDVAVKvlRPDLARdpefvARFRREAQSAASLSHPNIV-------SV-YDVGEDGGIP- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssrsktkclFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:NF033483  83 --------------------YIVMEYVDGRTLKDYI--REHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILI 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 423 VDTKQVKIGDFGLV-----TSLKNdgkrTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:NF033483 141 TKDGRVKVTDFGIAralssTTMTQ----TNSVlGTVHYLSPEQARGGTVDARSDIYSLGIVLYEML 202
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
266-534 4.95e-25

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: 104.82  E-value: 4.95e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEI--ELiGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER----EVKALAKLDHVNIVhynGCWDGVDYDPEtsdd 339
Cdd:cd06611    5 DIWEIigEL-GDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEdfmvEIDILSECKHPNIV---GLYEAYFYENK---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknssrsktkcLFIQMEFCDKGTLEQWIEnrrgeKLDKVLALE----LFEQITKGVDYIHSKKLIHRDL 415
Cdd:cd06611   77 ----------------------LWILIEFCDGGALDSIML-----ELERGLTEPqiryVCRQMLEALNFLHSHKVIHRDL 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 416 KPSNIFLVDTKQVKIGDFGLvtSLKNdgKRTRSK-----GTLRYMSPEQI-----SSQDYGKEVDLYALGLILAEL---- 481
Cdd:cd06611  130 KAGNILLTLDGDVKLADFGV--SAKN--KSTLQKrdtfiGTPYWMAPEVVacetfKDNPYDYKADIWSLGITLIELaqme 205
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 482 -----LHVCDTAFETSKffTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06611  206 pphheLNPMRVLLKILK--SEPPTLDQPSKWSSSFNDFLKSCLVKDPDDRPTAAELLK 261
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
267-483 6.30e-25

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: 104.01  E-value: 6.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE-------REVKALAKLDHVNIVHYNgcwdgvdydpetsdD 339
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEqdmvrirREIEIMSSLNHPHIIRIY--------------E 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14073   69 VFENKDK---------------IVIVMEYASGGELYDYISERR--RLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLEN 131
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELLH 483
Cdd:cd14073  132 ILLDQNGNAKIADFGLSNLYSKDKLLQTFCGSPLYASPEIVNGTPYqGPEVDCWSLGVLLYTLVY 196
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
273-526 6.37e-25

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: 103.84  E-value: 6.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNN-------EKAEREVKALAKLDHVNIVHYngcwdgvdydpetsddYLESSD 345
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHivqtrqqEHIFSEKEILEECNSPFIVKL----------------YRTFKD 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 ydpensknssrskTKCLFIQMEFCDKGTLeqWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDT 425
Cdd:cd05572   65 -------------KKYLYMLMEYCLGGEL--WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSN 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQVKIGDFGLVTSLKNdGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAFETS-----KFFTDLR 499
Cdd:cd05572  130 GYVKLVDFGFAKKLGS-GRKTWTfCGTPEYVAPEIILNKGYDFSVDYWSLGILLYELL-TGRPPFGGDdedpmKIYNIIL 207
                        250       260       270
                 ....*....|....*....|....*....|.
gi 525343631 500 DGI----ISDIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05572  208 KGIdkieFPKYIDKNAKNLIKQLLRRNPEER 238
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
266-534 6.70e-25

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


Pssm-ID: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 104.24  E-value: 6.70e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK------YNNEKAEREVKALAKL-DHVNIVHYNGCWdgvdydpeTSD 338
Cdd:cd14139    1 EFLELEKIGVGEFGSVYKCIKRLDGCVYAIKRSMrpfagsSNEQLALHEVYAHAVLgHHPHVVRYYSAW--------AED 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 DYLessdydpensknssrsktkclFIQMEFCDKGTLEQWI-ENRR-GEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd14139   73 DHM---------------------IIQNEYCNGGSLQDAIsENTKsGNHFEEPELKDILLQVSMGLKYIHNSGLVHLDIK 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQV----------------------KIGDFGLVTSLKNDgkrTRSKGTLRYMSPEqISSQDYG--KEVDLY 472
Cdd:cd14139  132 PSNIFICHKMQSssgvgeevsneedeflsanvvyKIGDLGHVTSINKP---QVEEGDSRFLANE-ILQEDYRhlPKADIF 207
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 473 ALGLILAeLLHVCDTAFETSKFFTDLRDGIISDIFDKKE---KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14139  208 ALGLTVA-LAAGAEPLPTNGAAWHHIRKGNFPDVPQELPesfSSLLKNMIQPDPEQRPSATALAR 271
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
270-534 6.86e-25

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: 104.29  E-value: 6.86e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKA----EREVKALAKL-DHVNIVHYngcwdgVDYdpetsddyless 344
Cdd:cd14037    8 EKYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDlnvcKREIEIMKRLsGHKNIVGY------IDS------------ 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpenSKNSSRSKTKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKK--LIHRDLKPSNIFL 422
Cdd:cd14037   70 ------SANRSGNGVYEVLLLMEYCKGGGVIDLMNQRLQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLI 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLVTS-------------LKNDGKRTRskgTLRYMSPEQI---SSQDYGKEVDLYALGLILAELLHVCd 486
Cdd:cd14037  144 SDSGNYKLCDFGSATTkilppqtkqgvtyVEEDIKKYT---TLQYRAPEMIdlyRGKPITEKSDIWALGCLLYKLCFYT- 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 487 TAFETSKFFtdlrdGIISDIFD--------KKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14037  220 TPFEESGQL-----AILNGNFTfpdnsrysKRLHKLIRYMLEEDPEKRPNIYQVSY 270
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
272-482 7.39e-25

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: 103.97  E-value: 7.39e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRIDGKTYVIKRVKY--NNEKAEREVKAL-------AKLDHVNIVHYNGCWDgvdyDPETsddyle 342
Cdd:cd06625    7 LLGQGAFGQVYLCYDADTGRELAVKQVEIdpINTEASKEVKALeceiqllKNLQHERIVQYYGCLQ----DEKS------ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssrsktkcLFIQMEFCDKGTLEQWIENRrGEkLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd06625   77 -------------------LSIFMEYMPGGSVKDEIKAY-GA-LTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILR 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 423 VDTKQVKIGDFGLVTSLKNDGKRTRSK---GTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd06625  136 DSNGNVKLGDFGASKRLQTICSSTGMKsvtGTPYWMSPEVINGEGYGRKADIWSVGCTVVEML 198
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
267-534 1.38e-24

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: 103.55  E-value: 1.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER---EVKALAKLDH-VNIVHYNGCWdgVDYDPETSDDYLe 342
Cdd:cd06636   18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEEEEiklEINMLKKYSHhRNIATYYGAF--IKKSPPGHDDQL- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssrsktkclFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd06636   95 --------------------WLVMEFCGAGSVTDLVKNTKGNALKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLL 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLVTSL-KNDGKRTRSKGTLRYMSPEQISSQD-----YGKEVDLYALGLILAELLH----VCDTAFETS 492
Cdd:cd06636  155 TENAEVKLVDFGVSAQLdRTVGRRNTFIGTPYWMAPEVIACDEnpdatYDYRSDIWSLGITAIEMAEgappLCDMHPMRA 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 493 KFFT--DLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06636  235 LFLIprNPPPKLKSKKWSKKFIDFIEGCLVKNYLSRPSTEQLLK 278
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
267-482 1.66e-24

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: 102.72  E-value: 1.66e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKrvkYNN-----EKAE-----REVKALAKLDHVNIVHyngcwdgvdydpet 336
Cdd:cd05578    2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMK---YMNkqkciEKDSvrnvlNELEILQELEHPFLVN-------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddyLESSDYDPENsknssrsktkcLFIQMEFCDKGTLEQWIENRR--GEKLDKVLALElfeqITKGVDYIHSKKLIHRD 414
Cdd:cd05578   65 ----LWYSFQDEED-----------MYMVVDLLLGGDLRYHLQQKVkfSEETVKFYICE----IVLALDYLHSKNIIHRD 125
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 415 LKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05578  126 IKPDNILLDEQGHVHITDFNIATKLTDGTLATSTSGTKPYMAPEVFMRAGYSFAVDWWSLGVTAYEML 193
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
271-482 1.82e-24

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: 102.85  E-value: 1.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER--------------EVKALAKLDHVNIVHYNGCwdgvdydpET 336
Cdd:cd06629    7 ELIGKGTYGRVYLAMNATTGEMLAVKQVELPKTSSDRadsrqktvvdalksEIDTLKDLDHPNIVQYLGF--------EE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 SDDYLEssdydpensknssrsktkclfIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd06629   79 TEDYFS---------------------IFLEYVPGGSIGSCL--RKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLK 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 417 PSNIfLVDTKQV-KIGDFGLVTSLKN---DGKRTRSKGTLRYMSPEQISS--QDYGKEVDLYALGLILAELL 482
Cdd:cd06629  136 ADNI-LVDLEGIcKISDFGISKKSDDiygNNGATSMQGSVFWMAPEVIHSqgQGYSAKVDIWSLGCVVLEML 206
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
267-481 2.00e-24

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: 102.94  E-value: 2.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE-----REVKALAKLDHV---NIVHYNGCWdgvdydpetsd 338
Cdd:cd06917    3 YRRLELVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDDDDvsdiqKEVALLSQLKLGqpkNIIKYYGSY----------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dyLEssdyDPEnsknssrsktkcLFIQMEFCDKGTLEQWIenrRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd06917   72 --LK----GPS------------LWIIMDYCEGGSIRTLM---RAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAA 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSL-KNDGKRTRSKGTLRYMSPEQISS-QDYGKEVDLYALGLILAEL 481
Cdd:cd06917  131 NILVTNTGNVKLCDFGVAASLnQNSSKRSTFVGTPYWMAPEVITEgKYYDTKADIWSLGITTYEM 195
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
272-535 2.20e-24

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: 102.48  E-value: 2.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRIDGKTYVIK-----RVKYNN--EKAEREVKALAKLDHVNIVHYngcwdgvdydpetsddyless 344
Cdd:cd14663    7 TLGEGTFAKVKFARNTKTGESVAIKiidkeQVAREGmvEQIKREIAIMKLLRHPNIVEL--------------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpensKNSSRSKTKcLFIQMEFCDKGTLEQWIENrrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd14663   66 -------HEVMATKTK-IFFVMELVTGGELFSKIAK--NGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDE 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGL---VTSLKNDGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELLHVCdTAFETS---KFFTD 497
Cdd:cd14663  136 DGNLKISDFGLsalSEQFRQDGLLHTTCGTPNYVAPEVLARRGYdGAKADIWSCGVILFVLLAGY-LPFDDEnlmALYRK 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 525343631 498 LRDG--IISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:cd14663  215 IMKGefEYPRWFSPGAKSLIKRILDPNPSTRITVEQIMAS 254
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
267-481 2.44e-24

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: 103.34  E-value: 2.44e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK------AEREVKALAKLDHVNIVHYNgcwdgvdydpETSDDY 340
Cdd:cd07864    9 FDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKegfpitAIREIKILRQLNHRSVVNLK----------EIVTDK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSDYdpensknssRSKTKCLFIQMEFCDK---GTLEQWIENRRGEKLDkvlalELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd07864   79 QDALDF---------KKDKGAFYLVFEYMDHdlmGLLESGLVHFSEDHIK-----SFMKQLLEGLNYCHKKNFLHRDIKC 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSLKNDGKR--TRSKGTLRYMSPEQISSQD-YGKEVDLYALGLILAEL 481
Cdd:cd07864  145 SNILLNNKGQIKLADFGLARLYNSEESRpyTNKVITLWYRPPELLLGEErYGPAIDVWSCGCILGEL 211
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
266-482 2.62e-24

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: 102.40  E-value: 2.62e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV--KYNNEKAE----REVKALAKLDHVNIVhyngcwdgvdydpetsdd 339
Cdd:cd14202    3 EFSRKDLIGHGAFAVVFKGRHKEKHDLEVAVKCinKKNLAKSQtllgKEIKILKELKHENIV------------------ 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylesSDYDPENSKNssrsktkCLFIQMEFCDKGTLEQWIENRRGEKLDKVLAleLFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14202   65 ----ALYDFQEIAN-------SVYLVMEYCNGGDLADYLHTMRTLSEDTIRL--FLQQIAGAMKMLHSKGIIHRDLKPQN 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 420 IFLV---------DTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14202  132 ILLSysggrksnpNNIRIKIADFGFARYLQNNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTIIYQCL 203
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
273-482 2.77e-24

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: 101.80  E-value: 2.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE--REVKALAKLDHVNIVHYNG-CWdgvdydpetsddylessdydpe 349
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSflKEVKLMRRLSHPNILRFIGvCV---------------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 350 nsknssrsKTKCLFIQMEFCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDT---K 426
Cdd:cd14065   59 --------KDNKLNFITEYVNGGTLEELLKSMD-EQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREAnrgR 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 427 QVKIGDFGLVTSL----KNDGKRTRS---KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14065  130 NAVVADFGLAREMpdekTKKPDRKKRltvVGSPYWMAPEMLRGESYDEKVDVFSFGIVLCEII 192
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
266-535 2.91e-24

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: 102.90  E-value: 2.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTyVIKRVKYNNEKAE------REVKALAKLDHVNIVHYNGCwdgvdydpetsdd 339
Cdd:cd06620    6 DLETLKDLGAGNGGSVSKVLHIPTGTI-MAKKVIHIDAKSSvrkqilRELQILHECHSPYIVSFYGA------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLessdydpeNSKNSsrsktkcLFIQMEFCDKGTLEqwienrRGEKLDKVLALELFEQIT----KGVDYIHSK-KLIHRD 414
Cdd:cd06620   72 FL--------NENNN-------IIICMEYMDCGSLD------KILKKKGPFPEEVLGKIAvavlEGLTYLYNVhRIIHRD 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSkGTLRYMSPEQISSQDYGKEVDLYALGLILAELL---------HVC 485
Cdd:cd06620  131 IKPSNILVNSKGQIKLCDFGVSGELINSIADTFV-GTSTYMSPERIQGGKYSVKSDVWSLGLSIIELAlgefpfagsNDD 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 486 DTAFETSKFFTDLRDGII---------SDIFDKKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:cd06620  210 DDGYNGPMGILDLLQRIVneppprlpkDRIFPKDLRDFVDRCLLKDPRERPSPQLLLDH 268
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
266-539 4.00e-24

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: 102.03  E-value: 4.00e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK---YNNEKAE----REVKALAKLDHVNIVHYngcwdgvdydpetSD 338
Cdd:cd08228    3 NFQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQifeMMDAKARqdcvKEIDLLKQLNHPNVIKY-------------LD 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 DYLESSDydpensknssrsktkcLFIQMEFCDKGTLEQWIENRRGEK--LDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd08228   70 SFIEDNE----------------LNIVLELADAGDLSQMIKYFKKQKrlIPERTVWKYFVQLCSAVEHMHSRRVMHRDIK 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELlhvcdtAFETSKFF 495
Cdd:cd08228  134 PANVFITATGVVKLGDLGLGRFFSSKTTAAHSlVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEM------AALQSPFY 207
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 496 TDLRD--------------GIISDIFDKKEKTLLQKLLSKKPEDRPNTS---EILRTLTVW 539
Cdd:cd08228  208 GDKMNlfslcqkieqcdypPLPTEHYSEKLRELVSMCIYPDPDQRPDIGyvhQIAKQMHVW 268
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
267-482 4.06e-24

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: 103.37  E-value: 4.06e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVkyNNE--------KAEREVKALAKLDHVNIVHYNgcwdgvdydpetsd 338
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKI--SNVfddlidakRILREIKILRHLKHENIIGLL-------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 DYLESSDYDPENSknssrsktkcLFIQMEFCDkgT-LEQWIENRRgekldkVLALELFE----QITKGVDYIHSKKLIHR 413
Cdd:cd07834   66 DILRPPSPEEFND----------VYIVTELME--TdLHKVIKSPQ------PLTDDHIQyflyQILRGLKYLHSAGVIHR 127
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 414 DLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKR--------TRskgtlRYMSPEQI-SSQDYGKEVDLYALGLILAELL 482
Cdd:cd07834  128 DLKPSNILVNSNCDLKICDFGLARGVDPDEDKgflteyvvTR-----WYRAPELLlSSKKYTKAIDIWSVGCIFAELL 200
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
303-532 4.73e-24

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: 102.05  E-value: 4.73e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 303 EKAEREVKALAKLDHVNIVHYNgcwdgvdydpETSDDYLEssDYdpensknssrsktkcLFIQMEFCDKGTLeqwIENRR 382
Cdd:cd14118   59 DRVYREIAILKKLDHPNVVKLV----------EVLDDPNE--DN---------------LYMVFELVDKGAV---MEVPT 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 383 GEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLK-NDGKRTRSKGTLRYMSPEQI- 460
Cdd:cd14118  109 DNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEgDDALLSSTAGTPAFMAPEALs 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 461 -SSQDY-GKEVDLYALGLILAELLhVCDTAFEtSKFFTDLRDGIISD--------IFDKKEKTLLQKLLSKKPEDRPNTS 530
Cdd:cd14118  189 eSRKKFsGKALDIWAMGVTLYCFV-FGRCPFE-DDHILGLHEKIKTDpvvfpddpVVSEQLKDLILRMLDKNPSERITLP 266

                 ..
gi 525343631 531 EI 532
Cdd:cd14118  267 EI 268
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
272-534 6.76e-24

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: 100.77  E-value: 6.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRIDGKTYVIK-----RVK--YNNEKAEREVKALAKLDHVNIVHYNgcwdgvdydpetsdDYLEss 344
Cdd:cd14189    8 LLGKGGFARCYEMTDLATNKTYAVKviphsRVAkpHQREKIVNEIELHRDLHHKHVVKFS--------------HHFE-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dyDPENsknssrsktkcLFIQMEFCDKGTLEQwIENRRGEKLDKVLALELfEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd14189   72 --DAEN-----------IYIFLELCSRKSLAH-IWKARHTLLEPEVRYYL-KQIISGLKYLHLKGILHRDLKLGNFFINE 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELLhvCDT-AFETSKFFTDLR--- 499
Cdd:cd14189  137 NMELKVGDFGLAARLEPPEQRKKTIcGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLL--CGNpPFETLDLKETYRcik 214
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 525343631 500 --DGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14189  215 qvKYTLPASLSLPARHLLAGILKRNPGDRLTLDQILE 251
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
273-534 7.15e-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: 100.81  E-value: 7.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKY---NNEKAEREVKALAKLDHVNIVHyngcwdgvdydpetsddyLESSdYDPE 349
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPKrdkKKEAVLREISILNQLQHPRIIQ------------------LHEA-YESP 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 350 NSknssrsktkcLFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK--Q 427
Cdd:cd14006   62 TE----------LVLILELCSGGELLDRLAER--GSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPspQ 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 428 VKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVC-----DTAFET------SKF-F 495
Cdd:cd14006  130 IKIIDFGLARKLNPGEELKEIFGTPEFVAPEIVNGEPVSLATDMWSIGVLTYVLLSGLspflgEDDQETlanisaCRVdF 209
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 525343631 496 TDLRDGIISDifdkKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14006  210 SEEYFSSVSQ----EAKDFIRKLLVKEPRKRPTAQEALQ 244
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
272-482 9.91e-24

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: 100.69  E-value: 9.91e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE-------------REVKALAKLDHVNIVHYNGCwdgvdydpETSD 338
Cdd:cd06628    7 LIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAEnkdrkksmldalqREIALLRELQHENIVQYLGS--------SSDA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 DYLEssdydpensknssrsktkclfIQMEFCDKGTLEQWIENRrGEkLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd06628   79 NHLN---------------------IFLEYVPGGSVATLLNNY-GA-FEESLVRNFVRQILKGLNYLHNRGIIHRDIKGA 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 419 NIfLVDTK-QVKIGDFGL-------VTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd06628  136 NI-LVDNKgGIKISDFGIskkleanSLSTKNNGARPSLQGSVFWMAPEVVKQTSYTRKADIWSLGCLVVEML 206
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
267-545 1.28e-23

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: 101.65  E-value: 1.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN----NEKAE---REVKALAKLDHVNIVHYNGCwdgvdydpetsdd 339
Cdd:cd06633   23 FVDLHEIGHGSFGAVYFATNSHTNEVVAIKKMSYSgkqtNEKWQdiiKEVKFLQQLKHPNTIEYKGC------------- 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLessdydpensknssrsKTKCLFIQMEFCdKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd06633   90 YL----------------KDHTAWLVMEYC-LGSASDLLEVHK-KPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGN 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGlvtSLKNDGKRTRSKGTLRYMSPEQISSQDYGK---EVDLYALGLILAELLHVCDTAFETSKFFT 496
Cdd:cd06633  152 ILLTEPGQVKLADFG---SASIASPANSFVGTPYWMAPEVILAMDEGQydgKVDIWSLGITCIELAERKPPLFNMNAMSA 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 497 ----------DLRDGIISDIFdkkeKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEK 545
Cdd:cd06633  229 lyhiaqndspTLQSNEWTDSF----RGFVDYCLQKIPQERPSSAELLRHDFVRRERPPR 283
DSRM_EIF2AK2_rpt1 cd19903
first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha ...
8-59 2.35e-23

first double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). This model describes the first motif. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380732  Cd Length: 68  Bit Score: 93.22  E-value: 2.35e-23
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631   8 GFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFRVIIDEREFPEGEGRS 59
Cdd:cd19903    1 GNYMGKLNEYCQKQKVVLDYVEVPTSGPSHDPRFTFQVVIDGKEYPEGEGKS 52
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
270-483 2.45e-23

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: 99.60  E-value: 2.45e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKhRIDGKTYVIKRVKYNNEKAE------REVKALAKL-DHVNIVHYngcwdgVDYDPETSDDYLe 342
Cdd:cd14131    6 LKQLGKGGSSKVYKVL-NPKKKIYALKRVDLEGADEQtlqsykNEIELLKKLkGSDRIIQL------YDYEVTDEDDYL- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssrsktkclFIQMEfCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd14131   78 --------------------YMVME-CGEIDLATILKKKRPKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLL 136
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 423 VDtKQVKIGDFGLVTSLKNDG---KRTRSKGTLRYMSPE--QISSQDY--------GKEVDLYALGLILAELLH 483
Cdd:cd14131  137 VK-GRLKLIDFGIAKAIQNDTtsiVRDSQVGTLNYMSPEaiKDTSASGegkpkskiGRPSDVWSLGCILYQMVY 209
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
267-533 3.93e-23

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: 99.37  E-value: 3.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK------AEREVKALAKLDHVNIVhyngcwdgvdydpetsddy 340
Cdd:cd07847    3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDpvikkiALREIRMLKQLKHPNLV------------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpeNSKNSSRSKTKcLFIQMEFCDKGTLEQWIENRRGekLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd07847   64 ---------NLIEVFRRKRK-LHLVFEYCDHTVLNELEKNPRG--VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENI 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 421 FLVDTKQVKIGDFGLVTSLKN-DGKRTRSKGTLRYMSPEQI-SSQDYGKEVDLYALGLILAELL---------------- 482
Cdd:cd07847  132 LITKQGQIKLCDFGFARILTGpGDDYTDYVATRWYRAPELLvGDTQYGPPVDVWAIGCVFAELLtgqplwpgksdvdqly 211
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 483 HVCDT----------AFETSKFFTDLRDGIISDIFDKKEK---------TLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd07847  212 LIRKTlgdliprhqqIFSTNQFFKGLSIPEPETREPLESKfpnisspalSFLKGCLQMDPTERLSCEELL 281
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
266-482 4.63e-23

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: 99.22  E-value: 4.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK------AEREVKALAKLDHVNIVHYNGCWDGVDYDPetsdd 339
Cdd:cd07843    6 EYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEKEKegfpitSLREINILLKLQHPNIVTVKEVVVGSNLDK----- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknssrsktkcLFIQMEFCD---KGTLEQWIEN-RRGEKldKVLALELFEqitkGVDYIHSKKLIHRDL 415
Cdd:cd07843   81 ----------------------IYMVMEYVEhdlKSLMETMKQPfLQSEV--KCLMLQLLS----GVAHLHDNWILHRDL 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 416 KPSNIFLVDTKQVKIGDFGLVTSL-KNDGKRTRSKGTLRYMSPEQI-SSQDYGKEVDLYALGLILAELL 482
Cdd:cd07843  133 KTSNLLLNNRGILKICDFGLAREYgSPLKPYTQLVVTLWYRAPELLlGAKEYSTAIDMWSVGCIFAELL 201
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
267-534 4.99e-23

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 98.68  E-value: 4.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE-------REVKALAKLDHVNIVHYNGCwdgvdydpetsdd 339
Cdd:cd06607    3 FEDLREIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQSTekwqdiiKEVKFLRQLRHPNTIEYKGC------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLessdydpensknssRSKTKCLFiqMEFCdKGTLEQWIE-NRRGEKLDKVLALelFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd06607   70 YL--------------REHTAWLV--MEYC-LGSASDIVEvHKKPLQEVEIAAI--CHGALQGLAYLHSHNRIHRDVKAG 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTKQVKIGDFGlVTSLKNDGkrTRSKGTLRYMSPEQISSQD---YGKEVDLYALGLI---LAE------------ 480
Cdd:cd06607  131 NILLTEPGTVKLADFG-SASLVCPA--NSFVGTPYWMAPEVILAMDegqYDGKVDVWSLGITcieLAErkpplfnmnams 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 481 -LLHVCDTAFETskfftdLRDGIISDIFdkkeKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06607  208 aLYHIAQNDSPT------LSSGEWSDDF----RNFVDSCLQKIPQDRPSAEDLLK 252
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
270-485 5.47e-23

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: 98.49  E-value: 5.47e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRiDGKTYVIKRVKYNNEKAE-------REVKALAKLDHVNIVHYNgcwdgvdydpetsddyle 342
Cdd:cd14161    8 LETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEqdllhirREIEIMSSLNHPHIISVY------------------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpENSKNSSRsktkcLFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd14161   69 ------EVFENSSK-----IVIVMEYASRGDLYDYISER--QRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILL 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 423 VDTKQVKIGDFGLvTSLKNDGKRTRSK-GTLRYMSPEQISSQDY-GKEVDLYALGLILAELLHVC 485
Cdd:cd14161  136 DANGNIKIADFGL-SNLYNQDKFLQTYcGSPLYASPEIVNGRPYiGPEVDSWSLGVLLYILVHGT 199
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
266-532 5.88e-23

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: 98.73  E-value: 5.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKA-KHRIDGKTYVIKRVKYNN-----EKAER---------EVKAL-AKLDHVNIVHYngcwdg 329
Cdd:cd08528    1 EYAVLELLGSGAFGCVYKVrKKSNGQTLLALKEINMTNpafgrTEQERdksvgdiisEVNIIkEQLRHPNIVRY------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 330 vdYDPETSDDYLessdydpensknssrsktkclFIQMEFCDKGTLEQWIEN--RRGEKLDKVLALELFEQITKGVDYIH- 406
Cdd:cd08528   75 --YKTFLENDRL---------------------YIVMELIEGAPLGEHFSSlkEKNEHFTEDRIWNIFVQMVLALRYLHk 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 407 SKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTS-LKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVC 485
Cdd:cd08528  132 EKQIVHRDLKPNNIMLGEDDKVTITDFGLAKQkGPESSKMTSVVGTILYSCPEIVQNEPYGEKADIWALGCILYQMCTLQ 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 525343631 486 DTAFET------SKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEI 532
Cdd:cd08528  212 PPFYSTnmltlaTKIVEAEYEPLPEGMYSDDITFVIRSCLTPDPEARPDIVEV 264
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
266-534 6.23e-23

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: 98.33  E-value: 6.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEI-ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKA----------EREVKALAKLDHVNIVhyngcwdgvdydp 334
Cdd:cd14105    5 DFYDIgEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKAsrrgvsrediEREVSILRQVLHPNII------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 335 eTSDDYLESsdydpensknssrsKTKCLFIqMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRD 414
Cdd:cd14105   72 -TLHDVFEN--------------KTDVVLI-LELVAGGELFDFLAEK--ESLSEEEATEFLKQILDGVNYLHTKNIAHFD 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFL----VDTKQVKIGDFGLVTSLKnDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVC---- 485
Cdd:cd14105  134 LKPENIMLldknVPIPRIKLIDFGLAHKIE-DGNEFKNIfGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGAspfl 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 525343631 486 -DTAFETSKFFTDLRDGIISDIFDKKE---KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14105  213 gDTKQETLANITAVNYDFDDEYFSNTSelaKDFIRQLLVKDPRKRMTIQESLR 265
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
264-482 6.27e-23

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: 100.24  E-value: 6.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 264 GMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK----AEREVKALAKLDHVNIVHYngcwdgvdYD---PET 336
Cdd:cd07854    4 GSRYMDLRPLGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQsvkhALREIKIIRRLDHDNIVKV--------YEvlgPSG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 SDDylessdydpeNSKNSSRSKTKCLFIQMEFCD---KGTLEQwieNRRGEKLDKVLALELFeqitKGVDYIHSKKLIHR 413
Cdd:cd07854   76 SDL----------TEDVGSLTELNSVYIVQEYMEtdlANVLEQ---GPLSEEHARLFMYQLL----RGLKYIHSANVLHR 138
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 414 DLKPSNIFL-VDTKQVKIGDFGLVTSLKND----GKRTRSKGTLRYMSPEQI-SSQDYGKEVDLYALGLILAELL 482
Cdd:cd07854  139 DLKPANVFInTEDLVLKIGDFGLARIVDPHyshkGYLSEGLVTKWYRSPRLLlSPNNYTKAIDMWAAGCIFAEML 213
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
273-533 6.50e-23

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


Pssm-ID: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 98.39  E-value: 6.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVkyNNEKA--------EREVKALAKLDHVNIVHYNGCWdgvdydpETSddyless 344
Cdd:cd14097    9 LGQGSFGVVIEATHKETQTKWAIKKI--NREKAgssavkllEREVDILKHVNHAHIIHLEEVF-------ETP------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpensknssrsktKCLFIQMEFCDKGTLEQwIENRRGEkLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL-- 422
Cdd:cd14097   73 ---------------KRMYLVMELCEDGELKE-LLLRKGF-FSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVks 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 -----VDTKQVKIGDFGL--VTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhvCD----TAFET 491
Cdd:cd14097  136 siidnNDKLNIKVTDFGLsvQKYGLGEDMLQETCGTPIYMAPEVISAHGYSQQCDIWSIGVIMYMLL--CGeppfVAKSE 213
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631 492 SKFFTDLRDG----------IISDifdkKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14097  214 EKLFEEIRKGdltftqsvwqSVSD----AAKNVLQQLLKVDPAHRMTASELL 261
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
256-535 6.98e-23

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: 98.62  E-value: 6.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 256 KYTVDKrfgmdfkeieLIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN------------EKAEREVKALAKLDHVNIVhy 323
Cdd:cd14084    7 KYIMSR----------TLGSGACGEVKLAYDKSTCKKVAIKIINKRKftigsrreinkpRNIETEIEILKKLSHPCII-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 324 ngcwdgvdydpeTSDDYLESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVD 403
Cdd:cd14084   75 ------------KIEDFFDAEDD---------------YYIVLELMEGGELFDRV--VSNKRLKEAICKLYFYQMLLAVK 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 404 YIHSKKLIHRDLKPSNIFLVDTKQ---VKIGDFGLVTSLKNDG-KRTRSkGTLRYMSPEQISS---QDYGKEVDLYALGL 476
Cdd:cd14084  126 YLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSKILGETSlMKTLC-GTPTYLAPEVLRSfgtEGYTRAVDCWSLGV 204
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 477 ILAELLhvCDT-AFETSKFFTDLRDGIISD--IFDKKE--------KTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:cd14084  205 ILFICL--SGYpPFSEEYTQMSLKEQILSGkyTFIPKAwknvseeaKDLVKKMLVVDPSRRPSIEEALEH 272
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
271-482 9.38e-23

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: 98.19  E-value: 9.38e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIK------------RVKYNNEKAEREVKALAKLD-HVNIVHYNgcwdgvdydpets 337
Cdd:cd14093    9 EILGRGVSSTVRRCIEKETGQEFAVKiiditgekssenEAEELREATRREIEILRQVSgHPNIIELH------------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 dDYLESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWIEN--RRGEKLDKVLALELFEqitkGVDYIHSKKLIHRDL 415
Cdd:cd14093   76 -DVFESPTF---------------IFLVFELCRKGELFDYLTEvvTLSEKKTRRIMRQLFE----AVEFLHSLNIVHRDL 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 416 KPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQ------DYGKEVDLYALGLILAELL 482
Cdd:cd14093  136 KPENILLDDNLNVKISDFGFATRLDEGEKLRELCGTPGYLAPEVLKCSmydnapGYGKEVDMWACGVIMYTLL 208
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
259-482 1.23e-22

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: 97.44  E-value: 1.23e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 259 VDKRFgmDFKEIelIGSGGFGQVFKAKHRIDGKTYVIK-----RVKYNNEKAEREVKALAKLDHVNIVhyngcwdgvdyd 333
Cdd:cd14083    1 IRDKY--EFKEV--LGTGAFSEVVLAEDKATGKLVAIKcidkkALKGKEDSLENEIAVLRKIKHPNIV------------ 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 334 peTSDDYLESsdydpensknssrskTKCLFIQMEFCDKGTLEQWIEnRRGEKLDKVlALELFEQITKGVDYIHSKKLIHR 413
Cdd:cd14083   65 --QLLDIYES---------------KSHLYLVMELVTGGELFDRIV-EKGSYTEKD-ASHLIRQVLEAVDYLHSLGIVHR 125
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 414 DLKPSNIFL----VDTKqVKIGDFGLvTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14083  126 DLKPENLLYyspdEDSK-IMISDFGL-SKMEDSGVMSTACGTPGYVAPEVLAQKPYGKAVDCWSIGVISYILL 196
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
266-480 1.58e-22

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 99.13  E-value: 1.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKA-----EREVKALAKLDHVNIVHyngCWDGVDYDPEtsddy 340
Cdd:PLN00034  75 ELERVNRIGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTvrrqiCREIEILRDVNHPNVVK---CHDMFDHNGE----- 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpensknssrsktkcLFIQMEFCDKGTLEqwienrrGEKLDKVLAL-ELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:PLN00034 147 ---------------------IQVLLEFMDGGSLE-------GTHIADEQFLaDVARQILSGIAYLHRRHIVHRDIKPSN 198
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQISSQ----DY-GKEVDLYALGLILAE 480
Cdd:PLN00034 199 LLINSAKNVKIADFGVSRILAQTMDPCNSSvGTIAYMSPERINTDlnhgAYdGYAGDIWSLGVSILE 265
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
266-526 1.71e-22

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 98.90  E-value: 1.71e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK---------YNNEKAEREVKALAKLDHVNIVHYngcwdgvdydpet 336
Cdd:cd05573    2 DFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRksdmlkreqIAHVRAERDILADADSPWIVRLHY------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddylesSDYDPENsknssrsktkcLFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd05573   69 -------AFQDEDH-----------LYLVMEYMPGGDLMNLLIKY--DVFPEETARFYIAELVLALDSLHKLGFIHRDIK 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSK------------------------------GTLRYMSPEQISSQDYG 466
Cdd:cd05573  129 PDNILLDADGHIKLADFGLCTKMNKSGDRESYLndsvntlfqdnvlarrrphkqrrvraysavGTPDYIAPEVLRGTGYG 208
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 467 KEVDLYALGLILAELLhvcdtaFETSKFFTDLRDGIISDIFDKKE--------------KTLLQKLLsKKPEDR 526
Cdd:cd05573  209 PECDWWSLGVILYEML------YGFPPFYSDSLVETYSKIMNWKEslvfpddpdvspeaIDLIRRLL-CDPEDR 275
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
265-482 2.00e-22

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: 97.77  E-value: 2.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 265 MDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK------AEREVKALAKLDHVNIVHyngcwdgvdydpetsd 338
Cdd:cd07866    8 RDYEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKdgfpitALREIKILKKLKHPNVVP---------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dyLESSDYDPenSKNSSRSKtKCLFIQMEFCDK---GTLEQwiENRRGEKLD-KVLALELFEqitkGVDYIHSKKLIHRD 414
Cdd:cd07866   72 --LIDMAVER--PDKSKRKR-GSVYMVTPYMDHdlsGLLEN--PSVKLTESQiKCYMLQLLE----GINYLHENHILHRD 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKG------------TLRYMSPEQI-SSQDYGKEVDLYALGLILAEL 481
Cdd:cd07866  141 IKAANILIDNQGILKIADFGLARPYDGPPPNPKGGGgggtrkytnlvvTRWYRPPELLlGERRYTTAVDIWGIGCVFAEM 220

                 .
gi 525343631 482 L 482
Cdd:cd07866  221 F 221
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
273-482 2.39e-22

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: 96.81  E-value: 2.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER----EVKALAKLDHVNIVHYngcwDGVDYdpetsddylessdydp 348
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKELIRFDEEAQRnflkEVKVMRSLDHPNVLKF----IGVLY---------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 349 ensknssrsKTKCLFIQMEFCDKGTLEQWIENRrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQV 428
Cdd:cd14154   61 ---------KDKKLNLITEYIPGGTLKDVLKDM-ARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTV 130
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 429 KIGDFGL----------------VTSLKNDGKRTRSK-----GTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14154  131 VVADFGLarliveerlpsgnmspSETLRHLKSPDRKKrytvvGNPYWMAPEMLNGRSYDEKVDIFSFGIVLCEII 205
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
273-526 2.67e-22

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: 97.67  E-value: 2.67e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIK-----RVKYNNE----KAEREVKALAkLDHVNIVHYNGCwdgvdydpetsddyLES 343
Cdd:cd05570    3 LGKGSFGKVMLAERKKTDELYAIKvlkkeVIIEDDDvectMTEKRVLALA-NRHPFLTGLHAC--------------FQT 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 SDYdpensknssrsktkcLFIQMEFCDKGTLEQWI--ENRRGEKLDKVLALElfeqITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd05570   68 EDR---------------LYFVMEYVNGGDLMFHIqrARRFTEERARFYAAE----ICLALQFLHERGIIYRDLKLDNVL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAFEtSKFFTDLRD 500
Cdd:cd05570  129 LDAEGHIKIADFGMCKEGIWGGNTTSTFcGTPDYIAPEILREQDYGFSVDWWALGVLLYEML-AGQSPFE-GDDEDELFE 206
                        250       260       270
                 ....*....|....*....|....*....|..
gi 525343631 501 GIISD------IFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05570  207 AILNDevlyprWLSREAVSILKGLLTKDPARR 238
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
267-482 3.97e-22

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: 96.59  E-value: 3.97e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK------AEREVKALAKLDHVNIVHYngcwdgvdYDPETSDdy 340
Cdd:cd07835    1 YQKLEKIGEGTYGVVYKARDKLTGEIVALKKIRLETEDegvpstAIREISLLKELNHPNIVRL--------LDVVHSE-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpensknssrsktKCLFIQMEFCDKgTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd07835   71 -------------------NKLYLVFEFLDL-DLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNL 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 421 fLVDTKQV-KIGDFGLVTS----LKNdgkRTRSKGTLRYMSPE-QISSQDYGKEVDLYALGLILAELL 482
Cdd:cd07835  131 -LIDTEGAlKLADFGLARAfgvpVRT---YTHEVVTLWYRAPEiLLGSKHYSTPVDIWSVGCIFAEMV 194
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
270-534 4.11e-22

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


Pssm-ID: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 96.62  E-value: 4.11e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIK---RVKYNNEKAEREVKALAKL-DHVNIVHYNGCwdgvdydpetsddylessd 345
Cdd:cd06638   23 IETIGKGTYGKVFKVLNKKNGSKAAVKildPIHDIDEEIEAEYNILKALsDHPNVVKFYGM------------------- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YDPENSKNSSRsktkcLFIQMEFCDKGTLEQWIEN--RRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd06638   84 YYKKDVKNGDQ-----LWLVLELCNGGSVTDLVKGflKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 424 DTKQVKIGDFGLVTSLKNDG-KRTRSKGTLRYMSPEQISSQD-----YGKEVDLYALGLILAEL---------LHVCDTA 488
Cdd:cd06638  159 TEGGVKLVDFGVSAQLTSTRlRRNTSVGTPFWMAPEVIACEQqldstYDARCDVWSLGITAIELgdgdppladLHPMRAL 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 525343631 489 FETSKF-FTDLRDgiiSDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06638  239 FKIPRNpPPTLHQ---PELWSNEFNDFIRKCLTKDYEKRPTVSDLLQ 282
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
266-482 4.20e-22

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: 96.23  E-value: 4.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHR--IDGKTYVIKRVKYNNEKAE----REVKALAKLDHVNIVHYngcwdgvdydpetsdd 339
Cdd:cd14201    7 EYSRKDLVGHGAFAVVFKGRHRkkTDWEVAIKSINKKNLSKSQillgKEIKILKELQHENIVAL---------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdYDPENSKNSsrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKVLALelFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14201   71 ------YDVQEMPNS-------VFLVMEYCNGGDLADYLQAKGTLSEDTIRVF--LQQIAAAMRILHSKGIIHRDLKPQN 135
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 420 IFL---------VDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14201  136 ILLsyasrkkssVSGIRIKIADFGFARYLQSNMMAATLCGSPMYMAPEVIMSQHYDAKADLWSIGTVIYQCL 207
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
272-534 5.30e-22

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: 95.38  E-value: 5.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKA----EREVKALAKLDHVNIVHYNGCwDGV----DYDpETSDDYLES 343
Cdd:cd14005    7 LLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEwamiNGPVPVPLEIALLLKASKPGV-PGVirllDWY-ERPDGFLLI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 SDYdPENSKNssrsktkcLFiqmEFC-DKGTLEqwiENrrgekldkvLALELFEQITKGVDYIHSKKLIHRDLKPSNIfL 422
Cdd:cd14005   85 MER-PEPCQD--------LF---DFItERGALS---EN---------LARIIFRQVVEAVRHCHQRGVLHRDIKDENL-L 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VD--TKQVKIGDFGLVTSLKNDGKRTRSkGTLRYMSPEQISSQDY-GKEVDLYALGLILAELLHvCDTAFETSKFFtdLR 499
Cdd:cd14005  140 INlrTGEVKLIDFGCGALLKDSVYTDFD-GTRVYSPPEWIRHGRYhGRPATVWSLGILLYDMLC-GDIPFENDEQI--LR 215
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 525343631 500 DGIISDIFDKKE-KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14005  216 GNVLFRPRLSKEcCDLISRCLQFDPSKRPSLEQILS 251
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
273-542 7.49e-22

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: 95.47  E-value: 7.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE---REVKALAKLDHVNIVHYNGcwdgvdydpetsddYLESSDYDpe 349
Cdd:cd14150    8 IGTGSFGTVFRGKWHGDVAVKILKVTEPTPEQLQafkNEMQVLRKTRHVNILLFMG--------------FMTRPNFA-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 350 nsknssrsktkclfIQMEFCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVK 429
Cdd:cd14150   72 --------------IITQWCEGSSLYRHLHVTE-TRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVK 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 430 IGDFGLVT-SLKNDGKRT--RSKGTLRYMSPEQISSQD---YGKEVDLYALGLILAELLhvcdtAFETSKFFTDLRDGII 503
Cdd:cd14150  137 IGDFGLATvKTRWSGSQQveQPSGSILWMAPEVIRMQDtnpYSFQSDVYAYGVVLYELM-----SGTLPYSNINNRDQII 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 525343631 504 ------------SDIFD---KKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKS 542
Cdd:cd14150  212 fmvgrgylspdlSKLSSncpKAMKRLLIDCLKFKREERPLFPQILVSIELLQRL 265
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
267-534 7.74e-22

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: 95.52  E-value: 7.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN-----EKAEREVKALAKLDHVNIVHYNGcwdgvdydpetsdDYL 341
Cdd:cd06641    6 FTKLEKIGKGSFGEVFKGIDNRTQKVVAIKIIDLEEaedeiEDIQQEITVLSQCDSPYVTKYYG-------------SYL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ESSDydpensknssrsktkcLFIQMEFCDKGTLEQWIENrrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd06641   73 KDTK----------------LWIIMEYLGGGSALDLLEP---GPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFGLVTSLKNDG-KRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAEL---------LHVCDTAFET 491
Cdd:cd06641  134 LSEHGEVKLADFGVAGQLTDTQiKRN*FVGTPFWMAPEVIKQSAYDSKADIWSLGITAIELargepphseLHPMKVLFLI 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 525343631 492 SKFFTDLRDGiisdIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06641  214 PKNNPPTLEG----NYSKPLKEFVEACLNKEPSFRPTAKELLK 252
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
273-478 9.80e-22

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: 94.94  E-value: 9.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDG--KTYVIKRVkyNNEKAE---------REVKALAKLDHVNIVH-YngcwdgvdydpetsdDY 340
Cdd:cd14080    8 IGEGSYSKVKLAEYTKSGlkEKVACKII--DKKKAPkdflekflpRELEILRKLRHPNIIQvY---------------SI 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWIeNRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd14080   71 FERGSK---------------VFIFMEYAEHGDLLEYI-QKRG-ALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENI 133
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 421 FLVDTKQVKIGDFGLVTSLKNDGKRTRSK---GTLRYMSPEQISSQDY-GKEVDLYALGLIL 478
Cdd:cd14080  134 LLDSNNNVKLSDFGFARLCPDDDGDVLSKtfcGSAAYAAPEILQGIPYdPKKYDIWSLGVIL 195
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
273-532 1.02e-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: 94.63  E-value: 1.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVfkaKHRIDGKTYV-----------IKRVKYNNEKAEREVKALAKLDHVNIVHyngcwdgvdydpetsddyL 341
Cdd:cd14119    1 LGEGSYGKV---KEVLDTETLCrravkilkkrkLRRIPNGEANVKREIQILRRLNHRNVIK------------------L 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ESSDYDPENSKnssrsktkcLFIQMEFCdKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd14119   60 VDVLYNEEKQK---------LYMVMEYC-VGGLQEMLDSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLL 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFGLVTSL---KNDGKRTRSKGTLRYMSPEQISSQDY--GKEVDLYALGLILAELLhvcdTA---FETS- 492
Cdd:cd14119  130 LTTDGTLKISDFGVAEALdlfAEDDTCTTSQGSPAFQPPEIANGQDSfsGFKVDIWSAGVTLYNMT----TGkypFEGDn 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 493 --KFFTDLRDG--IISDIFDKKEKTLLQKLLSKKPEDRPNTSEI 532
Cdd:cd14119  206 iyKLFENIGKGeyTIPDDVDPDLQDLLRGMLEKDPEKRFTIEQI 249
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
273-534 1.36e-21

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: 94.33  E-value: 1.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYN--NEKAER----EVKALAKLDHVNIVHYngcwdgvdYDP-ETsddylessd 345
Cdd:cd14075   10 LGSGNFSQVKLGIHQLTKEKVAIKILDKTklDQKTQRllsrEISSMEKLHHPNIIRL--------YEVvET--------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 ydpensknssRSKtkcLFIQMEFCDKGTLEQWIENrrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDT 425
Cdd:cd14075   73 ----------LSK---LHLVMEYASGGELYTKIST--EGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASN 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELLhVCDTAF--ETskfFTDLRDGI 502
Cdd:cd14075  138 NCVKVGDFGFSTHAKRGETLNTFCGSPPYAAPELFKDEHYiGIYVDIWALGVLLYFMV-TGVMPFraET---VAKLKKCI 213
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 525343631 503 ISDIF------DKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14075  214 LEGTYtipsyvSEPCQELIRGILQPVPSDRYSIDEIKN 251
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
254-535 1.62e-21

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 97.63  E-value: 1.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 254 ETKYTVDKRFGMDfkeiELIGSGGFGQVFKAKHRIDGKTYVIKRVK---YNNE---KAEREVKALAKLDHVNIVhyngcw 327
Cdd:PTZ00283  25 ATAKEQAKKYWIS----RVLGSGATGTVLCAKRVSDGEPFAVKVVDmegMSEAdknRAQAEVCCLLNCDFFSIV------ 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 328 dgvdydpETSDDYLESSDYDPENsknssrskTKCLFIQMEFCDKGTLEQWIENRR--GEKLDKVLALELFEQITKGVDYI 405
Cdd:PTZ00283  95 -------KCHEDFAKKDPRNPEN--------VLMIALVLDYANAGDLRQEIKSRAktNRTFREHEAGLLFIQVLLAVHHV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 406 HSKKLIHRDLKPSNIFLVDTKQVKIGDFGL----VTSLKNDGKRTRSkGTLRYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:PTZ00283 160 HSKHMIHRDIKSANILLCSNGLVKLGDFGFskmyAATVSDDVGRTFC-GTPYYVAPEIWRRKPYSKKADMFSLGVLLYEL 238
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 482 LHVcDTAFETSKfFTDLRDGIISDIFD-------KKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:PTZ00283 239 LTL-KRPFDGEN-MEEVMHKTLAGRYDplppsisPEMQEIVTALLSSDPKRRPSSSKLLNM 297
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
267-493 1.81e-21

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: 94.70  E-value: 1.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRI----DGKTYVIKRVKYNNEKA----EREVKALAKLDHVNIVHYNG-CWdgvdydpets 337
Cdd:cd14205    6 LKFLQQLGKGNFGSVEMCRYDPlqdnTGEVVAVKKLQHSTEEHlrdfEREIEILKSLQHDNIVKYKGvCY---------- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 ddylessdydpenskNSSRSKTKCLfiqMEFCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd14205   76 ---------------SAGRRNLRLI---MEYLPYGSLRDYLQKHK-ERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLAT 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSLKNDGK----RTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhvcdTAFETSK 493
Cdd:cd14205  137 RNILVENENRVKIGDFGLTKVLPQDKEyykvKEPGESPIFWYAPESLTESKFSVASDVWSFGVVLYELF----TYIEKSK 212
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
273-534 2.11e-21

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 93.44  E-value: 2.11e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNN----EKAEREVKALAKLDHVNIVHyngCWDGVDYDPETsddylessdydp 348
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKakdrEDVRNEIEIMNQLRHPRLLQ---LYDAFETPREM------------ 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 349 ensknssrsktkCLFiqMEFCDKGTLeqwienrrgekLDKVLA--LELFE--------QITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd14103   66 ------------VLV--MEYVAGGEL-----------FERVVDddFELTErdcilfmrQICEGVQYMHKQGILHLDLKPE 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTK--QVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLH-----VCDTAFET 491
Cdd:cd14103  121 NILCVSRTgnQIKIIDFGLARKYDPDKKLKVLFGTPEFVAPEVVNYEPISYATDMWSVGVICYVLLSglspfMGDNDAET 200
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 525343631 492 SKFFT----DLRDGIISDIFDKKeKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14103  201 LANVTrakwDFDDEAFDDISDEA-KDFISKLLVKDPRKRMSAAQCLQ 246
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
266-519 2.18e-21

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: 94.42  E-value: 2.18e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN-------EKAEREVKALAKLDHVNIVHyngcwdgvdydpetsd 338
Cdd:cd05612    2 DFERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEvirlkqeQHVHNEKRVLKEVSHPFIIR---------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dyLESSDYDPENsknssrsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd05612   66 --LFWTEHDQRF-----------LYMLMEYVPGGELFSYLRNSG--RFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPE 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSLKNdgkRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELLhvcdtaFETSKFFTD 497
Cdd:cd05612  131 NILLDKEGHIKLTDFGFAKKLRD---RTWTLcGTPEYLAPEVIQSKGHNKAVDWWALGILIYEML------VGYPPFFDD 201
                        250       260       270
                 ....*....|....*....|....*....|..
gi 525343631 498 LRDGIISDI----------FDKKEKTLLQKLL 519
Cdd:cd05612  202 NPFGIYEKIlagklefprhLDLYAKDLIKKLL 233
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
271-482 2.40e-21

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: 93.96  E-value: 2.40e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER---------EVKALAKLDHVNIVHYNGCWDgvdydpetsddyl 341
Cdd:cd06652    8 KLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESPETskevnalecEIQLLKNLLHERIVQYYGCLR------------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdyDPENsknssrsktKCLFIQMEFCDKGTLEQWIENRRGekLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd06652   75 -----DPQE---------RTLSIFMEYMPGGSIKDQLKSYGA--LTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANIL 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 422 LVDTKQVKIGDFGLVTSLKN---DGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd06652  139 RDSVGNVKLGDFGASKRLQTiclSGTGMKSvTGTPYWMSPEVISGEGYGRKADIWSVGCTVVEML 203
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
267-482 2.70e-21

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: 93.88  E-value: 2.70e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE-----REVKALAKL-DHVNIVHyngcwdgvdydpetsddy 340
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKHFKSLEqvnnlREIQALRRLsPHPNILR------------------ 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSDYDPensknssrsKTKCLFIQMEFCDkGTLEQWIENRRGEKLDKVLALELFeQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd07831   63 LIEVLFDR---------KTGRLALVFELMD-MNLYELIKGRKRPLPEKRVKNYMY-QLLKSLDHMHRNGIFHRDIKPENI 131
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 421 fLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQI-SSQDYGKEVDLYALGLILAELL 482
Cdd:cd07831  132 -LIKDDILKLADFGSCRGIYSKPPYTEYISTRWYRAPECLlTDGYYGPKMDIWAVGCVFFEIL 193
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
267-534 2.89e-21

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: 93.96  E-value: 2.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAkhrIDGKTYVIKRVKYNN--------EKAEREVKALAKLDHVNIVHYNGcwdgvdydpetsd 338
Cdd:cd06640    6 FTKLERIGKGSFGEVFKG---IDNRTQQVVAIKIIDleeaedeiEDIQQEITVLSQCDSPYVTKYYG------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 DYLESSDydpensknssrsktkcLFIQMEFCDKGTLeqwIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd06640   70 SYLKGTK----------------LWIIMEYLGGGSA---LDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAA 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSLKNDG-KRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAEL---------LHVCDTA 488
Cdd:cd06640  131 NVLLSEQGDVKLADFGVAGQLTDTQiKRNTFVGTPFWMAPEVIQQSAYDSKADIWSLGITAIELakgeppnsdMHPMRVL 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 525343631 489 FETSKFFTDLRDGiisdIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06640  211 FLIPKNNPPTLVG----DFSKPFKEFIDACLNKDPSFRPTAKELLK 252
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
250-544 4.59e-21

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: 93.96  E-value: 4.59e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 250 PDMKETKYTVD-KRFGMDFKEIeliGSGGFGQVFKAKHRIDGKTYVIKRVKYN----NEKAE---REVKALAKLDHVNIV 321
Cdd:cd06635   12 PDIAELFFKEDpEKLFSDLREI---GHGSFGAVYFARDVRTSEVVAIKKMSYSgkqsNEKWQdiiKEVKFLQRIKHPNSI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 322 HYNGCwdgvdydpetsddYLessdydpensknssRSKTKCLFiqMEFCdKGTLEQWIENRRgEKLDKVLALELFEQITKG 401
Cdd:cd06635   89 EYKGC-------------YL--------------REHTAWLV--MEYC-LGSASDLLEVHK-KPLQEIEIAAITHGALQG 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 402 VDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGlvtSLKNDGKRTRSKGTLRYMSPEQISSQDYGK---EVDLYALGLIL 478
Cdd:cd06635  138 LAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG---SASIASPANSFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITC 214
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 479 AELLHVCDTAFETSKFFT----------DLRDGIISDIFDKKEKTLLQKLlskkPEDRPNTSEILRTLTVWKKSPE 544
Cdd:cd06635  215 IELAERKPPLFNMNAMSAlyhiaqnespTLQSNEWSDYFRNFVDSCLQKI----PQDRPTSEELLKHMFVLRERPE 286
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
273-536 5.01e-21

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: 92.77  E-value: 5.01e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE---REVK-ALAKLDHVNIVhyngcwdgvdydpETSDDYLESSDYdp 348
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKLKdflREYNiSLELSVHPHII-------------KTYDVAFETEDY-- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 349 ensknssrsktkcLFIQMEFCDKGTLEQWIENRRGekLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDT--K 426
Cdd:cd13987   66 -------------YVFAQEYAPYGDLFSIIPPQVG--LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKdcR 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 427 QVKIGDFGLVTSLkndGKRTRSK-GTLRYMSPEQISSQDYGK-----EVDLYALGLILAELLHVC---------DTAFET 491
Cdd:cd13987  131 RVKLCDFGLTRRV---GSTVKRVsGTIPYTAPEVCEAKKNEGfvvdpSIDVWAFGVLLFCCLTGNfpwekadsdDQFYEE 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 525343631 492 skfFTDLRDGIISDI------FDKKEKTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd13987  208 ---FVRWQKRKNTAVpsqwrrFTPKALRMFKKLLAPEPERRCSIKEVFKYL 255
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
271-545 5.99e-21

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: 92.80  E-value: 5.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKrVKYNNEK----AEREVKALAKLDHVNIVHYNG-CwdgvdYDPETsddylessd 345
Cdd:cd14063    6 EVIGKGRFGRVHRGRWHGDVAIKLLN-IDYLNEEqleaFKEEVAAYKNTRHDNLVLFMGaC-----MDPPH--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 ydpensknssrsktkcLFIQMEFCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLvDT 425
Cdd:cd14063   71 ----------------LAIVTSLCKGRTLYSLIHERK-EKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFL-EN 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQVKIGDFGLVtSLKNDGKRTRSKGTLR-------YMSPEQI----------SSQDYGKEVDLYALGLILAELLhVCDTA 488
Cdd:cd14063  133 GRVVITDFGLF-SLSGLLQPGRREDTLVipngwlcYLAPEIIralspdldfeESLPFTKASDVYAFGTVWYELL-AGRWP 210
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 489 FETSKFftdlrDGII-----------SDI-FDKKEKTLLQKLLSKKPEDRPNTSEILRTLtvwKKSPEK 545
Cdd:cd14063  211 FKEQPA-----ESIIwqvgcgkkqslSQLdIGREVKDILMQCWAYDPEKRPTFSDLLRML---ERLPKK 271
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
273-526 7.32e-21

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: 92.05  E-value: 7.32e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYV-IKRV-KYNNEKA----EREVKALAKLDHVNIVhyngcwdgvdydpetsddylesSDY 346
Cdd:cd14120    1 IGHGAFAVVFKGRHRKKPDLPVaIKCItKKNLSKSqnllGKEIKILKELSHENVV----------------------ALL 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 DPENSKNssrsktkCLFIQMEFCDKGTLEQWIENRRGEKLDKVlalELF-EQITKGVDYIHSKKLIHRDLKPSNIFLVDT 425
Cdd:cd14120   59 DCQETSS-------SVYLVMEYCNGGDLADYLQAKGTLSEDTI---RVFlQQIAAAMKALHSKGIVHRDLKPQNILLSHN 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 K---------QVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL-----HVCDTAFET 491
Cdd:cd14120  129 SgrkpspndiRLKIADFGFARFLQDGMMAATLCGSPMYMAPEVIMSLQYDAKADLWSIGTIVYQCLtgkapFQAQTPQEL 208
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 525343631 492 SKFF---TDLRDGIISDIfDKKEKTLLQKLLSKKPEDR 526
Cdd:cd14120  209 KAFYeknANLRPNIPSGT-SPALKDLLLGLLKRNPKDR 245
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
255-533 7.67e-21

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: 92.82  E-value: 7.67e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 255 TKYTVDKRfgmDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVkYNNEKAEREVKALAKLDHV-------NIVHYNGCw 327
Cdd:cd06618    8 KKYKADLN---DLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQM-RRSGNKEENKRILMDLDVVlkshdcpYIVKCYGY- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 328 dgvdydpetsddYLESSDydpensknssrsktkcLFIQMEF----CDKgtleqwIENRRGEKLDKVLALELFEQITKGVD 403
Cdd:cd06618   83 ------------FITDSD----------------VFICMELmstcLDK------LLKRIQGPIPEDILGKMTVSIVKALH 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 404 YIHSKK-LIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGK---EVDLYALGLILA 479
Cdd:cd06618  129 YLKEKHgVIHRDVKPSNILLDESGNVKLCDFGISGRLVDSKAKTRSAGCAAYMAPERIDPPDNPKydiRADVWSLGISLV 208
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 480 EL------LHVCDTAFET-SKFFTD------LRDGiisdiFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd06618  209 ELatgqfpYRNCKTEFEVlTKILNEeppslpPNEG-----FSPDFCSFVDLCLTKDHRYRPKYRELL 270
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
273-533 8.28e-21

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: 92.79  E-value: 8.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER----EVKALAKLDHVNIVHYNGC--WDGVdydpetsddylessdy 346
Cdd:cd06644   20 LGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEdymvEIEILATCNHPYIVKLLGAfyWDGK---------------- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 dpensknssrsktkcLFIQMEFCDKGTLEQ-WIENRRGEKLDKVLALelFEQITKGVDYIHSKKLIHRDLKPSNIFLVDT 425
Cdd:cd06644   84 ---------------LWIMIEFCPGGAVDAiMLELDRGLTEPQIQVI--CRQMLEALQYLHSMKIIHRDLKAGNVLLTLD 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQVKIGDFGL-VTSLKNDGKRTRSKGTLRYMSPEQISSQD-----YGKEVDLYALGLILAELLHV--------------- 484
Cdd:cd06644  147 GDIKLADFGVsAKNVKTLQRRDSFIGTPYWMAPEVVMCETmkdtpYDYKADIWSLGITLIEMAQIepphhelnpmrvllk 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 525343631 485 -----CDTAFETSKFFTDLRDgiisdifdkkektLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd06644  227 iaksePPTLSQPSKWSMEFRD-------------FLKTALDKHPETRPSAAQLL 267
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
271-490 9.42e-21

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: 92.50  E-value: 9.42e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKhrIDGKTYVIKRVKYNNEKA---EREVKALAKLDHVNIVHYngcwdgvdydpetsddylessdYD 347
Cdd:cd13998    1 EVIGKGRFGEVWKAS--LKNEPVAVKIFSSRDKQSwfrEKEIYRTPMLKHENILQF----------------------IA 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 PENSKNSSRSKtkcLFIQMEFCDKGTLEQWIenrRGEKLDKVLALELFEQITKGVDYIHS--------KKLI-HRDLKPS 418
Cdd:cd13998   57 ADERDTALRTE---LWLVTAFHPNGSL*DYL---SLHTIDWVSLCRLALSVARGLAHLHSeipgctqgKPAIaHRDLKSK 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSL-----KNDGKRTRSKGTLRYMSPE------QISSQDYGKEVDLYALGLILAELLHVCDT 487
Cdd:cd13998  131 NILVKNDGTCCIADFGLAVRLspstgEEDNANNGQVGTKRYMAPEvlegaiNLRDFESFKRVDIYAMGLVLWEMASRCTD 210

                 ...
gi 525343631 488 AFE 490
Cdd:cd13998  211 LFG 213
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
266-534 1.05e-20

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 91.94  E-value: 1.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEI-ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKA----------EREVKALAKLDHVNIVhyngcwdgvdydp 334
Cdd:cd14196    5 DFYDIgEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgvsreeiEREVSILRQVLHPNII------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 335 eTSDDYLESsdydpensknssrsKTKCLFIqMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRD 414
Cdd:cd14196   72 -TLHDVYEN--------------RTDVVLI-LELVSGGELFDFLAQK--ESLSEEEATSFIKQILDGVNYLHTKKIAHFD 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFLVDTK----QVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHvcdtafE 490
Cdd:cd14196  134 LKPENIMLLDKNipipHIKLIDFGLAHEIEDGVEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS------G 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 491 TSKFFTDLRDGIISDI------FDKK--------EKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14196  208 ASPFLGDTKQETLANItavsydFDEEffshtselAKDFIRKLLVKETRKRLTIQEALR 265
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
271-534 1.10e-20

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: 91.95  E-value: 1.10e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQ-VFKAKhrIDGKTYVIKRV-KYNNEKAEREVKALAKLD-HVNIVHYngcwdgvdYDPETSDDYLessdyd 347
Cdd:cd13982    7 KVLGYGSEGTiVFRGT--FDGRPVAVKRLlPEFFDFADREVQLLRESDeHPNVIRY--------FCTEKDRQFL------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 pensknssrsktkclFIQMEFCdKGTLEQWIENRRGEKLDKVLALE---LFEQITKGVDYIHSKKLIHRDLKPSNIfLVD 424
Cdd:cd13982   71 ---------------YIALELC-AASLQDLVESPRESKLFLRPGLEpvrLLRQIASGLAHLHSLNIVHRDLKPQNI-LIS 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TK------QVKIGDFGLVTSLkNDGKRTRSK-----GTLRYMSPEQISSQDYG---KEVDLYALGLILAELLHVCDTAFE 490
Cdd:cd13982  134 TPnahgnvRAMISDFGLCKKL-DVGRSSFSRrsgvaGTSGWIAPEMLSGSTKRrqtRAVDIFSLGCVFYYVLSGGSHPFG 212
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 525343631 491 TS----------KFFTDLRDGIISDIFDKKEktLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd13982  213 DKlereanilkgKYSLDKLLSLGEHGPEAQD--LIERMIDFDPEKRPSAEEVLN 264
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
267-526 1.68e-20

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: 91.89  E-value: 1.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV------KYNNEK-AEREVKALAKLDHVNIVHYNGCWDgvdydpetsdd 339
Cdd:cd05607    4 FYEFRVLGKGGFGEVCAVQVKNTGQMYACKKLdkkrlkKKSGEKmALLEKEILEKVNSPFIVSLAYAFE----------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknssrSKTKcLFIQMEFCDKGTLEQWIEN--RRGEKLDKVLALElfEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd05607   73 -----------------TKTH-LCLVMSLMNGGDLKYHIYNvgERGIEMERVIFYS--AQITCGILHLHSLKIVYRDMKP 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAFETSKFFTD 497
Cdd:cd05607  133 ENVLLDDNGNCRLSDLGLAVEVKEGKPITQRAGTNGYMAPEILKEESYSYPVDWFAMGCSIYEMV-AGRTPFRDHKEKVS 211
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 525343631 498 --------LRDGII--SDIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05607  212 keelkrrtLEDEVKfeHQNFTEEAKDICRLFLAKKPENR 250
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
269-534 1.80e-20

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: 91.18  E-value: 1.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 269 EIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVK----ALAKLDHVNIVHYngcwdgvdydpetsddyless 344
Cdd:cd14192    8 PHEVLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKneinIMNQLNHVNLIQL--------------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dYDPENSKNSsrsktkCLFIqMEFCDKGTLEQWI--ENRRGEKLDKVLaleLFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd14192   67 -YDAFESKTN------LTLI-MEYVDGGELFDRItdESYQLTELDAIL---FTRQICEGVHYLHQHYILHLDLKPENILC 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDT--KQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLH-----VCDTAFETSKFF 495
Cdd:cd14192  136 VNStgNQIKIIDFGLARRYKPREKLKVNFGTPEFLAPEVVNYDFVSFPTDMWSVGVITYMLLSglspfLGETDAETMNNI 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 525343631 496 TDLRDGIISDIFD---KKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14192  216 VNCKWDFDAEAFEnlsEEAKDFISRLLVKEKSCRMSATQCLK 257
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
273-534 2.75e-20

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: 91.01  E-value: 2.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVF------KAKHRIdGKTYVIKRVKYNNE-------KAEREVKALAKLDHVNIVHYngcwdgvdydpetsDD 339
Cdd:cd14076    9 LGEGEFGKVKlgwplpKANHRS-GVQVAIKLIRRDTQqencqtsKIMREINILKGLTHPNIVRL--------------LD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14076   74 VLKTKKY---------------IGIVLEFVSGGELFDYILARR--RLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLEN 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSL---KNDGKRTrSKGTLRYMSPEQISSQD--YGKEVDLYALGLILAELL------------ 482
Cdd:cd14076  137 LLLDKNRNLVITDFGFANTFdhfNGDLMST-SCGSPCYAAPELVVSDSmyAGRKADIWSCGVILYAMLagylpfdddphn 215
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 483 -----------HVCDTAFETSKFFTdlrdgiisdifdKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14076  216 pngdnvprlyrYICNTPLIFPEYVT------------PKARDLLRRILVPNPRKRIRLSAIMR 266
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
267-482 3.57e-20

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: 90.94  E-value: 3.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV------KYNNEKAEREVKALAKLDHVNIVhyngcwdgvdydpetsddy 340
Cdd:cd07846    3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFleseddKMVKKIAMREIKMLKQLRHENLV------------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpeNSKNSSRSKtKCLFIQMEFCDKGTLEQwIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd07846   64 ---------NLIEVFRRK-KRWYLVFEFVDHTVLDD-LEKYPN-GLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENI 131
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 421 FLVDTKQVKIGDFGLVTSLKNDGKR-TRSKGTLRYMSPEQ-ISSQDYGKEVDLYALGLILAELL 482
Cdd:cd07846  132 LVSQSGVVKLCDFGFARTLAAPGEVyTDYVATRWYRAPELlVGDTKYGKAVDVWAVGCLVTEML 195
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
267-481 3.63e-20

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: 90.96  E-value: 3.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNE------KAEREVKALAKLDHVNIVHYngcwdgvdYDPETSDdy 340
Cdd:cd07839    2 YEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDdegvpsSALREICLLKELKHKNIVRL--------YDVLHSD-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpensknssrsktKCLFIQMEFCDKgTLEQWIENRRGEkLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd07839   72 -------------------KKLTLVFEYCDQ-DLKKYFDSCNGD-IDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNL 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 421 FLVDTKQVKIGDFGLVtslKNDGKRTRSKG----TLRYMSPEQI-SSQDYGKEVDLYALGLILAEL 481
Cdd:cd07839  131 LINKNGELKLADFGLA---RAFGIPVRCYSaevvTLWYRPPDVLfGAKLYSTSIDMWSAGCIFAEL 193
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
273-482 4.05e-20

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: 90.20  E-value: 4.05e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKY------NNEKAEREVKALAKLDHVNIVhyngCWDGVdydpetsddYLESSDY 346
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSspncieERKALLKEAEKMERARHSYVL----PLLGV---------CVERRSL 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 DpensknssrsktkclfIQMEFCDKGTLEQWIEnRRGEKLDKVLALELFEQITKGVDYIH--SKKLIHRDLKPSNIFLVD 424
Cdd:cd13978   68 G----------------LVMEYMENGSLKSLLE-REIQDVPWSLRFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDN 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 425 TKQVKIGDFGLVT----SLKNDGKRTRSK--GTLRYMSPEQISSQDYGKEV--DLYALGLILAELL 482
Cdd:cd13978  131 HFHVKISDFGLSKlgmkSISANRRRGTENlgGTPIYMAPEAFDDFNKKPTSksDVYSFAIVIWAVL 196
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
267-481 4.33e-20

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: 90.83  E-value: 4.33e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE------REVKALAKLDHVNIVHYngcwdgvdydpetsddy 340
Cdd:cd07848    3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEvkettlRELKMLRTLKQENIVEL----------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpensKNSSRSKTKcLFIQMEFCDKGTLEQWIENRRGEKLDKVLALelFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd07848   66 -----------KEAFRRRGK-LYLVFEYVEKNMLELLEEMPNGVPPEKVRSY--IYQLIKAIHWCHKNDIVHRDIKPENL 131
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 421 FLVDTKQVKIGDFGLVTSLK--NDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd07848  132 LISHNDVLKLCDFGFARNLSegSNANYTEYVATRWYRSPELLLGAPYGKAVDMWSVGCILGEL 194
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
273-480 4.50e-20

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: 90.75  E-value: 4.50e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKY-----NNEKAEREVKALAKLDHVNIVhyngcwdgvdydpeTSDDYLESSDYD 347
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSCRLelsvkNKDRWCHEIQIMKKLNHPNVV--------------KACDVPEEMNFL 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 PENSKnssrsktkclFIQMEFCDKGTLEQWI---ENRRGEKLDKVLALelFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd14039   67 VNDVP----------LLAMEYCSGGDLRKLLnkpENCCGLKESQVLSL--LSDIGSGIQYLHENKIIHRDLKPENIVLQE 134
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 425 T--KQV-KIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAE 480
Cdd:cd14039  135 IngKIVhKIIDLGYAKDLDQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFE 193
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
270-483 4.95e-20

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: 91.18  E-value: 4.95e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN---NEKAEREVKA-----LAKLDHVNIVhyngcwdGVDYDPETSDDyl 341
Cdd:cd05604    1 LKVIGKGSFGKVLLAKRKRDGKYYAVKVLQKKvilNRKEQKHIMAernvlLKNVKHPFLV-------GLHYSFQTTDK-- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdydpensknssrsktkcLFIQMEFCDKGTLeqWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd05604   72 --------------------LYFVLDFVNGGEL--FFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENIL 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 422 LVDTKQVKIGDFGLVTS-LKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLH 483
Cdd:cd05604  130 LDSQGHIVLTDFGLCKEgISNSDTTTTFCGTPEYLAPEVIRKQPYDNTVDWWCLGSVLYEMLY 192
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
265-526 5.54e-20

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: 90.33  E-value: 5.54e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 265 MDFKeieLIGSGGFGQVFKAKHRIDGKTYVIKRV-------KYNNEKAEREVKALAKLDHVNIVhyngcwdGVDYDPETS 337
Cdd:cd05608    4 LDFR---VLGKGGFGEVSACQMRATGKLYACKKLnkkrlkkRKGYEGAMVEKRILAKVHSRFIV-------SLAYAFQTK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 DDYlessdydpensknssrsktkCLFiqMEFCDKGTLEQWIENRRGEK--LDKVLALELFEQITKGVDYIHSKKLIHRDL 415
Cdd:cd05608   74 TDL--------------------CLV--MTIMNGGDLRYHIYNVDEENpgFQEPRACFYTAQIISGLEHLHQRRIIYRDL 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 416 KPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHV-----CDTAF 489
Cdd:cd05608  132 KPENVLLDDDGNVRISDLGLAVELKDGQTKTKGyAGTPGFMAPELLLGEEYDYSVDYFTLGVTLYEMIAArgpfrARGEK 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 525343631 490 ETSKFFTD--LRDGII-SDIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05608  212 VENKELKQriLNDSVTySEKFSPASKSICEALLAKDPEKR 251
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
266-533 6.29e-20

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: 89.37  E-value: 6.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIK-----RVKYNNEKAER-------EVKALAKLD---HVNIVHYngcwdgv 330
Cdd:cd14004    1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKfifkeRILVDTWVRDRklgtvplEIHILDTLNkrsHPNIVKL------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 331 dydpetsDDYLESSDYdpensknssrsktkcLFIQMEfCDKGTLEQW--IENRRGekLDKVLALELFEQITKGVDYIHSK 408
Cdd:cd14004   74 -------LDFFEDDEF---------------YYLVME-KHGSGMDLFdfIERKPN--MDEKEAKYIFRQVADAVKHLHDQ 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 409 KLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNdGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELLHvcdt 487
Cdd:cd14004  129 GIVHRDIKDENVILDGNGTIKLIDFGSAAYIKS-GPFDTFVGTIDYAAPEVLRGNPYgGKEQDIWALGVLLYTLVF---- 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 525343631 488 aFETSkfFTDLRDGIISDI-FDKKEK----TLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14004  204 -KENP--FYNIEEILEADLrIPYAVSedliDLISRMLNRDVGDRPTIEELL 251
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
303-532 6.32e-20

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: 90.01  E-value: 6.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 303 EKAEREVKALAKLDHVNIVHYngcwdgvdydPETSDDYLESSdydpensknssrsktkcLFIQMEFCDKGTLeqwIENRR 382
Cdd:cd14200   68 ERVYQEIAILKKLDHVNIVKL----------IEVLDDPAEDN-----------------LYMVFDLLRKGPV---MEVPS 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 383 GEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLK-NDGKRTRSKGTLRYMSPEQIS 461
Cdd:cd14200  118 DKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEgNDALLSSTAGTPAFMAPETLS 197
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 462 S--QDY-GKEVDLYALGLILAELLH-VCDTAFEtskFFTDLRDGIISDIFDKKE--------KTLLQKLLSKKPEDRPNT 529
Cdd:cd14200  198 DsgQSFsGKALDVWAMGVTLYCFVYgKCPFIDE---FILALHNKIKNKPVEFPEepeiseelKDLILKMLDKNPETRITV 274

                 ...
gi 525343631 530 SEI 532
Cdd:cd14200  275 PEI 277
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
271-482 7.78e-20

Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of uncharacterized proteins with similarity to MEKK3, MEKK2, and related proteins; they contain an N-terminal PB1 domain, which mediates oligomerization, and a C-terminal catalytic domain. MEKK2 and MEKK3 are MAPK kinase kinases (MAPKKKs or MKKKs), proteins that phosphorylate and activate MAPK kinases (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MEKK2 and MEKK3 activate MEK5 (also called MKK5), which activates ERK5. The ERK5 cascade plays roles in promoting cell proliferation, differentiation, neuronal survival, and neuroprotection. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. MEKK2 and MEKK3 can also activate the MAPKs, c-Jun N-terminal kinase (JNK) and p38, through their respective MAPKKs. The MEKK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 89.31  E-value: 7.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER---------EVKALAKLDHVNIVHYNGCWDgvdydpetsddyl 341
Cdd:cd06653    8 KLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSQETskevnalecEIQLLKNLRHDRIVQYYGCLR------------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdyDPENSKnssrsktkcLFIQMEFCDKGTLEQWIENRRGekLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd06653   75 -----DPEEKK---------LSIFVEYMPGGSVKDQLKAYGA--LTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANIL 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 422 LVDTKQVKIGDFGL---VTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd06653  139 RDSAGNVKLGDFGAskrIQTICMSGTGIKSvTGTPYWMSPEVISGEGYGRKADVWSVACTVVEML 203
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
266-526 8.30e-20

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: 89.31  E-value: 8.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEI-ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKA----------EREVKALAKLDHVNIVhyngcwdgvdydp 334
Cdd:cd14194    5 DYYDTgEELGSGQFAVVKKCREKSTGLQYAAKFIKKRRTKSsrrgvsrediEREVSILKEIQHPNVI------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 335 eTSDDYLESsdydpensknssrsKTKCLFIqMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRD 414
Cdd:cd14194   72 -TLHEVYEN--------------KTDVILI-LELVAGGELFDFLAEK--ESLTEEEATEFLKQILNGVYYLHSLQIAHFD 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFLVDTK----QVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFE 490
Cdd:cd14194  134 LKPENIMLLDRNvpkpRIKIIDFGLAHKIDFGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLSGASPFLG 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 491 TSKFFTDLRDGIISDIFDKK--------EKTLLQKLLSKKPEDR 526
Cdd:cd14194  214 DTKQETLANVSAVNYEFEDEyfsntsalAKDFIRRLLVKDPKKR 257
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
262-534 8.49e-20

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: 90.50  E-value: 8.49e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 262 RFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKY------NNEKAEREVKALAKLDHVNIVhyngCWDGVDYDPE 335
Cdd:cd07855    2 DVGDRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNafdvvtTAKRTLRELKILRHFKHDNII----AIRDILRPKV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 336 TSDDYlessdydpensknssrsktKCLFIQMEFCDkGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDL 415
Cdd:cd07855   78 PYADF-------------------KDVYVVLDLME-SDLHHII--HSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDL 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 416 KPSNIFLVDTKQVKIGDFGLVTSLKNDGKR-----TRSKGTLRYMSPE-QISSQDYGKEVDLYALGLILAELL------- 482
Cdd:cd07855  136 KPSNLLVNENCELKIGDFGMARGLCTSPEEhkyfmTEYVATRWYRAPElMLSLPEYTQAIDMWSVGCIFAEMLgrrqlfp 215
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 483 --------------------HVCDT--AFETSKFFTDL--RDGI-ISDIFDKKEK---TLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd07855  216 gknyvhqlqliltvlgtpsqAVINAigADRVRRYIQNLpnKQPVpWETLYPKADQqalDLLSQMLRFDPSERITVAEALQ 295
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
267-482 9.15e-20

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: 89.49  E-value: 9.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK------AEREVKALAKLDHVNIVHYngcwdgvdydpetsddy 340
Cdd:cd07860    2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETegvpstAIREISLLKELNHPNIVKL----------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdYDPENSKNSsrsktkcLFIQMEFCDKgTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd07860   65 -----LDVIHTENK-------LYLVFEFLHQ-DLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNL 131
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 421 FLVDTKQVKIGDFGLVTSLkndGKRTRSKG----TLRYMSPE-QISSQDYGKEVDLYALGLILAELL 482
Cdd:cd07860  132 LINTEGAIKLADFGLARAF---GVPVRTYThevvTLWYRAPEiLLGCKYYSTAVDIWSLGCIFAEMV 195
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
266-533 1.10e-19

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: 88.86  E-value: 1.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV-KYNNEKA------EREVKALAKLDHVNIVHYNGCWdgvdydpetsd 338
Cdd:cd14116    6 DFEIGRPLGKGKFGNVYLAREKQSKFILALKVLfKAQLEKAgvehqlRREVEIQSHLRHPNILRLYGYF----------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dylessdydpensKNSSRsktkcLFIQMEFCDKGTLeqWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd14116   75 -------------HDATR-----VYLILEYAPLGTV--YRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPE 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSLKNDgKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAFETSKFFTDL 498
Cdd:cd14116  135 NLLLGSAGELKIADFGWSVHAPSS-RRTTLCGTLDYLPPEMIEGRMHDEKVDLWSLGVLCYEFL-VGKPPFEANTYQETY 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 525343631 499 RDgiIS-------DIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14116  213 KR--ISrveftfpDFVTEGARDLISRLLKHNPSQRPMLREVL 252
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
273-489 1.18e-19

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 89.25  E-value: 1.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKY-----NNEKAEREVKALAKLDHVNIVhyngcwdgvdydpetsddyleSSDYD 347
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQCRQelspkNRERWCLEIQIMKRLNHPNVV---------------------AARDV 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 PENSKNSSRSKTKCLfiQMEFCDKGTLEQWI---ENRRGEKLDKVLALelFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd14038   61 PEGLQKLAPNDLPLL--AMEYCQGGDLRKYLnqfENCCGLREGAILTL--LSDISSALRYLHENRIIHRDLKPENIVLQQ 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 425 TKQV---KIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAEllhvCDTAF 489
Cdd:cd14038  137 GEQRlihKIIDLGYAKELDQGSLCTSFVGTLQYLAPELLEQQKYTVTVDYWSFGTLAFE----CITGF 200
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
265-537 1.43e-19

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: 88.27  E-value: 1.43e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 265 MDFKEIELIGSGGFGQVFKAKHR--IDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVH-YNGCwdgvdydpetsddyl 341
Cdd:cd05059    4 SELTFLKELGSGQFGVVHLGKWRgkIDVAIKMIKEGSMSEDDFIEEAKVMMKLSHPKLVQlYGVC--------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdydpensknssrSKTKCLFIQMEFCDKGTLEQWIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd05059   69 ---------------TKQRPIFIVTEYMANGCLLNYLRERRG-KFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCL 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFGLVTSLKNDgKRTRSKGT---LRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFET---SKFF 495
Cdd:cd05059  133 VGEQNVVKVSDFGLARYVLDD-EYTSSVGTkfpVKWSPPEVFMYSKFSSKSDVWSFGVLMWEVFSEGKMPYERfsnSEVV 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 525343631 496 TDLRDGIISD---IFDKKEKTLLQKLLSKKPEDRPNTSEILRTLT 537
Cdd:cd05059  212 EHISQGYRLYrphLAPTEVYTIMYSCWHEKPEERPTFKILLSQLT 256
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
273-532 1.61e-19

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: 88.36  E-value: 1.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRidGKTYVIKRVKYNN--EKAE-----REVKALAKLDHVNIVHYNG-CWDgvdydpetsddyless 344
Cdd:cd14064    1 IGSGSFGKVYKGRCR--NKIVAIKRYRANTycSKSDvdmfcREVSILCRLNHPCVIQFVGaCLD---------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dyDPENsknssrsktkcLFIQMEFCDKGTLEQwIENRRGEKLDKVLALELFEQITKGVDYIH--SKKLIHRDLKPSNIFL 422
Cdd:cd14064   63 --DPSQ-----------FAIVTQYVSGGSLFS-LLHEQKRVIDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFG---LVTSLKNDgKRTRSKGTLRYMSPEQIS-SQDYGKEVDLYALGLILAELL-------HVCDTAFET 491
Cdd:cd14064  129 YEDGHAVVADFGesrFLQSLDED-NMTKQPGNLRWMAPEVFTqCTRYSIKADVFSYALCLWELLtgeipfaHLKPAAAAA 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 525343631 492 SKFFTDLRDGiISDIFDKKEKTLLQKLLSKKPEDRPNTSEI 532
Cdd:cd14064  208 DMAYHHIRPP-IGYSIPKPISSLLMRGWNAEPESRPSFVEI 247
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
267-482 1.62e-19

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: 88.35  E-value: 1.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN------EKAEREVKALAKLDHVNIVHYngcwdgvdydpetsddy 340
Cdd:cd14072    2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQlnpsslQKLFREVRIMKILNHPNIVKL----------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSDYDpensknssrsktKCLFIQMEFCDKGTLEQWI--ENRRGEKLDKVLalelFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd14072   65 FEVIETE------------KTLYLVMEYASGGEVFDYLvaHGRMKEKEARAK----FRQIVSAVQYCHQKRIVHRDLKAE 128
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELL 482
Cdd:cd14072  129 NLLLDADMNIKIADFGFSNEFTPGNKLDTFCGSPPYAAPELFQGKKYdGPEVDVWSLGVILYTLV 193
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
257-534 1.84e-19

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 88.43  E-value: 1.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 257 YTVDKRfgmdfkeiELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVK----ALAKLDHVNIVHYngcwdgvdy 332
Cdd:cd14193    4 YNVNKE--------EILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKneieVMNQLNHANLIQL--------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 333 dpetsddylessdYDPENSKNSsrsktkcLFIQMEFCDKGTLEQWI--ENRRGEKLDKVLaleLFEQITKGVDYIHSKKL 410
Cdd:cd14193   67 -------------YDAFESRND-------IVLVMEYVDGGELFDRIidENYNLTELDTIL---FIKQICEGIQYMHQMYI 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 411 IHRDLKPSNIFLV--DTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLH----- 483
Cdd:cd14193  124 LHLDLKPENILCVsrEANQVKIIDFGLARRYKPREKLRVNFGTPEFLAPEVVNYEFVSFPTDMWSLGVIAYMLLSglspf 203
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 484 -------------VCDTAFETSKFftdlrdgiiSDIFDKKeKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14193  204 lgeddnetlnnilACQWDFEDEEF---------ADISEEA-KDFISKLLIKEKSWRMSASEALK 257
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
273-542 1.97e-19

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: 88.58  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE---REVKALAKLDHVNIVHYNGcwdgvdydpetsddylessdydpe 349
Cdd:cd14151   16 IGSGSFGTVYKGKWHGDVAVKMLNVTAPTPQQLQafkNEVGVLRKTRHVNILLFMG------------------------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 350 nsknssRSKTKCLFIQMEFCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVK 429
Cdd:cd14151   72 ------YSTKPQLAIVTQWCEGSSLYHHLHIIE-TKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 430 IGDFGLVT---SLKNDGKRTRSKGTLRYMSPEQISSQD---YGKEVDLYALGLILAELLhvcDTAFETSKFftDLRDGII 503
Cdd:cd14151  145 IGDFGLATvksRWSGSHQFEQLSGSILWMAPEVIRMQDknpYSFQSDVYAFGIVLYELM---TGQLPYSNI--NNRDQII 219
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 525343631 504 SDI---------------FDKKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKS 542
Cdd:cd14151  220 FMVgrgylspdlskvrsnCPKAMKRLMAECLKKKRDERPLFPQILASIELLARS 273
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
273-535 2.03e-19

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: 88.12  E-value: 2.03e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRV-------KYNNEKAEREVKALAKLDHVNIVHYngcwdgvdydpetsddyLESSD 345
Cdd:cd14162    8 LGHGSYAVVKKAYSTKHKCKVAIKIVskkkapeDYLQKFLPREIEVIKGLKHPNLICF-----------------YEAIE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 ydpenskNSSRsktkcLFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDT 425
Cdd:cd14162   71 -------TTSR-----VYIIMELAENGDLLDYI--RKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKN 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQVKIGDFGLV-TSLKN-DGKRTRSK---GTLRYMSPEQISSQDY-GKEVDLYALGLILAELLHvCDTAFETSKFFTDLR 499
Cdd:cd14162  137 NNLKITDFGFArGVMKTkDGKPKLSEtycGSYAYASPEILRGIPYdPFLSDIWSMGVVLYTMVY-GRLPFDDSNLKVLLK 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 525343631 500 DGIISDIFDKKE------KTLLQKLLSKKPEdRPNTSEILRT 535
Cdd:cd14162  216 QVQRRVVFPKNPtvseecKDLILRMLSPVKK-RITIEEIKRD 256
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
273-526 2.29e-19

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: 89.30  E-value: 2.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKR------VKYNNEK---AEREVkaLAKldhvNIVHyngcwdgvdydPetsddYLES 343
Cdd:cd05575    3 IGKGSFGKVLLARHKAEGKLYAVKVlqkkaiLKRNEVKhimAERNV--LLK----NVKH-----------P-----FLVG 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 SDYdpensknSSRSKTKCLFIqMEFCDKGTLEQWIENRR--GEKLDKVLALElfeqITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd05575   61 LHY-------SFQTKDKLYFV-LDYVNGGELFFHLQRERhfPEPRARFYAAE----IASALGYLHSLNIIYRDLKPENIL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFetSKFFTDLRD 500
Cdd:cd05575  129 LDSQGHVVLTDFGLCKEGIEPSDTTSTfCGTPEYLAPEVLRKQPYDRTVDWWCLGAVLYEMLYGLPPFY--SRDTAEMYD 206
                        250       260       270
                 ....*....|....*....|....*....|..
gi 525343631 501 GIISDIFDKKE------KTLLQKLLSKKPEDR 526
Cdd:cd05575  207 NILHKPLRLRTnvspsaRDLLEGLLQKDRTKR 238
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
273-482 2.37e-19

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: 87.53  E-value: 2.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE--REVKALAKLDHVNIVHYNGCwdgvdydpetsddylessdydpen 350
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRANmlREVQLMNRLSHPNILRFMGV------------------------ 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 351 sknssrsktkC-----LFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL--- 422
Cdd:cd14155   57 ----------CvhqgqLHALTEYINGGNLEQLLDSN--EPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrd 124
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 423 VDTKQVKIGDFGL---VTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14155  125 ENGYTAVVGDFGLaekIPDYSDGKEKLAVVGSPYWMAPEVLRGEPYNEKADVFSYGIILCEII 187
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
266-481 2.51e-19

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: 88.25  E-value: 2.51e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK------AEREVKALAKLDHVNIVhyngCWDGVDYDPetsdd 339
Cdd:cd07861    1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEegvpstAIREISLLKELQHPNIV----CLEDVLMQE----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknsSRsktkcLFIQMEF--CDkgtLEQWIEN-RRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd07861   72 ---------------NR-----LYLVFEFlsMD---LKKYLDSlPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLK 128
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 417 PSNIfLVDTKQV-KIGDFGLVTSLKNDGK-RTRSKGTLRYMSPE-QISSQDYGKEVDLYALGLILAEL 481
Cdd:cd07861  129 PQNL-LIDNKGViKLADFGLARAFGIPVRvYTHEVVTLWYRAPEvLLGSPRYSTPVDIWSIGTIFAEM 195
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
271-535 2.71e-19

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: 87.73  E-value: 2.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKrVKYNNEKAEREVKALAKL-DHVNIVHyngcwdgvdydpeTSDDYlessdydpE 349
Cdd:cd14089    7 QVLGLGINGKVLECFHKKTGEKFALK-VLRDNPKARREVELHWRAsGCPHIVR-------------IIDVY--------E 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 350 NSKNssrsKTKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK--- 426
Cdd:cd14089   65 NTYQ----GRKCLLVVMECMEGGELFSRIQERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGpna 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 427 QVKIGDFGLvtslkndGKRTRSKGTLR-------YMSPEQISSQDYGKEVDLYALGLILAELLhvC-------DTAFETS 492
Cdd:cd14089  141 ILKLTDFGF-------AKETTTKKSLQtpcytpyYVAPEVLGPEKYDKSCDMWSLGVIMYILL--CgyppfysNHGLAIS 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 525343631 493 KfftDLRDGIISDIFD----------KKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:cd14089  212 P---GMKKRIRNGQYEfpnpewsnvsEEAKDLIRGLLKTDPSERLTIEEVMNH 261
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
272-482 2.81e-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: 87.77  E-value: 2.81e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRIDGKTYVIK-----RVKYNNEKAEREVKALAKLDHVNIVHYngcwdgvdydpetsddyLESSDY 346
Cdd:cd14095    7 VIGDGNFAVVKECRDKATDKEYALKiidkaKCKGKEHMIENEVAILRRVKHPNIVQL-----------------IEEYDT 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 DPEnsknssrsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD-- 424
Cdd:cd14095   70 DTE------------LYLVMELVKGGDLFDAITSST--KFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEhe 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 --TKQVKIGDFGLVTSLKNdgKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14095  136 dgSKSLKLADFGLATEVKE--PLFTVCGTPTYVAPEILAETGYGLKVDIWAAGVITYILL 193
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
264-482 2.89e-19

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: 89.29  E-value: 2.89e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 264 GMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNE-----KAEREVKALAKLDHVNIVHYngcwdgvdYDPETSD 338
Cdd:cd07849    4 GPRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISPFEHqtyclRTLREIKILLRFKHENIIGI--------LDIQRPP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 DYLESSD-YdpensknssrsktkclFIQ--MEfcdkgtleqwienrrgEKLDKVLALELFE---------QITKGVDYIH 406
Cdd:cd07849   76 TFESFKDvY----------------IVQelME----------------TDLYKLIKTQHLSndhiqyflyQILRGLKYIH 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 407 SKKLIHRDLKPSNIFLVDTKQVKIGDFGL--VTSLKND--GKRTRSKGTLRYMSPE-QISSQDYGKEVDLYALGLILAEL 481
Cdd:cd07849  124 SANVLHRDLKPSNLLLNTNCDLKICDFGLarIADPEHDhtGFLTEYVATRWYRAPEiMLNSKGYTKAIDIWSVGCILAEM 203

                 .
gi 525343631 482 L 482
Cdd:cd07849  204 L 204
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
273-532 2.96e-19

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 88.16  E-value: 2.96e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVK---YNNEKAE----REVKALAKLDHVNIVHYNgcwdgvdydpetsddylesSD 345
Cdd:cd08229   32 IGRGQFSEVYRATCLLDGVPVALKKVQifdLMDAKARadciKEIDLLKQLNHPNVIKYY-------------------AS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YDPENSKNssrsktkclfIQMEFCDKGTLEQWIENRRGEK--LDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd08229   93 FIEDNELN----------IVLELADAGDLSRMIKHFKKQKrlIPEKTVWKYFVQLCSALEHMHSRRVMHRDIKPANVFIT 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 424 DTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELlhvcdtAFETSKFFTDLRD-- 500
Cdd:cd08229  163 ATGVVKLGDLGLGRFFSSKTTAAHSlVGTPYYMSPERIHENGYNFKSDIWSLGCLLYEM------AALQSPFYGDKMNly 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 501 ------------GIISDIFDKKEKTLLQKLLSKKPEDRPNTSEI 532
Cdd:cd08229  237 slckkieqcdypPLPSDHYSEELRQLVNMCINPDPEKRPDITYV 280
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
267-543 3.14e-19

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: 88.54  E-value: 3.14e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN----NEKAE---REVKALAKLDHVNIVHYNGCwdgvdydpetsdd 339
Cdd:cd06634   17 FSDLREIGHGSFGAVYFARDVRNNEVVAIKKMSYSgkqsNEKWQdiiKEVKFLQKLRHPNTIEYRGC------------- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLessdydpensknssrsKTKCLFIQMEFCdKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd06634   84 YL----------------REHTAWLVMEYC-LGSASDLLEVHK-KPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGN 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLkndGKRTRSKGTLRYMSPEQISSQDYGK---EVDLYALGLILAELLHVCDTAFETSKFFT 496
Cdd:cd06634  146 ILLTEPGLVKLGDFGSASIM---APANSFVGTPYWMAPEVILAMDEGQydgKVDVWSLGITCIELAERKPPLFNMNAMSA 222
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 497 ----------DLRDGIISDIFDKKEKTLLQKLlskkPEDRPNTSEILRTLTVWKKSP 543
Cdd:cd06634  223 lyhiaqnespALQSGHWSEYFRNFVDSCLQKI----PQDRPTSDVLLKHRFLLRERP 275
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
273-534 3.37e-19

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: 87.50  E-value: 3.37e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKrvKYNNEKAER------EVKALAKLDHVNIVhyngcwdgvdydpETSDDYLESSDy 346
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVK--KMDLRKQQRrellfnEVVIMRDYQHPNIV-------------EMYSSYLVGDE- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 dpensknssrsktkcLFIQMEFCDKGTLEQWIENRRgekLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK 426
Cdd:cd06648   79 ---------------LWVVMEFLEGGALTDIVTHTR---MNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDG 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 427 QVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKF--FTDLRDGII 503
Cdd:cd06648  141 RVKLSDFGFCAQVSKEVPRRKSlVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLqaMKRIRDNEP 220
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 525343631 504 SDIFDKKE-----KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06648  221 PKLKNLHKvsprlRSFLDRMLVRDPAQRATAAELLN 256
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
273-548 3.53e-19

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


Pssm-ID: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 87.78  E-value: 3.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE---REVKALAKLDHVNIVHYNGcwdgvdydpetsddYLESSDydpe 349
Cdd:cd14149   20 IGSGSFGTVYKGKWHGDVAVKILKVVDPTPEQFQafrNEVAVLRKTRHVNILLFMG--------------YMTKDN---- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 350 nsknssrsktkcLFIQMEFCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVK 429
Cdd:cd14149   82 ------------LAIVTQWCEGSSLYKHLHVQE-TKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVK 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 430 IGDFGLVT---SLKNDGKRTRSKGTLRYMSPEQISSQD---YGKEVDLYALGLILAELL-------HVCDtafETSKFFT 496
Cdd:cd14149  149 IGDFGLATvksRWSGSQQVEQPTGSILWMAPEVIRMQDnnpFSFQSDVYSYGIVLYELMtgelpysHINN---RDQIIFM 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 497 DLRDGIISDIFD------KKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNER 548
Cdd:cd14149  226 VGRGYASPDLSKlykncpKAMKRLVADCIKKVKEERPLFPQILSSIELLQHSLPKINR 283
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
267-481 4.63e-19

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: 87.54  E-value: 4.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK-----AEREVKALAKLDHVNIVhyngcwdgvdydpetsddyl 341
Cdd:cd07836    2 FKQLEKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEgtpstAIREISLMKELKHENIV-------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 esSDYDPENSKNSsrsktkcLFIQMEFCDKgTLEQWIE---NRRGekLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd07836   62 --RLHDVIHTENK-------LMLVFEYMDK-DLKKYMDthgVRGA--LDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQ 129
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 419 NIFLVDTKQVKIGDFGL-------VTSLKNDgkrtrsKGTLRYMSPE-QISSQDYGKEVDLYALGLILAEL 481
Cdd:cd07836  130 NLLINKRGELKLADFGLarafgipVNTFSNE------VVTLWYRAPDvLLGSRTYSTSIDIWSVGCIMAEM 194
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
271-536 4.73e-19

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: 87.86  E-value: 4.73e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHR-IDGK-----TYVIKRVKYN-NEK------AEREV-KALAKldHVNIVHYNGCwdgvdydpet 336
Cdd:cd05053   18 KPLGEGAFGQVVKAEAVgLDNKpnevvTVAVKMLKDDaTEKdlsdlvSEMEMmKMIGK--HKNIINLLGA---------- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddyleSSDYDPensknssrsktkcLFIQMEFCDKGTLEQWIENRR--GEKLDKVLALELFEQIT------------KGV 402
Cdd:cd05053   86 ------CTQDGP-------------LYVVVEYASKGNLREFLRARRppGEEASPDDPRVPEEQLTqkdlvsfayqvaRGM 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 403 DYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKN-DGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILA 479
Cdd:cd05053  147 EYLASKKCIHRDLAARNVLVTEDNVMKIADFGLARDIHHiDYYRKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLLW 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 480 ELLHVCDTAF---ETSKFFTDLRDG--------IISDIFdkkekTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd05053  227 EIFTLGGSPYpgiPVEELFKLLKEGhrmekpqnCTQELY-----MLMRDCWHEVPSQRPTFKQLVEDL 289
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
267-534 5.97e-19

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: 86.68  E-value: 5.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIE-LIGSGGFGQVFKAKHRIDGKTYVIKRV------KYNNEKAEREVKALAKLDHVNIVHYngcwdgvdydpetsdd 339
Cdd:cd14071    1 FYDIErTIGKGNFAVVKLARHRITKTEVAIKIIdksqldEENLKKIYREVQIMKMLNHPHIIKL---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdYDPENSKNSsrsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14071   65 ------YQVMETKDM-------LYLVTEYASNGEIFDYLAQHG--RMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAEN 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELlhVCDT-AFETSKFFTd 497
Cdd:cd14071  130 LLLDANMNIKIADFGFSNFFKPGELLKTWCGSPPYAAPEVFEGKEYeGPQLDIWSLGVVLYVL--VCGAlPFDGSTLQT- 206
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 525343631 498 LRDGIISDIF------DKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14071  207 LRDRVLSGRFripffmSTDCEHLIRRMLVLDPSKRLTIEQIKK 249
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
267-482 5.99e-19

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: 87.73  E-value: 5.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKA--KHRIDGKTYVIKRVKYNNEK-------AEREVKALAKLDHVNIVhyngcwdgvdydpETS 337
Cdd:cd07842    2 YEIEGCIGRGTYGRVYKAkrKNGKDGKEYAIKKFKGDKEQytgisqsACREIALLRELKHENVV-------------SLV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 DDYLESSDydpensknssrsktKCLFIQMEFC--DKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDL 415
Cdd:cd07842   69 EVFLEHAD--------------KSVYLLFDYAehDLWQIIKFHRQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 416 KPSNIFLV----DTKQVKIGDFG--------LVTSLKNDGKRTrskgTLRYMSPEQI-SSQDYGKEVDLYALGLILAELL 482
Cdd:cd07842  135 KPANILVMgegpERGVVKIGDLGlarlfnapLKPLADLDPVVV----TIWYRAPELLlGARHYTKAIDIWAIGCIFAELL 210
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
267-545 6.82e-19

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


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 87.08  E-value: 6.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIEL-----IGSGGFGQVFKAKHRIDGKT----YVIKRVK-----YNNEKAEREVKALAKLDHVNIVHYNGCwdgvdy 332
Cdd:cd05057    4 VKETELekgkvLGSGAFGTVYKGVWIPEGEKvkipVAIKVLReetgpKANEEILDEAYVMASVDHPHLVRLLGI------ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 333 dpetsddylessdydpensknsSRSKTKCLFIQ-MEFcdkGTLEQWIENRRGEkLDKVLALELFEQITKGVDYIHSKKLI 411
Cdd:cd05057   78 ----------------------CLSSQVQLITQlMPL---GCLLDYVRNHRDN-IGSQLLLNWCVQIAKGMSYLEEKRLV 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 412 HRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKG---TLRYMSPEQISSQDYGKEVDLYALGLILAELLhvcdtA 488
Cdd:cd05057  132 HRDLAARNVLVKTPNHVKITDFGLAKLLDVDEKEYHAEGgkvPIKWMALESIQYRIYTHKSDVWSYGVTVWELM-----T 206
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 489 FeTSKFFTDLRDGIISDIFDKKEK------------TLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEK 545
Cdd:cd05057  207 F-GAKPYEGIPAVEIPDLLEKGERlpqppictidvyMVLVKCWMIDAESRPTFKELANEFSKMARDPQR 274
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
270-532 7.12e-19

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: 87.61  E-value: 7.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIKRVK----YNNEKAEREVKALAKLD--HVNIVHYNGCW---DGV----DYDPET 336
Cdd:cd13977    5 IREVGRGSYGVVYEAVVRRTGARVAVKKIRcnapENVELALREFWALSSIQrqHPNVIQLEECVlqrDGLaqrmSHGSSK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 SDDYLESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIENRRGeklDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd13977   85 SDLYLLLVETSLKGERCFDPRSACYLWFVMEFCDGGDMNEYLLSRRP---DRQTNTSFMLQLSSALAFLHRNQIVHRDLK 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLV---DTKQVKIGDFGLVTSLKNDGKRTRSK------------GTLRYMSPEqISSQDYGKEVDLYALGLIL--- 478
Cdd:cd13977  162 PDNILIShkrGEPILKVADFGLSKVCSGSGLNPEEPanvnkhflssacGSDFYMAPE-VWEGHYTAKADIFALGIIIwam 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 479 AELLHVCDTAFETSKFFTDLRDG--IIS-------------DIFDKKEKT-------LLQKLLSKKPEDRPNTSEI 532
Cdd:cd13977  241 VERITFRDGETKKELLGTYIQQGkeIVPlgeallenpklelQIPLKKKKSmnddmkqLLRDMLAANPQERPDAFQL 316
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
267-534 7.71e-19

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: 86.65  E-value: 7.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN-----EKAEREVKALAKLDHVNIVHYNGcwdgvdydpetsdDYL 341
Cdd:cd06642    6 FTKLERIGKGSFGEVYKGIDNRTKEVVAIKIIDLEEaedeiEDIQQEITVLSQCDSPYITRYYG-------------SYL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ESSDydpensknssrsktkcLFIQMEFCDKGTLeqwIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd06642   73 KGTK----------------LWIIMEYLGGGSA---LDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFGLVTSLKNDG-KRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAEL---------LHVCDTAFET 491
Cdd:cd06642  134 LSEQGDVKLADFGVAGQLTDTQiKRNTFVGTPFWMAPEVIKQSAYDFKADIWSLGITAIELakgeppnsdLHPMRVLFLI 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 525343631 492 SKFFTDLRDGIISDIFdkkeKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06642  214 PKNSPPTLEGQHSKPF----KEFVEACLNKDPRFRPTAKELLK 252
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
251-482 7.97e-19

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: 87.73  E-value: 7.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 251 DMKETKYTVDKRFgmdfKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE------REVKALAKLDHVNIVhyn 324
Cdd:cd07851    5 ELNKTVWEVPDRY----QNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIhakrtyRELRLLKHMKHENVI--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 325 gCWDGVDYDPETSDDYLEssdydpensknssrsktkcLFIQMEFCDKgTLEQWIenrRGEKL--DKVLALelFEQITKGV 402
Cdd:cd07851   78 -GLLDVFTPASSLEDFQD-------------------VYLVTHLMGA-DLNNIV---KCQKLsdDHIQFL--VYQILRGL 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 403 DYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLvtSLKNDGKRTRSKGTLRYMSPEQI-SSQDYGKEVDLYALGLILAEL 481
Cdd:cd07851  132 KYIHSAGIIHRDLKPSNLAVNEDCELKILDFGL--ARHTDDEMTGYVATRWYRAPEIMlNWMHYNQTVDIWSVGCIMAEL 209

                 .
gi 525343631 482 L 482
Cdd:cd07851  210 L 210
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
266-526 8.29e-19

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 87.57  E-value: 8.29e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKynnekaEREVKALAKLDHVNivhyngcwdgvdydpETSDDYLESSD 345
Cdd:PTZ00263  19 DFEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLK------KREILKMKQVQHVA---------------QEKSILMELSH 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YDPENSKNSSRSKTKcLFIQMEFCDKGtlEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDT 425
Cdd:PTZ00263  78 PFIVNMMCSFQDENR-VYFLLEFVVGG--ELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNK 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQVKIGDFGLvtslkndGKRTRSK-----GTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTdlRD 500
Cdd:PTZ00263 155 GHVKVTDFGF-------AKKVPDRtftlcGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRI--YE 225
                        250       260       270
                 ....*....|....*....|....*....|..
gi 525343631 501 GIIS------DIFDKKEKTLLQKLLSKKPEDR 526
Cdd:PTZ00263 226 KILAgrlkfpNWFDGRARDLVKGLLQTDHTKR 257
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
267-526 9.17e-19

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: 86.59  E-value: 9.17e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER-------EVKALAKLDHVNIVhyngcwdGVDYDPETSDd 339
Cdd:cd05631    2 FRHYRVLGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKgeamalnEKRILEKVNSRFVV-------SLAYAYETKD- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknssrskTKCLFIQMefCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd05631   74 -------------------ALCLVLTI--MNGGDLKFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPEN 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKnDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELLHvCDTAFETSKFFTDl 498
Cdd:cd05631  133 ILLDDRGHIRISDLGLAVQIP-EGETVRGRvGTVGYMAPEVINNEKYTFSPDWWGLGCLIYEMIQ-GQSPFRKRKERVK- 209
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 525343631 499 RDGI----------ISDIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05631  210 REEVdrrvkedqeeYSEKFSEDAKSICRMLLTKNPKER 247
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
271-535 9.33e-19

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: 85.93  E-value: 9.33e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGK---TYVIKRVKYNNEKAE---REVKALAKLDHVNIVH-YngcwdgvdydpETSDdyles 343
Cdd:cd14074    9 ETLGRGHFAVVKLARHVFTGEkvaVKVIDKTKLDDVSKAhlfQEVRCMKLVQHPNVVRlY-----------EVID----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 sdydpensknssrSKTKcLFIQMEFCDKGTLEQWIeNRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN-IFL 422
Cdd:cd14074   73 -------------TQTK-LYLILELGDGGDMYDYI-MKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENvVFF 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELlhVCDTA-FET---SKFFTD 497
Cdd:cd14074  138 EKQGLVKLTDFGFSNKFQPGEKLETSCGSLAYSAPEILLGDEYdAPAVDIWSLGVILYML--VCGQPpFQEandSETLTM 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 525343631 498 LRDG--IISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:cd14074  216 IMDCkyTVPAHVSPECKDLIRRMLIRDPKKRASLEEIENH 255
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
273-482 1.30e-18

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: 86.17  E-value: 1.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKY-NNEKA-----EREVKALAKL---DHVNIVHYNgcwdgvdydpetsdDYLES 343
Cdd:cd07863    8 IGVGAYGTVYKARDPHSGHFVALKSVRVqTNEDGlplstVREVALLKRLeafDHPNIVRLM--------------DVCAT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 SDYDPEnsknssrSKTKCLFiqmEFCDKgTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd07863   74 SRTDRE-------TKVTLVF---EHVDQ-DLRTYLDKVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVT 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 424 DTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd07863  143 SGGQVKLADFGLARIYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMF 201
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
272-482 1.31e-18

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: 85.52  E-value: 1.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRidGKTYVIKRVKYNN--------EKAEREVKALAKLDHVNIVHYNG-CwdgvdydpetsddyLE 342
Cdd:cd14061    1 VIGVGGFGKVYRGIWR--GEEVAVKAARQDPdedisvtlENVRQEARLFWMLRHPNIIALRGvC--------------LQ 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydPENSknssrsktkCLFiqMEFCDKGTLeqwieNR--RGEKLDKVLALELFEQITKGVDYIHSKK---LIHRDLKP 417
Cdd:cd14061   65 -----PPNL---------CLV--MEYARGGAL-----NRvlAGRKIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKS 123
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 418 SNIFL--------VDTKQVKIGDFGLVTSLKNDgKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14061  124 SNILIleaienedLENKTLKITDFGLAREWHKT-TRMSAAGTYAWMAPEVIKSSTFSKASDVWSYGVLLWELL 195
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
266-529 1.33e-18

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: 86.31  E-value: 1.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN-------EKA--EREVKALAklDHVNIVHYNGCWdgvdydpET 336
Cdd:cd05609    1 DFETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQNlilrnqiQQVfvERDILTFA--ENPFVVSMYCSF-------ET 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 SddylessdydpensknssrsktKCLFIQMEFCDKGTLEQWIENRRGEKLDkvLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd05609   72 K----------------------RHLCMVMEYVEGGDCATLLKNIGPLPVD--MARMYFAETVLALEYLHSYGIVHRDLK 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGL--------VTSL-----KNDGKRTRSK---GTLRYMSPEQISSQDYGKEVDLYALGLILAE 480
Cdd:cd05609  128 PDNLLITSMGHIKLTDFGLskiglmslTTNLyeghiEKDTREFLDKqvcGTPEYIAPEVILRQGYGKPVDWWAMGIILYE 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 481 LLHVCDTAF-ETSK--FFTDLRDGII----SDIFDKKEKTLLQKLLSKKPEDRPNT 529
Cdd:cd05609  208 FLVGCVPFFgDTPEelFGQVISDEIEwpegDDALPDDAQDLITRLLQQNPLERLGT 263
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
384-534 1.43e-18

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: 85.45  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 384 EKLDKVLALELFE------QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIgDFGLVTSLKNDGKRTRS-KGTLRYMS 456
Cdd:cd13995   85 EKLESCGPMREFEiiwvtkHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVLV-DFGLSVQMTEDVYVPKDlRGTEIYMS 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 457 PEQISSQDYGKEVDLYALGlilAELLHVCD-----------TAFETSKFFTDLRDGIISDIFDK---KEKTLLQKLLSKK 522
Cdd:cd13995  164 PEVILCRGHNTKADIYSLG---ATIIHMQTgsppwvrryprSAYPSYLYIIHKQAPPLEDIAQDcspAMRELLEAALERN 240
                        170
                 ....*....|..
gi 525343631 523 PEDRPNTSEILR 534
Cdd:cd13995  241 PNHRSSAAELLK 252
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
267-482 1.59e-18

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: 86.69  E-value: 1.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKH--RIDGKTYVIKRVK--YNNE----KAEREVKALAKL-DHVNIVHYngcwdgVDYDPETS 337
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNaeTSEEETVAIKKITnvFSKKilakRALRELKLLRHFrGHKNITCL------YDMDIVFP 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 DDYLEssdydpensknssrsktkcLFIQMEF--CDkgtLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDL 415
Cdd:cd07857   76 GNFNE-------------------LYLYEELmeAD---LHQII--RSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDL 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 416 KPSNIFLVDTKQVKIGDFGLVTSL-----KNDGKRTRSKGTLRYMSPE-QISSQDYGKEVDLYALGLILAELL 482
Cdd:cd07857  132 KPGNLLVNADCELKICDFGLARGFsenpgENAGFMTEYVATRWYRAPEiMLSFQSYTKAIDVWSVGCILAELL 204
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
273-534 1.74e-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: 1.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKhriDGKTYVIKRVKYNNEKAEREVKAL-------AKLDHVNIVHYNGCwdgvdydpETSDDYLEssd 345
Cdd:cd06624   16 LGKGTFGVVYAAR---DLSTQVRIAIKEIPERDSREVQPLheeialhSRLSHKNIVQYLGS--------VSEDGFFK--- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 ydpensknssrsktkclfIQMEFCDKGTLEQWIENRRGEKLDKVLALELF-EQITKGVDYIHSKKLIHRDLKPSNIfLVD 424
Cdd:cd06624   82 ------------------IFMEQVPGGSLSALLRSKWGPLKDNENTIGYYtKQILEGLKYLHDNKIVHRDIKGDNV-LVN 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 T--KQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISS--QDYGKEVDLYALGLILAEL---------LHVCDTAFE 490
Cdd:cd06624  143 TysGVVKISDFGTSKRLAGINPCTETfTGTLQYMAPEVIDKgqRGYGPPADIWSLGCTIIEMatgkppfieLGEPQAAMF 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 491 TSKFFTDLRDgiISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06624  223 KVGMFKIHPE--IPESLSEEAKSFILRCFEPDPDKRATASDLLQ 264
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
273-536 1.84e-18

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: 85.26  E-value: 1.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIK--RVKYNNEKAEREVKALAKLDHVNIVHYNG-Cwdgvdydpetsddylessdydpe 349
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKiyKNDVDQHKIVREISLLQKLSHPNIVRYLGiC----------------------- 57
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 350 nsknssrSKTKCLFIQMEFCDKGTLEQWIEnrrgeklDKVLAL------ELFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd14156   58 -------VKDEKLHPILEYVSGGCLEELLA-------REELPLswrekvELACDISRGMVYLHSKNIYHRDLNSKNCLIR 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 424 DTKQVK---IGDFGLVTSL----KNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVC----DTAFET 491
Cdd:cd14156  124 VTPRGReavVTDFGLAREVgempANDPERKLSlVGSAFWMAPEMLRGEPYDRKVDVFSFGIVLCEILARIpadpEVLPRT 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 525343631 492 SKF------FTDLRDGIISDIFDkkektLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd14156  204 GDFgldvqaFKEMVPGCPEPFLD-----LAASCCRMDAFKRPSFAELLDEL 249
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
266-489 2.27e-18

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: 86.66  E-value: 2.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV-KYNNEK--------AEREVKALAKLDHVNIVHYngcwdgvdydpet 336
Cdd:cd05596   27 DFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLsKFEMIKrsdsaffwEERDIMAHANSEWIVQLHY------------- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddylessdydpensknsSRSKTKCLFIQMEFCDKGTL----------EQWIENRRGEKldkVLALelfeqitkgvDYIH 406
Cdd:cd05596   94 ------------------AFQDDKYLYMVMDYMPGGDLvnlmsnydvpEKWARFYTAEV---VLAL----------DAIH 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 407 SKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKrTRSK---GTLRYMSPEQISSQD----YGKEVDLYALGLILA 479
Cdd:cd05596  143 SMGFVHRDVKPDNMLLDASGHLKLADFGTCMKMDKDGL-VRSDtavGTPDYISPEVLKSQGgdgvYGRECDWWSVGVFLY 221
                        250
                 ....*....|
gi 525343631 480 ELLhVCDTAF 489
Cdd:cd05596  222 EML-VGDTPF 230
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
271-534 2.27e-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: 85.04  E-value: 2.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVkynnEKAER-----EVKALAKLDHVNIVHYNGCWdgvdydpETSddylessd 345
Cdd:cd14010    6 DEIGRGKHSVVYKGRRKGTIEFVAIKCV----DKSKRpevlnEVRLTHELKHPNVLKFYEWY-------ETS-------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 ydpenskNSsrsktkcLFIQMEFCDKGTLEQWIENRRG--EKLDKVLALELFeqitKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd14010   67 -------NH-------LWLVVEYCTGGDLETLLRQDGNlpESSVRKFGRDLV----RGLHYIHSKGIIYCDLKPSNILLD 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 424 DTKQVKIGDFGL-----------------VTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAElLHVCD 486
Cdd:cd14010  129 GNGTLKLSDFGLarregeilkelfgqfsdEGNVNKVSKKQAKRGTPYYMAPELFQGGVHSFASDLWALGCVLYE-MFTGK 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 487 TAFeTSKFFTDLRDGIISD--------IFDKKE---KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14010  208 PPF-VAESFTELVEKILNEdppppppkVSSKPSpdfKSLLKGLLEKDPAKRLSWDELVK 265
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
272-482 2.34e-18

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: 85.09  E-value: 2.34e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRidGKTYVIKR--------VKYNNEKAEREVKALAKLDHVNIVHYNG-CWdgvdydpetsddyle 342
Cdd:cd14146    1 IIGVGGFGKVYRATWK--GQEVAVKAarqdpdedIKATAESVRQEAKLFSMLRHPNIIKLEGvCL--------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssRSKTKCLFiqMEFCDKGTLEQWI-------ENRRGEKLDKVLALELFEQITKGVDYIHSKK---LIH 412
Cdd:cd14146   64 -------------EEPNLCLV--MEFARGGTLNRALaaanaapGPRRARRIPPHILVNWAVQIARGMLYLHEEAvvpILH 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 413 RDLKPSNIFLVD--------TKQVKIGDFGLVTSLKNDGKRTrSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14146  129 RDLKSSNILLLEkiehddicNKTLKITDFGLAREWHRTTKMS-AAGTYAWMAPEVIKSSLFSKGSDIWSYGVLLWELL 205
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
267-482 2.54e-18

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: 85.51  E-value: 2.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK-----AEREVKALAKLDHVNIVhyngcwdgvdydpeTSDDYL 341
Cdd:cd07844    2 YKKLDKLGEGSYATVYKGRSKLTGQLVALKEIRLEHEEgapftAIREASLLKDLKHANIV--------------TLHDII 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ESsdydpensknssrskTKCLFIQMEFCDKgTLEQWIENR-RGEKLDKVlALELFeQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd07844   68 HT---------------KKTLTLVFEYLDT-DLKQYMDDCgGGLSMHNV-RLFLF-QLLRGLAYCHQRRVLHRDLKPQNL 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 421 FLVDTKQVKIGDFGLVTSlKNDGKRTRSKG--TLRYMSPEQI-SSQDYGKEVDLYALGLILAELL 482
Cdd:cd07844  130 LISERGELKLADFGLARA-KSVPSKTYSNEvvTLWYRPPDVLlGSTEYSTSLDMWGVGCIFYEMA 193
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
266-526 2.54e-18

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 85.05  E-value: 2.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEI-ELIGSGGFGQVFKAKHRIDGKTYVIKRVK----------YNNEKAEREVKALAKLDHVNIVhyngcwdgvdydp 334
Cdd:cd14195    5 DHYEMgEELGSGQFAIVRKCREKGTGKEYAAKFIKkrrlsssrrgVSREEIEREVNILREIQHPNII------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 335 eTSDDYLEssdydpensknssrSKTKCLFIqMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRD 414
Cdd:cd14195   72 -TLHDIFE--------------NKTDVVLI-LELVSGGELFDFLAEK--ESLTEEEATQFLKQILDGVHYLHSKRIAHFD 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFLVD----TKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHvcdtafE 490
Cdd:cd14195  134 LKPENIMLLDknvpNPRIKLIDFGIAHKIEAGNEFKNIFGTPEFVAPEIVNYEPLGLEADMWSIGVITYILLS------G 207
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 525343631 491 TSKFFTDLRDGIISDI------FDKK--------EKTLLQKLLSKKPEDR 526
Cdd:cd14195  208 ASPFLGETKQETLTNIsavnydFDEEyfsntselAKDFIRRLLVKDPKKR 257
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
261-482 2.57e-18

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


Pssm-ID: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 85.41  E-value: 2.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 261 KRFGMDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE----REVKaLAKLDHVNIVHYngcwdgVDYDPE- 335
Cdd:cd14181    6 KEFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERLSpeqlEEVR-SSTLKEIHILRQ------VSGHPSi 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 336 -TSDDYLESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWIENR--RGEKLDKVLALELFEqitkGVDYIHSKKLIH 412
Cdd:cd14181   79 iTLIDSYESSTF---------------IFLVFDLMRRGELFDYLTEKvtLSEKETRSIMRSLLE----AVSYLHANNIVH 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 413 RDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQIS-SQD-----YGKEVDLYALGLILAELL 482
Cdd:cd14181  140 RDLKPENILLDDQLHIKLSDFGFSCHLEPGEKLRELCGTPGYLAPEILKcSMDethpgYGKEVDLWACGVILFTLL 215
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
265-482 3.35e-18

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 85.74  E-value: 3.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 265 MDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK-----YNNE----KAEREVkaLAKLDHVNIVHyngcwdgvdydpe 335
Cdd:cd05599    1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRksemlEKEQvahvRAERDI--LAEADNPWVVK------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 336 tsddyLESSDYDPENsknssrsktkcLFIQMEFCDKGTLEQWIEnrrgeKLDKvlaleLFEQITK--------GVDYIHS 407
Cdd:cd05599   66 -----LYYSFQDEEN-----------LYLIMEFLPGGDMMTLLM-----KKDT-----LTEEETRfyiaetvlAIESIHK 119
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 408 KKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05599  120 LGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKSHLAYSTVGTPDYIAPEVFLQKGYGKECDWWSLGVIMYEML 194
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
270-481 3.35e-18

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: 85.04  E-value: 3.35e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIK---RVKYNNEKAEREVKALAKL-DHVNIVHYNGCWdgvdydpETSDDYLESSd 345
Cdd:cd06639   27 IETIGKGTYGKVYKVTNKKDGSLAAVKildPISDVDEEIEAEYNILRSLpNHPNVVKFYGMF-------YKADQYVGGQ- 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 ydpensknssrsktkcLFIQMEFCDKGTLEQWIEN--RRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd06639   99 ----------------LWLVLELCNGGSVTELVKGllKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLT 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 424 DTKQVKIGDFGLVTSLKNDG-KRTRSKGTLRYMSPEQISSQ---DYGKEV--DLYALGLILAEL 481
Cdd:cd06639  163 TEGGVKLVDFGVSAQLTSARlRRNTSVGTPFWMAPEVIACEqqyDYSYDArcDVWSLGITAIEL 226
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
265-482 3.57e-18

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 85.25  E-value: 3.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 265 MD-FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNE------KAEREVKALAKLDHVNIVHYngcwdgvdYDPETS 337
Cdd:PLN00009   1 MDqYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEdegvpsTAIREISLLKEMQHGNIVRL--------QDVVHS 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 DdylessdydpensknssrsktKCLFIQMEFCD---KGTLEQWIENRRGEKLDKVLalelFEQITKGVDYIHSKKLIHRD 414
Cdd:PLN00009  73 E---------------------KRLYLVFEYLDldlKKHMDSSPDFAKNPRLIKTY----LYQILRGIAYCHSHRVLHRD 127
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 415 LKPSNIfLVD--TKQVKIGDFGLVTSLKNDGKR-TRSKGTLRYMSPE-QISSQDYGKEVDLYALGLILAELL 482
Cdd:PLN00009 128 LKPQNL-LIDrrTNALKLADFGLARAFGIPVRTfTHEVVTLWYRAPEiLLGSRHYSTPVDIWSVGCIFAEMV 198
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
273-482 3.59e-18

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: 85.08  E-value: 3.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYV-IKRVKYNNEKAE------REVKALAKLD---HVNIVHYngcwdgvdYDPETSddyle 342
Cdd:cd07862    9 IGEGAYGKVFKARDLKNGGRFVaLKRVRVQTGEEGmplstiREVAVLRHLEtfeHPNVVRL--------FDVCTV----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpenSKNSSRSKTKCLFiqmEFCDKgTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd07862   76 --------SRTDRETKLTLVF---EHVDQ-DLTTYLDKVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILV 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd07862  144 TSSGQIKLADFGLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMF 203
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
273-482 3.69e-18

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 84.45  E-value: 3.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALaKLDHVNIVhyngcWDGvdYDPETSDDY--LESSDYdpen 350
Cdd:cd05611    4 ISKGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNQVTNV-KAERAIMM-----IQG--ESPYVAKLYysFQSKDY---- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 351 sknssrsktkcLFIQMEFCDKGTLEQWIENRRGekLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKI 430
Cdd:cd05611   72 -----------LYLVMEYLNGGDCASLIKTLGG--LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKL 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631 431 GDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05611  139 TDFGLSRNGLEKRHNKKFVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFL 190
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
271-534 3.71e-18

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


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 84.41  E-value: 3.71e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRiDGKTYVIKRVKYNN----------EKAEREVKALAKLDHVNIVHYNGcwdgvdydpeTSDDy 340
Cdd:cd06631    7 NVLGKGAYGTVYCGLTS-TGQLIAVKQVELDTsdkekaekeyEKLQEEVDLLKTLKHVNIVGYLG----------TCLE- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpENSKNssrsktkclfIQMEFCDKGTLEQwIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd06631   75 --------DNVVS----------IFMEFVPGGSIAS-ILARFG-ALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNI 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 421 FLVDTKQVKIGDFG------LVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGlilaellhvCdTAFE--T 491
Cdd:cd06631  135 MLMPNGVIKLIDFGcakrlcINLSSGSQSQLLKSmRGTPYWMAPEVINETGHGRKSDIWSIG---------C-TVFEmaT 204
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 492 SK------------FFTDLRDGI---ISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06631  205 GKppwadmnpmaaiFAIGSGRKPvprLPDKFSPEARDFVHACLTRDQDERPSAEQLLK 262
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
266-533 3.73e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 88.26  E-value: 3.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631  266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKaERE-------VKALAKLDHVNIVHYngcwdgvdydpetSD 338
Cdd:PTZ00266   14 EYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLK-EREksqlvieVNVMRELKHKNIVRY-------------ID 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631  339 DYLESSdydpeNSKnssrsktkcLFIQMEFCDKGTLEQWIEN--RRGEKLDKVLALELFEQITKGVDYIHS-------KK 409
Cdd:PTZ00266   80 RFLNKA-----NQK---------LYILMEFCDAGDLSRNIQKcyKMFGKIEEHAIVDITRQLLHALAYCHNlkdgpngER 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631  410 LIHRDLKPSNIFLVD--------TKQ---------VKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQI--SSQDYGKEVD 470
Cdd:PTZ00266  146 VLHRDLKPQNIFLSTgirhigkiTAQannlngrpiAKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLlhETKSYDDKSD 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631  471 LYALGLILAELlhvCD--TAFET----SKFFTDLRDGIISDIFDKKEK--TLLQKLLSKKPEDRPNTSEIL 533
Cdd:PTZ00266  226 MWALGCIIYEL---CSgkTPFHKannfSQLISELKRGPDLPIKGKSKElnILIKNLLNLSAKERPSALQCL 293
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
267-537 4.11e-18

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: 84.23  E-value: 4.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIK--RVKYNNEKAEREVKALAKLDhvnivhyngcwdGVDYDPETSDdyless 344
Cdd:cd14017    2 WKVVKKIGGGGFGEIYKVRDVVDGEEVAMKveSKSQPKQVLKMEVAVLKKLQ------------GKPHFCRLIG------ 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpensknSSRSKTKClFIQMEFCDKgTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL-- 422
Cdd:cd14017   64 ---------CGRTERYN-YIVMTLLGP-NLAELRRSQPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgr 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 --VDTKQVKIGDFGL---VTSLKNDGKRTRSK-----GTLRYMSPEQISSQDYGKEVDLYALGLILAELlhvcdtaFETS 492
Cdd:cd14017  133 gpSDERTVYILDFGLarqYTNKDGEVERPPRNaagfrGTVRYASVNAHRNKEQGRRDDLWSWFYMLIEF-------VTGQ 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 525343631 493 KFFTDLRDGIisDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLT 537
Cdd:cd14017  206 LPWRKLKDKE--EVGKMKEKIDHEELLKGLPKEFFQILKHIRSLS 248
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
273-537 4.23e-18

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The STK_BAK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 84.47  E-value: 4.23e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRiDGKTYVIKRVKYNNEKA-----EREVKALAKLDHVNIVHYNGCWdgvdydpETSDDYLESSDYD 347
Cdd:cd14664    1 IGRGGAGTVYKGVMP-NGTLVAVKRLKGEGTQGgdhgfQAEIQTLGMIRHRNIVRLRGYC-------SNPTTNLLVYEYM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 PENSKNSsrsktkCLFIQMEfcdkgtleqwienrRGEKLDKVLALELFEQITKGVDYIH---SKKLIHRDLKPSNIFLVD 424
Cdd:cd14664   73 PNGSLGE------LLHSRPE--------------SQPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDE 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLVTSLKNDGKRTRS--KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAFETSKFFTD----- 497
Cdd:cd14664  133 EFEAHVADFGLAKLMDDKDSHVMSsvAGSYGYIAPEYAYTGKVSEKSDVYSYGVVLLELI-TGKRPFDEAFLDDGvdivd 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 498 -----LRDGIISDIFD--------KKEKTLLQKL----LSKKPEDRPNTSEILRTLT 537
Cdd:cd14664  212 wvrglLEEKKVEALVDpdlqgvykLEEVEQVFQVallcTQSSPMERPTMREVVRMLE 268
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
273-526 4.62e-18

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 84.50  E-value: 4.62e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRV-KYNNEKAEREVKALAKLDHVNIVHyngcwdgvdydpetsDDYLESSDYDPEns 351
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLdKKRIKKKKGETMALNEKIILEKVS---------------SPFIVSLAYAFE-- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 352 knssrSKTKCLFIqMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIG 431
Cdd:cd05577   64 -----TKDKLCLV-LTLMNGGDLKYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRIS 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 432 DFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQ-DYGKEVDLYALGLILAELLhVCDTAFETSKFFTD--------LRDGI 502
Cdd:cd05577  138 DLGLAVEFKGGKKIKGRVGTHGYMAPEVLQKEvAYDFSVDWFALGCMLYEMI-AGRSPFRQRKEKVDkeelkrrtLEMAV 216
                        250       260
                 ....*....|....*....|....*
gi 525343631 503 -ISDIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05577  217 eYPDSFSPEARSLCEGLLQKDPERR 241
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
274-482 4.96e-18

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: 83.47  E-value: 4.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 274 GSGGFGQVFKAKHRIDGKTYVIKRVKynneKAEREVKALAKLDHVNIVHYNGCwdgvdydpetsddYLESSDYDpenskn 353
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVKKLL----KIEKEAEILSVLSHRNIIQFYGA-------------ILEAPNYG------ 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 354 ssrsktkclfIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSK---KLIHRDLKPSNIFLVDTKQVKI 430
Cdd:cd14060   59 ----------IVTEYASYGSLFDYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKI 128
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631 431 GDFGlVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14060  129 CDFG-ASRFHSHTTHMSLVGTFPWMAPEVIQSLPVSETCDTYSYGVVLWEML 179
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
303-532 6.28e-18

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: 84.25  E-value: 6.28e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 303 EKAEREVKALAKLDHVNIVHYNGCWDgvdyDPetSDDYLessdydpensknssrsktkclFIQMEFCDKGTLeqwIENRR 382
Cdd:cd14199   70 ERVYQEIAILKKLDHPNVVKLVEVLD----DP--SEDHL---------------------YMVFELVKQGPV---MEVPT 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 383 GEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLK-NDGKRTRSKGTLRYMSPEQIS 461
Cdd:cd14199  120 LKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGVSNEFEgSDALLTNTVGTPAFMAPETLS 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 462 SQD---YGKEVDLYALGLILA-----------ELLHVCDTAFETSKF-FTDLRDgiISDIFdkkeKTLLQKLLSKKPEDR 526
Cdd:cd14199  200 ETRkifSGKALDVWAMGVTLYcfvfgqcpfmdERILSLHSKIKTQPLeFPDQPD--ISDDL----KDLLFRMLDKNPESR 273

                 ....*.
gi 525343631 527 PNTSEI 532
Cdd:cd14199  274 ISVPEI 279
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
265-482 6.48e-18

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: 83.98  E-value: 6.48e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 265 MDFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER---------EVKALAKLDHVNIVHYNGCWDgvdydpe 335
Cdd:cd06651    7 INWRRGKLLGQGAFGRVYLCYDVDTGRELAAKQVQFDPESPETskevsalecEIQLLKNLQHERIVQYYGCLR------- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 336 tsdDYLEssdydpensknssrsktKCLFIQMEFCDKGTLEQWIENRRGekLDKVLALELFEQITKGVDYIHSKKLIHRDL 415
Cdd:cd06651   80 ---DRAE-----------------KTLTIFMEYMPGGSVKDQLKAYGA--LTESVTRKYTRQILEGMSYLHSNMIVHRDI 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 416 KPSNIFLVDTKQVKIGDFGLVTSLKN---DGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd06651  138 KGANILRDSAGNVKLGDFGASKRLQTicmSGTGIRSvTGTPYWMSPEVISGEGYGRKADVWSLGCTVVEML 208
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
266-537 6.66e-18

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: 83.46  E-value: 6.66e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYV--IKRVKYNNEKAEREVKALAKLDHVNIVH-YNGCWdgvdydpetsddyle 342
Cdd:cd05112    5 ELTFVQEIGSGQFGLVHLGYWLNKDKVAIktIREGAMSEEDFIEEAEVMMKLSHPKLVQlYGVCL--------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpENSKnssrsktkcLFIQMEFCDKGTLEQWIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd05112   70 ------EQAP---------ICLVFEFMEHGCLSDYLRTQRG-LFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLV 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLvTSLKNDGKRTRSKGT---LRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFE---TSKFFT 496
Cdd:cd05112  134 GENQVVKVSDFGM-TRFVLDDQYTSSTGTkfpVKWSSPEVFSFSRYSSKSDVWSFGVLMWEVFSEGKIPYEnrsNSEVVE 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 497 DLRDG---IISDIFDKKEKTLLQKLLSKKPEDRPNTSEILRTLT 537
Cdd:cd05112  213 DINAGfrlYKPRLASTHVYEIMNHCWKERPEDRPSFSLLLRQLA 256
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
267-482 6.72e-18

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 86.24  E-value: 6.72e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVhyngcwdgvdydpetsddYLESSDY 346
Cdd:PTZ00036  68 YKLGNIIGNGSFGVVYEAICIDTSEKVAIKKVLQDPQYKNRELLIMKNLNHINII------------------FLKDYYY 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 DPENSKNSsrsKTKCLFIQMEFCDKgTLEQWIE--NRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIfLVD 424
Cdd:PTZ00036 130 TECFKKNE---KNIFLNVVMEFIPQ-TVHKYMKhyARNNHALPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNL-LID 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 425 --TKQVKIGDFGlvtSLKN--DGKRTRSKGTLR-YMSPE-QISSQDYGKEVDLYALGLILAELL 482
Cdd:PTZ00036 205 pnTHTLKLCDFG---SAKNllAGQRSVSYICSRfYRAPElMLGATNYTTHIDLWSLGCIIAEMI 265
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
273-482 8.70e-18

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: 83.47  E-value: 8.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER----EVKALAKLDHVNIVHYngcwDGVDYdpetsddylessdydp 348
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMKELIRFDEETQRtflkEVKVMRCLEHPNVLKF----IGVLY---------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 349 ensknssrsKTKCLFIQMEFCDKGTLEQWIENrrgekLDKVLA----LELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd14221   61 ---------KDKRLNFITEYIKGGTLRGIIKS-----MDSHYPwsqrVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRE 126
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 425 TKQVKIGDFGL----------VTSLKNDGKRTRSK-----GTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14221  127 NKSVVVADFGLarlmvdektqPEGLRSLKKPDRKKrytvvGNPYWMAPEMINGRSYDEKVDVFSFGIVLCEII 199
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
271-537 9.04e-18

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: 83.55  E-value: 9.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGK--TYVIKRVK-YNNEKAER----EVKALAKL-DHVNIVHYNGCWDGVDYDpetsddYLe 342
Cdd:cd05047    1 DVIGEGNFGQVLKARIKKDGLrmDAAIKRMKeYASKDDHRdfagELEVLCKLgHHPNIINLLGACEHRGYL------YL- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 SSDYDPENSKNSSRSKTKCLFIQMEFCdkgtleqwIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd05047   74 AIEYAPHGNLLDFLRKSRVLETDPAFA--------IANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILV 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAF---ETSKFFTDLR 499
Cdd:cd05047  146 GENYVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYcgmTCAELYEKLP 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 525343631 500 DGIISDI---FDKKEKTLLQKLLSKKPEDRPNTSEILRTLT 537
Cdd:cd05047  226 QGYRLEKplnCDDEVYDLMRQCWREKPYERPSFAQILVSLN 266
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
273-482 9.17e-18

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: 83.45  E-value: 9.17e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER----EVKALAKLDHVNIVHYngcwDGVDYdpetsddylessdydp 348
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMKELIRCDEETQKtfltEVKVMRSLDHPNVLKF----IGVLY---------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 349 ensknssrsKTKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALElfEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQV 428
Cdd:cd14222   61 ---------KDKRLNLLTEFIEGGTLKDFLRADDPFPWQQKVSFA--KGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTV 129
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 429 KIGDFGLVTSLKNDGKR------TRSKGTLR---------------YMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14222  130 VVADFGLSRLIVEEKKKpppdkpTTKKRTLRkndrkkrytvvgnpyWMAPEMLNGKSYDEKVDIFSFGIVLCEII 204
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
397-482 1.07e-17

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 84.53  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKR------TRSKGTLRYMSPE-QISSQDYGKEV 469
Cdd:cd07852  115 QLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEEDdenpvlTDYVATRWYRAPEiLLGSTRYTKGV 194
                         90
                 ....*....|...
gi 525343631 470 DLYALGLILAELL 482
Cdd:cd07852  195 DMWSVGCILGEML 207
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
266-534 1.17e-17

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: 83.17  E-value: 1.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKY----NNEKAEREVKALAKLDHVNIVHYNGcwdgvdydpetsdDYL 341
Cdd:cd06645   12 DFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLepgeDFAVVQQEIIMMKDCKHSNIVAYFG-------------SYL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 EssdydpensknssRSKtkcLFIQMEFCDKGTLEQwIENRRGEKLDKVLALELFEQItKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd06645   79 R-------------RDK---LWICMEFCGGGSLQD-IYHVTGPLSESQIAYVSRETL-QGLYYLHSKGKMHRDIKGANIL 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFGLVTSLKND-GKRTRSKGTLRYMSPEQISSQ---DYGKEVDLYALGLILAELLHVCDTAFE----TSK 493
Cdd:cd06645  141 LTDNGHVKLADFGVSAQITATiAKRKSFIGTPYWMAPEVAAVErkgGYNQLCDIWAVGITAIELAELQPPMFDlhpmRAL 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 525343631 494 FFTDLRDGIISDIFDKKEKT-----LLQKLLSKKPEDRPNTSEILR 534
Cdd:cd06645  221 FLMTKSNFQPPKLKDKMKWSnsfhhFVKMALTKNPKKRPTAEKLLQ 266
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
271-478 1.22e-17

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: 82.85  E-value: 1.22e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIK---RVKYNNEKAER---EVKALAKLDHVNIVHYNGCWdgvdydpETSDDyless 344
Cdd:cd14082    9 EVLGSGQFGIVYGGKHRKTGRDVAIKvidKLRFPTKQESQlrnEVAILQQLSHPGVVNLECMF-------ETPER----- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpensknssrsktkcLFIQMEFCDKGTLEQWIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd14082   77 -----------------VFVVMEKLHGDMLEMILSSEKG-RLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLAS 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 425 TK---QVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLIL 478
Cdd:cd14082  139 AEpfpQVKLCDFGFARIIGEKSFRRSVVGTPAYLAPEVLRNKGYNRSLDMWSVGVII 195
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
272-536 1.30e-17

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: 82.85  E-value: 1.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFK--AKHRIDGKTYVIK-RVK------YNNEKAE--REVKALAKLDHVNIVHYNG-CwdgVDYDPEtsdd 339
Cdd:cd05044    2 FLGSGAFGEVFEgtAKDILGDGSGETKvAVKtlrkgaTDQEKAEflKEAHLMSNFKHPNILKLLGvC---LDNDPQ---- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknssrsktkclFIQMEFCDKGTLEQWIENRRGEKLDKVLaLELFEQIT------KGVDYIHSKKLIHR 413
Cdd:cd05044   75 -----------------------YIILELMEGGDLLSYLRAARPTAFTPPL-LTLKDLLSicvdvaKGCVYLEDMHFVHR 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 414 DLKPSNIfLVDTKQ-----VKIGDFGLVTSL-KNDGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAELL--- 482
Cdd:cd05044  131 DLAARNC-LVSSKDyrervVKIGDFGLARDIyKNDYYRKEGEGLLpvRWMAPESLVDGVFTTQSDVWAFGVLMWEILtlg 209
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 483 ---HVCDTAFETSKFFT-----DLRDGIISDIFDkkektLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd05044  210 qqpYPARNNLEVLHFVRaggrlDQPDNCPDDLYE-----LMLRCWSTDPEERPSFARILEQL 266
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
267-481 1.52e-17

Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 83.35  E-value: 1.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK------AEREVKALAKLDHVNIVHYNGCWDGVDYDPETsddy 340
Cdd:cd07837    3 YEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEegvpstALREVSLLQMLSQSIYIVRLLDVEHVEENGKP---- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpensknssrsktkCLFIQMEFCDKgTLEQWIE-NRRGE--KLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd07837   79 --------------------LLYLVFEYLDT-DLKKFIDsYGRGPhnPLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKP 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 418 SNIFLVDTKQV-KIGDFGLVTSLKNDGKR-TRSKGTLRYMSPE-QISSQDYGKEVDLYALGLILAEL 481
Cdd:cd07837  138 QNLLVDKQKGLlKIADLGLGRAFTIPIKSyTHEIVTLWYRAPEvLLGSTHYSTPVDMWSVGCIFAEM 204
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
261-498 1.62e-17

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 83.03  E-value: 1.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 261 KRFgmdFKEIELIGSGGFGQV----FKAKHRIDGKTYVIKRVKYNNEKAER-----EVKALAKLDHVNIVHYNGCwdgvd 331
Cdd:cd05080    3 KRY---LKKIRDLGEGHFGKVslycYDPTNDGTGEMVAVKALKADCGPQHRsgwkqEIDILKTLYHENIVKYKGC----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 332 ydpetsddylessdydpensknSSRSKTKCLFIQMEFCDKGTLEQWIEnRRGEKLDKVLaleLF-EQITKGVDYIHSKKL 410
Cdd:cd05080   75 ----------------------CSEQGGKSLQLIMEYVPLGSLRDYLP-KHSIGLAQLL---LFaQQICEGMAYLHSQHY 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 411 IHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGK--RTRSKGT--LRYMSPEQISSQDYGKEVDLYALGLILAELLHVCD 486
Cdd:cd05080  129 IHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEyyRVREDGDspVFWYAPECLKEYKFYYASDVWSFGVTLYELLTHCD 208
                        250
                 ....*....|..
gi 525343631 487 TAFETSKFFTDL 498
Cdd:cd05080  209 SSQSPPTKFLEM 220
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
273-481 1.62e-17

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 82.74  E-value: 1.62e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAkhrIDGKTYV---------IKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWdgvdydpetsddyles 343
Cdd:cd14033    9 IGRGSFKTVYRG---LDTETTVevawcelqtRKLSKGERQRFSEEVEMLKGLQHPNIVRFYDSW---------------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 sdydpenskNSSRSKTKCLFIQMEFCDKGTLEQWIENRRGEKLdKVLALELFeQITKGVDYIHSK--KLIHRDLKPSNIF 421
Cdd:cd14033   70 ---------KSTVRGHKCIILVTELMTSGTLKTYLKRFREMKL-KLLQRWSR-QILKGLHFLHSRcpPILHRDLKCDNIF 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 422 LVD-TKQVKIGDFGLVTsLKNDGKRTRSKGTLRYMSPEqISSQDYGKEVDLYALGLILAEL 481
Cdd:cd14033  139 ITGpTGSVKIGDLGLAT-LKRASFAKSVIGTPEFMAPE-MYEEKYDEAVDVYAFGMCILEM 197
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
256-526 1.68e-17

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: 82.60  E-value: 1.68e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 256 KYTVDkrfgmDFKEIELIGSGGFGQVFKAKHRiDGKTYVIKRVKYNNE--------KAEREVKALAKLDHVNIVH-YNGC 326
Cdd:cd14117    2 KFTID-----DFDIGRPLGKGKFGNVYLAREK-QSKFIVALKVLFKSQiekegvehQLRREIEIQSHLRHPNILRlYNYF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 327 WDgvdydpetsddylessdydpensknssrskTKCLFIQMEFCDKGtlEQWIENRRGEKLDKVLALELFEQITKGVDYIH 406
Cdd:cd14117   76 HD------------------------------RKRIYLILEYAPRG--ELYKELQKHGRFDEQRTATFMEELADALHYCH 123
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 407 SKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSkGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCD 486
Cdd:cd14117  124 EKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLRRRTMC-GTLDYLPPEMIEGRTHDEKVDLWCIGVLCYELL-VGM 201
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 525343631 487 TAFETSKFFTDLRDGIISDI-----FDKKEKTLLQKLLSKKPEDR 526
Cdd:cd14117  202 PPFESASHTETYRRIVKVDLkfppfLSDGSRDLISKLLRYHPSER 246
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
266-538 1.71e-17

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: 82.77  E-value: 1.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN----EKAEREVKALAKLDHVNIVHYNGcwdgvdydpetsdDYL 341
Cdd:cd06646   10 DYELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPgddfSLIQQEIFMVKECKHCNIVAYFG-------------SYL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdydpensknsSRSKtkcLFIQMEFCDKGTLEQwIENRRGEKLDKVLALELFEQItKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd06646   77 -------------SREK---LWICMEYCGGGSLQD-IYHVTGPLSELQIAYVCRETL-QGLAYLHSKGKMHRDIKGANIL 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFGLVTSLKND-GKRTRSKGTLRYMSPEQISSQD---YGKEVDLYALGLI---LAEL------LHVCDTA 488
Cdd:cd06646  139 LTDNGDVKLADFGVAAKITATiAKRKSFIGTPYWMAPEVAAVEKnggYNQLCDIWAVGITaieLAELqppmfdLHPMRAL 218
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631 489 FETSKffTDLRDGIISD--IFDKKEKTLLQKLLSKKPEDRPNTSEILRTLTV 538
Cdd:cd06646  219 FLMSK--SNFQPPKLKDktKWSSTFHNFVKISLTKNPKKRPTAERLLTHLFV 268
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
271-483 1.75e-17

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: 83.48  E-value: 1.75e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTY---------VIKRVKYNNEKAEREVkALAKLDHVNIVhyngcwdGVDYDPETSDDyl 341
Cdd:cd05603    1 KVIGKGSFGKVLLAKRKCDGKFYavkvlqkktILKKKEQNHIMAERNV-LLKNLKHPFLV-------GLHYSFQTSEK-- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdydpensknssrsktkcLFIQMEFCDKGTLEQWIENRR--GEKLDKVLALElfeqITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd05603   71 --------------------LYFVLDYVNGGELFFHLQRERcfLEPRARFYAAE----VASAIGYLHSLNIIYRDLKPEN 126
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 420 IFLVDTKQVKIGDFGLVTS-LKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLH 483
Cdd:cd05603  127 ILLDCQGHVVLTDFGLCKEgMEPEETTSTFCGTPEYLAPEVLRKEPYDRTVDWWCLGAVLYEMLY 191
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
265-482 2.07e-17

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: 82.40  E-value: 2.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 265 MDFKEI---ELIGSGGFGQVFKAKHriDGKTYVIKRVKYNN--------EKAEREVKALAKLDHVNIVHYNG-CWdgvdy 332
Cdd:cd14145    3 IDFSELvleEIIGIGGFGKVYRAIW--IGDEVAVKAARHDPdedisqtiENVRQEAKLFAMLKHPNIIALRGvCL----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 333 dpetsddylessdydpensknssrsKTKCLFIQMEFCDKGTLEQWIEnrrGEKLDKVLALELFEQITKGVDYIHSKKL-- 410
Cdd:cd14145   76 -------------------------KEPNLCLVMEFARGGPLNRVLS---GKRIPPDILVNWAVQIARGMNYLHCEAIvp 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 411 -IHRDLKPSNIFLVD--------TKQVKIGDFGLVTSLKNDGKRTrSKGTLRYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd14145  128 vIHRDLKSSNILILEkvengdlsNKILKITDFGLAREWHRTTKMS-AAGTYAWMAPEVIRSSMFSKGSDVWSYGVLLWEL 206

                 .
gi 525343631 482 L 482
Cdd:cd14145  207 L 207
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
273-538 2.40e-17

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 82.05  E-value: 2.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQvfkAKHRIDGKTYVIKRV--KYNNEKAE------REVKALAKLDHVNIVHYNG-Cwdgvdydpetsddyles 343
Cdd:cd13992    6 GASSHTGE---PKYVKKVGVYGGRTVaiKHITFSRTekrtilQELNQLKELVHDNLNKFIGiC----------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 sdYDPENsknssrsktkcLFIQMEFCDKGTLEQWIENRrGEKLDKVLALELFEQITKGVDYIHSKKLI-HRDLKPSNIfL 422
Cdd:cd13992   66 --INPPN-----------IAVVTEYCTRGSLQDVLLNR-EIKMDWMFKSSFIKDIVKGMNYLHSSSIGyHGRLKSSNC-L 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTK-QVKIGDFGLVTSLKNDGKRTRSKGTLR----YMSPEQISSQDYGKEV----DLYALGLILAELLHVCDT-AFET- 491
Cdd:cd13992  131 VDSRwVVKLTDFGLRNLLEEQTNHQLDEDAQHkkllWTAPELLRGSLLEVRGtqkgDVYSFAIILYEILFRSDPfALERe 210
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 492 -SKFFTDLRDGI----ISDIFDKKEKT-----LLQKLLSKKPEDRPNTSEILRTLTV 538
Cdd:cd13992  211 vAIVEKVISGGNkpfrPELAVLLDEFPprlvlLVKQCWAENPEKRPSFKQIKKTLTE 267
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
266-481 2.58e-17

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: 83.18  E-value: 2.58e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAERE--VKALAKLDHVNIVHYNGCWDGVDYDPETSddyles 343
Cdd:cd06650    6 DFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIRNqiIRELQVLHECNSPYIVGFYGAFYSDGEIS------ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 sdydpensknssrsktkclfIQMEFCDKGTLEQWIEnRRGEKLDKVLAlELFEQITKGVDYIHSK-KLIHRDLKPSNIFL 422
Cdd:cd06650   80 --------------------ICMEHMDGGSLDQVLK-KAGRIPEQILG-KVSIAVIKGLTYLREKhKIMHRDVKPSNILV 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 423 VDTKQVKIGDFG----LVTSLKNDGKRTRSkgtlrYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd06650  138 NSRGEIKLCDFGvsgqLIDSMANSFVGTRS-----YMSPERLQGTHYSVQSDIWSMGLSLVEM 195
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
267-481 2.59e-17

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: 82.36  E-value: 2.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK-----AEREVKALAKLDHVNIVhyngcwdgvdydpeTSDDYL 341
Cdd:cd07871    7 YVKLDKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEgapctAIREVSLLKNLKHANIV--------------TLHDII 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ESSdydpensknssrsktKCLFIQMEFCDKgTLEQWIENrrGEKLDKVLALELFE-QITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd07871   73 HTE---------------RCLTLVFEYLDS-DLKQYLDN--CGNLMSMHNVKIFMfQLLRGLSYCHKRKILHRDLKPQNL 134
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 421 FLVDTKQVKIGDFGLVTSlKNDGKRTRSKG--TLRYMSPE-QISSQDYGKEVDLYALGLILAEL 481
Cdd:cd07871  135 LINEKGELKLADFGLARA-KSVPTKTYSNEvvTLWYRPPDvLLGSTEYSTPIDMWGVGCILYEM 197
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
273-536 2.71e-17

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: 81.63  E-value: 2.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYV---IKRVKYNNEKAE-----REVKALAKLDHVNIVHYNGCwdgvdydpetsddyless 344
Cdd:cd05060    3 LGHGNFGSVRKGVYLMKSGKEVevaVKTLKQEHEKAGkkeflREASVMAQLDHPCIVRLIGV------------------ 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpensknssrSKTKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLalELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd05060   65 ------------CKGEPLMLVMELAPLGPLLKYLKKRREIPVSDLK--ELAHQVAMGMAYLESKHFVHRDLAARNVLLVN 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLVTSLK--NDGKRTRSKGT--LRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDtafetsKFFTDLRD 500
Cdd:cd05060  131 RHQAKISDFGMSRALGagSDYYRATTAGRwpLKWYAPECINYGKFSSKSDVWSYGVTLWEAFSYGA------KPYGEMKG 204
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 525343631 501 GIISDIFDKKEK------------TLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd05060  205 PEVIAMLESGERlprpeecpqeiySIMLSCWKYRPEDRPTFSELESTF 252
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
260-545 2.88e-17

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: 82.28  E-value: 2.88e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 260 DKRFgmdFKEIELIGSGGFGQV----FKAKHRIDGKTYVIKRVKYNNEKAE-----REVKALAKLDHVNIVHYNG-CWDG 329
Cdd:cd05079    2 EKRF---LKRIRDLGEGHFGKVelcrYDPEGDNTGEQVAVKSLKPESGGNHiadlkKEIEILRNLYHENIVKYKGiCTED 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 330 VDydpetsddylessdydpensknssrsktKCLFIQMEFCDKGTLEQWIEnRRGEKLDKVLALELFEQITKGVDYIHSKK 409
Cdd:cd05079   79 GG----------------------------NGIKLIMEFLPSGSLKEYLP-RNKNKINLKQQLKYAVQICKGMDYLGSRQ 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 410 LIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLR----YMSPEQISSQDYGKEVDLYALGLILAELLHVC 485
Cdd:cd05079  130 YVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVKDDLDspvfWYAPECLIQSKFYIASDVWSFGVTLYELLTYC 209
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 486 DTAFETSKFFTDLrdgiISDIFDKKEKTLLQKLLS--KKPEDRPNTSEILRTLT--VWKKSPEK 545
Cdd:cd05079  210 DSESSPMTLFLKM----IGPTHGQMTVTRLVRVLEegKRLPRPPNCPEEVYQLMrkCWEFQPSK 269
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
266-485 3.04e-17

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: 81.72  E-value: 3.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIK---RVKYNNEKAEREVKAlakldhvnivhyngcwdgvdyDPETSDD--- 339
Cdd:cd14077    2 NWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKiipRASNAGLKKEREKRL---------------------EKEISRDirt 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ----YLESSDYDPE--NSKNSSRSKTkCLFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHR 413
Cdd:cd14077   61 ireaALSSLLNHPHicRLRDFLRTPN-HYYMLFEYVDGGQLLDYIISH--GKLKEKQARKFARQIASALDYLHRNSIVHR 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 414 DLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELlhVC 485
Cdd:cd14077  138 DLKIENILISKSGNIKIIDFGLSNLYDPRRLLRTFCGSLYFAAPELLQAQPYtGPEVDVWSFGVVLYVL--VC 208
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
267-482 3.16e-17

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: 81.51  E-value: 3.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNE-KAE---REVKALAKLDHVNIVHYngcwdgvdydpetSDDYLE 342
Cdd:cd06647    9 YTRFEKIGQGASGTVYTAIDVATGQEVAIKQMNLQQQpKKEliiNEILVMRENKNPNIVNY-------------LDSYLV 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 SSDydpensknssrsktkcLFIQMEFCDKGTLEQWIENrrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd06647   76 GDE----------------LWVVMEYLAGGSLTDVVTE---TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 423 VDTKQVKIGDFGLVTSLKND-GKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd06647  137 GMDGSVKLTDFGFCAQITPEqSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV 197
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
271-534 3.21e-17

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: 81.86  E-value: 3.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKA-----EREVKALAKLDHVNIVhyngcwdgvdydpeTSDDYLESSD 345
Cdd:cd14169    9 EKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGkeamvENEIAVLRRINHENIV--------------SLEDIYESPT 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YdpensknssrsktkcLFIQMEFCDKGTL-EQWIEnrRGEKLDKVlALELFEQITKGVDYIHSKKLIHRDLKPSNIF--- 421
Cdd:cd14169   75 H---------------LYLAMELVTGGELfDRIIE--RGSYTEKD-ASQLIGQVLQAVKYLHQLGIVHRDLKPENLLyat 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 -LVDTKqVKIGDFGLvTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKffTDLRD 500
Cdd:cd14169  137 pFEDSK-IMISDFGL-SKIEAQGMLSTACGTPGYVAPELLEQKPYGKAVDVWAIGVISYILLCGYPPFYDEND--SELFN 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 501 GIIS----------DIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14169  213 QILKaeyefdspywDDISESAKDFIRHLLERDPEKRFTCEQALQ 256
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
270-526 3.56e-17

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: 82.84  E-value: 3.56e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRI---DGKTYVIKRVK----YNNEK------AEREVkaLAKLDHVNIV--HYNGCWDGVDYdp 334
Cdd:cd05584    1 LKVLGKGGYGKVFQVRKTTgsdKGKIFAMKVLKkasiVRNQKdtahtkAERNI--LEAVKHPFIVdlHYAFQTGGKLY-- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 335 eTSDDYLESSDydpensknssrsktkcLFIQMEfcdkgtleqwienRRGEKLDKVLALELFEqITKGVDYIHSKKLIHRD 414
Cdd:cd05584   77 -LILEYLSGGE----------------LFMHLE-------------REGIFMEDTACFYLAE-ITLALGHLHSLGIIYRD 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFLVDTKQVKIGDFGLVT-SLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhvcdTAfeTSK 493
Cdd:cd05584  126 LKPENILLDAQGHVKLTDFGLCKeSIHDGTVTHTFCGTIEYMAPEILTRSGHGKAVDWWSLGALMYDML----TG--APP 199
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 525343631 494 FFTDLRDGIISDIFDKK----------EKTLLQKLLSKKPEDR 526
Cdd:cd05584  200 FTAENRKKTIDKILKGKlnlppyltneARDLLKKLLKRNVSSR 242
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
273-482 3.74e-17

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: 82.80  E-value: 3.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVK--YNN----EKAEREVKALAKLDHVNIVHYNGCWDGVDYDpETSDDYL--ESS 344
Cdd:cd07858   13 IGRGAYGIVCSAKNSETNEKVAIKKIAnaFDNridaKRTLREIKLLRHLDHENVIAIKDIMPPPHRE-AFNDVYIvyELM 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 DYDPENSKNSSRSKTKclfiqmEFCdkgtleQWIenrrgekldkvlaleLFeQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd07858   92 DTDLHQIIRSSQTLSD------DHC------QYF---------------LY-QLLRGLKYIHSANVLHRDLKPSNLLLNA 143
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLV-TSLKNDGKRTRSKGTLRYMSPEQI-SSQDYGKEVDLYALGLILAELL 482
Cdd:cd07858  144 NCDLKICDFGLArTTSEKGDFMTEYVVTRWYRAPELLlNCSEYTTAIDVWSVGCIFAELL 203
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
271-485 4.72e-17

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: 82.02  E-value: 4.72e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKhrIDGKTYVIKRVKYNNEK---AEREVKALAKLDHVNIVHYNGCWDGVDydPETSDDYLessdyd 347
Cdd:cd14054    1 QLIGQGRYGTVWKGS--LDERPVAVKVFPARHRQnfqNEKDIYELPLMEHSNILRFIGADERPT--ADGRMEYL------ 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 pensknssrsktkclfIQMEFCDKGTLEQWIenrRGEKLDKVLALELFEQITKGVDYIHSKKLI---------HRDLKPS 418
Cdd:cd14054   71 ----------------LVLEYAPKGSLCSYL---RENTLDWMSSCRMALSLTRGLAYLHTDLRRgdqykpaiaHRDLNSR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSLK-NDGKRTRSK----------GTLRYMSPEQI-------SSQDYGKEVDLYALGLILAE 480
Cdd:cd14054  132 NVLVKADGSCVICDFGLAMVLRgSSLVRGRPGaaenasisevGTLRYMAPEVLegavnlrDCESALKQVDVYALGLVLWE 211

                 ....*
gi 525343631 481 LLHVC 485
Cdd:cd14054  212 IAMRC 216
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
271-482 4.99e-17

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 81.39  E-value: 4.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIK-------RVKYNNEKAEREVK-ALAKLDHVNIVhYNGCWDGVDydpetsddyle 342
Cdd:cd14025    2 EKVGSGGFGQVYKVRHKHWKTWLAIKcppslhvDDSERMELLEEAKKmEMAKFRHILPV-YGICSEPVG----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssrsktkclfIQMEFCDKGTLEQWIENrrgEKLDKVLALELFEQITKGVDYIHSKK--LIHRDLKPSNI 420
Cdd:cd14025   70 ---------------------LVMEYMETGSLEKLLAS---EPLPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANI 125
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 421 FLVDTKQVKIGDFGLVT----SLKNDGKRTRSKGTLRYMSPEQI--SSQDYGKEVDLYALGLILAELL 482
Cdd:cd14025  126 LLDAHYHVKISDFGLAKwnglSHSHDLSRDGLRGTIAYLPPERFkeKNRCPDTKHDVYSFAIVIWGIL 193
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
266-534 5.01e-17

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: 81.23  E-value: 5.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIelIGSGGFGQVFKAKHRIDGKTYVIK----RVKYNNEKA-EREVKALAKLDHVNIVhyngcwdgvdydpeTSDDY 340
Cdd:cd14167    6 DFREV--LGTGAFSEVVLAEEKRTQKLVAIKciakKALEGKETSiENEIAVLHKIKHPNIV--------------ALDDI 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSDYdpensknssrsktkcLFIQMEFCDKGTL-EQWIENRRGEKLDkvlALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14167   70 YESGGH---------------LYLIMQLVSGGELfDRIVEKGFYTERD---ASKLIFQILDAVKYLHDMGIVHRDLKPEN 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IF---LVDTKQVKIGDFGLvTSLKNDGK-RTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFET--SK 493
Cdd:cd14167  132 LLyysLDEDSKIMISDFGL-SKIEGSGSvMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEndAK 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 525343631 494 FFTDLR------DGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14167  211 LFEQILkaeyefDSPYWDDISDSAKDFIQHLMEKDPEKRFTCEQALQ 257
DSRM_EIF2AK2 cd20314
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
8-59 5.14e-17

double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. EIF2AK2 proteins contain two to three double-stranded RNA binding motifs (DSRMs). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380746  Cd Length: 68  Bit Score: 75.51  E-value: 5.14e-17
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631   8 GFFMEELNTYRQKQGVVLKYQELPNSGPPHDRRFTFRVIIDEREFPEGEGRS 59
Cdd:cd20314    1 GNYVSLLNEYCQKERLTVKYEEEKRSGPTHKPRFFCKYIIDGKEYPEGEGKS 52
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
267-526 5.23e-17

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


Pssm-ID: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 81.61  E-value: 5.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV-KYNNEKAEREVKALAK---LDHVN---IVhyngcwdGVDYDPETSDd 339
Cdd:cd05630    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKKLeKKRIKKRKGEAMALNEkqiLEKVNsrfVV-------SLAYAYETKD- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknssrskTKCLFIQMefCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd05630   74 -------------------ALCLVLTL--MNGGDLKFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPEN 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHvCDTAF---------- 489
Cdd:cd05630  133 ILLDDHGHIRISDLGLAVHVPEGQTIKGRVGTVGYMAPEVVKNERYTFSPDWWALGCLLYEMIA-GQSPFqqrkkkikre 211
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 525343631 490 ETSKFFTDLRDGiISDIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05630  212 EVERLVKEVPEE-YSEKFSPQARSLCSMLLCKDPAER 247
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
266-533 5.93e-17

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: 81.32  E-value: 5.93e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREvKALAKLD-------HVNIVHYNG----------CWD 328
Cdd:cd06617    2 DLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATVNSQEQK-RLLMDLDismrsvdCPYTVTFYGalfregdvwiCME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 329 GVDydpeTSDDYLESSDYDPEnsknssrsktkcLFIQMEFCDKGTLeqwienrrgekldkvlalelfeQITKGVDYIHSK 408
Cdd:cd06617   81 VMD----TSLDKFYKKVYDKG------------LTIPEDILGKIAV----------------------SIVKALEYLHSK 122
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 409 -KLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQI----SSQDYGKEVDLYALGLILAELlh 483
Cdd:cd06617  123 lSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVDSVAKTIDAGCKPYMAPERInpelNQKGYDVKSDVWSLGITMIEL-- 200
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 484 vcdtafETSKF--------FTDLRD-------GIISDIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd06617  201 ------ATGRFpydswktpFQQLKQvveepspQLPAEKFSPEFQDFVNKCLKKNYKERPNYPELL 259
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
268-536 6.59e-17

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: 80.97  E-value: 6.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 268 KEIELIGSGGFGQVF--KAKHRIDGKTYVIKRVKYNNEKAE--------REVKALAKLDHVNIVHYNG-Cwdgvdydpet 336
Cdd:cd05046    8 QEITTLGRGEFGEVFlaKAKGIEEEGGETLVLVKALQKTKDenlqsefrRELDMFRKLSHKNVVRLLGlC---------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddylesSDYDPEnsknssrsktkclFIQMEFCDKGTLEQW-------IENRRGEKLDKVLALELFEQITKGVDYIHSKK 409
Cdd:cd05046   78 -------REAEPH-------------YMILEYTDLGDLKQFlratkskDEKLKPPPLSTKQKVALCTQIALGMDHLSNAR 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 410 LIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDG--KRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELlhvcdt 487
Cdd:cd05046  138 FVHRDLAARNCLVSSQREVKVSLLSLSKDVYNSEyyKLRNALIPLRWLAPEAVQEDDFSTKSDVWSFGVLMWEV------ 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 488 aFETSKF-FTDLRD-GIISDIFDKKEK--------TLLQKLLSK----KPEDRPNTSEILRTL 536
Cdd:cd05046  212 -FTQGELpFYGLSDeEVLNRLQAGKLElpvpegcpSRLYKLMTRcwavNPKDRPSFSELVSAL 273
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
271-534 6.60e-17

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: 81.14  E-value: 6.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKL-DHVNIVhyngcwdgvdydpeTSDDYlessdYDPE 349
Cdd:cd14091    6 EEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDPSEEIEILLRYgQHPNII--------------TLRDV-----YDDG 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 350 NSknssrsktkcLFIQMEFCdkgtleqwienRRGEKLDKVLALELF-EQ--------ITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd14091   67 NS----------VYLVTELL-----------RGGELLDRILRQKFFsEReasavmktLTKTVEYLHSQGVVHRDLKPSNI 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 421 FLVDTKQ----VKIGDFGLVTSLKNDgkrtrsKG-------TLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCdTAF 489
Cdd:cd14091  126 LYADESGdpesLRICDFGFAKQLRAE------NGllmtpcyTANFVAPEVLKKQGYDAACDIWSLGVLLYTMLAGY-TPF 198
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 490 ETSKffTDLRDGIISDIFDKK--------------EKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14091  199 ASGP--NDTPEVILARIGSGKidlsggnwdhvsdsAKDLVRKMLHVDPSQRPTAAQVLQ 255
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
267-495 6.64e-17

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


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 81.09  E-value: 6.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAkhRID------GKTYVIKRVKYNNEKA----EREVKALAKLDHVNIVHYNGcwdgVDYDPet 336
Cdd:cd05081    6 LKYISQLGKGNFGSVELC--RYDplgdntGALVAVKQLQHSGPDQqrdfQREIQILKALHSDFIVKYRG----VSYGP-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddylessdydpensknSSRSktkcLFIQMEFCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd05081   78 -----------------GRRS----LRLVMEYLPSGCLRDFLQRHR-ARLDASRLLLYSSQICKGMEYLGSRRCVHRDLA 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLKNDGK----RTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETS 492
Cdd:cd05081  136 ARNILVESEAHVKIADFGLAKLLPLDKDyyvvREPGQSPIFWYAPESLSDNIFSRQSDVWSFGVVLYELFTYCDKSCSPS 215

                 ...
gi 525343631 493 KFF 495
Cdd:cd05081  216 AEF 218
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
272-548 8.65e-17

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


Pssm-ID: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 81.01  E-value: 8.65e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAkhRIDGKTYVIKR------VKYNNEKA--EREVKALAKLDHVNIVHYNGCwdgvdydpetsddyleS 343
Cdd:cd14158   22 KLGEGGFGVVFKG--YINDKNVAVKKlaamvdISTEDLTKqfEQEIQVMAKCQHENLVELLGY----------------S 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 SDYDPensknssrsktKCLFiqMEFCDKGTLEQwienrRGEKLDKVLALELFEQI------TKGVDYIHSKKLIHRDLKP 417
Cdd:cd14158   84 CDGPQ-----------LCLV--YTYMPNGSLLD-----RLACLNDTPPLSWHMRCkiaqgtANGINYLHENNHIHRDIKS 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSLKNDGKR---TRSKGTLRYMSPEQISSQDYGKEvDLYALGLILAELLHVCdTAFETSKF 494
Cdd:cd14158  146 ANILLDETFVPKISDFGLARASEKFSQTimtERIVGTTAYMAPEALRGEITPKS-DIFSFGVVLLEIITGL-PPVDENRD 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 525343631 495 FTDLRDgIISDIFDkKEKTLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEKNER 548
Cdd:cd14158  224 PQLLLD-IKEEIED-EEKTIEDYVDKKMGDWDSTSIEAMYSVASQCLNDKKNRR 275
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
271-526 8.86e-17

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: 81.49  E-value: 8.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN---------NEKAEREVKALAKlDHVNIVHYNGCWDGVDYdpetsddyl 341
Cdd:cd05590    1 RVLGKGSFGKVMLARLKESGRLYAVKVLKKDvilqdddveCTMTEKRILSLAR-NHPFLTQLYCCFQTPDR--------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdydpensknssrsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd05590   71 --------------------LFFVMEFVNGGDLMFHIQKSR--RFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVL 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhvCDTA-FETSK----FF 495
Cdd:cd05590  129 LDHEGHCKLADFGMCKEGIFNGKTTSTfCGTPDYIAPEILQEMLYGPSVDWWAMGVLLYEML--CGHApFEAENeddlFE 206
                        250       260       270
                 ....*....|....*....|....*....|..
gi 525343631 496 TDLRDGIISDIFDKKEKT-LLQKLLSKKPEDR 526
Cdd:cd05590  207 AILNDEVVYPTWLSQDAVdILKAFMTKNPTMR 238
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
271-482 9.13e-17

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: 80.93  E-value: 9.13e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN------EKAEREVKALAKLDHVNIVHYNgcwdgvdydpetsDDYLESS 344
Cdd:cd14086    7 EELGKGAFSVVRRCVQKSTGQEFAAKIINTKKlsardhQKLEREARICRLLKHPNIVRLH-------------DSISEEG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpensknssrsktkCLFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd14086   74 ----------------FHYLVFDLVTGGELFEDIVAR--EFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLAS 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 425 TKQ---VKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14086  136 KSKgaaVKLADFGLAIEVQGDQQAWFGfAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILL 197
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
266-483 1.07e-16

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: 81.60  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV------KYNNEK---AEREVkALAKLDHVNIVhyngcwdGVDYDPET 336
Cdd:cd05602    8 DFHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLqkkailKKKEEKhimSERNV-LLKNVKHPFLV-------GLHFSFQT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 SDDylessdydpensknssrsktkcLFIQMEFCDKGTLEQWIENRRG--EKLDKVLALElfeqITKGVDYIHSKKLIHRD 414
Cdd:cd05602   80 TDK----------------------LYFVLDYINGGELFYHLQRERCflEPRARFYAAE----IASALGYLHSLNIVYRD 133
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFLVDTKQVKIGDFGLVT-SLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLH 483
Cdd:cd05602  134 LKPENILLDSQGHIVLTDFGLCKeNIEPNGTTSTFCGTPEYLAPEVLHKQPYDRTVDWWCLGAVLYEMLY 203
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
267-526 1.16e-16

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


Pssm-ID: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 80.48  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIK-----RVKynNEKAER----EVKALAKLDHVNIVHyngcwdgVDYDPETS 337
Cdd:cd05605    2 FRQYRVLGKGGFGEVCACQVRATGKMYACKklekkRIK--KRKGEAmalnEKQILEKVNSRFVVS-------LAYAYETK 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 DdylessdydpensknssrskTKCLFIQMefCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd05605   73 D--------------------ALCLVLTI--MNGGDLKFHIYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKP 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSLKnDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELL-------------- 482
Cdd:cd05605  131 ENILLDDHGHVRISDLGLAVEIP-EGETIRGRvGTVGYMAPEVVKNERYTFSPDWWGLGCLIYEMIegqapfrarkekvk 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 525343631 483 ------HVCDTAFETSKFFTDlrdgiisdifdkKEKTLLQKLLSKKPEDR 526
Cdd:cd05605  210 reevdrRVKEDQEEYSEKFSE------------EAKSICSQLLQKDPKTR 247
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
266-482 1.69e-16

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


Pssm-ID: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 80.56  E-value: 1.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKA-----EREVKALAKLDHVNIVHYNGCWdgvdYDpetsddy 340
Cdd:cd06615    2 DFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLEIKPAirnqiIRELKVLHECNSPYIVGFYGAF----YS------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdyDPENSknssrsktkclfIQMEFCDKGTLEQwIENRRGEKLDKVLAlELFEQITKGVDYIHSK-KLIHRDLKPSN 419
Cdd:cd06615   71 ------DGEIS------------ICMEHMDGGSLDQ-VLKKAGRIPENILG-KISIAVLRGLTYLREKhKIMHRDVKPSN 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 420 IFLVDTKQVKIGDFG----LVTSLKNDGKRTRSkgtlrYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd06615  131 ILVNSRGEIKLCDFGvsgqLIDSMANSFVGTRS-----YMSPERLQGTHYTVQSDIWSLGLSLVEMA 192
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
267-533 1.70e-16

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 80.17  E-value: 1.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKH-RIDGKTYVIKRVK------YNNEKAER-----EVKALAKLDHVNIVHYNgcwdgvdydp 334
Cdd:cd14096    3 YRLINKIGEGAFSNVYKAVPlRNTGKPVAIKVVRkadlssDNLKGSSRanilkEVQIMKRLSHPNIVKLL---------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 335 etsdDYLESSDYdpensknssrsktkCLFIQmEFCDKGTLEQWIEnrRGEKLDKVLALELFEQITKGVDYIHSKKLIHRD 414
Cdd:cd14096   73 ----DFQESDEY--------------YYIVL-ELADGGEIFHQIV--RLTYFSEDLSRHVITQVASAVKYLHEIGVVHRD 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFL---------------------VDTK------------QVKIGDFGLVTSLKNDGKRTRSkGTLRYMSPEQIS 461
Cdd:cd14096  132 IKPENLLFepipfipsivklrkadddetkVDEGefipgvggggigIVKLADFGLSKQVWDSNTKTPC-GTVGYTAPEVVK 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 462 SQDYGKEVDLYALGLILAELLhvC------DTAFET---------SKFFTDLRDGIISDifdkkEKTLLQKLLSKKPEDR 526
Cdd:cd14096  211 DERYSKKVDMWALGCVLYTLL--CgfppfyDESIETltekisrgdYTFLSPWWDEISKS-----AKDLISHLLTVDPAKR 283

                 ....*..
gi 525343631 527 PNTSEIL 533
Cdd:cd14096  284 YDIDEFL 290
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
271-533 1.90e-16

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: 80.28  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN---------EKAEREVKALAKLDHVNIVhyngcwdgvdydpETSDDYl 341
Cdd:cd14094    9 EVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKftsspglstEDLKREASICHMLKHPHIV-------------ELLETY- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 eSSDYdpensknssrsktkCLFIQMEFCDKGTLEQWIENR--RGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14094   75 -SSDG--------------MLYMVFEFMDGADLCFEIVKRadAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHC 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQ---VKIGDFGLVTSLKNDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCdTAFETSKff 495
Cdd:cd14094  140 VLLASKENsapVKLGGFGVAIQLGESGLVAGGRvGTPHFMAPEVVKREPYGKPVDVWGCGVILFILLSGC-LPFYGTK-- 216
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 525343631 496 TDLRDGIISDIFDKK----------EKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14094  217 ERLFEGIIKGKYKMNprqwshisesAKDLVRRMLMLDPAERITVYEAL 264
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
266-482 1.92e-16

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: 79.69  E-value: 1.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEI---ELIGSGGFGQVFKAKHRidGKTYVIKRVKYN--------NEKAEREVKALAKLDHVNIVHYNG-Cwdgvdyd 333
Cdd:cd14147    1 SFQELrleEVIGIGGFGKVYRGSWR--GELVAVKAARQDpdedisvtAESVRQEARLFAMLAHPNIIALKAvC------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 334 petsddyLESSDYdpensknssrsktkCLFiqMEFCDKGTLEQWIENRRgekLDKVLALELFEQITKGVDYIHSKKL--- 410
Cdd:cd14147   72 -------LEEPNL--------------CLV--MEYAAGGPLSRALAGRR---VPPHVLVNWAVQIARGMHYLHCEALvpv 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 411 IHRDLKPSNIFL--------VDTKQVKIGDFGLVTSLKNDGKRTrSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14147  126 IHRDLKSNNILLlqpienddMEHKTLKITDFGLAREWHKTTQMS-AAGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELL 204
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
273-533 1.97e-16

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: 80.03  E-value: 1.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIK----RVKYNNEKAEREVKALAKLDHVNIVhyngcwdgvdydpETSDDYLESSDydp 348
Cdd:cd06659   29 IGEGSTGVVCIAREKHSGRQVAVKmmdlRKQQRRELLFNEVVIMRDYQHPNVV-------------EMYKSYLVGEE--- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 349 ensknssrsktkcLFIQMEFCDKGTLEQWIENRRgekLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQV 428
Cdd:cd06659   93 -------------LWVLMEYLQGGALTDIVSQTR---LNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 429 KIGDFGLVTSLKND-GKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL-----HVCDTAFETSKFFTD----- 497
Cdd:cd06659  157 KLSDFGFCAQISKDvPKRKSLVGTPYWMAPEVISRCPYGTEVDIWSLGIMVIEMVdgeppYFSDSPVQAMKRLRDspppk 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 525343631 498 LRDG-IISDIFdkkeKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd06659  237 LKNShKASPVL----RDFLERMLVRDPQERATAQELL 269
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
381-534 2.01e-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: 80.07  E-value: 2.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 381 RRGEKLDKVLALELFEQ---------ITKGVDYIHSKKLIHRDLKPSNIFLVDT----KQVKIGDFGLVTSLKND-GKRT 446
Cdd:cd14175   78 RGGELLDKILRQKFFSEreassvlhtICKTVEYLHSQGVVHRDLKPSNILYVDEsgnpESLRICDFGFAKQLRAEnGLLM 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 447 RSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVC--------DTAFET-----SKFFTdLRDGIISDIFDKKeKT 513
Cdd:cd14175  158 TPCYTANFVAPEVLKRQGYDEGCDIWSLGILLYTMLAGYtpfangpsDTPEEIltrigSGKFT-LSGGNWNTVSDAA-KD 235
                        170       180
                 ....*....|....*....|.
gi 525343631 514 LLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14175  236 LVSKMLHVDPHQRLTAKQVLQ 256
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
270-482 2.41e-16

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: 79.23  E-value: 2.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNE---KAEREVKALAKLdhvnivhyngcwdgvdydpetsddylesSDY 346
Cdd:cd14133    4 LEVLGKGTFGQVVKCYDLLTGEEVALKIIKNNKDyldQSLDEIRLLELL----------------------------NKK 55
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 DPENSKNSSRSKT-----KCLFIQMEFCDKgTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd14133   56 DKADKYHIVRLKDvfyfkNHLCIVFELLSQ-NLYEFLKQNKFQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENIL 134
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 422 LV--DTKQVKIGDFGLVTSLkNDGKRT----RSkgtlrYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14133  135 LAsySRCQIKIIDFGSSCFL-TQRLYSyiqsRY-----YRAPEVILGLPYDEKIDMWSLGCILAELY 195
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
266-536 2.43e-16

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 80.04  E-value: 2.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDG--KTYVIKRVK-YNNEKAER----EVKALAKLD-HVNIVHYNGCWDGVDYDpets 337
Cdd:cd05088    8 DIKFQDVIGEGNFGQVLKARIKKDGlrMDAAIKRMKeYASKDDHRdfagELEVLCKLGhHPNIINLLGACEHRGYL---- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 ddYLeSSDYDPENSKNSSRSKTKCLFIQMEFCdkgtleqwIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd05088   84 --YL-AIEYAPHGNLLDFLRKSRVLETDPAFA--------IANSTASTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAA 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAF---ETSKF 494
Cdd:cd05088  153 RNILVGENYVAKIADFGLSRGQEVYVKKTMGRLPVRWMAIESLNYSVYTTNSDVWSYGVLLWEIVSLGGTPYcgmTCAEL 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 525343631 495 FTDLRDGIISDI---FDKKEKTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd05088  233 YEKLPQGYRLEKplnCDDEVYDLMRQCWREKPYERPSFAQILVSL 277
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
266-484 2.47e-16

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: 79.69  E-value: 2.47e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEI--ELiGSGGFGQVFKAKHRidgKTYVIKRVKYNNEKAERE-------VKALAKLDHVNIVhyngcwdgvdydpet 336
Cdd:cd06643    5 DFWEIvgEL-GDGAFGKVYKAQNK---ETGILAAAKVIDTKSEEEledymveIDILASCDHPNIV--------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sdDYLESSDYdpENSknssrsktkcLFIQMEFCDKGTLEQW---IENRRGEKLDKVLAlelfEQITKGVDYIHSKKLIHR 413
Cdd:cd06643   66 --KLLDAFYY--ENN----------LWILIEFCAGGAVDAVmleLERPLTEPQIRVVC----KQTLEALVYLHENKIIHR 127
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 414 DLKPSNIFLVDTKQVKIGDFGLvtSLKND---GKRTRSKGTLRYMSPEQI---SSQD--YGKEVDLYALGLILAELLHV 484
Cdd:cd06643  128 DLKAGNILFTLDGDIKLADFGV--SAKNTrtlQRRDSFIGTPYWMAPEVVmceTSKDrpYDYKADVWSLGVTLIEMAQI 204
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
272-526 2.67e-16

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: 79.92  E-value: 2.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRIDGKTYVIK---------RVKYNNEKAEREVkaLAKLDHVNIVHYngcwdgvdydpetsddyle 342
Cdd:cd05585    1 VIGKGSFGKVMQVRKKDTSRIYALKtirkahivsRSEVTHTLAERTV--LAQVDCPFIVPL------------------- 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensKNSSRSKTKcLFIQMEFCDKGTLEQWIEnrRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd05585   60 ---------KFSFQSPEK-LYLVLAFINGGELFHHLQ--REGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILL 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLVT-SLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL------HVCDTAFETSKFF 495
Cdd:cd05585  128 DYTGHIALCDFGLCKlNMKDDDKTNTFCGTPEYLAPELLLGHGYTKAVDWWTLGVLLYEMLtglppfYDENTNEMYRKIL 207
                        250       260       270
                 ....*....|....*....|....*....|..
gi 525343631 496 TD-LRdgiISDIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05585  208 QEpLR---FPDGFDRDAKDLLIGLLNRDPTKR 236
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
273-531 2.89e-16

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 79.48  E-value: 2.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRidGKTYVIKRVKYNNE--------KAEREVKALAKLDHVNIVHYNG-CWDGVDYdpetsddyles 343
Cdd:cd14159    1 IGEGGFGCVYQAVMR--NTEYAVKRLKEDSEldwsvvknSFLTEVEKLSRFRHPNIVDLAGySAQQGNY----------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 sdydpensknssrsktkCLFIQmeFCDKGTLEQWIENR-RGEKLDKVLALELFEQITKGVDYIH--SKKLIHRDLKPSNI 420
Cdd:cd14159   68 -----------------CLIYV--YLPNGSLEDRLHCQvSCPCLSWSQRLHVLLGTARAIQYLHsdSPSLIHGDVKSSNI 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 421 FLVDTKQVKIGDFGLV---TSLKNDGK-----RTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAFET 491
Cdd:cd14159  129 LLDAALNPKLGDFGLArfsRRPKQPGMsstlaRTQTvRGTLAYLPEEYVKTGTLSVEIDVYSFGVVLLELL-TGRRAMEV 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 525343631 492 skfftdlrdgiisdifDKKEKTLLQKLLSKKPEDRPNTSE 531
Cdd:cd14159  208 ----------------DSCSPTKYLKDLVKEEEEAQHTPT 231
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
270-482 3.16e-16

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: 79.51  E-value: 3.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIKRVKyNNEK----AEREVKALAKL------DHVNIVHYNgcwdgvdydpetsdD 339
Cdd:cd14210   18 LSVLGKGSFGQVVKCLDHKTGQLVAIKIIR-NKKRfhqqALVEVKILKHLndndpdDKHNIVRYK--------------D 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLESSDYdpensknssrsktkcLFIQMEFCDKgTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14210   83 SFIFRGH---------------LCIVFELLSI-NLYELLKSNNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPEN 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 420 IFL--VDTKQVKIGDFGlvtSLKNDGKRTRSKGTLR-YMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14210  147 ILLkqPSKSSIKVIDFG---SSCFEGEKVYTYIQSRfYRAPEVILGLPYDTAIDMWSLGCILAELY 209
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
266-534 3.31e-16

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: 80.13  E-value: 3.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNivhyngcwdgvdydPETSDDYLESSD 345
Cdd:cd05593   16 DFDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDEVAHTLTESRVL--------------KNTRHPFLTSLK 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YdpensknSSRSKTKCLFIqMEFCDKGTLEQWIENRRGEKLDKVLALElfEQITKGVDYIHSKKLIHRDLKPSNIFLVDT 425
Cdd:cd05593   82 Y-------SFQTKDRLCFV-MEYVNGGELFFHLSRERVFSEDRTRFYG--AEIVSALDYLHSGKIVYRDLKLENLMLDKD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAEL----LHVCDTAFETSKFFTDLRD 500
Cdd:cd05593  152 GHIKITDFGLCKEGITDAATMKTfCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMmcgrLPFYNQDHEKLFELILMED 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 525343631 501 GIISDIFDKKEKTLLQKLLSKKPEDR-----PNTSEILR 534
Cdd:cd05593  232 IKFPRTLSADAKSLLSGLLIKDPNKRlgggpDDAKEIMR 270
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
267-483 3.65e-16

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: 79.35  E-value: 3.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK-----AEREVKALAKLDHVNIVHYNGcwdgVDYDPETSDDYL 341
Cdd:cd07869    7 YEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEgtpftAIREASLLKGLKHANIVLLHD----IIHTKETLTLVF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 EssdydpensknssrsktkclFIQMEFCdkgtleQWIENRRGEKLDKVLALELFeQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd07869   83 E--------------------YVHTDLC------QYMDKHPGGLHPENVKLFLF-QLLRGLSYIHQRYILHRDLKPQNLL 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 422 LVDTKQVKIGDFGLVTSlKNDGKRTRSKG--TLRYMSPE-QISSQDYGKEVDLYALGLILAELLH 483
Cdd:cd07869  136 ISDTGELKLADFGLARA-KSVPSHTYSNEvvTLWYRPPDvLLGSTEYSTCLDMWGVGCIFVEMIQ 199
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
271-482 3.71e-16

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: 78.62  E-value: 3.71e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKA--KHRIDGKTYV-IKRVKYNNEKAEREvKALA------KLDHVNIVHYNG-CWDgvdydpetsddy 340
Cdd:cd05056   12 RCIGEGQFGDVYQGvyMSPENEKIAVaVKTCKNCTSPSVRE-KFLQeayimrQFDHPHIVKLIGvITE------------ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdyDPensknssrsktkcLFIQMEFCDKGTLEQWIENRRgEKLDkVLALELFE-QITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd05056   79 ------NP-------------VWIVMELAPLGELRSYLQVNK-YSLD-LASLILYAyQLSTALAYLESKRFVHRDIAARN 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05056  138 VLVSSPDCVKLGDFGLSRYMEDESYYKASKGKLpiKWMAPESINFRRFTSASDVWMFGVCMWEIL 202
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
272-536 3.77e-16

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: 78.81  E-value: 3.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRidGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHynGCWDGVDYDPETSddyLESSDYDPeNS 351
Cdd:cd14000    1 LLGDGGFGSVYRASYK--GEPVAVKIFNKHTSSNFANVPADTMLRHLRATD--AMKNFRLLRQELT---VLSHLHHP-SI 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 352 KNSSRSKTKCLFIQMEFCDKGTLEQWI-ENRR-GEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQ-- 427
Cdd:cd14000   73 VYLLGIGIHPLMLVLELAPLGSLDHLLqQDSRsFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPns 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 428 ---VKIGDFGLVTSLKNDGKRTrSKGTLRYMSPEQIS-SQDYGKEVDLYALGLILAELLHVCDTAFETSKF--FTDLRDG 501
Cdd:cd14000  153 aiiIKIADYGISRQCCRMGAKG-SEGTPGFRAPEIARgNVIYNEKVDVFSFGMLLYEILSGGAPMVGHLKFpnEFDIHGG 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 525343631 502 IISDIFDKKE------KTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd14000  232 LRPPLKQYECapwpevEVLMKKCWKENPQQRPTAVTVVSIL 272
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
267-481 3.80e-16

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: 79.28  E-value: 3.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK-----AEREVKALAKLDHVNIVhyngcwdgvdydpeTSDDYL 341
Cdd:cd07873    4 YIKLDKLGEGTYATVYKGRSKLTDNLVALKEIRLEHEEgapctAIREVSLLKDLKHANIV--------------TLHDII 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ESSdydpensknssrsktKCLFIQMEFCDKgTLEQWIENRRGEKLDKVLALELFeQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd07873   70 HTE---------------KSLTLVFEYLDK-DLKQYLDDCGNSINMHNVKLFLF-QLLRGLAYCHRRKVLHRDLKPQNLL 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 422 LVDTKQVKIGDFGLVTSlKNDGKRTRSKG--TLRYMSPE-QISSQDYGKEVDLYALGLILAEL 481
Cdd:cd07873  133 INERGELKLADFGLARA-KSIPTKTYSNEvvTLWYRPPDiLLGSTDYSTQIDMWGVGCIFYEM 194
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
266-481 3.89e-16

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: 78.77  E-value: 3.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN-----NEKAEREVKALAKLDHVNIVHYNGCWdgvdydpetsddY 340
Cdd:cd06619    2 DIQYQEILGHGNGGTVYKAYHLLTRRILAVKVIPLDitvelQKQIMSELEILYKCDSPYIIGFYGAF------------F 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSdydpensknssrsktkcLFIQMEFCDKGTLEQWienrrGEKLDKVLAlELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd06619   70 VENR-----------------ISICTEFMDGGSLDVY-----RKIPEHVLG-RIAVAVVKGLTYLWSLKILHRDVKPSNM 126
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 421 fLVDTK-QVKIGDFGLVTSLKNDGKRTRSkGTLRYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd06619  127 -LVNTRgQVKLCDFGVSTQLVNSIAKTYV-GTNAYMAPERISGEQYGIHSDVWSLGISFMEL 186
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
271-486 3.92e-16

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: 78.91  E-value: 3.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDgktYVIKRVKYNNEKA----EREVKALAKLDHVNIVHYngcwdgVDYDPETSDDYLEssdy 346
Cdd:cd14053    1 EIKARGRFGAVWKAQYLNR---LVAVKIFPLQEKQswltEREIYSLPGMKHENILQF------IGAEKHGESLEAE---- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 dpensknssrsktkcLFIQMEFCDKGTLEQWIENRrgeKLDKVLALELFEQITKGVDYIHS---------KKLI-HRDLK 416
Cdd:cd14053   68 ---------------YWLITEFHERGSLCDYLKGN---VISWNELCKIAESMARGLAYLHEdipatngghKPSIaHRDFK 129
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSK---GTLRYMSPE----QIS-SQDYGKEVDLYALGLILAELLHVCD 486
Cdd:cd14053  130 SKNVLLKSDLTACIADFGLALKFEPGKSCGDTHgqvGTRRYMAPEvlegAINfTRDAFLRIDMYAMGLVLWELLSRCS 207
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
266-526 3.94e-16

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 79.58  E-value: 3.94e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN---------NEKAEREVKALAkLDHVNIVHyngcwdgvdydpet 336
Cdd:cd05619    6 DFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKKDvvlmdddveCTMVEKRVLSLA-WEHPFLTH-------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddyLESSDYDPENsknssrsktkcLFIQMEFCDKGTLEQWIENrrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd05619   71 ----LFCTFQTKEN-----------LFFVMEYLNGGDLMFHIQS--CHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLK 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVT-SLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAF---ETS 492
Cdd:cd05619  134 LDNILLDKDGHIKIADFGMCKeNMLGDAKTSTFCGTPDYIAPEILLGQKYNTSVDWWSFGVLLYEML-IGQSPFhgqDEE 212
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 525343631 493 KFFTDLR--DGIISDIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05619  213 ELFQSIRmdNPFYPRWLEKEAKDILVKLFVREPERR 248
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
273-536 3.97e-16

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: 79.11  E-value: 3.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHR--IDGKTYVIKRVKYNNEKA--------EREVKALAKLDHVNIVHYNG-CWDG------VDY-DP 334
Cdd:cd05050   13 IGQGAFGRVFQARAPglLPYEPFTMVAVKMLKEEAsadmqadfQREAALMAEFDHPNIVKLLGvCAVGkpmcllFEYmAY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 335 ETSDDYLESSDydPENSKNSSRSKTKCLFIQMEFCDKGTLEQwienrrgekldkvlaLELFEQITKGVDYIHSKKLIHRD 414
Cdd:cd05050   93 GDLNEFLRHRS--PRAQCSLSHSTSSARKCGLNPLPLSCTEQ---------------LCIAKQVAAGMAYLSERKFVHRD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTL---RYMSPEQISSQDYGKEVDLYALGLILAELLhvcdtAFET 491
Cdd:cd05050  156 LATRNCLVGENMVVKIADFGLSRNIYSADYYKASENDAipiRWMPPESIFYNRYTTESDVWAYGVVLWEIF-----SYGM 230
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 492 SKFFT--------DLRDGII--------SDIFDkkektLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd05050  231 QPYYGmaheeviyYVRDGNVlscpdncpLELYN-----LMRLCWSKLPSDRPSFASINRIL 286
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
273-536 4.00e-16

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


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 79.07  E-value: 4.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYV-----IKRVKYNNEKAER-----EVKALAKL-DHVNIVHYNG-Cwdgvdydpetsddy 340
Cdd:cd05055   43 LGAGAFGKVVEATAYGLSKSDAvmkvaVKMLKPTAHSSERealmsELKIMSHLgNHENIVNLLGaC-------------- 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpensknssrSKTKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd05055  109 ----------------TIGGPILVITEYCCYGDLLNFLRRKRESFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 421 FLVDTKQVKIGDFGLVTSLKNDGKRTrSKGT----LRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFE----TS 492
Cdd:cd05055  173 LLTHGKIVKICDFGLARDIMNDSNYV-VKGNarlpVKWMAPESIFNCVYTFESDVWSYGILLWEIFSLGSNPYPgmpvDS 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 525343631 493 KFFTDLRDG--IISDIFDKKE-KTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd05055  252 KFYKLIKEGyrMAQPEHAPAEiYDIMKTCWDADPLKRPTFKQIVQLI 298
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
273-536 4.16e-16

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: 78.71  E-value: 4.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE----REVKALAKLD-HVNIVHYNGcwdGVDYDPETSD----DYLes 343
Cdd:cd14036    8 IAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNkaiiQEINFMKKLSgHPNIVQFCS---AASIGKEESDqgqaEYL-- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 sdydpensknssrsktkclfIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKK--LIHRDLKPSNIF 421
Cdd:cd14036   83 --------------------LLTELCKGQLVDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLL 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQVKIGDFGLVTSLK-------NDGKR-------TRSKgTLRYMSPEQI---SSQDYGKEVDLYALGLILAeLLHV 484
Cdd:cd14036  143 IGNQGQIKLCDFGSATTEAhypdyswSAQKRslvedeiTRNT-TPMYRTPEMIdlySNYPIGEKQDIWALGCILY-LLCF 220
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 485 CDTAFETSkffTDLRdgIISDIF-----DKKEKT---LLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd14036  221 RKHPFEDG---AKLR--IINAKYtippnDTQYTVfhdLIRSTLKVNPEERLSITEIVEQL 275
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
267-478 4.35e-16

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: 78.36  E-value: 4.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE-------REVKALAKLDHVNIVHYNGCWDGVDydpetsdd 339
Cdd:cd14164    2 YTLGTTIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDfvqkflpRELSILRRVNHPNIVQMFECIEVAN-------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknssrsktKCLFIQMEFCDKgTLEQWIEnrRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14164   74 --------------------GRLYIVMEAAAT-DLLQKIQ--EVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCEN 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 420 IFL-VDTKQVKIGDFGLVTSLKNDGK-RTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLIL 478
Cdd:cd14164  131 ILLsADDRKIKIADFGFARFVEDYPElSTTFCGSRAYTPPEVILGTPYdPKKYDVWSLGVVL 192
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
271-487 4.49e-16

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: 78.96  E-value: 4.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKT-YVIKRVK------YNNEKAEREVKALAKLDHVNIVHYngcwdgvdydpetsddyles 343
Cdd:cd14055    1 KLVGKGRFAEVWKAKLKQNASGqYETVAVKifpyeeYASWKNEKDIFTDASLKHENILQF-------------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 sdYDPENSKNSSRsKTKCLFiqMEFCDKGTLEQWIenrRGEKLDKVLALELFEQITKGVDYIHSKK---------LIHRD 414
Cdd:cd14055   61 --LTAEERGVGLD-RQYWLI--TAYHENGSLQDYL---TRHILSWEDLCKMAGSLARGLAHLHSDRtpcgrpkipIAHRD 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 415 LKPSNIFLVDTKQVKIGDFGLvtSLKNDGKRTRSK-------GTLRYMSPEQISS----QDYG--KEVDLYALGLILAEL 481
Cdd:cd14055  133 LKSSNILVKNDGTCVLADFGL--ALRLDPSLSVDElansgqvGTARYMAPEALESrvnlEDLEsfKQIDVYSMALVLWEM 210

                 ....*.
gi 525343631 482 LHVCDT 487
Cdd:cd14055  211 ASRCEA 216
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
266-535 4.62e-16

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


Pssm-ID: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 78.95  E-value: 4.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE-----REVKALAKL-DHVNIVHYNG-------CWdgvdy 332
Cdd:cd06616    7 DLKDLGEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDEKEqkrllMDLDVVMRSsDCPYIVKFYGalfregdCW----- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 333 dpetsddylessdydpensknssrsktkclfIQMEFCDKgTLEQWIEnRRGEKLDKVLALELFEQIT----KGVDYIHSK 408
Cdd:cd06616   82 -------------------------------ICMELMDI-SLDKFYK-YVYEVLDSVIPEEILGKIAvatvKALNYLKEE 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 409 -KLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQI----SSQDYGKEVDLYALGLILAELlh 483
Cdd:cd06616  129 lKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVDSIAKTRDAGCRPYMAPERIdpsaSRDGYDVRSDVWSLGITLYEV-- 206
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 484 vcdtafETSKF--------FTDLRDGIISD----------IFDKKEKTLLQKLLSKKPEDRPNTSEILRT 535
Cdd:cd06616  207 ------ATGKFpypkwnsvFDQLTQVVKGDppilsnseerEFSPSFVNFVNLCLIKDESKRPKYKELLKH 270
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
272-482 5.30e-16

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: 78.10  E-value: 5.30e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRidGKTYVIKRVKYNNEK-----AE---REVKALAKLDHVNIVHYNG-CWdgvdydpetsddyle 342
Cdd:cd14148    1 IIGVGGFGKVYKGLWR--GEEVAVKAARQDPDEdiavtAEnvrQEARLFWMLQHPNIIALRGvCL--------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssRSKTKCLFiqMEFCDKGTLEQWIEnrrGEKLDKVLALELFEQITKGVDYIHSKK---LIHRDLKPSN 419
Cdd:cd14148   64 -------------NPPHLCLV--MEYARGGALNRALA---GKKVPPHVLVNWAVQIARGMNYLHNEAivpIIHRDLKSSN 125
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 420 IFLVD--------TKQVKIGDFGLVTSLKNDGKRTrSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14148  126 ILILEpienddlsGKTLKITDFGLAREWHKTTKMS-AAGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELL 195
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
273-482 5.48e-16

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 79.42  E-value: 5.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE------------------REVKALAKLDHVNIVhyngcwdgvdydp 334
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNDvtkdrqlvgmcgihfttlRELKIMNEIKHENIM------------- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 335 ETSDDYLESSdydpensknssrsktkclFIQ--MEFCDkGTLEQWIEN--RRGEKLDKVLALelfeQITKGVDYIHSKKL 410
Cdd:PTZ00024  84 GLVDVYVEGD------------------FINlvMDIMA-SDLKKVVDRkiRLTESQVKCILL----QILNGLNVLHKWYF 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 411 IHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDG-KRTRSKG--------------TLRYMSPEQI-SSQDYGKEVDLYAL 474
Cdd:PTZ00024 141 MHRDLSPANIFINSKGICKIADFGLARRYGYPPySDTLSKDetmqrreemtskvvTLWYRAPELLmGAEKYHFAVDMWSV 220

                 ....*...
gi 525343631 475 GLILAELL 482
Cdd:PTZ00024 221 GCIFAELL 228
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
273-481 5.98e-16

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: 77.71  E-value: 5.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRidGKTYV-IKRVKYNNEKAE---REVKALAKLDHVNIVH-YNGCwdgvdydpetsddylesSDYD 347
Cdd:cd05034    3 LGAGQFGEVWMGVWN--GTTKVaVKTLKPGTMSPEaflQEAQIMKKLRHDKLVQlYAVC-----------------SDEE 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 PensknssrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQ 427
Cdd:cd05034   64 P-------------IYIVTELMSKGSLLDYLRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNV 130
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 428 VKIGDFGLVTSLKNDGKRTR--SKGTLRYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd05034  131 CKVADFGLARLIEDDEYTARegAKFPIKWTAPEAALYGRFTIKSDVWSFGILLYEI 186
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
367-533 6.18e-16

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


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 77.94  E-value: 6.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 367 EFCDKGTLEQWIENRRGEKLDKVLALELfeQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVT-----SLKN 441
Cdd:cd14111   79 EFCSGKELLHSLIDRFRYSEDDVVGYLV--QILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQsfnplSLRQ 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 442 DGKRTrskGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRdgIISDIFD---------KKEK 512
Cdd:cd14111  157 LGRRT---GTLEYMAPEMVKGEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAK--ILVAKFDafklypnvsQSAS 231
                        170       180
                 ....*....|....*....|.
gi 525343631 513 TLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14111  232 LFLKKVLSSYPWSRPTTKDCF 252
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
266-481 6.88e-16

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: 78.21  E-value: 6.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVkyNNEKAER---------EVKALAKLDHVNIVhyngcwdgvdydpet 336
Cdd:cd14209    2 DFDRIKTLGTGSFGRVMLVRHKETGNYYAMKIL--DKQKVVKlkqvehtlnEKRILQAINFPFLV--------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddYLESSDYDPENsknssrsktkcLFIQMEFCDKGtlEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd14209   65 ---KLEYSFKDNSN-----------LYMVMEYVPGG--EMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLK 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGLvtslkndGKRTRSK-----GTLRYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd14209  129 PENLLIDQQGYIKVTDFGF-------AKRVKGRtwtlcGTPEYLAPEIILSKGYNKAVDWWALGVLIYEM 191
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
267-482 7.31e-16

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: 78.84  E-value: 7.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV--KYNNE----KAEREVKALAKLDHVNIVhynGCWDGVDYDpETSDDY 340
Cdd:cd07880   17 YRDLKQVGSGAYGTVCSALDRRTGAKVAIKKLyrPFQSElfakRAYRELRLLKHMKHENVI---GLLDVFTPD-LSLDRF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lesSDYdpensknssrsktkclFIQMEF--CDKGTLeqwienRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd07880   93 ---HDF----------------YLVMPFmgTDLGKL------MKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPG 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 419 NIFLVDTKQVKIGDFGLvtSLKNDGKRTRSKGTLRYMSPEQISS-QDYGKEVDLYALGLILAELL 482
Cdd:cd07880  148 NLAVNEDCELKILDFGL--ARQTDSEMTGYVVTRWYRAPEVILNwMHYTQTVDIWSVGCIMAEML 210
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
272-482 7.40e-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: 77.57  E-value: 7.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRIDGKTYVIKRV--KYNNEKA-EREVKALAKLDHVNIVHyngcwdgvdydpetsddyLEssdydp 348
Cdd:cd14087    8 LIGRGSFSRVVRVEHRVTRQPYAIKMIetKCRGREVcESELNVLRRVRHTNIIQ------------------LI------ 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 349 ENSKNSSRsktkcLFIQMEFCDKGTL-EQWIENRRGEKLDKVLALELfeqITKGVDYIHSKKLIHRDLKPSNIFLVDTK- 426
Cdd:cd14087   64 EVFETKER-----VYMVMELATGGELfDRIIAKGSFTERDATRVLQM---VLDGVKYLHGLGITHRDLKPENLLYYHPGp 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 427 --QVKIGDFGLVTSLK--NDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14087  136 dsKIMITDFGLASTRKkgPNCLMKTTCGTPEYIAPEILLRKPYTQSVDMWAVGVIAYILL 195
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
261-482 7.59e-16

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 77.68  E-value: 7.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 261 KRFGMDFKEIELiGSGGFGQVFKAKHRIDGKT--YVIKRVKYNNEKAER-----EVKALAKLDHVNIVHYNGCwdgvdyd 333
Cdd:cd05115    1 KRDNLLIDEVEL-GSGNFGCVKKGVYKMRKKQidVAIKVLKQGNEKAVRdemmrEAQIMHQLDNPYIVRMIGV------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 334 petsddylessdydpensknssrSKTKCLFIQMEFCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHR 413
Cdd:cd05115   73 -----------------------CEAEALMLVMEMASGGPLNKFLSGKK-DEITVSNVVELMHQVSMGMKYLEEKNFVHR 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 414 DLKPSNIFLVDTKQVKIGDFGLVTSLKNDGK----RTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05115  129 DLAARNVLLVNQHYAKISDFGLSKALGADDSyykaRSAGKWPLKWYAPECINFRKFSSRSDVWSYGVTMWEAF 201
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
266-482 8.53e-16

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: 78.50  E-value: 8.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN---------NEKAEREVKALAKLDHVnIVHYNGCWDGVDYdpet 336
Cdd:cd05616    1 DFNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDvviqdddveCTMVEKRVLALSGKPPF-LTQLHSCFQTMDR---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddylessdydpensknssrsktkcLFIQMEFCDKGTLEQWIEnrRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd05616   76 -------------------------LYFVMEYVNGGDLMYHIQ--QVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLK 128
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05616  129 LDNVMLDSEGHIKIADFGMCKENIWDGVTTKTfCGTPDYIAPEIIAYQPYGKSVDWWAFGVLLYEML 195
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
266-534 9.90e-16

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: 77.35  E-value: 9.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIE-LIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKAlaKLDHVNIVHYNGCWDGVDYDPETSDdyless 344
Cdd:cd14191    2 DFYDIEeRLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQ--EISIMNCLHHPKLVQCVDAFEEKAN------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpensknssrsktkcLFIQMEFCDKGTLEQWIENRRGEkLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd14191   74 -----------------IVMVLEMVSGGELFERIIDEDFE-LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVN 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 T--KQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLH-----VCDTAFETSKFFT- 496
Cdd:cd14191  136 KtgTKIKLIDFGLARRLENAGSLKVLFGTPEFVAPEVINYEPIGYATDMWSIGVICYILVSglspfMGDNDNETLANVTs 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 525343631 497 ---DLRDGIISDIFDKKeKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14191  216 atwDFDDEAFDEISDDA-KDFISNLLKKDMKARLTCTQCLQ 255
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
267-482 1.05e-15

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: 78.38  E-value: 1.05e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN------NEKAEREVKALAKLDHVNIVHYngcwdgvdydpetSDDY 340
Cdd:cd07856   12 YSDLQPVGMGAFGLVCSARDQLTGQNVAVKKIMKPfstpvlAKRTYRELKLLKHLRHENIISL-------------SDIF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LessdydpensknssrSKTKCLFIQMEFcdKGT-LEQWIENRRgekLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd07856   79 I---------------SPLEDIYFVTEL--LGTdLHRLLTSRP---LEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSN 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 420 IFLVDTKQVKIGDFGLVTSlkNDGKRTRSKGTLRYMSPE-QISSQDYGKEVDLYALGLILAELL 482
Cdd:cd07856  139 ILVNENCDLKICDFGLARI--QDPQMTGYVSTRYYRAPEiMLTWQKYDVEVDIWSAGCIFAEML 200
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
271-526 1.06e-15

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: 78.12  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNivhyngcwdgvdydPETSDDYLESSDYdpen 350
Cdd:cd05595    1 KLLGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDEVAHTVTESRVL--------------QNTRHPFLTALKY---- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 351 sknSSRSKTKCLFIqMEFCDKGTLEQWIENRRGEKLDKvlALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKI 430
Cdd:cd05595   63 ---AFQTHDRLCFV-MEYANGGELFFHLSRERVFTEDR--ARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKI 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 431 GDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhvCDTAFETSKFFTDLRDGIISD---- 505
Cdd:cd05595  137 TDFGLCKEGITDGATMKTfCGTPEYLAPEVLEDNDYGRAVDWWGLGVVMYEMM--CGRLPFYNQDHERLFELILMEeirf 214
                        250       260
                 ....*....|....*....|...
gi 525343631 506 --IFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05595  215 prTLSPEAKSLLAGLLKKDPKQR 237
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
265-526 1.06e-15

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: 78.05  E-value: 1.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 265 MDFKEIELIGSGGFGQVFKAKHRIDGKTY---------VIKRVKYNNEKAEREVkaLAKLDHVNIVHYNGCwdgvdydpe 335
Cdd:cd05574    1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFamkvldkeeMIKRNKVKRVLTEREI--LATLDHPFLPTLYAS--------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 336 tsddyLESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDK----------VLALElfeqitkgvdYI 405
Cdd:cd05574   70 -----FQTSTH---------------LCFVMDYCPGGELFRLLQKQPGKRLPEevarfyaaevLLALE----------YL 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 406 HSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSL----------KNDGKRTRSK--------------------GTLRYM 455
Cdd:cd05574  120 HLLGFVYRDLKPENILLHESGHIMLTDFDLSKQSsvtpppvrksLRKGSRRSSVksieketfvaepsarsnsfvGTEEYI 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 456 SPEQISSQDYGKEVDLYALGLILAELLhvcdtaFETSKFFTDLRDGIISDIFDKK------------EKTLLQKLLSKKP 523
Cdd:cd05574  200 APEVIKGDGHGSAVDWWTLGILLYEML------YGTTPFKGSNRDETFSNILKKEltfpesppvsseAKDLIRKLLVKDP 273

                 ...
gi 525343631 524 EDR 526
Cdd:cd05574  274 SKR 276
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
271-537 1.12e-15

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


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 77.10  E-value: 1.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN-----NEKAEREVKALAKLDHVNIVHYNG-CWDgvdydpetsddyless 344
Cdd:cd05041    1 EKIGRGNFGDVYRGVLKPDNTEVAVKTCRETlppdlKRKFLQEARILKQYDHPNIVKLIGvCVQ---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpensknssrskTKCLFIQMEFCDKGTLEQWIEnRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd05041   65 --------------KQPIMIVMELVPGGSLLTFLR-KKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGE 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLvTSLKNDGKRTRSKGT----LRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAF------ETSKF 494
Cdd:cd05041  130 NNVLKISDFGM-SREEEDGEYTVSDGLkqipIKWTAPEALNYGRYTSESDVWSFGILLWEIFSLGATPYpgmsnqQTREQ 208
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 525343631 495 F-TDLR----DGIISDIFDkkektLLQKLLSKKPEDRPNTSEILRTLT 537
Cdd:cd05041  209 IeSGYRmpapELCPEAVYR-----LMLQCWAYDPENRPSFSEIYNELQ 251
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
267-434 1.18e-15

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


Pssm-ID: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 77.34  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN----EKAEREVKALAKLDHVNIVHYngcwdgVDYD--PETSDdy 340
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILCHSkedvKEAMREIENYRLFNHPNILRL------LDSQivKEAGG-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpensknssrskTKCLFIQMEFCDKGTLEQWIENRR--GEKLDKVLALELFEQITKGVDYIHS---KKLIHRDL 415
Cdd:cd13986   74 ------------------KKEVYLLLPYYKRGSLQDEIERRLvkGTFFPEDRILHIFLGICRGLKAMHEpelVPYAHRDI 135
                        170
                 ....*....|....*....
gi 525343631 416 KPSNIFLVDTKQVKIGDFG 434
Cdd:cd13986  136 KPGNVLLSEDDEPILMDLG 154
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
273-482 1.21e-15

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 76.91  E-value: 1.21e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIK-----RVKYNNEKAEREVKALAKLDHVNIVHYNgcwdgvdydpetsddylesSDYD 347
Cdd:cd14185    8 IGDGNFAVVKECRHWNENQEYAMKiidksKLKGKEDMIESEILIIKSLSHPNIVKLF-------------------EVYE 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 PEnsknssrsktKCLFIQMEFCDKGTL-EQWIENRRGEKLDKVLaleLFEQITKGVDYIHSKKLIHRDLKPSNIFLV--- 423
Cdd:cd14185   69 TE----------KEIYLILEYVRGGDLfDAIIESVKFTEHDAAL---MIIDLCEALVYIHSKHIVHRDLKPENLLVQhnp 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 424 -DTKQVKIGDFGLVTSLKndGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14185  136 dKSTTLKLADFGLAKYVT--GPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILL 193
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
267-533 1.44e-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: 76.61  E-value: 1.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN-----EKAEREVKALAKLDHVNIVHYngcwdgvdydpetsddyL 341
Cdd:cd14184    3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKccgkeHLIENEVSILRRVKHPNIIML-----------------I 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ESSDYDPEnsknssrsktkcLFIQMEFCDKGTLEQWI--ENRRGEKLDKVLALELfeqiTKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14184   66 EEMDTPAE------------LYLVMELVKGGDLFDAItsSTKYTERDASAMVYNL----ASALKYLHGLCIVHRDIKPEN 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVD----TKQVKIGDFGLVTSLknDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFF 495
Cdd:cd14184  130 LLVCEypdgTKSLKLGDFGLATVV--EGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNLQ 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 525343631 496 TDLRDGIIS----------DIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14184  208 EDLFDQILLgklefpspywDNITDSAKELISHMLQVNVEARYTAEQIL 255
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
271-538 1.53e-15

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


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 76.58  E-value: 1.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRiDGKTYVIKRVKYN-----NEKAEREVKALAKLDHVNIVHYNG-Cwdgvdydpetsddyless 344
Cdd:cd05085    2 ELLGKGNFGEVYKGTLK-DKTPVAVKTCKEDlpqelKIKFLSEARILKQYDHPNIVKLIGvC------------------ 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpensknssrSKTKCLFIQMEFCDKGTLEQWIENRRGE-KLDKVLALELfeQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd05085   63 ------------TQRQPIYIVMELVPGGDFLSFLRKKKDElKTKQLVKFSL--DAAAGMAYLESKNCIHRDLAARNCLVG 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 424 DTKQVKIGDFGLvtSLKNDGKRTRSKG----TLRYMSPEQISSQDYGKEVDLYALGLILAEL--LHVCDTAFETSK---- 493
Cdd:cd05085  129 ENNALKISDFGM--SRQEDDGVYSSSGlkqiPIKWTAPEALNYGRYSSESDVWSFGILLWETfsLGVCPYPGMTNQqare 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 525343631 494 -----FFTDLRDGIISDIFdkkekTLLQKLLSKKPEDRPNTSEILRTLTV 538
Cdd:cd05085  207 qvekgYRMSAPQRCPEDIY-----KIMQRCWDYNPENRPKFSELQKELAA 251
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
261-482 1.56e-15

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: 77.60  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 261 KRFGMDFKEIELiGSGGFGQVFKAKHRIDGKTYVIKRV-KYNNEKAEREVKALAKLD-HVNIVHYNgcwdgvdydpETSD 338
Cdd:cd14180    3 QCYELDLEEPAL-GEGSFSVCRKCRHRQSGQEYAVKIIsRRMEANTQREVAALRLCQsHPNIVALH----------EVLH 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 DYLESsdydpensknssrsktkclFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd14180   72 DQYHT-------------------YLVMELLRGGELLDRI--KKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPE 130
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 419 NIFLVDTKQ---VKIGDFGLVtslkndgkRTRSKG---------TLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14180  131 NILYADESDgavLKVIDFGFA--------RLRPQGsrplqtpcfTLQYAAPELFSNQGYDESCDLWSLGVILYTML 198
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
271-532 1.60e-15

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: 76.60  E-value: 1.60e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKR-VKYNNEK----AEREVKALAKLDHVNIVhyngcwdgvdydpETSDDYLESSD 345
Cdd:cd14088    7 QVIKTEEFCEIFRAKDKTTGKLYTCKKfLKRDGRKvrkaAKNEINILKMVKHPNIL-------------QLVDVFETRKE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YdpensknssrsktkclFIQMEFCDKGTLEQWIenrrgekLDKVLALE-----LFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd14088   74 Y----------------FIFLELATGREVFDWI-------LDQGYYSErdtsnVIRQVLEAVAYLHSLKIVHRNLKLENL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 421 FLVD---TKQVKIGDFGLvTSLKNdGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHvcdtafETSKFFTD 497
Cdd:cd14088  131 VYYNrlkNSKIVISDFHL-AKLEN-GLIKEPCGTPEYLAPEVVGRQRYGRPVDCWAIGVIMYILLS------GNPPFYDE 202
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 525343631 498 LRDgiisDIFDKKEKTLLQKLLSKKPE-DRPNTSEI 532
Cdd:cd14088  203 AEE----DDYENHDKNLFRKILAGDYEfDSPYWDDI 234
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
267-456 1.89e-15

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: 76.34  E-value: 1.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIK--RVKYNNEKAEREVKALAKL-DHVNI--VHYNGcwdgvdydpetsddyl 341
Cdd:cd14016    2 YKLVKKIGSGSFGEVYLGIDLKTGEEVAIKieKKDSKHPQLEYEAKVYKLLqGGPGIprLYWFG---------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ESSDYDpensknssrsktkclFIQMEFCDKgTLEQwIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNiF 421
Cdd:cd14016   66 QEGDYN---------------VMVMDLLGP-SLED-LFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPEN-F 127
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 525343631 422 LVDT----KQVKIGDFGLVTSLKNDGKRT----RSK----GTLRYMS 456
Cdd:cd14016  128 LMGLgknsNKVYLIDFGLAKKYRDPRTGKhipyREGksltGTARYAS 174
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
273-536 1.96e-15

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 77.15  E-value: 1.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKA-----KHRIDGKTYVIKRVKYNNEKAER-----EVKALAKL-DHVNIVHYNG-CwdgvdydPETSDDY 340
Cdd:cd05054   15 LGRGAFGKVIQAsafgiDKSATCRTVAVKMLKEGATASEHkalmtELKILIHIgHHLNVVNLLGaC-------TKPGGPL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSDYDPE-NSKNSSRSKTKCLFIQMefcDKGTLEQWIENRRGEKLDKVLALELFE----QITKGVDYIHSKKLIHRDL 415
Cdd:cd05054   88 MVIVEFCKFgNLSNYLRSKREEFVPYR---DKGARDVEEEEDDDELYKEPLTLEDLIcysfQVARGMEFLASRKCIHRDL 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 416 KPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGT---LRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFE-- 490
Cdd:cd05054  165 AARNILLSENNVVKICDFGLARDIYKDPDYVRKGDArlpLKWMAPESIFDKVYTTQSDVWSFGVLLWEIFSLGASPYPgv 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 525343631 491 --TSKFFTDLRDGIISDIFDKKEKTLLQKLLS---KKPEDRPNTSEILRTL 536
Cdd:cd05054  245 qmDEEFCRRLKEGTRMRAPEYTTPEIYQIMLDcwhGEPKERPTFSELVEKL 295
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
266-510 2.27e-15

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: 78.12  E-value: 2.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV-KYNNEK--------AEREVKALAkldhvnivhyNGCWDgVDYDPET 336
Cdd:cd05621   53 DYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLsKFEMIKrsdsaffwEERDIMAFA----------NSPWV-VQLFCAF 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 SDDylessdydpensknssrsktKCLFIQMEFCDKGTLEQWIENRR-GEKLDKVLALElfeqITKGVDYIHSKKLIHRDL 415
Cdd:cd05621  122 QDD--------------------KYLYMVMEYMPGGDLVNLMSNYDvPEKWAKFYTAE----VVLALDAIHSMGLIHRDV 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 416 KPSNIFLVDTKQVKIGDFGlvTSLKNDGKRT----RSKGTLRYMSPEQISSQD----YGKEVDLYALGLILAELLhVCDT 487
Cdd:cd05621  178 KPDNMLLDKYGHLKLADFG--TCMKMDETGMvhcdTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLFEML-VGDT 254
                        250       260
                 ....*....|....*....|...
gi 525343631 488 AfetskFFTDLRDGIISDIFDKK 510
Cdd:cd05621  255 P-----FYADSLVGTYSKIMDHK 272
pknD PRK13184
serine/threonine-protein kinase PknD;
270-482 2.38e-15

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 79.43  E-value: 2.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN---NEKAE----REVKALAKLDHVNIVH-YNGCwdgvdydpetsddyl 341
Cdd:PRK13184   7 IRLIGKGGMGEVYLAYDPVCSRRVALKKIREDlseNPLLKkrflREAKIAADLIHPGIVPvYSIC--------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 esSDYDPensknssrsktkcLFIQMEFCDKGTLEQWIEN-RRGEKLDKVLA--------LELFEQITKGVDYIHSKKLIH 412
Cdd:PRK13184  72 --SDGDP-------------VYYTMPYIEGYTLKSLLKSvWQKESLSKELAektsvgafLSIFHKICATIEYVHSKGVLH 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 413 RDLKPSNIFLVDTKQVKIGDFGLVTSLK-------------------NDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYA 473
Cdd:PRK13184 137 RDLKPDNILLGLFGEVVILDWGAAIFKKleeedlldidvdernicysSMTIPGKIVGTPDYMAPERLLGVPASESTDIYA 216

                 ....*....
gi 525343631 474 LGLILAELL 482
Cdd:PRK13184 217 LGVILYQML 225
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
397-536 2.54e-15

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: 77.35  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGT---LRYMSPEQISSQDYGKEVDLYA 473
Cdd:cd14207  188 QVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARDIYKNPDYVRKGDArlpLKWMAPESIFDKIYSTKSDVWS 267
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 474 LGLILAELLHVCDTAFE----TSKFFTDLRDGIISDIFDKKEKTLLQKLLS---KKPEDRPNTSEILRTL 536
Cdd:cd14207  268 YGVLLWEIFSLGASPYPgvqiDEDFCSKLKEGIRMRAPEFATSEIYQIMLDcwqGDPNERPRFSELVERL 337
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
263-482 2.69e-15

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: 76.11  E-value: 2.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 263 FGMDFKEIelIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER----EVKALAKLDHVNIVHYngcwdgvdydpetsd 338
Cdd:cd14190    4 FSIHSKEV--LGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEmvllEIQVMNQLNHRNLIQL--------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dylessdYDPENSKNSsrsktkcLFIQMEFCDKGTLEQWIENRrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd14190   67 -------YEAIETPNE-------IVLFMEYVEGGELFERIVDE-DYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPE 131
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 419 NIFLVDTK--QVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14190  132 NILCVNRTghQVKIIDFGLARRYNPREKLKVNFGTPEFLSPEVVNYDQVSFPTDMWSMGVITYMLL 197
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
269-533 2.72e-15

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: 76.30  E-value: 2.72e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 269 EIELiGSGGFGQVFKAkhrIDGKTYV---------IKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDGVdydpetsdd 339
Cdd:cd14031   15 DIEL-GRGAFKTVYKG---LDTETWVevawcelqdRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYDSWESV--------- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknssRSKTKCLFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKK--LIHRDLKP 417
Cdd:cd14031   82 ----------------LKGKKCIVLVTELMTSGTLKTYL--KRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKC 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 418 SNIFLVD-TKQVKIGDFGLVTSLKNDGKRTrSKGTLRYMSPEqISSQDYGKEVDLYALGLILAEL------LHVCDTAFE 490
Cdd:cd14031  144 DNIFITGpTGSVKIGDLGLATLMRTSFAKS-VIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMatseypYSECQNAAQ 221
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 491 T-SKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14031  222 IyRKVTSGIKPASFNKVTDPEVKEIIEGCIRQNKSERLSIKDLL 265
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
266-477 3.08e-15

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: 75.71  E-value: 3.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEI-ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK---AEREVKALAKLDHVNIVHYNGCWDgvdydpetsddyl 341
Cdd:cd14108    2 DYYDIhKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKktsARRELALLAELDHKSIVRFHDAFE------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 essdydpensknssrsKTKCLFIQMEFCDKGTLEqwienrRGEKLDKVLALEL---FEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd14108   69 ----------------KRRVVIIVTELCHEELLE------RITKRPTVCESEVrsyMRQLLEGIEYLHQNDVLHLDLKPE 126
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 419 NIFLVD--TKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLI 477
Cdd:cd14108  127 NLLMADqkTDQVRICDFGNAQELTPNEPQYCKYGTPEFVAPEIVNQSPVSKVTDIWPVGVI 187
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
271-482 3.30e-15

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: 76.21  E-value: 3.30e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKL-DHVNIVHYNGCWDgvdydpetsddylessdydpe 349
Cdd:cd14178    9 EDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPSEEIEILLRYgQHPNIITLKDVYD--------------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 350 nsknssrsKTKCLFIQMEFCdkgtleqwienRRGEKLDKVLALELFEQ---------ITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd14178   68 --------DGKFVYLVMELM-----------RGGELLDRILRQKCFSEreasavlctITKTVEYLHSQGVVHRDLKPSNI 128
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 421 FLVDT----KQVKIGDFGLVTSLK-NDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14178  129 LYMDEsgnpESIRICDFGFAKQLRaENGLLMTPCYTANFVAPEVLKRQGYDAACDIWSLGILLYTML 195
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
273-478 3.52e-15

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


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 76.76  E-value: 3.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKrvKYNN-------EKAEREVKALAKLDHVNIVHyngcwdgvdydpetsddyLESSD 345
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVK--VFNNlsfmrplDVQMREFEVLKKLNHKNIVK------------------LFAIE 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YDpensknsSRSKTKCLFiqMEFCDKGTLEQWIE---NRRGEKLDKVLALelFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd13988   61 EE-------LTTRHKVLV--MELCPCGSLYTVLEepsNAYGLPESEFLIV--LRDVVAGMNHLRENGIVHRDIKPGNIMR 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 423 V---DTKQV-KIGDFGLVTSLKNDGKRTRSKGTLRYMSPE--------QISSQDYGKEVDLYALGLIL 478
Cdd:cd13988  130 VigeDGQSVyKLTDFGAARELEDDEQFVSLYGTEEYLHPDmyeravlrKDHQKKYGATVDLWSIGVTF 197
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
357-482 4.08e-15

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: 75.85  E-value: 4.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 357 SKTKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLV 436
Cdd:cd05072   72 TKEEPIYIITEYMAKGSLLDFLKSDEGGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLA 151
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 525343631 437 TSLKNDGKRTR--SKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05072  152 RVIEDNEYTARegAKFPIKWTAPEAINFGSFTIKSDVWSFGILLYEIV 199
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
270-481 4.43e-15

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 75.58  E-value: 4.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAK--HRIDGKTYVIKRVKYNNEKA--------EREVKALAKLDHVNIVHYNG-CWDGvdyDPETSD 338
Cdd:cd05049   10 KRELGEGAFGKVFLGEcyNLEPEQDKMLVAVKTLKDASspdarkdfEREAELLTNLQHENIVKFYGvCTEG---DPLLMV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 -DYLESSDYDPensknssrsktkclFIQMEFCDKGTLEQwIENRRGEkLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd05049   87 fEYMEHGDLNK--------------FLRSHGPDAAFLAS-EDSAPGE-LTLSQLLHIAVQIASGMVYLASQHFVHRDLAT 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSL-KNDGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd05049  151 RNCLVGTNLVVKIGDFGMSRDIySTDYYRVGGHTMLpiRWMPPESILYRKFTTESDVWSFGVVLWEI 217
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
273-545 4.44e-15

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: 75.77  E-value: 4.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKA-KHRIDGK----TYVIKRVKYNNEKAE-----REVKALAKLDHVNIVH-YNGCwdgvdydpeTSDDYL 341
Cdd:cd05045    8 LGEGEFGKVVKAtAFRLKGRagytTVAVKMLKENASSSElrdllSEFNLLKQVNHPHVIKlYGAC---------SQDGPL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ----ESSDYDPENSKNSSRSKTKCLFIQmefCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd05045   79 llivEYAKYGSLRSFLRESRKVGPSYLG---SDGNRNSSYLDNPDERALTMGDLISFAWQISRGMQYLAEMKLVHRDLAA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSLKNDG---KRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFEtskf 494
Cdd:cd05045  156 RNVLVAEGRKMKISDFGLSRDVYEEDsyvKRSKGRIPVKWMAIESLFDHIYTTQSDVWSFGVLLWEIVTLGGNPYP---- 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 525343631 495 ftdlrdGIisdifdkKEKTLLQKLLSKKPEDRP-NTSEILRTL--TVWKKSPEK 545
Cdd:cd05045  232 ------GI-------APERLFNLLKTGYRMERPeNCSEEMYNLmlTCWKQEPDK 272
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
267-531 4.45e-15

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: 76.16  E-value: 4.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER-------EVKALAKLDHVNIVHyngcwdgVDYDPETSDd 339
Cdd:cd05632    4 FRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKgesmalnEKQILEKVNSQFVVN-------LAYAYETKD- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknssrsktkCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd05632   76 ---------------------ALCLVLTIMNGGDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPEN 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKnDGKRTRSK-GTLRYMSPEQISSQDYGKEVDLYALGLILAELLHvCDTAFETSKFF--- 495
Cdd:cd05632  135 ILLDDYGHIRISDLGLAVKIP-EGESIRGRvGTVGYMAPEVLNNQRYTLSPDYWGLGCLIYEMIE-GQSPFRGRKEKvkr 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 525343631 496 --TDLR----DGIISDIFDKKEKTLLQKLLSKKPEDRPNTSE 531
Cdd:cd05632  213 eeVDRRvletEEVYSAKFSEEAKSICKMLLTKDPKQRLGCQE 254
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
273-543 5.02e-15

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: 75.83  E-value: 5.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER----EVKALAKLDHVNIVhyngcwdgvdydpETSDDYLESSDydp 348
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQRREllfnEVVIMRDYQHENVV-------------EMYNSYLVGDE--- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 349 ensknssrsktkcLFIQMEFCDKGTLEQWIENRRGEKlDKVLALELfeQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQV 428
Cdd:cd06657   92 -------------LWVVMEFLEGGALTDIVTHTRMNE-EQIAAVCL--AVLKALSVLHAQGVIHRDIKSDSILLTHDGRV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 429 KIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETS--KFFTDLRDGIISD 505
Cdd:cd06657  156 KLSDFGFCAQVSKEVPRRKSlVGTPYWMAPELISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPplKAMKMIRDNLPPK 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 525343631 506 IFDKKE-----KTLLQKLLSKKPEDRPNTSEILRTLTVWKKSP 543
Cdd:cd06657  236 LKNLHKvspslKGFLDRLLVRDPAQRATAAELLKHPFLAKAGP 278
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
269-533 5.66e-15

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: 75.11  E-value: 5.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 269 EIELiGSGGFGQVFKAkhrIDGKTYV---------IKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDgvdydpetsdd 339
Cdd:cd14032    6 DIEL-GRGSFKTVYKG---LDTETWVevawcelqdRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWE----------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 ylessdydpensknSSRSKTKCLFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKK--LIHRDLKP 417
Cdd:cd14032   71 --------------SCAKGKRCIVLVTELMTSGTLKTYL--KRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKC 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 418 SNIFLVD-TKQVKIGDFGLVTsLKNDGKRTRSKGTLRYMSPEqISSQDYGKEVDLYALGLILAEL------LHVCDTAFE 490
Cdd:cd14032  135 DNIFITGpTGSVKIGDLGLAT-LKRASFAKSVIGTPEFMAPE-MYEEHYDESVDVYAFGMCMLEMatseypYSECQNAAQ 212
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 491 TSKFFT-DLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14032  213 IYRKVTcGIKPASFEKVTDPEIKEIIGECICKNKEERYEIKDLL 256
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
271-482 5.81e-15

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: 75.01  E-value: 5.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYV---IKRVKYNNEKAER-----EVKALAKLDHVNIVHYNGCwdgvdydpetsddyle 342
Cdd:cd05063   11 KVIGAGEFGEVFRGILKMPGRKEVavaIKTLKPGYTEKQRqdflsEASIMGQFSHHNIIRLEGV---------------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssRSKTKCLFIQMEFCDKGTLEQWIENRRGEkLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd05063   75 -------------VTKFKPAMIITEYMENGALDKYLRDHDGE-FSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILV 140
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 423 VDTKQVKIGDFGLVTSLKND--GKRTRSKGT--LRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05063  141 NSNLECKVSDFGLSRVLEDDpeGTYTTSGGKipIRWTAPEAIAYRKFTSASDVWSFGIVMWEVM 204
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
272-536 6.88e-15

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: 74.60  E-value: 6.88e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRidGKTYVIKrvKYNNEKAER----EVKALAKLDHVNIVhyngcwdgvdydpetsddYLESSDYD 347
Cdd:cd14068    1 LLGDGGFGSVYRAVYR--GEDVAVK--IFNKHTSFRllrqELVVLSHLHHPSLV------------------ALLAAGTA 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 PEnsknssrsktkclFIQMEFCDKGTLEQWIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQ 427
Cdd:cd14068   59 PR-------------MLVMELAPKGSLDALLQQDNA-SLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLFTLYP 124
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 428 -----VKIGDFGLVTSLKNDGKRTrSKGTLRYMSPEQISSQ-DYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRDG 501
Cdd:cd14068  125 ncaiiAKIADYGIAQYCCRMGIKT-SEGTPGFRAPEVARGNvIYNQQADVYSFGLLLYDILTCGERIVEGLKFPNEFDEL 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 525343631 502 IISDIFDKKEK-----------TLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd14068  204 AIQGKLPDPVKeygcapwpgveALIKDCLKENPQCRPTSAQVFDIL 249
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
266-481 8.56e-15

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


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 74.31  E-value: 8.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRidGKTYVIKRVKYNNEKAER---EVKALAKLDHVNIVhyngCWDGVdydpetsddyle 342
Cdd:cd05039    7 DLKLGELIGKGEFGDVMLGDYR--GQKVAVKCLKDDSTAAQAflaEASVMTTLRHPNLV----QLLGV------------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 SSDYDPensknssrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd05039   69 VLEGNG-------------LYIVTEYMAKGSLVDYLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLV 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 423 VDTKQVKIGDFGLV--TSLKNDGkrtrSKGTLRYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd05039  136 SEDNVAKVSDFGLAkeASSNQDG----GKLPIKWTAPEALREKKFSTKSDVWSFGILLWEI 192
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
267-482 8.83e-15

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: 75.15  E-value: 8.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER----EVKALAKLDHVNIVHYngcwdgvdydpetSDDYLE 342
Cdd:cd06655   21 YTRYEKIGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKEliinEILVMKELKNPNIVNF-------------LDSFLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 SSDydpensknssrsktkcLFIQMEFCDKGTLEQWIENrrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd06655   88 GDE----------------LFVVMEYLAGGSLTDVVTE---TCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLL 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 423 VDTKQVKIGDFGLVTSLKND-GKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd06655  149 GMDGSVKLTDFGFCAQITPEqSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV 209
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
266-482 9.03e-15

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: 75.80  E-value: 9.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNN-------EKAEREVKALAKLDHVN-IVHYNGCWDGVDYdpets 337
Cdd:cd05615   11 DFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVviqdddvECTMVEKRVLALQDKPPfLTQLHSCFQTVDR----- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 ddylessdydpensknssrsktkcLFIQMEFCDKGTLEQWIEnrRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd05615   86 ------------------------LYFVMEYVNGGDLMYHIQ--QVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKL 139
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05615  140 DNVMLDSEGHIKIADFGMCKEHMVEGVTTRTfCGTPDYIAPEIIAYQPYGRSVDWWAYGVLLYEML 205
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
266-510 9.24e-15

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: 76.20  E-value: 9.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKrvkynnekaerevkALAKLDHVNIVHYNGCWDGVDYDPETSDDYLESSD 345
Cdd:cd05622   74 DYEVVKVIGRGAFGEVQLVRHKSTRKVYAMK--------------LLSKFEMIKRSDSAFFWEERDIMAFANSPWVVQLF 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YDPENSKNssrsktkcLFIQMEFCDKGTLEQWIENRR-GEKLDKVLALElfeqITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd05622  140 YAFQDDRY--------LYMVMEYMPGGDLVNLMSNYDvPEKWARFYTAE----VVLALDAIHSMGFIHRDVKPDNMLLDK 207
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLVTSLKNDG--KRTRSKGTLRYMSPEQISSQD----YGKEVDLYALGLILAELLhVCDTAfetskFFTDL 498
Cdd:cd05622  208 SGHLKLADFGTCMKMNKEGmvRCDTAVGTPDYISPEVLKSQGgdgyYGRECDWWSVGVFLYEML-VGDTP-----FYADS 281
                        250
                 ....*....|..
gi 525343631 499 RDGIISDIFDKK 510
Cdd:cd05622  282 LVGTYSKIMNHK 293
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
266-534 9.43e-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: 75.08  E-value: 9.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEI----ELIGSGGFGQVFKAKHRIDGKTYVIK-----RVKYNNEKAEREVKALAKLDHVNIVhyngcwdgvdydpeT 336
Cdd:cd14168    7 DIKKIfefkEVLGTGAFSEVVLAEERATGKLFAVKcipkkALKGKESSIENEIAVLRKIKHENIV--------------A 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 SDDYLESSDYdpensknssrsktkcLFIQMEFCDKGTL-EQWIENRRGEKLDkvlALELFEQITKGVDYIHSKKLIHRDL 415
Cdd:cd14168   73 LEDIYESPNH---------------LYLVMQLVSGGELfDRIVEKGFYTEKD---ASTLIRQVLDAVYYLHRMGIVHRDL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 416 KPSNIFLV---DTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFET- 491
Cdd:cd14168  135 KPENLLYFsqdEESKIMISDFGLSKMEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDEn 214
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 525343631 492 -SKFFTDLR------DGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14168  215 dSKLFEQILkadyefDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQALR 264
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
362-482 9.89e-15

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: 75.12  E-value: 9.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKN 441
Cdd:cd05587   72 LYFVMEYVNGGDLMYHIQQV--GKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKEGIF 149
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 525343631 442 DGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05587  150 GGKTTRTfCGTPDYIAPEIIAYQPYGKSVDWWAYGVLLYEML 191
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
242-482 1.16e-14

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: 75.45  E-value: 1.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 242 SLAPRFDLPDMKETKYTVDKRFGM-DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNI 320
Cdd:cd05594    1 SPSDNSGAEEMEVSLTKPKHKVTMnDFEYLKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDEVAHTLTENRVLQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 321 VHYNGCWDGVDYDPETSDdylessdydpensknssrsktKCLFIqMEFCDKGTLEQWIENRRGEKLDKvlALELFEQITK 400
Cdd:cd05594   81 NSRHPFLTALKYSFQTHD---------------------RLCFV-MEYANGGELFFHLSRERVFSEDR--ARFYGAEIVS 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 401 GVDYIHSKK-LIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLIL 478
Cdd:cd05594  137 ALDYLHSEKnVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGATMKTfCGTPEYLAPEVLEDNDYGRAVDWWGLGVVM 216

                 ....
gi 525343631 479 AELL 482
Cdd:cd05594  217 YEMM 220
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
271-480 1.19e-14

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 73.81  E-value: 1.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN-----NEKAEREVKALAKLDHVNIVHYNG-Cwdgvdydpetsddyless 344
Cdd:cd05084    2 ERIGRGNFGEVFSGRLRADNTPVAVKSCRETlppdlKAKFLQEARILKQYSHPNIVRLIGvC------------------ 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpensknssrSKTKCLFIQMEFCDKGTLEQWIENRrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd05084   64 ------------TQKQPIYIVMELVQGGDFLTFLRTE-GPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTE 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLvTSLKNDGKRTRSKGT----LRYMSPEQISSQDYGKEVDLYALGLILAE 480
Cdd:cd05084  131 KNVLKISDFGM-SREEEDGVYAATGGMkqipVKWTAPEALNYGRYSSESDVWSFGILLWE 189
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
266-537 1.48e-14

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


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 74.27  E-value: 1.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGK--TYVIKRVK-YNNEKAER----EVKALAKL-DHVNIVHYNGCWDGVDYdpets 337
Cdd:cd05089    3 DIKFEDVIGEGNFGQVIKAMIKKDGLkmNAAIKMLKeFASENDHRdfagELEVLCKLgHHPNIINLLGACENRGY----- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 ddylessdydpensknssrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKVLA--------------LELFEQITKGVD 403
Cdd:cd05089   78 ------------------------LYIAIEYAPYGNLLDFLRKSRVLETDPAFAkehgtastltsqqlLQFASDVAKGMQ 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 404 YIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLH 483
Cdd:cd05089  134 YLSEKQFIHRDLAARNVLVGENLVSKIADFGLSRGEEVYVKKTMGRLPVRWMAIESLNYSVYTTKSDVWSFGVLLWEIVS 213
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 484 VCDTAF---ETSKFFTDLRDGIISDI---FDKKEKTLLQKLLSKKPEDRPNTSEILRTLT 537
Cdd:cd05089  214 LGGTPYcgmTCAELYEKLPQGYRMEKprnCDDEVYELMRQCWRDRPYERPPFSQISVQLS 273
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
270-541 1.56e-14

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: 74.23  E-value: 1.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK-----AEREVKALAKLDHVNIVHYNGcwdgVDYDPETSDDYLESS 344
Cdd:cd07870    5 LEKLGEGSYATVYKGISRINGQLVALKVISMKTEEgvpftAIREASLLKGLKHANIVLLHD----IIHTKETLTFVFEYM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 DYDpensknssrsktkclfiqmefcdkgtLEQWIENRRGEKLDKVLALELFeQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd07870   81 HTD--------------------------LAQYMIQHPGGLHPYNVRLFMF-QLLRGLAYIHGQHILHRDLKPQNLLISY 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLVTSlKNDGKRTRSKG--TLRYMSPEQI-SSQDYGKEVDLYALGLILAELlhvcdtaFETSKFFTDlrdg 501
Cdd:cd07870  134 LGELKLADFGLARA-KSIPSQTYSSEvvTLWYRPPDVLlGATDYSSALDIWGAGCIFIEM-------LQGQPAFPG---- 201
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 525343631 502 iISDIFDKKEKTL-------------LQKLLSKKPE-DRPNTSEILRtlTVWKK 541
Cdd:cd07870  202 -VSDVFEQLEKIWtvlgvptedtwpgVSKLPNYKPEwFLPCKPQQLR--VVWKR 252
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
261-526 1.91e-14

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: 74.31  E-value: 1.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 261 KRFGMDFKEiELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNE-KAEREVKALAKLD-HVNIVHYNgcwdgvdydpETSD 338
Cdd:cd14179    4 QHYELDLKD-KPLGEGSFSICRKCLHKKTNQEYAVKIVSKRMEaNTQREIAALKLCEgHPNIVKLH----------EVYH 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 DYLESsdydpensknssrsktkclFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd14179   73 DQLHT-------------------FLVMELLKGGELLERI--KKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPE 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVD---TKQVKIGDFGLVTSLKNDGKRTRSKG-TLRYMSPEQISSQDYGKEVDLYALGLILAELLH----------- 483
Cdd:cd14179  132 NLLFTDesdNSEIKIIDFGFARLKPPDNQPLKTPCfTLHYAAPELLNYNGYDESCDLWSLGVILYTMLSgqvpfqchdks 211
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 525343631 484 -VCDTAFETSKfftDLRDGIIS------DIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd14179  212 lTCTSAEEIMK---KIKQGDFSfegeawKNVSQEAKDLIQGLLTVDPNKR 258
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
383-534 1.91e-14

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: 74.67  E-value: 1.91e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 383 GEKLDKVLALELFEQ---------ITKGVDYIHSKKLIHRDLKPSNIFLVDT----KQVKIGDFGLVTSLK-NDGKRTRS 448
Cdd:cd14176   98 GELLDKILRQKFFSEreasavlftITKTVEYLHAQGVVHRDLKPSNILYVDEsgnpESIRICDFGFAKQLRaENGLLMTP 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 449 KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVC--------DTAFE------TSKFftDLRDGIISDIFDKKeKTL 514
Cdd:cd14176  178 CYTANFVAPEVLERQGYDAACDIWSLGVLLYTMLTGYtpfangpdDTPEEilarigSGKF--SLSGGYWNSVSDTA-KDL 254
                        170       180
                 ....*....|....*....|
gi 525343631 515 LQKLLSKKPEDRPNTSEILR 534
Cdd:cd14176  255 VSKMLHVDPHQRLTAALVLR 274
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
269-533 2.11e-14

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


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 73.73  E-value: 2.11e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 269 EIEL---IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE-----REVKALAKLDHVNIVHYNGCWdgvdydpetsddY 340
Cdd:cd06622    2 EIEVldeLGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKfnqiiMELDILHKAVSPYIVDFYGAF------------F 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESsdydpensknssrsktkCLFIQMEFCDKGTLEQ-WIENRRGEKLDKVLALELFEQITKGVDYIHSK-KLIHRDLKPS 418
Cdd:cd06622   70 IEG-----------------AVYMCMEYMDAGSLDKlYAGGVATEGIPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPT 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSLKNDGKRTrSKGTLRYMSPEQISSQD------YGKEVDLYALGLILAELLHVC------- 485
Cdd:cd06622  133 NVLVNGNGQVKLCDFGVSGNLVASLAKT-NIGCQSYMAPERIKSGGpnqnptYTVQSDVWSLGLSILEMALGRypyppet 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 525343631 486 -DTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd06622  212 yANIFAQLSAIVDGDPPTLPSGYSDDAQDFVAKCLNKIPNRRPTYAQLL 260
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
271-481 2.28e-14

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: 73.56  E-value: 2.28e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKA----KHRIDGKTYV-IKRVKYNNEKA-----EREVKALAKLDHVNIVhyngCWDGVdydpetsddy 340
Cdd:cd05048   11 EELGEGAFGKVYKGellgPSSEESAISVaIKTLKENASPKtqqdfRREAELMSDLQHPNIV----CLLGV---------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpensknSSRSKTKC-LFiqmEFCDKGTLEQWI------------ENRRGEK--LDKVLALELFEQITKGVDYI 405
Cdd:cd05048   77 -------------CTKEQPQCmLF---EYMAHGDLHEFLvrhsphsdvgvsSDDDGTAssLDQSDFLHIAIQIAAGMEYL 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 406 HSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSL-KNDGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd05048  141 SSHHYVHRDLAARNCLVGDGLTVKISDFGLSRDIySSDYYRVQSKSLLpvRWMPPEAILYGKFTTESDVWSFGVVLWEI 219
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
273-536 2.49e-14

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: 74.25  E-value: 2.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAK-HRIDG----KTYVIKRVKYNNEKAER-----EVKALAKL-DHVNIVHYNG---------------C 326
Cdd:cd05103   15 LGRGAFGQVIEADaFGIDKtatcRTVAVKMLKEGATHSEHralmsELKILIHIgHHLNVVNLLGactkpggplmvivefC 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 327 WDG----------VDYDPETSDD--YLESSDYDPE---------NSKNSSRSKTKCLFIQ-MEFCDkgtleqwIENRRGE 384
Cdd:cd05103   95 KFGnlsaylrskrSEFVPYKTKGarFRQGKDYVGDisvdlkrrlDSITSSQSSASSGFVEeKSLSD-------VEEEEAG 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 385 KLD---KVLALELFE----QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRsKGT----LR 453
Cdd:cd05103  168 QEDlykDFLTLEDLIcysfQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVR-KGDarlpLK 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 454 YMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSK----FFTDLRDGIISDIFDKKEKTLLQKLLS---KKPEDR 526
Cdd:cd05103  247 WMAPETIFDRVYTIQSDVWSFGVLLWEIFSLGASPYPGVKideeFCRRLKEGTRMRAPDYTTPEMYQTMLDcwhGEPSQR 326
                        330
                 ....*....|
gi 525343631 527 PNTSEILRTL 536
Cdd:cd05103  327 PTFSELVEHL 336
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
362-533 2.76e-14

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: 73.53  E-value: 2.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRRGEKlDKVLALELfeQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSL-K 440
Cdd:cd06658   94 LWVVMEFLEGGALTDIVTHTRMNE-EQIATVCL--SVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVsK 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 441 NDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKF--FTDLRDGIISDIFDKKE-----KT 513
Cdd:cd06658  171 EVPKRKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMIDGEPPYFNEPPLqaMRRIRDNLPPRVKDSHKvssvlRG 250
                        170       180
                 ....*....|....*....|
gi 525343631 514 LLQKLLSKKPEDRPNTSEIL 533
Cdd:cd06658  251 FLDLMLVREPSQRATAQELL 270
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
397-526 2.88e-14

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: 73.20  E-value: 2.88e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKND-GKRTRSK-GTLRYMSPEQISSQDYG--KEVDLY 472
Cdd:cd05583  107 EIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGeNDRAYSFcGTIEYMAPEVVRGGSDGhdKAVDWW 186
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 473 ALGLILAELLHVCdtafetSKFFTDLRDGIISDI--------------FDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05583  187 SLGVLTYELLTGA------SPFTVDGERNSQSEIskrilkshppipktFSAEAKDFILKLLEKDPKKR 248
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
271-533 2.94e-14

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: 73.23  E-value: 2.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKY-NNEKAER---------EVKALAKLDHVNIVHYNGcwdgvdydpetsddy 340
Cdd:cd06630    6 PLLGTGAFSSCYQARDVKTGTLMAVKQVSFcRNSSSEQeevveaireEIRMMARLNHPNIVRMLG--------------- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpensknSSRSKTKcLFIQMEFCDKGTLEQWIENRrGEKLDKVLaLELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd06630   71 -------------ATQHKSH-FNIFVEWMAGGSVASLLSKY-GAFSENVI-INYTLQILRGLAYLHDNQIIHRDLKGANL 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 421 fLVDT--KQVKIGDFGLVTSLKNDGKRT-----RSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL------HVCDT 487
Cdd:cd06630  135 -LVDStgQRLRIADFGAAARLASKGTGAgefqgQLLGTIAFMAPEVLRGEQYGRSCDVWSVGCVIIEMAtakppwNAEKI 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 525343631 488 AFETSKFF---TDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd06630  214 SNHLALIFkiaSATTPPPIPEHLSPGLRDVTLRCLELQPEDRPPARELL 262
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
273-534 3.15e-14

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: 72.89  E-value: 3.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKA-KHRIDGKTYV--IKRVKYNNEKAE----REVKALAKLDHVNIVHYngcwdgvdYDP-ETSDDYLess 344
Cdd:cd14165    9 LGEGSYAKVKSAySERLKCNVAIkiIDKKKAPDDFVEkflpRELEILARLNHKSIIKT--------YEIfETSDGKV--- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpensknssrsktkclFIQMEFCDKGTLEQWIEnRRGEkLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd14165   78 ------------------YIVMELGVQGDLLEFIK-LRGA-LPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLVTSLKND--GKRTRSK---GTLRYMSPEQISSQDYGKEV-DLYALGLILaeLLHVCDT-AFETSKFFTD 497
Cdd:cd14165  138 DFNIKLTDFGFSKRCLRDenGRIVLSKtfcGSAAYAAPEVLQGIPYDPRIyDIWSLGVIL--YIMVCGSmPYDDSNVKKM 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 525343631 498 LRDGIISDI-FDKKE------KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14165  216 LKIQKEHRVrFPRSKnltsecKDLIYRLLQPDVSQRLCIDEVLS 259
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
362-526 3.38e-14

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: 73.68  E-value: 3.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIEnrRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKN 441
Cdd:cd05591   71 LFFVMEYVNGGDLMFQIQ--RARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGIL 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 442 DGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAFETSK----FFTDLRDGIISDIFDKKEKT-LL 515
Cdd:cd05591  149 NGKTTTTfCGTPDYIAPEILQELEYGPSVDWWALGVLMYEMM-AGQPPFEADNeddlFESILHDDVLYPVWLSKEAVsIL 227
                        170
                 ....*....|.
gi 525343631 516 QKLLSKKPEDR 526
Cdd:cd05591  228 KAFMTKNPAKR 238
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
271-482 3.51e-14

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 72.71  E-value: 3.51e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKrVKYNNEKAEREVKalakldhvniVHYNGcwDGVDYDPETSDDYlessdydpen 350
Cdd:cd14172   10 QVLGLGVNGKVLECFHRRTGQKCALK-LLYDSPKARREVE----------HHWRA--SGGPHIVHILDVY---------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 351 sKNSSRSKtKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV---DTKQ 427
Cdd:cd14172   67 -ENMHHGK-RCLLIIMECMEGGELFSRIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTskeKDAV 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 428 VKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14172  145 LKLTDFGFAKETTVQNALQTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILL 199
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
392-533 3.66e-14

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: 72.65  E-value: 3.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 392 LELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK---QVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKE 468
Cdd:cd14198  113 IRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYplgDIKIVDFGMSRKIGHACELREIMGTPEYLAPEILNYDPITTA 192
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 469 VDLYALGLILAELL-----HVCDTAFET----SKFFTDLRDGIISDIfDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14198  193 TDMWNIGVIAYMLLthespFVGEDNQETflniSQVNVDYSEETFSSV-SQLATDFIQKLLVKNPEKRPTAEICL 265
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
362-526 3.84e-14

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 73.57  E-value: 3.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIEN--RRGEKLDKVLALElfeqITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGL-VTS 438
Cdd:cd05592   71 LFFVMEYLNGGDLMFHIQQsgRFDEDRARFYGAE----IICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMcKEN 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 439 LKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL------HVCDtafETSKFFTDLRDGIISDIFDKKE- 511
Cdd:cd05592  147 IYGENKASTFCGTPDYIAPEILKGQKYNQSVDWWSFGVLLYEMLigqspfHGED---EDELFWSICNDTPHYPRWLTKEa 223
                        170
                 ....*....|....*
gi 525343631 512 KTLLQKLLSKKPEDR 526
Cdd:cd05592  224 ASCLSLLLERNPEKR 238
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
357-536 4.26e-14

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: 72.76  E-value: 4.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 357 SKTKCLFIQMEFCDKGTLEQWIENRRGE-----KLDKVLALELFE---QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQV 428
Cdd:cd05032   79 STGQPTLVVMELMAKGDLKSYLRSRRPEaennpGLGPPTLQKFIQmaaEIADGMAYLAAKKFVHRDLAARNCMVAEDLTV 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 429 KIGDFGLVTSLKN-DGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAF------ETSKFFTDlr 499
Cdd:cd05032  159 KIGDFGMTRDIYEtDYYRKGGKGLLpvRWMAPESLKDGVFTTKSDVWSFGVVLWEMATLAEQPYqglsneEVLKFVID-- 236
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 525343631 500 dgiiSDIFDKKE------KTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd05032  237 ----GGHLDLPEncpdklLELMRMCWQYNPKMRPTFLEIVSSL 275
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
305-533 4.60e-14

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: 72.39  E-value: 4.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 305 AEREVKALAKLDHVNIVHYNGcwdgvdydpetsddYLESSDYDPENSKnssrsktkcLFIQMEFCDKGTLEQWIENRRGE 384
Cdd:cd14012   45 LEKELESLKKLRHPNLVSYLA--------------FSIERRGRSDGWK---------VYLLTEYAPGGSLSELLDSVGSV 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 385 KLDKVLALELfeQITKGVDYIHSKKLIHRDLKPSNIFLV----DTKqVKIGDFGLVTSLkNDGKRTRSKGTLR---YMSP 457
Cdd:cd14012  102 PLDTARRWTL--QLLEALEYLHRNGVVHKSLHAGNVLLDrdagTGI-VKLTDYSLGKTL-LDMCSRGSLDEFKqtyWLPP 177
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 458 EQI-SSQDYGKEVDLYALGLILAELLhvcdTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14012  178 ELAqGSKSPTRKTDVWDLGLLFLQML----FGLDVLEKYTSPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTALELL 250
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
362-536 4.97e-14

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: 72.37  E-value: 4.97e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKN 441
Cdd:cd05073   80 IYIITEFMAKGSLLDFLKSDEGSKQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIED 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 442 DGKRTR--SKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAF---ETSKFFTDLRDGIISDIFDKKEKTLLQ 516
Cdd:cd05073  160 NEYTARegAKFPIKWTAPEAINFGSFTIKSDVWSFGILLMEIVTYGRIPYpgmSNPEVIRALERGYRMPRPENCPEELYN 239
                        170       180
                 ....*....|....*....|...
gi 525343631 517 KLL---SKKPEDRPnTSEILRTL 536
Cdd:cd05073  240 IMMrcwKNRPEERP-TFEYIQSV 261
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
341-536 5.10e-14

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


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 73.91  E-value: 5.10e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSDYD-PENSKNSSRSKTKCLFiqmefCDKGTleqwienrrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd05105  203 IQRSNYDrPASYKGSNDSEVKNLL-----SDDGS----------EGLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARN 267
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTrSKGT----LRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFE----T 491
Cdd:cd05105  268 VLLAQGKIVKICDFGLARDIMHDSNYV-SKGStflpVKWMAPESIFDNLYTTLSDVWSYGILLWEIFSLGGTPYPgmivD 346
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 492 SKFFTDLRDG--------IISDIFDkkektLLQKLLSKKPEDRPN---TSEILRTL 536
Cdd:cd05105  347 STFYNKIKSGyrmakpdhATQEVYD-----IMVKCWNSEPEKRPSflhLSDIVESL 397
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
383-482 5.26e-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: 72.74  E-value: 5.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 383 GEKLDKVLALELFEQ---------ITKGVDYIHSKKLIHRDLKPSNIFLVD----TKQVKIGDFGLVTSLKND-GKRTRS 448
Cdd:cd14177   83 GELLDRILRQKFFSEreasavlytITKTVDYLHCQGVVHRDLKPSNILYMDdsanADSIRICDFGFAKQLRGEnGLLLTP 162
                         90       100       110
                 ....*....|....*....|....*....|....
gi 525343631 449 KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14177  163 CYTANFVAPEVLMRQGYDAACDIWSLGVLLYTML 196
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
362-526 5.62e-14

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: 73.05  E-value: 5.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVT-SLK 440
Cdd:cd05620   71 LFFVMEFLNGGDLMFHIQDK--GRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKeNVF 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 441 NDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhvcdtaFETSKFFTDLRDGIISDI----------FDKK 510
Cdd:cd05620  149 GDNRASTFCGTPDYIAPEILQGLKYTFSVDWWSFGVLLYEML------IGQSPFHGDDEDELFESIrvdtphyprwITKE 222
                        170
                 ....*....|....*.
gi 525343631 511 EKTLLQKLLSKKPEDR 526
Cdd:cd05620  223 SKDILEKLFERDPTRR 238
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
267-481 6.79e-14

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: 72.72  E-value: 6.79e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEK-----AEREVKALAKLDHVNIVhyngcwdgvdydpeTSDDYL 341
Cdd:cd07872    8 YIKLEKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEgapctAIREVSLLKDLKHANIV--------------TLHDIV 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ESSdydpensknssrsktKCLFIQMEFCDKgTLEQWIENRRGEKLDKVLALELFeQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd07872   74 HTD---------------KSLTLVFEYLDK-DLKQYMDDCGNIMSMHNVKIFLY-QILRGLAYCHRRKVLHRDLKPQNLL 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 422 LVDTKQVKIGDFGLVTSlKNDGKRTRSKG--TLRYMSPE-QISSQDYGKEVDLYALGLILAEL 481
Cdd:cd07872  137 INERGELKLADFGLARA-KSVPTKTYSNEvvTLWYRPPDvLLGSSEYSTQIDMWGVGCIFFEM 198
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
267-482 7.14e-14

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: 71.95  E-value: 7.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKA-----EREVKALAKLDHVNIVHYngcwdgvdydPETSDDYL 341
Cdd:cd14183    8 YKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGkehmiQNEVSILRRVKHPNIVLL----------IEEMDMPT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 EssdydpensknssrsktkcLFIQMEFCDKGTLEQWIE--NRRGEKLdkvlALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14183   78 E-------------------LYLVMELVKGGDLFDAITstNKYTERD----ASGMLYNLASAIKYLHSLNIVHRDIKPEN 134
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 420 IFLVD----TKQVKIGDFGLVTSLknDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14183  135 LLVYEhqdgSKSLKLGDFGLATVV--DGPLYTVCGTPTYVAPEIIAETGYGLKVDIWAAGVITYILL 199
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
245-521 7.39e-14

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: 73.15  E-value: 7.39e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 245 PRFDLPDMKETKYTVDKRFgmdfKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK------YNNEKAEREVKALAKLDHV 318
Cdd:cd07877    1 PTFYRQELNKTIWEVPERY----QNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSrpfqsiIHAKRTYRELRLLKHMKHE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 319 NIVHYNGCWDGVDYDPETSDDYLESS--DYDPENSknssrskTKClfiqmefcdkgtleqwienrrgEKLDKVLALELFE 396
Cdd:cd07877   77 NVIGLLDVFTPARSLEEFNDVYLVTHlmGADLNNI-------VKC----------------------QKLTDDHVQFLIY 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLvtSLKNDGKRTRSKGTLRYMSPE-QISSQDYGKEVDLYALG 475
Cdd:cd07877  128 QILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGL--ARHTDDEMTGYVATRWYRAPEiMLNWMHYNQTVDIWSVG 205
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 525343631 476 LILAELLhVCDTAFETSKFFTDLRdgIISDIFDKKEKTLLQKLLSK 521
Cdd:cd07877  206 CIMAELL-TGRTLFPGTDHIDQLK--LILRLVGTPGAELLKKISSE 248
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
255-534 7.60e-14

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


Pssm-ID: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 72.33  E-value: 7.60e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 255 TKYTVDKRfgmdfkeIELIGSGGFGQVFKAKHRIDGKTYVIKRV--KYNnekAEREVKALAKLD-HVNIVHyngcwdgvd 331
Cdd:cd14092    3 QNYELDLR-------EEALGDGSFSVCRKCVHKKTGQEFAVKIVsrRLD---TSREVQLLRLCQgHPNIVK--------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 332 ydpetsddyLESSDYDPENSknssrsktkclFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLI 411
Cdd:cd14092   64 ---------LHEVFQDELHT-----------YLVMELLRGGELLERI--RKKKRFTESEASRIMRQLVSAVSFMHSKGVV 121
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 412 HRDLKPSNIFLVD---TKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPE---QISSQD-YGKEVDLYALGLILAELL-- 482
Cdd:cd14092  122 HRDLKPENLLFTDeddDAEIKIVDFGFARLKPENQPLKTPCFTLPYAAPEvlkQALSTQgYDESCDLWSLGVILYTMLsg 201
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 483 ----HVCDTAFETSKFFTDLRDGIISdiFD--------KKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14092  202 qvpfQSPSRNESAAEIMKRIKSGDFS--FDgeewknvsSEAKSLIQGLLTVDPSKRLTMSELRN 263
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
381-490 8.55e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 72.99  E-value: 8.55e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 381 RRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQI 460
Cdd:PHA03209 149 KRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVVAPAFLGLAGTVETNAPEVL 228
                         90       100       110
                 ....*....|....*....|....*....|
gi 525343631 461 SSQDYGKEVDLYALGLILAELLHVCDTAFE 490
Cdd:PHA03209 229 ARDKYNSKADIWSAGIVLFEMLAYPSTIFE 258
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
272-533 9.56e-14

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: 71.42  E-value: 9.56e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFkAKHRI-DGKTYVIKRVKYNnekaerEVKALAKLDHVNIV--------------HYNGCWDGVDYDpET 336
Cdd:cd14101    7 LLGKGGFGTVY-AGHRIsDGLQVAIKQISRN------RVQQWSKLPGVNPVpnevallqsvgggpGHRGVIRLLDWF-EI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 SDDYLESSDyDPENSKNssrsktkcLFIQMEfcDKGTLeqwienrrgeklDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd14101   79 PEGFLLVLE-RPQHCQD--------LFDYIT--ERGAL------------DESLARRFFKQVVEAVQHCHSKGVVHRDIK 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIfLVDTKQ--VKIGDFGLVTSLKnDGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELlhVC-DTAFETS 492
Cdd:cd14101  136 DENI-LVDLRTgdIKLIDFGSGATLK-DSMYTDFDGTRVYSPPEWILYHQYhALPATVWSLGILLYDM--VCgDIPFERD 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 525343631 493 kffTDLRDGIISdiFDKKE----KTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14101  212 ---TDILKAKPS--FNKRVsndcRSLIRSCLAYNPSDRPSLEQIL 251
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
268-481 9.57e-14

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: 71.31  E-value: 9.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 268 KEIEL---IGSGGFGQVFKAKHRiDGKTYVIKRVKYNNEKAER----EVKALAKLDHVNIVHYngcwdgvdydpetsddY 340
Cdd:cd05148    6 EEFTLerkLGSGYFGEVWEGLWK-NRVRVAIKILKSDDLLKQQdfqkEVQALKRLRHKHLISL----------------F 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSDYDPensknssrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd05148   69 AVCSVGEP-------------VYIITELMEKGSLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNI 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 421 FLVDTKQVKIGDFGLVTSLKNDGKRTRSKGT-LRYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd05148  136 LVGEDLVCKVADFGLARLIKEDVYLSSDKKIpYKWTAPEAASHGTFSTKSDVWSFGILLYEM 197
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
267-482 9.92e-14

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: 72.06  E-value: 9.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER----EVKALAKLDHVNIVHYngcwdgvdydpetSDDYLE 342
Cdd:cd06656   21 YTRFEKIGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKEliinEILVMRENKNPNIVNY-------------LDSYLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 SSDydpensknssrsktkcLFIQMEFCDKGTLEQWIENrrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd06656   88 GDE----------------LWVVMEYLAGGSLTDVVTE---TCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILL 148
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 423 VDTKQVKIGDFGLVTSLKND-GKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd06656  149 GMDGSVKLTDFGFCAQITPEqSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMV 209
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
362-536 1.00e-13

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: 71.46  E-value: 1.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKN 441
Cdd:cd05067   76 IYIITEYMENGSLVDFLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIED 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 442 DGKRTR--SKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL---HVCDTAFETSKFFTDLR--------DGIISDIFD 508
Cdd:cd05067  156 NEYTARegAKFPIKWTAPEAINYGTFTIKSDVWSFGILLTEIVthgRIPYPGMTNPEVIQNLErgyrmprpDNCPEELYQ 235
                        170       180
                 ....*....|....*....|....*...
gi 525343631 509 kkektLLQKLLSKKPEDRPnTSEILRTL 536
Cdd:cd05067  236 -----LMRLCWKERPEDRP-TFEYLRSV 257
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
254-482 1.06e-13

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: 72.75  E-value: 1.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 254 ETKYTVDKRFgmdfKEIELIGSGGFGQVFKAKHRIDGKTYVIKRV--KYNNE----KAEREVKALAKLDHVNIVHYNGCW 327
Cdd:cd07876   14 DSTFTVLKRY----QQLKPIGSGAQGIVCAAFDTVLGINVAVKKLsrPFQNQthakRAYRELVLLKCVNHKNIISLLNVF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 328 DGVDYDPETSDDYLESSDYDpensknssrsKTKCLFIQMEfcdkgtleqwienrrgekLDKVLALELFEQITKGVDYIHS 407
Cdd:cd07876   90 TPQKSLEEFQDVYLVMELMD----------ANLCQVIHME------------------LDHERMSYLLYQMLCGIKHLHS 141
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 408 KKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd07876  142 AGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELV 216
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
397-526 1.14e-13

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: 72.00  E-value: 1.14e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALG 475
Cdd:cd05571  103 EIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEISYGATTKTfCGTPEYLAPEVLEDNDYGRAVDWWGLG 182
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 476 LILAELLhvCDTAFETSKFFTDLRDGIISD------IFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05571  183 VVMYEMM--CGRLPFYNRDHEVLFELILMEevrfpsTLSPEAKSLLAGLLKKDPKKR 237
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
271-534 1.15e-13

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: 71.68  E-value: 1.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIK----RVKYNNEKAEREVKALAKLD-HVNIVHYngcwdgVDYDPETSDDYLessd 345
Cdd:cd14090    8 ELLGEGAYASVQTCINLYTGKEYAVKiiekHPGHSRSRVFREVETLHQCQgHPNILQL------IEYFEDDERFYL---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 ydpensknssrsktkcLFIQMEfcdKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDT 425
Cdd:cd14090   78 ----------------VFEKMR---GGPLLSHIEKRV--HFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESM 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQ---VKIGDFGLVTSLKNDGKRTRSK---------GTLRYMSPEQI-----SSQDYGKEVDLYALGLILAELL------ 482
Cdd:cd14090  137 DKvspVKICDFDLGSGIKLSSTSMTPVttpelltpvGSAEYMAPEVVdafvgEALSYDKRCDLWSLGVILYIMLcgyppf 216
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 483 -------------HVCDTAFEtsKFFTDLRDGIISdiFDKKE--------KTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14090  217 ygrcgedcgwdrgEACQDCQE--LLFHSIQEGEYE--FPEKEwshisaeaKDLISHLLVRDASQRYTAEQVLQ 285
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
266-545 1.27e-13

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: 71.98  E-value: 1.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKT----YVIKRVK-YNNEKAEREVkalakLDhvnivhyngcwdgvdydpetsDDY 340
Cdd:cd05108    8 EFKKIKVLGSGAFGTVYKGLWIPEGEKvkipVAIKELReATSPKANKEI-----LD---------------------EAY 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd05108   62 VMASVDNPHVCRLLGICLTSTVQLITQLMPFGCLLDYVREHK-DNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 421 FLVDTKQVKIGDFGLVTSLKNDGKRTRSKG---TLRYMSPEQISSQDYGKEVDLYALGLILAELLhvcdtafetsKFFTD 497
Cdd:cd05108  141 LVKTPQHVKITDFGLAKLLGAEEKEYHAEGgkvPIKWMALESILHRIYTHQSDVWSYGVTVWELM----------TFGSK 210
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 498 LRDGI----ISDIFDKKEK------------TLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEK 545
Cdd:cd05108  211 PYDGIpaseISSILEKGERlpqppictidvyMIMVKCWMIDADSRPKFRELIIEFSKMARDPQR 274
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
266-483 1.44e-13

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 72.73  E-value: 1.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQV--FKAKH-------RIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNgcwdgvdydpet 336
Cdd:cd05624   73 DFEIIKVIGRGAFGEVavVKMKNteriyamKILNKWEMLKRAETACFREERNVLVNGDCQWITTLHYA------------ 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddylessdYDPENSknssrsktkcLFIQMEFCDKG---TLEQWIENRRGEKLDKVLALELfeqiTKGVDYIHSKKLIHR 413
Cdd:cd05624  141 ---------FQDENY----------LYLVMDYYVGGdllTLLSKFEDKLPEDMARFYIGEM----VLAIHSIHQLHYVHR 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 414 DLKPSNIFLVDTKQVKIGDFGLVTSLKNDG--KRTRSKGTLRYMSPEQISSQD-----YGKEVDLYALGLILAELLH 483
Cdd:cd05624  198 DIKPDNVLLDMNGHIRLADFGSCLKMNDDGtvQSSVAVGTPDYISPEILQAMEdgmgkYGPECDWWSLGVCMYEMLY 274
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
266-481 1.64e-13

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


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 71.62  E-value: 1.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAERE--VKALAKLDHVNIVHYNGCWDGVDYDPETSddyles 343
Cdd:cd06649    6 DFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIRNqiIRELQVLHECNSPYIVGFYGAFYSDGEIS------ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 sdydpensknssrsktkclfIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSK-KLIHRDLKPSNIFL 422
Cdd:cd06649   80 --------------------ICMEHMDGGSLDQVLKEAK--RIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILV 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 423 VDTKQVKIGDFG----LVTSLKNDGKRTRSkgtlrYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd06649  138 NSRGEIKLCDFGvsgqLIDSMANSFVGTRS-----YMSPERLQGTHYSVQSDIWSMGLSLVEL 195
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
242-482 1.83e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 72.80  E-value: 1.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 242 SLAPRFDLP-DMKETKYTVDKRFGMDFKEIELIGSGGFGQVF-----------KAKHRIDG--------KTYVIKRVKYN 301
Cdd:PHA03210 124 EAPPDAAGPvPLAQAKLKHDDEFLAHFRVIDDLPAGAFGKIFicalrasteeaEARRGVNStnqgkpkcERLIAKRVKAG 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 302 NEKA---EREVKALAKLDHVNIVHYNGCWDGVDYDPETSDDY---LESSDYDPEnsknssrsktkclfiqMEFCDKGTLE 375
Cdd:PHA03210 204 SRAAiqlENEILALGRLNHENILKIEEILRSEANTYMITQKYdfdLYSFMYDEA----------------FDWKDRPLLK 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 376 QwieNRRgekldkvlaleLFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDgKRTRSK---GTL 452
Cdd:PHA03210 268 Q---TRA-----------IMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKE-REAFDYgwvGTV 332
                        250       260       270
                 ....*....|....*....|....*....|
gi 525343631 453 RYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:PHA03210 333 ATNSPEILAGDGYCEITDIWSCGLILLDML 362
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
251-482 2.43e-13

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: 71.66  E-value: 2.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 251 DMKETKYTVDKRFgmdfKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK--YNNE----KAEREVKALAKLDHVNIVHYN 324
Cdd:cd07874    7 EVGDSTFTVLKRY----QNLKPIGSGAQGIVCAAYDAVLDRNVAIKKLSrpFQNQthakRAYRELVLMKCVNHKNIISLL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 325 GCWDGVDYDPETSDDYLESSDYDpensknssrsKTKCLFIQMEfcdkgtleqwienrrgekLDKVLALELFEQITKGVDY 404
Cdd:cd07874   83 NVFTPQKSLEEFQDVYLVMELMD----------ANLCQVIQME------------------LDHERMSYLLYQMLCGIKH 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 405 IHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd07874  135 LHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMV 212
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
394-482 2.91e-13

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: 71.23  E-value: 2.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 394 LFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLvtSLKNDGKRTRSKGTLRYMSPE-QISSQDYGKEVDLY 472
Cdd:cd07878  123 LIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGL--ARQADDEMTGYVATRWYRAPEiMLNWMHYNQTVDIW 200
                         90
                 ....*....|
gi 525343631 473 ALGLILAELL 482
Cdd:cd07878  201 SVGCIMAELL 210
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
360-482 2.96e-13

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: 70.45  E-value: 2.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 360 KCLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQ---VKIGDFGLV 436
Cdd:cd14170   72 KCLLIVMECLDGGELFSRIQDRGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPnaiLKLTDFGFA 151
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 525343631 437 TSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14170  152 KETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVIMYILL 197
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
267-531 3.26e-13

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: 70.79  E-value: 3.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALA----------KLDHVNIVHYNGCWDGVDYdpet 336
Cdd:cd05589    1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKKGDIIARDEVESLMcekrifetvnSARHPFLVNLFACFQTPEH---- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddylessdydpensknssrsktkcLFIQMEFCDKGTLEQWIENrrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd05589   77 -------------------------VCFVMEYAAGGDLMMHIHE---DVFSEPRAVFYAACVVLGLQFLHEHKIVYRDLK 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhVCDTAF----ET 491
Cdd:cd05589  129 LDNLLLDTEGYVKIADFGLCKEGMGFGDRTSTfCGTPEFLAPEVLTDTSYTRAVDWWGLGVLIYEML-VGESPFpgddEE 207
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 525343631 492 SKFftdlrDGIISD-----IFDKKEKT-LLQKLLSKKPEDRPNTSE 531
Cdd:cd05589  208 EVF-----DSIVNDevrypRFLSTEAIsIMRRLLRKNPERRLGASE 248
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
261-530 3.31e-13

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: 71.22  E-value: 3.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 261 KRFGM---DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYnnekaerevKALAKLDHVNIVhyngcwdgvdydpETS 337
Cdd:cd05600    4 RRTRLklsDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKK---------KVLFKLNEVNHV-------------LTE 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 338 DDYLESSD--------Y---DPENsknssrsktkcLFIQMEFCDKGTLEQWIENRRGEKLD--KVLALELFEQItkgvDY 404
Cdd:cd05600   62 RDILTTTNspwlvkllYafqDPEN-----------VYLAMEYVPGGDFRTLLNNSGILSEEhaRFYIAEMFAAI----SS 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 405 IHSKKLIHRDLKPSNiFLVDTK-QVKIGDFGLVTSLKNDGKRTRSKGTLR------------------------------ 453
Cdd:cd05600  127 LHQLGYIHRDLKPEN-FLIDSSgHIKLTDFGLASGTLSPKKIESMKIRLEevkntafleltakerrniyramrkedqnya 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 454 --------YMSPEQISSQDYGKEVDLYALGLILAELL-----HVCDTAFETskfFTDLrdgiisdifdKKEKTLLQKLLS 520
Cdd:cd05600  206 nsvvgspdYMAPEVLRGEGYDLTVDYWSLGCILFECLvgfppFSGSTPNET---WANL----------YHWKKTLQRPVY 272
                        330
                 ....*....|
gi 525343631 521 KKPEDRPNTS 530
Cdd:cd05600  273 TDPDLEFNLS 282
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
267-482 3.73e-13

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: 70.91  E-value: 3.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK--YNN----EKAEREVKALAKLDHVNIVHYNGCwdgvdYDPETS-DD 339
Cdd:cd07850    2 YQNLKPIGSGAQGIVCAAYDTVTGQNVAIKKLSrpFQNvthaKRAYRELVLMKLVNHKNIIGLLNV-----FTPQKSlEE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLEssdydpensknssrsktkcLFIQMEFCDkGTLEQWIEnrrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd07850   77 FQD-------------------VYLVMELMD-ANLCQVIQ----MDLDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSN 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd07850  133 IVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMI 195
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
270-533 3.74e-13

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: 69.53  E-value: 3.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIK--RVKYNNEK--AEREVKALAKLDHVNIVHYNGCWDgvdydpetsDDYLessd 345
Cdd:cd14114    7 LEELGTGAFGVVHRCTERATGNNFAAKfiMTPHESDKetVRKEIQIMNQLHHPKLINLHDAFE---------DDNE---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 ydpensknssrsktkcLFIQMEFCDKGTLEQWIENRrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIfLVDT 425
Cdd:cd14114   74 ----------------MVLILEFLSGGELFERIAAE-HYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENI-MCTT 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQ---VKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL------------------HV 484
Cdd:cd14114  136 KRsneVKLIDFGLATHLDPKESVKVTTGTAEFAAPEIVEREPVGFYTDMWAVGVLSYVLLsglspfagenddetlrnvKS 215
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 525343631 485 CDTAFETSKFFTDLRDGiisdifdkkeKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14114  216 CDWNFDDSAFSGISEEA----------KDFIRKLLLADPNKRMTIHQAL 254
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
366-533 3.79e-13

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: 69.69  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 366 MEFCDKGTLEQWIENrrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK---QVKIGDFGLVTSLKND 442
Cdd:cd14106   87 LELAAGGELQTLLDE--EECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEFplgDIKLCDFGISRVIGEG 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 443 GKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVC-----DTAFET----SK----FFTDLRDGIISDIFDk 509
Cdd:cd14106  165 EEIREILGTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTGHspfggDDKQETflniSQcnldFPEELFKDVSPLAID- 243
                        170       180
                 ....*....|....*....|....
gi 525343631 510 kektLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14106  244 ----FIKRLLVKDPEKRLTAKECL 263
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
275-532 3.88e-13

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 69.84  E-value: 3.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 275 SGGFGQVFKAKHRIDGktYVIKRVKYN-------NEKAEREVKALAKLDHVNIVHYNGCwdgvdydpetsddYLESSDYD 347
Cdd:cd14027    3 SGGFGKVSLCFHRTQG--LVVLKTVYTgpnciehNEALLEEGKMMNRLRHSRVVKLLGV-------------ILEEGKYS 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 pensknssrsktkclfIQMEFCDKGTLEQWIEnrrgeKLDKVLALE--LFEQITKGVDYIHSKKLIHRDLKPSNIFLVDT 425
Cdd:cd14027   68 ----------------LVMEYMEKGNLMHVLK-----KVSVPLSVKgrIILEIIEGMAYLHGKGVIHKDLKPENILVDND 126
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQVKIGDFGLVTS-----LKNDGKRTRSK---------GTLRYMSPEQISSQDY--GKEVDLYALGLILAELLhVCDTAF 489
Cdd:cd14027  127 FHIKIADLGLASFkmwskLTKEEHNEQREvdgtakknaGTLYYMAPEHLNDVNAkpTEKSDVYSFAIVLWAIF-ANKEPY 205
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 525343631 490 ETSKFFTDLRDGIIS----DIFDKKEKT------LLQKLLSKKPEDRPNTSEI 532
Cdd:cd14027  206 ENAINEDQIIMCIKSgnrpDVDDITEYCpreiidLMKLCWEANPEARPTFPGI 258
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
267-482 3.94e-13

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


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 70.14  E-value: 3.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER----EVKALAKLDHVNIVHYngcwdgvdydpetSDDYLE 342
Cdd:cd06654   22 YTRFEKIGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKEliinEILVMRENKNPNIVNY-------------LDSYLV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 SSDydpensknssrsktkcLFIQMEFCDKGTLEQWIENrrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd06654   89 GDE----------------LWVVMEYLAGGSLTDVVTE---TCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILL 149
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 423 VDTKQVKIGDFGLVTSLKND-GKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd06654  150 GMDGSVKLTDFGFCAQITPEqSKRSTMVGTPYWMAPEVVTRKAYGPKVDIWSLGIMAIEMI 210
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
352-482 4.03e-13

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: 69.94  E-value: 4.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 352 KNSSRSKTkCLFIQMEFCDKGTLEQWIENR--RGEKLDKVLALELFEQITkgvdYIHSKKLIHRDLKPSNIFLVDTKQVK 429
Cdd:cd14182   76 KDTYETNT-FFFLVFDLMKKGELFDYLTEKvtLSEKETRKIMRALLEVIC----ALHKLNIVHRDLKPENILLDDDMNIK 150
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 430 IGDFGLVTSLKNDGKRTRSKGTLRYMSPEQI------SSQDYGKEVDLYALGLILAELL 482
Cdd:cd14182  151 LTDFGFSCQLDPGEKLREVCGTPGYLAPEIIecsmddNHPGYGKEVDMWSTGVIMYTLL 209
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
266-482 4.26e-13

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


Pssm-ID: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 70.45  E-value: 4.26e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTY---------VIKRVKYNNEKAEREVKALAKLDHVNIVHYngcwdgvdydpet 336
Cdd:cd05597    2 DFEILKVIGRGAFGEVAVVKLKSTEKVYamkilnkweMLKRAETACFREERDVLVNGDRRWITKLHY------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddylesSDYDPENsknssrsktkcLFIQMEFCDKG---TLEQWIENRRGEKLDKVLALELFEQItkgvDYIHSKKLIHR 413
Cdd:cd05597   69 -------AFQDENY-----------LYLVMDYYCGGdllTLLSKFEDRLPEEMARFYLAEMVLAI----DSIHQLGYVHR 126
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 414 DLKPSNIFLVDTKQVKIGDFGLVTSLKNDGK--RTRSKGTLRYMSPEQISSQD-----YGKEVDLYALGLILAELL 482
Cdd:cd05597  127 DIKPDNVLLDRNGHIRLADFGSCLKLREDGTvqSSVAVGTPDYISPEILQAMEdgkgrYGPECDWWSLGVCMYEML 202
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
271-533 4.56e-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: 4.56e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNE---KAEREVKALAKLDHVNIVHYNgcwdgvdydpetsdDYLESSdyd 347
Cdd:cd14107    8 EEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSStraRAFQERDILARLSHRRLTCLL--------------DQFETR--- 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 pensknssrsktKCLFIQMEFCDKGTLEQWIeNRRGEKLDKVLALELfEQITKGVDYIHSKKLIHRDLKPSNIFLV--DT 425
Cdd:cd14107   71 ------------KTLILILELCSSEELLDRL-FLKGVVTEAEVKLYI-QQVLEGIGYLHGMNILHLDIKPDNILMVspTR 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLIlAELLHVCDTAF--ETSK-FFTDLRDGI 502
Cdd:cd14107  137 EDIKICDFGFAQEITPSEHQFSKYGSPEFVAPEIVHQEPVSAATDIWALGVI-AYLSLTCHSPFagENDRaTLLNVAEGV 215
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 525343631 503 IS----DIFDKKE--KTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14107  216 VSwdtpEITHLSEdaKDFIKRVLQPDPEKRPSASECL 252
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
397-536 5.75e-13

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR3 (or Flt4) preferentially binds the ligands VEGFC and VEGFD. VEGFR3 is essential for lymphatic endothelial cell (EC) development and function. It has been shown to regulate adaptive immunity during corneal transplantation. VEGFR3 is upregulated on blood vascular ECs in pathological conditions such as vascular tumors and the periphery of solid tumors. It plays a role in cancer progression and lymph node metastasis. Missense mutations in the VEGFR3 gene are associated with primary human lymphedema. VEGFR3 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 70.01  E-value: 5.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRsKGT----LRYMSPEQISSQDYGKEVDLY 472
Cdd:cd05102  180 QVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARDIYKDPDYVR-KGSarlpLKWMAPESIFDKVYTTQSDVW 258
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 473 ALGLILAELLHVCDTAFE----TSKFFTDLRDGIISDIFDKKEKTLLQKLLS---KKPEDRPNTSEILRTL 536
Cdd:cd05102  259 SFGVLLWEIFSLGASPYPgvqiNEEFCQRLKDGTRMRAPEYATPEIYRIMLScwhGDPKERPTFSDLVEIL 329
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
271-489 5.91e-13

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: 69.61  E-value: 5.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRidGKTYVIKRVKYNNEKA---EREVKALAKLDHVNIVHYNGcwdgvdydpetSDDYlessdyd 347
Cdd:cd14056    1 KTIGKGRYGEVWLGKYR--GEKVAVKIFSSRDEDSwfrETEIYQTVMLRHENILGFIA-----------ADIK------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 pensknSSRSKTKCLFIqMEFCDKGTLEQWIENrrgEKLDKVLALELFEQITKGVDYIHS-------KKLI-HRDLKPSN 419
Cdd:cd14056   61 ------STGSWTQLWLI-TEYHEHGSLYDYLQR---NTLDTEEALRLAYSAASGLAHLHTeivgtqgKPAIaHRDLKSKN 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGKRTRSK-----GTLRYMSPEQISSQ------DYGKEVDLYALGLILAELLHVCDTA 488
Cdd:cd14056  131 ILVKRDGTCCIADLGLAVRYDSDTNTIDIPpnprvGTKRYMAPEVLDDSinpksfESFKMADIYSFGLVLWEIARRCEIG 210

                 .
gi 525343631 489 F 489
Cdd:cd14056  211 G 211
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
271-482 7.04e-13

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: 68.94  E-value: 7.04e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYV---IKRVKYNNEKAER-----EVKALAKLDHVNIVHYNGCwdgvdydpetsddyle 342
Cdd:cd05033   10 KVIGGGEFGEVCSGSLKLPGKKEIdvaIKTLKSGYSDKQRldfltEASIMGQFDHPNVIRLEGV---------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssRSKTKCLFIQMEFCDKGTLEQWIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIfL 422
Cdd:cd05033   74 -------------VTKSRPVMIVTEYMENGSLDKFLRENDG-KFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNI-L 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 423 VDTKQV-KIGDFGL--VTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05033  139 VNSDLVcKVSDFGLsrRLEDSEATYTTKGgKIPIRWTAPEAIAYRKFTSASDVWSFGIVMWEVM 202
DSRM smart00358
Double-stranded RNA binding motif;
101-165 7.41e-13

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 63.44  E-value: 7.41e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631   101 YIGLINRIAQKKRLTVNYEQCA-SGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQI 165
Cdd:smart00358   1 PKSLLQELAQKRKLPPEYELVKeEGPDHAPRFTVTVKVGGKRTGEGEGSSKKEAKQRAAEAALRSL 66
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
266-551 8.17e-13

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 69.08  E-value: 8.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIEL-IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKA--EREVKALAKLDHVNIVHYNGCWDgvdydpetsddyle 342
Cdd:cd14085    3 DFFEIESeLGRGATSVVYRCRQKGTQKPYAVKKLKKTVDKKivRTEIGVLLRLSHPNIIKLKEIFE-------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdyDPENsknssrsktkcLFIQMEFCDKGTL-EQWIENRRGEKLDkvlALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd14085   69 ----TPTE-----------ISLVLELVTGGELfDRIVEKGYYSERD---AADAVKQILEAVAYLHENGIVHRDLKPENLL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 422 LVDTKQ---VKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLhvCdtAFEtsKFFTDL 498
Cdd:cd14085  131 YATPAPdapLKIADFGLSKIVDQQVTMKTVCGTPGYCAPEILRGCAYGPEVDMWSVGVITYILL--C--GFE--PFYDER 204
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 499 RD------------GIISDIFDK---KEKTLLQKLLSKKPEDRPNTSEILRtlTVWKKSPEKNERHTC 551
Cdd:cd14085  205 GDqymfkrilncdyDFVSPWWDDvslNAKDLVKKLIVLDPKKRLTTQQALQ--HPWVTGKAANFAHMD 270
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
273-481 8.41e-13

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: 68.92  E-value: 8.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAkhrIDGKTYV---------IKRVKYNNEKAEREVKALAKLDHVNIVHYNGCWDgvdydpetsddyles 343
Cdd:cd14030   33 IGRGSFKTVYKG---LDTETTVevawcelqdRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWE--------------- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 sdydpensknSSRSKTKCLFIQMEFCDKGTLEQWIENRRGEKLdKVLAlELFEQITKGVDYIHSKK--LIHRDLKPSNIF 421
Cdd:cd14030   95 ----------STVKGKKCIVLVTELMTSGTLKTYLKRFKVMKI-KVLR-SWCRQILKGLQFLHTRTppIIHRDLKCDNIF 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 422 LVD-TKQVKIGDFGLVTsLKNDGKRTRSKGTLRYMSPEqISSQDYGKEVDLYALGLILAEL 481
Cdd:cd14030  163 ITGpTGSVKIGDLGLAT-LKRASFAKSVIGTPEFMAPE-MYEEKYDESVDVYAFGMCMLEM 221
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
296-533 8.43e-13

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 68.33  E-value: 8.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 296 KRVKYNNEKAEREVKALAKLDHVNIVHYNGCWdgVDYDPEtsddylessdydpensknssrsKTKCLFIQmEFCDKGTLE 375
Cdd:cd13984   33 KIFKAQEEKIRAVFDNLIQLDHPNIVKFHRYW--TDVQEE----------------------KARVIFIT-EYMSSGSLK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 376 QWIenRRGEKLDKVLALELFE----QITKGVDYIHS--KKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSK 449
Cdd:cd13984   88 QFL--KKTKKNHKTMNEKSWKrwctQILSALSYLHScdPPIIHGNLTCDTIFIQHNGLIKIGSVAPDAIHNHVKTCREEH 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 450 GTLRYMSPEQISSQDYGKEVDLYALGLILAE--LLHVCDTAFETskffTDLRDGIISDIF---DKKEKTLLQKLLSKKPE 524
Cdd:cd13984  166 RNLHFFAPEYGYLEDVTTAVDIYSFGMCALEmaALEIQSNGEKV----SANEEAIIRAIFsleDPLQKDFIRKCLSVAPQ 241

                 ....*....
gi 525343631 525 DRPNTSEIL 533
Cdd:cd13984  242 DRPSARDLL 250
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
362-482 8.90e-13

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: 69.66  E-value: 8.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRRGEKLDKVL-ALELFE-------------QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQ 427
Cdd:cd05100   93 LYVLVEYASKGNLREYLRARRPPGMDYSFdTCKLPEeqltfkdlvscayQVARGMEYLASQKCIHRDLAARNVLVTEDNV 172
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 428 VKIGDFGLVTSLKNDG---KRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05100  173 MKIADFGLARDVHNIDyykKTTNGRLPVKWMAPEALFDRVYTHQSDVWSFGVLLWEIF 230
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
247-482 9.75e-13

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: 69.55  E-value: 9.75e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 247 FDLPDMKETKYTVDKRFgmdfKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK--YNNE----KAEREVKALAKLDHVNI 320
Cdd:cd07879    1 FYREEVNKTVWELPERY----TSLKQVGSGAYGSVCSAIDKRTGEKVAIKKLSrpFQSEifakRAYRELTLLKHMQHENV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 321 VHyngcWDGVDYDPETSDDYlessdYDpensknssrsktkcLFIQMEFcdkgtLEQWIENRRGEKLDKVLALELFEQITK 400
Cdd:cd07879   77 IG----LLDVFTSAVSGDEF-----QD--------------FYLVMPY-----MQTDLQKIMGHPLSEDKVQYLVYQMLC 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 401 GVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLknDGKRTRSKGTLRYMSPEQISS-QDYGKEVDLYALGLILA 479
Cdd:cd07879  129 GLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHA--DAEMTGYVVTRWYRAPEVILNwMHYNQTVDIWSVGCIMA 206

                 ...
gi 525343631 480 ELL 482
Cdd:cd07879  207 EML 209
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
273-537 1.07e-12

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: 68.35  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYV--IKRVKYNNEKAEREVKALAKLDHVNIVH-YNGCwdgvdydpetsddylessdydpe 349
Cdd:cd05114   12 LGSGLFGVVRLGKWRAQYKVAIkaIREGAMSEEDFIEEAKVMMKLTHPKLVQlYGVC----------------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 350 nsknssrSKTKCLFIQMEFCDKGTLEQWIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVK 429
Cdd:cd05114   69 -------TQQKPIYIVTEFMENGCLLNYLRQRRG-KLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVK 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 430 IGDFGLVTSLKNDgKRTRSKGT---LRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRdgIISDI 506
Cdd:cd05114  141 VSDFGMTRYVLDD-QYTSSSGAkfpVKWSPPEVFNYSKFSSKSDVWSFGVLMWEVFTEGKMPFESKSNYEVVE--MVSRG 217
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 525343631 507 FDKKEKTLLQKLLSK--------KPEDRPNTSEILRTLT 537
Cdd:cd05114  218 HRLYRPKLASKSVYEvmyscwheKPEGRPTFADLLRTIT 256
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
273-480 1.11e-12

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


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 68.07  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRID--GKTYVIKRVKYNNEKAE------REVKALAKLDHVNIVHYNGCWDGvdydpetsddyless 344
Cdd:cd05116    3 LGSGNFGTVKKGYYQMKkvVKTVAVKILKNEANDPAlkdellREANVMQQLDNPYIVRMIGICEA--------------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpensknssrsktKCLFIQMEFCDKGTLEQWIENRRGEKLDKVLalELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd05116   68 ---------------ESWMLVMEMAELGPLNKFLQKNRHVTEKNIT--ELVHQVSMGMKYLEESNFVHRDLAARNVLLVT 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLVTSLKNDGKRTRSKGT----LRYMSPEQISSQDYGKEVDLYALGLILAE 480
Cdd:cd05116  131 QHYAKISDFGLSKALRADENYYKAQTHgkwpVKWYAPECMNYYKFSSKSDVWSFGVLMWE 190
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
397-482 1.12e-12

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: 69.77  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKR--TRSKGTLRYMSPEQI-SSQDYGKEVDLYA 473
Cdd:cd07853  111 QILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPDESKhmTQEVVTQYYRAPEILmGSRHYTSAVDIWS 190

                 ....*....
gi 525343631 474 LGLILAELL 482
Cdd:cd07853  191 VGCIFAELL 199
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
362-482 1.21e-12

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: 68.89  E-value: 1.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRRGEKL----------DKVLALELF----EQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQ 427
Cdd:cd05098   94 LYVIVEYASKGNLREYLQARRPPGMeycynpshnpEEQLSSKDLvscaYQVARGMEYLASKKCIHRDLAARNVLVTEDNV 173
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 428 VKIGDFGLVTSLKNDG---KRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05098  174 MKIADFGLARDIHHIDyykKTTNGRLPVKWMAPEALFDRIYTHQSDVWSFGVLLWEIF 231
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
247-482 1.25e-12

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: 69.30  E-value: 1.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 247 FDLPDMKETKYTVDKRFgmdfKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK--YNNE----KAEREVKALAKLDHVNI 320
Cdd:cd07875   10 FYSVEIGDSTFTVLKRY----QNLKPIGSGAQGIVCAAYDAILERNVAIKKLSrpFQNQthakRAYRELVLMKCVNHKNI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 321 VHYNGCwdgvdYDPETSDDYLESsdydpensknssrsktkcLFIQMEFCDkGTLEQWIEnrrgEKLDKVLALELFEQITK 400
Cdd:cd07875   86 IGLLNV-----FTPQKSLEEFQD------------------VYIVMELMD-ANLCQVIQ----MELDHERMSYLLYQMLC 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 401 GVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAE 480
Cdd:cd07875  138 GIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGE 217

                 ..
gi 525343631 481 LL 482
Cdd:cd07875  218 MI 219
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
270-482 1.36e-12

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: 68.72  E-value: 1.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNE-KAEREVKALAKL-DHVNIVhynGCWDGVdYDPETSD-----DYLE 342
Cdd:cd14132   23 IRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKkKIKREIKILQNLrGGPNIV---KLLDVV-KDPQSKTpslifEYVN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 SSDYdpensknssrsktKCLFiqmefcdkGTLEqwienrrgeklDKVLALELFeQITKGVDYIHSKKLIHRDLKPSNIfL 422
Cdd:cd14132   99 NTDF-------------KTLY--------PTLT-----------DYDIRYYMY-ELLKALDYCHSKGIMHRDVKPHNI-M 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 423 VD--TKQVKIGDFGLVtslknD----GKRTRSK-GTLRYMSPEQ-ISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14132  145 IDheKRKLRLIDWGLA-----EfyhpGQEYNVRvASRYYKGPELlVDYQYYDYSLDMWSLGCMLASMI 207
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
270-485 1.47e-12

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: 68.62  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAkhRIDGKTYVIKRVKYNNEKA---EREVKALAKLDHVNIVHYNGcwdgvdydpetsddylessdy 346
Cdd:cd14142   10 VECIGKGRYGEVWRG--QWQGESVAVKIFSSRDEKSwfrETEIYNTVLLRHENILGFIA--------------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 dpenSKNSSRSKTKCLFIQMEFCDKGTLEQWIENrrgEKLDKVLALELFEQITKGVDYIH-------SKKLI-HRDLKPS 418
Cdd:cd14142   67 ----SDMTSRNSCTQLWLITHYHENGSLYDYLQR---TTLDHQEMLRLALSAASGLVHLHteifgtqGKPAIaHRDLKSK 139
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 419 NIFLVDTKQVKIGDFGL-VTSLKNDGK----RTRSKGTLRYMSPE------QISSQDYGKEVDLYALGLILAELLHVC 485
Cdd:cd14142  140 NILVKSNGQCCIADLGLaVTHSQETNQldvgNNPRVGTKRYMAPEvldetiNTDCFESYKRVDIYAFGLVLWEVARRC 217
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
296-536 1.47e-12

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: 68.19  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 296 KRVKYNnEKAEREVKALAKLDHVNIVHYNGcwdgvdydpetsddYLESSDYDPensknssrsktkCLfiQMEFCDKgTLE 375
Cdd:cd14001   44 QRSLYQ-ERLKEEAKILKSLNHPNIVGFRA--------------FTKSEDGSL------------CL--AMEYGGK-SLN 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 376 QWIENRRGEKLDKVLALELFE---QITKGVDYIHS-KKLIHRDLKPSNIfLV--DTKQVKIGDFGLVTSLKNDGKrTRSK 449
Cdd:cd14001   94 DLIEERYEAGLGPFPAATILKvalSIARALEYLHNeKKILHGDIKSGNV-LIkgDFESVKLCDFGVSLPLTENLE-VDSD 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 450 GTLRYMSPEQISSQDYGKE-------VDLYALGLILAELL-----HV---------CDTAFETSKFFTDL-------RDG 501
Cdd:cd14001  172 PKAQYVGTEPWKAKEALEEggvitdkADIFAYGLVLWEMMtlsvpHLnlldiedddEDESFDEDEEDEEAyygtlgtRPA 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 525343631 502 IISDIFDKKektlLQKLL-------SKKPEDRPNTSEILRTL 536
Cdd:cd14001  252 LNLGELDDS----YQKVIelfyactQEDPKDRPSAAHIVEAL 289
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
266-481 1.49e-12

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: 67.70  E-value: 1.49e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRidGKTYVIKRVKyNNEKAER---EVKALAKLDHVNIVHYNGcwdgVDYDPETSddyle 342
Cdd:cd05082    7 ELKLLQTIGKGEFGDVMLGDYR--GNKVAVKCIK-NDATAQAflaEASVMTQLRHSNLVQLLG----VIVEEKGG----- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd05082   75 -------------------LYIVTEYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLV 135
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 423 VDTKQVKIGDFGL---VTSLKNDGKRtrskgTLRYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd05082  136 SEDNVAKVSDFGLtkeASSTQDTGKL-----PVKWTAPEALREKKFSTKSDVWSFGILLWEI 192
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
101-165 1.60e-12

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 62.63  E-value: 1.60e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631  101 YIGLINRIAQKKRLTVNYE--QCASGVHGPEgFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLAYLQI 165
Cdd:pfam00035   1 PKSLLQEYAQKNGKPPPYEyvSEEGPPHSPK-FTVTVKVDGKLYGSGTGSSKKEAEQLAAEKALEKL 66
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
397-533 1.64e-12

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: 69.27  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTrSKGT----LRYMSPEQISSQDYGKEVDLY 472
Cdd:cd05107  247 QVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLARDIMRDSNYI-SKGStflpLKWMAPESIFNNLYTTLSDVW 325
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 473 ALGLILAELLHVCDTAFE----TSKFFTDLRDGI-------ISD-IFDkkektLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd05107  326 SFGILLWEIFTLGGTPYPelpmNEQFYNAIKRGYrmakpahASDeIYE-----IMQKCWEEKFEIRPDFSQLV 393
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
273-534 1.76e-12

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 67.53  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRV--------KYNNEKAEREVKALAKLDHVNIVHYNgcwdgvdydpetsdDYLESs 344
Cdd:cd14070   10 LGEGSFAKVREGLHAVTGEKVAIKVIdkkkakkdSYVTKNLRREGRIQQMIRHPNITQLL--------------DILET- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 dydpENSknssrsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD 424
Cdd:cd14070   75 ----ENS----------YYLVMELCPGGNLMHRIYDKK--RLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDE 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 425 TKQVKIGDFGLVTSLK----NDGKRTRSkGTLRYMSPEQISSQDYGKEVDLYALGL----ILAELLHVCDTAFETSKFFT 496
Cdd:cd14070  139 NDNIKLIDFGLSNCAGilgySDPFSTQC-GSPAYAAPELLARKKYGPKVDVWSIGVnmyaMLTGTLPFTVEPFSLRALHQ 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 525343631 497 DLRDGIISDI---FDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14070  218 KMVDKEMNPLptdLSPGAISFLRSLLEPDPLKRPNIKQALA 258
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
273-534 1.76e-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: 67.64  E-value: 1.76e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE---REVKALAKLDHVNIVHYNGCwdgvdydpetsddYLESsdydpe 349
Cdd:cd14110   11 INRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQlvlREYQVLRRLSHPRIAQLHSA-------------YLSP------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 350 nsknssrsktKCLFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVK 429
Cdd:cd14110   72 ----------RHLVLIEELCSGPELLYNLAER--NSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLK 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 430 IGDFGLVTSLkNDGKRTRSKGTLRY---MSPEQISSQDYGKEVDLYALGlILAELLHVCDTAFETS---KFFTDLRDGII 503
Cdd:cd14110  140 IVDLGNAQPF-NQGKVLMTDKKGDYvetMAPELLEGQGAGPQTDIWAIG-VTAFIMLSADYPVSSDlnwERDRNIRKGKV 217
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 525343631 504 SdiFDKKEKTL-------LQKLLSKKPEDRPNTSEILR 534
Cdd:cd14110  218 Q--LSRCYAGLsggavnfLKSTLCAKPWGRPTASECLQ 253
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
316-537 1.90e-12

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 67.82  E-value: 1.90e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 316 DHVNIVHYNGCWDGVDYDPETsddylessdyDPENSKNSSRSKTK-CL----FIQMEFCDKGT----LEQWIEnrRGEKL 386
Cdd:cd13974   62 DQDGVVHHHGLFQDRACEIKE----------DKSSNVYTGRVRKRlCLvldcLCAHDFSDKTAdlinLQHYVI--REKRL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 387 DKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL-VDTKQVKIGDFGLVTSLKNDGKR-TRSKGTLRYMSPEQISSQD 464
Cdd:cd13974  130 SEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLnKRTRKITITNFCLGKHLVSEDDLlKDQRGSPAYISPDVLSGKP 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 465 Y-GKEVDLYALGLILAELLH----VCDTAfeTSKFFTDLR--------DGIISDifdkKEKTLLQKLLSKKPEDRPNTSE 531
Cdd:cd13974  210 YlGKPSDMWALGVVLFTMLYgqfpFYDSI--PQELFRKIKaaeytipeDGRVSE----NTVCLIRKLLVLNPQKRLTASE 283

                 ....*.
gi 525343631 532 ILRTLT 537
Cdd:cd13974  284 VLDSLE 289
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
362-501 2.11e-12

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: 68.07  E-value: 2.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRRGEKLDKVLAL-ELFE-------------QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQ 427
Cdd:cd05099   93 LYVIVEYAAKGNLREFLRARRPPGPDYTFDItKVPEeqlsfkdlvscayQVARGMEYLESRRCIHRDLAARNVLVTEDNV 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 428 VKIGDFGLVTSLKN-DGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAF---ETSKFFTDLRDG 501
Cdd:cd05099  173 MKIADFGLARGVHDiDYYKKTSNGRLpvKWMAPEALFDRVYTHQSDVWSFGILMWEIFTLGGSPYpgiPVEELFKLLREG 252
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
362-482 2.42e-12

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 68.12  E-value: 2.42e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRR--------------GEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQ 427
Cdd:cd05101  105 LYVIVEYASKGNLREYLRARRppgmeysydinrvpEEQMTFKDLVSCTYQLARGMEYLASQKCIHRDLAARNVLVTENNV 184
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 428 VKIGDFGLVTSLKN-DGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05101  185 MKIADFGLARDINNiDYYKKTTNGRLpvKWMAPEALFDRVYTHQSDVWSFGVLMWEIF 242
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
266-536 2.47e-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: 68.11  E-value: 2.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN---------NEKAEREVKALAKLDHVNIVHYngcwdgvdydpet 336
Cdd:cd05601    2 DFEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSetlaqeevsFFEEERDIMAKANSPWITKLQY------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddylesSDYDPENsknssrsktkcLFIQMEFCDKGTLEQWIeNRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd05601   69 -------AFQDSEN-----------LYLVMEYHPGGDLLSLL-SRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIK 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLkNDGKRTRSK---GTLRYMSPEQISSQD------YGKEVDLYALGLILAELLhvcdt 487
Cdd:cd05601  130 PENILIDRTGHIKLADFGSAAKL-SSDKTVTSKmpvGTPDYIAPEVLTSMNggskgtYGVECDWWSLGIVAYEML----- 203
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 525343631 488 aFETSKFFTDLRDGIISDIFDKKEKtllqkllSKKPEDrPNTSEILRTL 536
Cdd:cd05601  204 -YGKTPFTEDTVIKTYSNIMNFKKF-------LKFPED-PKVSESAVDL 243
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
273-482 2.94e-12

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 66.93  E-value: 2.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYN---NEKAEREVKALAKLDHVNIVHYngcwdgvdydpetsddylessdydpe 349
Cdd:cd14665    8 IGSGNFGVARLMRDKQTKELVAVKYIERGekiDENVQREIINHRSLRHPNIVRF-------------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 350 nsKNSSRSKTKcLFIQMEFCDKGTLEQWIENrrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK--Q 427
Cdd:cd14665   62 --KEVILTPTH-LAIVMEYAAGGELFERICN--AGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapR 136
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 428 VKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELL 482
Cdd:cd14665  137 LKICDFGYSKSSVLHSQPKSTVGTPAYIAPEVLLKKEYdGKIADVWSCGVTLYVML 192
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
394-534 3.10e-12

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


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 67.27  E-value: 3.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 394 LFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK---QVKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVD 470
Cdd:cd14197  116 LMKQILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKIVDFGLSRILKNSEELREIMGTPEYVAPEILSYEPISTATD 195
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 471 LYALGlILAELLHVCDTAF---ETSKFFTDLRDGIIS------DIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14197  196 MWSIG-VLAYVMLTGISPFlgdDKQETFLNISQMNVSyseeefEHLSESAIDFIKTLLIKKPENRATAEDCLK 267
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
266-482 3.29e-12

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: 68.12  E-value: 3.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVnivhyngcwdgvdYDPETSDDYLESSd 345
Cdd:cd05617   16 DFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQTEKHV-------------FEQASSNPFLVGL- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 ydpenskNSSRSKTKCLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDT 425
Cdd:cd05617   82 -------HSCFQTTSRLFLVIEYVNGGDLMFHMQRQR--KLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDAD 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 426 KQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05617  153 GHIKLTDYGMCKEGLGPGDTTSTfCGTPNYIAPEILRGEEYGFSVDWWALGVLMFEMM 210
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
271-534 3.40e-12

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: 67.36  E-value: 3.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYN----NEKAEREVKALakldhvnivhyngcwdgvdYDPETSDDYLESSDY 346
Cdd:cd14174    8 ELLGEGAYAKVQGCVSLQNGKEYAVKIIEKNaghsRSRVFREVETL-------------------YQCQGNKNILELIEF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 DPENSknssrsktkCLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK 426
Cdd:cd14174   69 FEDDT---------RFYLVFEKLRGGSILAHIQKRK--HFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPD 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 427 Q---VKIGDFGLVTSLKNDG--------KRTRSKGTLRYMSPEQI-----SSQDYGKEVDLYALGLIL------------ 478
Cdd:cd14174  138 KvspVKICDFDLGSGVKLNSactpittpELTTPCGSAEYMAPEVVevftdEATFYDKRCDLWSLGVILyimlsgyppfvg 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 479 ----------AELLHVC-DTAFET---SKFftDLRDGIISDIfDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14174  218 hcgtdcgwdrGEVCRVCqNKLFESiqeGKY--EFPDKDWSHI-SSEAKDLISKLLVRDAKERLSAAQVLQ 284
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
272-481 3.73e-12

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: 67.32  E-value: 3.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSG--GFGQVFKAKHRIDGKTYVIKrvKYNNEKA--------EREVKALAKLDHVNIVHYNGCwdgvdydpetsddYL 341
Cdd:cd08216    5 EIGKCfkGGGVVHLAKHKPTNTLVAVK--KINLESDskedlkflQQEILTSRQLQHPNILPYVTS-------------FV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ESSDydpensknssrsktkcLFIQMEFCDKGTLEQWIENRRGEKL-DKVLALELFEqITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd08216   70 VDND----------------LYVVTPLMAYGSCRDLLKTHFPEGLpELAIAFILRD-VLNALEYIHSKGYIHRSVKASHI 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 421 FLVDTKQVKIGDFGLVTSLKNDGKRTR--------SKGTLRYMSPE--QISSQDYGKEVDLYALGLILAEL 481
Cdd:cd08216  133 LISGDGKVVLSGLRYAYSMVKHGKRQRvvhdfpksSEKNLPWLSPEvlQQNLLGYNEKSDIYSVGITACEL 203
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
397-501 3.94e-12

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


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 68.01  E-value: 3.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTrSKGTLR----YMSPEQISSQDYGKEVDLY 472
Cdd:cd05104  222 QVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNYV-VKGNARlpvkWMAPESIFECVYTFESDVW 300
                         90       100       110
                 ....*....|....*....|....*....|...
gi 525343631 473 ALGLILAELLHVCDTAFE----TSKFFTDLRDG 501
Cdd:cd05104  301 SYGILLWEIFSLGSSPYPgmpvDSKFYKMIKEG 333
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
362-532 4.17e-12

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: 66.68  E-value: 4.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKN 441
Cdd:cd05052   77 FYIITEFMPYGNLLDYLRECNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTG 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 442 D--GKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELlhvcdTAFETSKFftdlrDGI-ISDIFDKKEK------ 512
Cdd:cd05052  157 DtyTAHAGAKFPIKWTAPESLAYNKFSIKSDVWAFGVLLWEI-----ATYGMSPY-----PGIdLSQVYELLEKgyrmer 226
                        170       180
                 ....*....|....*....|....*....
gi 525343631 513 ---------TLLQKLLSKKPEDRPNTSEI 532
Cdd:cd05052  227 pegcppkvyELMRACWQWNPSDRPSFAEI 255
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
261-482 4.19e-12

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 66.42  E-value: 4.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 261 KRFGMDFKEIELIGS-----GGFGQVFKAKHRIDGKTYVIKRVKYNNEKA-EREVKALAKlDHVNIV--HYNGCWDgvdy 332
Cdd:PHA03390   7 SELVQFLKNCEIVKKlklidGKFGKVSVLKHKPTQKLFVQKIIKAKNFNAiEPMVHQLMK-DNPNFIklYYSVTTL---- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 333 dpetsddylessdydpensknssrsktKCLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIH 412
Cdd:PHA03390  82 ---------------------------KGHVLIMDYIKDGDLFDLLKKEG--KLSEAEVKKIIRQLVEALNDLHKHNIIH 132
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 413 RDLKPSNIFLVDTK-QVKIGDFGLVtslKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:PHA03390 133 NDIKLENVLYDRAKdRIYLCDYGLC---KIIGTPSCYDGTLDYFSPEKIKGHNYDVSFDWWAVGVLTYELL 200
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
273-482 4.41e-12

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 66.91  E-value: 4.41e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAK-HRI---DGKTYV-IKRVKYNNEKA----EREVKALAKLDHVNIVHYNG-CWDGvdyDPETSD-DYL 341
Cdd:cd05092   13 LGEGAFGKVFLAEcHNLlpeQDKMLVaVKALKEATESArqdfQREAELLTVLQHQHIVRFYGvCTEG---EPLIMVfEYM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ESSDYDPensknssrsktkclFIQMEFCDKGTLEQWIENRRGEkLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd05092   90 RHGDLNR--------------FLRSHGPDAKILDGGEGQAPGQ-LTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCL 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 422 LVDTKQVKIGDFGLVTSL-KNDGKRT--RSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05092  155 VGQGLVVKIGDFGMSRDIySTDYYRVggRTMLPIRWMPPESILYRKFTTESDIWSFGVVLWEIF 218
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
357-536 6.05e-12

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 66.53  E-value: 6.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 357 SKTKCLFIQMEFCDKGTLEQWI-------ENRRGEKLDKVLAL-ELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQV 428
Cdd:cd05061   79 SKGQPTLVVMELMAHGDLKSYLrslrpeaENNPGRPPPTLQEMiQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTV 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 429 KIGDFGLVTSL-KNDGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFE---TSKFFTDLRDGI 502
Cdd:cd05061  159 KIGDFGMTRDIyETDYYRKGGKGLLpvRWMAPESLKDGVFTTSSDMWSFGVVLWEITSLAEQPYQglsNEQVLKFVMDGG 238
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 525343631 503 ISDIFD---KKEKTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd05061  239 YLDQPDncpERVTDLMRMCWQFNPKMRPTFLEIVNLL 275
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
266-482 6.18e-12

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


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 66.13  E-value: 6.18e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIK-RVKYNNEKAERE--------VKALAKLDHVNIVHYNGCWDGVDydpet 336
Cdd:cd05111    8 ELRKLKVLGSGVFGTVHKGIWIPEGDSIKIPvAIKVIQDRSGRQsfqavtdhMLAIGSLDHAYIVRLLGICPGAS----- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddylessdydpensknssrsktkcLFIQMEFCDKGTLEQWIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd05111   83 -------------------------LQLVTQLLPLGSLLDHVRQHRG-SLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLA 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLKNDGKR---TRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05111  137 ARNVLLKSPSQVQVADFGVADLLYPDDKKyfySEAKTPIKWMALESIHFGKYTHQSDVWSYGVTVWEMM 205
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
273-482 6.77e-12

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: 67.01  E-value: 6.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHR--IDGKTYVIKRVKYN--NEKAEREVKALAKLDHVNIVHYNGCW-DGVDYDPETSDDYLESSDYD 347
Cdd:cd07868   25 VGRGTYGHVYKAKRKdgKDDKDYALKQIEGTgiSMSACREIALLRELKHPNVISLQKVFlSHADRKVWLLFDYAEHDLWH 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 PENSKNSSRSktkclfiqmefcdkgtleqwieNRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV---- 423
Cdd:cd07868  105 IIKFHRASKA----------------------NKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegp 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 424 DTKQVKIGDFGLV----TSLKNDGKRTRSKGTLRYMSPE-QISSQDYGKEVDLYALGLILAELL 482
Cdd:cd07868  163 ERGRVKIADMGFArlfnSPLKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFAELL 226
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
401-482 6.80e-12

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: 66.66  E-value: 6.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 401 GVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILA 479
Cdd:cd05582  109 ALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKESIDHEKKAYSfCGTVEYMAPEVVNRRGHTQSADWWSFGVLMF 188

                 ...
gi 525343631 480 ELL 482
Cdd:cd05582  189 EML 191
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
266-483 6.91e-12

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 67.35  E-value: 6.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAK---------HRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNgcwdgvdydpet 336
Cdd:cd05623   73 DFEILKVIGRGAFGEVAVVKlknadkvfaMKILNKWEMLKRAETACFREERDVLVNGDSQWITTLHYA------------ 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddylessdYDPENSknssrsktkcLFIQMEFCDKG---TLEQWIENRRGEKLDKVLALELfeqiTKGVDYIHSKKLIHR 413
Cdd:cd05623  141 ---------FQDDNN----------LYLVMDYYVGGdllTLLSKFEDRLPEDMARFYLAEM----VLAIDSVHQLHYVHR 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 414 DLKPSNIFLVDTKQVKIGDFGLVTSLKNDG--KRTRSKGTLRYMSPEQISSQD-----YGKEVDLYALGLILAELLH 483
Cdd:cd05623  198 DIKPDNILMDMNGHIRLADFGSCLKLMEDGtvQSSVAVGTPDYISPEILQAMEdgkgkYGPECDWWSLGVCMYEMLY 274
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
271-481 7.27e-12

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 65.66  E-value: 7.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRidGKTYVIKRVKYN--NEKAEREVKALAKLDHVNIVHYNGCwdgvdydpetsddYLESSdydp 348
Cdd:cd05083   12 EIIGEGEFGAVLQGEYM--GQKVAVKNIKCDvtAQAFLEETAVMTKLQHKNLVRLLGV-------------ILHNG---- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 349 ensknssrsktkcLFIQMEFCDKGTLEQWIENRrGEKLDKVLALELFE-QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQ 427
Cdd:cd05083   73 -------------LYIVMELMSKGNLVNFLRSR-GRALVPVIQLLQFSlDVAEGMEYLESKKLVHRDLAARNILVSEDGV 138
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 428 VKIGDFGL--VTSLKNDGKRTRSKGTlrymSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd05083  139 AKISDFGLakVGSMGVDNSRLPVKWT----APEALKNKKFSSKSDVWSYGVLLWEV 190
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
273-482 7.69e-12

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: 66.63  E-value: 7.69e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHR--IDGKTYVIKRVKYN--NEKAEREVKALAKLDHVNIVHYNGCW-DGVDYDPETSDDYLESSDYD 347
Cdd:cd07867   10 VGRGTYGHVYKAKRKdgKDEKEYALKQIEGTgiSMSACREIALLRELKHPNVIALQKVFlSHSDRKVWLLFDYAEHDLWH 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 PENSKNSSRSktkclfiqmefcdkgtleqwieNRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV---- 423
Cdd:cd07867   90 IIKFHRASKA----------------------NKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVMgegp 147
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 424 DTKQVKIGDFGLV----TSLKNDGKRTRSKGTLRYMSPE-QISSQDYGKEVDLYALGLILAELL 482
Cdd:cd07867  148 ERGRVKIADMGFArlfnSPLKPLADLDPVVVTFWYRAPElLLGARHYTKAIDIWAIGCIFAELL 211
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
273-532 7.72e-12

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


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 67.18  E-value: 7.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGK-----TYVIKRVKYNNEKAERE-----VKALAKL-DHVNIVHYNG-CWDG----------- 329
Cdd:cd05106   46 LGAGAFGKVVEATAFGLGKednvlRVAVKMLKASAHTDEREalmseLKILSHLgQHKNIVNLLGaCTHGgpvlviteycc 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 330 ----VDYDPETSDDYLESSDYDPENSKNSSRSKTKCL---FIQME--FCDKGTlEQWIENRRGEKL-------------D 387
Cdd:cd05106  126 ygdlLNFLRKKAETFLNFVMALPEISETSSDYKNITLekkYIRSDsgFSSQGS-DTYVEMRPVSSSssqssdskdeedtE 204
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 388 KVLALELFE------QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGKRTrSKGTLR----YMSP 457
Cdd:cd05106  205 DSWPLDLDDllrfssQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIMNDSNYV-VKGNARlpvkWMAP 283
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 458 EQISSQDYGKEVDLYALGLILAELLHVCDTAFET----SKFFTDLRDGIISD--IFDKKE-KTLLQKLLSKKPEDRPNTS 530
Cdd:cd05106  284 ESIFDCVYTVQSDVWSYGILLWEIFSLGKSPYPGilvnSKFYKMVKRGYQMSrpDFAPPEiYSIMKMCWNLEPTERPTFS 363

                 ..
gi 525343631 531 EI 532
Cdd:cd05106  364 QI 365
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
271-482 7.79e-12

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: 66.05  E-value: 7.79e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGK--TYV-IKRVKYNNEKAER-----EVKALAKLDHVNIVHYNGCwdgvdydpetsddyle 342
Cdd:cd05065   10 EVIGAGEFGEVCRGRLKLPGKreIFVaIKTLKSGYTEKQRrdflsEASIMGQFDHPNIIHLEGV---------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssRSKTKCLFIQMEFCDKGTLEQWIENRRGEkLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIfL 422
Cdd:cd05065   74 -------------VTKSRPVMIITEFMENGALDSFLRQNDGQ-FTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNI-L 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 423 VDTKQV-KIGDFGLVTSLKNDGKRTRSKGTL------RYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05065  139 VNSNLVcKVSDFGLSRFLEDDTSDPTYTSSLggkipiRWTAPEAIAYRKFTSASDVWSYGIVMWEVM 205
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
271-537 8.78e-12

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: 65.44  E-value: 8.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAK-HRIDGKTY-----VIKRVKYNNEKAE----REVKALAKLDHVNIVHYNGCwdgVDYDPetsddy 340
Cdd:cd05040    1 EKLGDGSFGVVRRGEwTTPSGKVIqvavkCLKSDVLSQPNAMddflKEVNAMHSLDHPNLIRLYGV---VLSSP------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 lessdydpensknssrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKVLAlELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd05040   72 ---------------------LMMVTELAPLGSLLDRLRKDQGHFLISTLC-DYAVQIANGMAYLESKRFIHRDLAARNI 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 421 FLVDTKQVKIGDFGLVTSLKNDGKRTRSKGTLR----YMSPEQISSQDYGKEVDLYALGLILAELLHVCdtaFETSKFFT 496
Cdd:cd05040  130 LLASKDKVKIGDFGLMRALPQNEDHYVMQEHRKvpfaWCAPESLKTRKFSHASDVWMFGVTLWEMFTYG---EEPWLGLN 206
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 525343631 497 DLRdgIISDIFDKKEK------------TLLQKLLSKKPEDRPNTSEILRTLT 537
Cdd:cd05040  207 GSQ--ILEKIDKEGERlerpddcpqdiyNVMLQCWAHKPADRPTFVALRDFLP 257
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
266-545 9.70e-12

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: 65.82  E-value: 9.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKT----YVIKRVKYNNE-KAEREVkalakLDhvnivhyngcwdgvdydpetsDDY 340
Cdd:cd05109    8 ELKKVKVLGSGAFGTVYKGIWIPDGENvkipVAIKVLRENTSpKANKEI-----LD---------------------EAY 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSDYDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIENRRGeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNI 420
Cdd:cd05109   62 VMAGVGSPYVCRLLGICLTSTVQLVTQLMPYGCLLDYVRENKD-RIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNV 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 421 FLVDTKQVKIGDFGLVTSLKNDGKRTRSKG---TLRYMSPEQISSQDYGKEVDLYALGLILAELLhvcdtafetsKFFTD 497
Cdd:cd05109  141 LVKSPNHVKITDFGLARLLDIDETEYHADGgkvPIKWMALESILHRRFTHQSDVWSYGVTVWELM----------TFGAK 210
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 498 LRDGI----ISDIFDKKEK------------TLLQKLLSKKPEDRPNTSEILRTLTVWKKSPEK 545
Cdd:cd05109  211 PYDGIpareIPDLLEKGERlpqppictidvyMIMVKCWMIDSECRPRFRELVDEFSRMARDPSR 274
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
397-526 1.10e-11

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: 66.10  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTS-LKNDGKRTRS-KGTLRYMSPEQISSQD-YGKEVDLYA 473
Cdd:cd05614  113 EIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEfLTEEKERTYSfCGTIEYMAPEIIRGKSgHGKAVDWWS 192
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 474 LGLILAELLHVC---------DTAFETSKFFTDLRDGIISdIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05614  193 LGILMFELLTGAspftlegekNTQSEVSRRILKCDPPFPS-FIGPVARDLLQKLLCKDPKKR 253
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
266-482 1.19e-11

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 66.19  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTY---------VIKRVKYNNEKAEREVkaLAKLDHVNIVHyngcwdgvdydpet 336
Cdd:cd05598    2 MFEKIKTIGVGAFGEVSLVRKKDTNALYamktlrkkdVLKRNQVAHVKAERDI--LAEADNEWVVK-------------- 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddyLESSDYDPENsknssrsktkcLFIQMEFCDKGTLeqwienrrgekLDKVLALELFEQ---------ITKGVDYIHS 407
Cdd:cd05598   66 ----LYYSFQDKEN-----------LYFVMDYIPGGDL-----------MSLLIKKGIFEEdlarfyiaeLVCAIESVHK 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 408 KKLIHRDLKPSNIfLVDTK-QVKIGDFGLVTSL--KNDGKRTRSK---GTLRYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd05598  120 MGFIHRDIKPDNI-LIDRDgHIKLTDFGLCTGFrwTHDSKYYLAHslvGTPNYIAPEVLLRTGYTQLCDWWSVGVILYEM 198

                 .
gi 525343631 482 L 482
Cdd:cd05598  199 L 199
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
271-482 1.19e-11

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: 65.27  E-value: 1.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYV---IKRVKYN-NEKAER----EVKALAKLDHVNIVHYNGCwdgvdydpetsddyle 342
Cdd:cd05066   10 KVIGAGEFGEVCSGRLKLPGKREIpvaIKTLKAGyTEKQRRdflsEASIMGQFDHPNIIHLEGV---------------- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssRSKTKCLFIQMEFCDKGTLEQWIENRRGEkLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIfL 422
Cdd:cd05066   74 -------------VTRSKPVMIVTEYMENGSLDAFLRKHDGQ-FTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNI-L 138
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 423 VDTKQV-KIGDFGLVTSLKNDGK----RTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05066  139 VNSNLVcKVSDFGLSRVLEDDPEaaytTRGGKIPIRWTAPEAIAYRKFTSASDVWSYGIVMWEVM 203
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
362-482 1.41e-11

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: 64.94  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKN 441
Cdd:cd14203   64 IYIVTEFMSKGSLLDFLKDGEGKYLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIED 143
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 525343631 442 DGKRTR--SKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14203  144 NEYTARqgAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELV 186
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
266-526 1.50e-11

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 66.21  E-value: 1.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKynnekaerevKALAKLDhvnivhyngcwDGVDYDPETSDDYLESSD 345
Cdd:cd05618   21 DFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVK----------KELVNDD-----------EDIDWVQTEKHVFEQASN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YDPENSKNSSRSKTKCLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDT 425
Cdd:cd05618   80 HPFLVGLHSCFQTESRLFFVIEYVNGGDLMFHMQRQR--KLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQVKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL---HVCDTAFETSKFFTDLRDG 501
Cdd:cd05618  158 GHIKLTDYGMCKEGLRPGDTTSTfCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEMMagrSPFDIVGSSDNPDQNTEDY 237
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 525343631 502 IISDIFDK----------KEKTLLQKLLSKKPEDR 526
Cdd:cd05618  238 LFQVILEKqiriprslsvKAASVLKSFLNKDPKER 272
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
267-533 1.80e-11

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 65.57  E-value: 1.80e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE------REVKALAKLDHVNIVhyngcwdgvdydpETSDDY 340
Cdd:cd07859    2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSdatrilREIKLLRLLRHPDIV-------------EIKHIM 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSdydpensknssRSKTKCLFIQMEFCDKgTLEQWIenrrgeKLDKVLALELFE----QITKGVDYIHSKKLIHRDLK 416
Cdd:cd07859   69 LPPS-----------RREFKDIYVVFELMES-DLHQVI------KANDDLTPEHHQfflyQLLRALKYIHTANVFHRDLK 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLKNDGKR----TRSKGTLRYMSPEQISS--QDYGKEVDLYALGLILAELL-------- 482
Cdd:cd07859  131 PKNILANADCKLKICDFGLARVAFNDTPTaifwTDYVATRWYRAPELCGSffSKYTPAIDIWSIGCIFAEVLtgkplfpg 210
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 483 ----HVCD--TAF---------------ETSKFFTDLRDGI---ISDIF---DKKEKTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd07859  211 knvvHQLDliTDLlgtpspetisrvrneKARRYLSSMRKKQpvpFSQKFpnaDPLALRLLERLLAFDPKDRPTAEEAL 288
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
362-481 2.00e-11

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 64.60  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLvDTKQVKIGDFGL--VTSL 439
Cdd:cd14152   71 LAIITSFCKGRTLYSFVRDPK-TSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFY-DNGKVVITDFGLfgISGV 148
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 525343631 440 KNDGKRTR----SKGTLRYMSPEQISSQDYGKE---------VDLYALGLILAEL 481
Cdd:cd14152  149 VQEGRRENelklPHDWLCYLAPEIVREMTPGKDedclpfskaADVYAFGTIWYEL 203
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
397-526 2.42e-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: 64.38  E-value: 2.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLkNDGKRTRSKGTLRYMSPEQISS-QDYGKEVDLYALG 475
Cdd:cd05606  106 EVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDF-SKKKPHASVGTHGYMAPEVLQKgVAYDSSADWFSLG 184
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 476 LILAELLHvCDTAFETSKffTDLRDGI----------ISDIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05606  185 CMLYKLLK-GHSPFRQHK--TKDKHEIdrmtltmnveLPDSFSPELKSLLEGLLQRDVSKR 242
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
266-512 2.61e-11

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: 64.70  E-value: 2.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIK-RVKYNNE----KAE----REVKALAKLDHVNIVHYNGCwdgvdydpet 336
Cdd:cd05110    8 ELKRVKVLGSGAFGTVYKGIWVPEGETVKIPvAIKILNEttgpKANvefmDEALIMASMDHPHLVRLLGV---------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddylessdydpensknsSRSKTKCLFIQMefCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd05110   78 ------------------CLSPTIQLVTQL--MPHGCLLDYVHEHK-DNIGSQLLLNWCVQIAKGMMYLEERRLVHRDLA 136
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLKNDGKRTRSKG---TLRYMSPEQISSQDYGKEVDLYALGLILAELLhvcdtafetsK 493
Cdd:cd05110  137 ARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGgkmPIKWMALECIHYRKFTHQSDVWSYGVTIWELM----------T 206
                        250       260
                 ....*....|....*....|...
gi 525343631 494 FFTDLRDGI----ISDIFDKKEK 512
Cdd:cd05110  207 FGGKPYDGIptreIPDLLEKGER 229
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
272-533 2.67e-11

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: 64.22  E-value: 2.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRIDGKTYVIKRVKY----------NNEKAEREVKALAKLDhvniVHYNGCWDGVDY--DPETSDD 339
Cdd:cd14100    7 LLGSGGFGSVYSGIRVADGAPVAIKHVEKdrvsewgelpNGTRVPMEIVLLKKVG----SGFRGVIRLLDWfeRPDSFVL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 340 YLESsdydPENSKNssrsktkcLFiqmEF-CDKGTLEQwienrrgekldkVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd14100   83 VLER----PEPVQD--------LF---DFiTERGALPE------------ELARSFFRQVLEAVRHCHNCGVLHRDIKDE 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFL-VDTKQVKIGDFGLVTSLKnDGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELlhVC-DTAFETSKff 495
Cdd:cd14100  136 NILIdLNTGELKLIDFGSGALLK-DTVYTDFDGTRVYSPPEWIRFHRYhGRSAAVWSLGILLYDM--VCgDIPFEHDE-- 210
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 525343631 496 tDLRDGIIsdIFDKKEKTLLQKL----LSKKPEDRPNTSEIL 533
Cdd:cd14100  211 -EIIRGQV--FFRQRVSSECQHLikwcLALRPSDRPSFEDIQ 249
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
271-491 3.55e-11

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 63.87  E-value: 3.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAE---REVKALAKLDHVNIVHYNGcwdgVDYDPetsddylessdyd 347
Cdd:cd14153    6 ELIGKGRFGQVYHGRWHGEVAIRLIDIERDNEEQLKafkREVMAYRQTRHENVVLFMG----ACMSP------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 PENSKNSSRSKTKCLFIQMEfcDKGTLeqwienrrgekLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLvDTKQ 427
Cdd:cd14153   69 PHLAIITSLCKGRTLYSVVR--DAKVV-----------LDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFY-DNGK 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 428 VKIGDFGLVT-------SLKNDGKRTRSkGTLRYMSPE---QISSQD------YGKEVDLYALGLILAElLHVCDTAFET 491
Cdd:cd14153  135 VVITDFGLFTisgvlqaGRREDKLRIQS-GWLCHLAPEiirQLSPETeedklpFSKHSDVFAFGTIWYE-LHAREWPFKT 212
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
377-527 3.71e-11

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 65.02  E-value: 3.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 377 WIENRRGEKLDKVLALElfEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLK--NDGKRTRSKGTLRY 454
Cdd:PHA03212 172 YLAAKRNIAICDILAIE--RSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAACFPVdiNANKYYGWAGTIAT 249
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 455 MSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFEtskfftdlRDGIISDIFDKKEKTLLQKLLSKKPEDRP 527
Cdd:PHA03212 250 NAPELLARDPYGPAVDIWSAGIVLFEMATCHDSLFE--------KDGLDGDCDSDRQIKLIIRRSGTHPNEFP 314
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
362-482 5.17e-11

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


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 63.55  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKN 441
Cdd:cd05069   81 IYIVTEFMGKGSLLDFLKEGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIED 160
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 525343631 442 DGKRTR--SKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05069  161 NEYTARqgAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELV 203
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
266-482 5.35e-11

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


Pssm-ID: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 64.49  E-value: 5.35e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKynneKAEREVKAlaKLDHVnivhyngcwdgvdydpETSDDYLESSD 345
Cdd:cd05629    2 DFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLL----KSEMFKKD--QLAHV----------------KAERDVLAESD 59
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YDPENSKNSSRSKTKCLFIQMEFCDKGTLeqwienrrgekLDKVLALELF-EQITK--------GVDYIHSKKLIHRDLK 416
Cdd:cd05629   60 SPWVVSLYYSFQDAQYLYLIMEFLPGGDL-----------MTMLIKYDTFsEDVTRfymaecvlAIEAVHKLGFIHRDIK 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLK------------------------------------------NDGKRTRSK----- 449
Cdd:cd05629  129 PDNILIDRGGHIKLSDFGLSTGFHkqhdsayyqkllqgksnknridnrnsvavdsinltmsskdqiATWKKNRRLmayst 208
                        250       260       270
                 ....*....|....*....|....*....|....
gi 525343631 450 -GTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05629  209 vGTPDYIAPEIFLQQGYGQECDWWSLGAIMFECL 242
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
386-533 5.36e-11

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


Pssm-ID: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 63.05  E-value: 5.36e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 386 LDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIfLVDTK--QVKIGDFGLVTSLKnDGKRTRSKGTLRYMSPEQISSQ 463
Cdd:cd14102  102 LDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENL-LVDLRtgELKLIDFGSGALLK-DTVYTDFDGTRVYSPPEWIRYH 179
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 464 DY-GKEVDLYALGLILAELlhVC-DTAFETSKFFTDLRdgiisDIFDKKEKTLLQKL----LSKKPEDRPNTSEIL 533
Cdd:cd14102  180 RYhGRSATVWSLGVLLYDM--VCgDIPFEQDEEILRGR-----LYFRRRVSPECQQLikwcLSLRPSDRPTLEQIF 248
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
273-534 5.93e-11

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: 64.00  E-value: 5.93e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKA-----KHRIDGKTYVIKRVK-------YNNEKAEREVkalakldhvnivhyngcwdgvdydPETSDDY 340
Cdd:cd14013    3 LGEGGFGTVYKGsllqkDPGGEKRRVVLKKAKeygeveiWMNERVRRAC------------------------PSSCAEF 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 341 LESSDydpenSKNSSRSKTKCLFIQMEFCDKGTLEQWIENR------------------RGEKLDKVLALELFEQITKGV 402
Cdd:cd14013   59 VGAFL-----DTTSKKFTKPSLWLVWKYEGDATLADLMQGKefpynlepiifgrvlippRGPKRENVIIKSIMRQILVAL 133
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 403 DYIHSKKLIHRDLKPSN-IFLVDTKQVKIGDFGLVTSLKNdGKRTRSKGTL---RYMSPEQ-ISSQDYGK---------- 467
Cdd:cd14013  134 RKLHSTGIVHRDVKPQNiIVSEGDGQFKIIDLGAAADLRI-GINYIPKEFLldpRYAPPEQyIMSTQTPSappapvaaal 212
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 468 -----------EVDLYALGLILAEL-----------------LHVCD------TAFETSKFFTDLRDGI-ISDIFDKKEK 512
Cdd:cd14013  213 spvlwqmnlpdRFDMYSAGVILLQMafpnlrsdsnliafnrqLKQCDydlnawRMLVEPRASADLREGFeILDLDDGAGW 292
                        330       340
                 ....*....|....*....|..
gi 525343631 513 TLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd14013  293 DLVTKLIRYKPRGRLSASAALA 314
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
272-536 6.41e-11

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 63.26  E-value: 6.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKAKHRIDgktYVIKRVKYNNEKA----EREVKALAKLDHVNIVHYngcwdgVDYDPETSDDYLEssdyd 347
Cdd:cd14144    2 SVGKGRYGEVWKGKWRGE---KVAVKIFFTTEEAswfrETEIYQTVLMRHENILGF------IAADIKGTGSWTQ----- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 pensknssrsktkcLFIQMEFCDKGTLEQWIenrRGEKLDKVLALELFEQITKGVDYIHS-------KKLI-HRDLKPSN 419
Cdd:cd14144   68 --------------LYLITDYHENGSLYDFL---RGNTLDTQSMLKLAYSAACGLAHLHTeifgtqgKPAIaHRDIKSKN 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 420 IFLVDTKQVKIGDFGLVTSLKNDGK-----RTRSKGTLRYMSPEQISSQ------DYGKEVDLYALGLILAELLHVCDTA 488
Cdd:cd14144  131 ILVKKNGTCCIADLGLAVKFISETNevdlpPNTRVGTKRYMAPEVLDESlnrnhfDAYKMADMYSFGLVLWEIARRCISG 210
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 525343631 489 FETSKFFTDLRDGIISD--IFDKKEKTLLQKLLSKKPeDRPNTSEILRTL 536
Cdd:cd14144  211 GIVEEYQLPYYDAVPSDpsYEDMRRVVCVERRRPSIP-NRWSSDEVLRTM 259
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
272-531 8.08e-11

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: 63.11  E-value: 8.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 272 LIGSGGFGQVFKA----KHRI--------------DGKTYVIKRvkynnekAEREVKALAKLDHVNIVHYngcWDGVDYD 333
Cdd:cd13990    7 LLGKGGFSEVYKAfdlvEQRYvackihqlnkdwseEKKQNYIKH-------ALREYEIHKSLDHPRIVKL---YDVFEID 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 334 PETsddylessdydpensknssrsktkcLFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYI--HSKKLI 411
Cdd:cd13990   77 TDS-------------------------FCTVLEYCDGNDLDFYL--KQHKSIPEREARSIIMQVVSALKYLneIKPPII 129
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 412 HRDLKPSNIFLVDTKQ---VKIGDFGLVT-----SLKNDGKRTRSK--GTLRYMSPE---------QISSQdygkeVDLY 472
Cdd:cd13990  130 HYDLKPGNILLHSGNVsgeIKITDFGLSKimddeSYNSDGMELTSQgaGTYWYLPPEcfvvgktppKISSK-----VDVW 204
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 473 ALGLILAELLHVCDTAFETSKFFTDLRDGII-----SDIFDK-----KEKTLLQKLLSKKPEDRPNTSE 531
Cdd:cd13990  205 SVGVIFYQMLYGRKPFGHNQSQEAILEENTIlkateVEFPSKpvvssEAKDFIRRCLTYRKEDRPDVLQ 273
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
273-533 8.15e-11

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: 63.25  E-value: 8.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKrVKYNNEKAEREVKALAKL-DHVNIVhyngcwdgvdydpETSDDYLESSDYdPENS 351
Cdd:cd14171   14 LGTGISGPVRVCVKKSTGERFALK-ILLDRPKARTEVRLHMMCsGHPNIV-------------QIYDVYANSVQF-PGES 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 352 KNSSRsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKvlALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQ---V 428
Cdd:cd14171   79 SPRAR-----LLIVMELMEGGELFDRISQHRHFTEKQ--AAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 429 KIGDFGLVTSlkNDGKRTRSKGTLRYMSPEQISSQD-----------------YGKEVDLYALGLILAELLhvCD----- 486
Cdd:cd14171  152 KLCDFGFAKV--DQGDLMTPQFTPYYVAPQVLEAQRrhrkersgiptsptpytYDKSCDMWSLGVIIYIML--CGyppfy 227
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 487 TAFETSKFFTDLRDGIISDIFDKKE----------KTLLQKLLSKKPEDRPNTSEIL 533
Cdd:cd14171  228 SEHPSRTITKDMKRKIMTGSYEFPEeewsqisemaKDIVRKLLCVDPEERMTIEEVL 284
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
266-482 8.75e-11

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: 63.74  E-value: 8.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVK---------YNNEKAEREVKALAKLDHVNIVHYNgcwdgvdydpet 336
Cdd:cd05610    5 EFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVKkadminknmVHQVQAERDALALSKSPFIVHLYYS------------ 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 337 sddyLESSDYdpensknssrsktkcLFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLK 416
Cdd:cd05610   73 ----LQSANN---------------VYLVMEYLIGGDVKSLLHIY--GYFDEEMAVKYISEVALALDYLHRHGIIHRDLK 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 417 PSNIFLVDTKQVKIGDFGL-------------------VTSLKNDGKRT------------------------------- 446
Cdd:cd05610  132 PDNMLISNEGHIKLTDFGLskvtlnrelnmmdilttpsMAKPKNDYSRTpgqvlslisslgfntptpyrtpksvrrgaar 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 525343631 447 ----RSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05610  212 vegeRILGTPDYLAPELLLGKPHGPAVDWWALGVCLFEFL 251
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
271-482 1.02e-10

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: 62.74  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAKHRIDGKTYVIK----RVKYNNEKAEREVKALakldhvnivhyngcwdgvdYDPETSDDYLESSDY 346
Cdd:cd14173    8 EVLGEGAYARVQTCINLITNKEYAVKiiekRPGHSRSRVFREVEML-------------------YQCQGHRNVLELIEF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 DPENSKnssrsktkcLFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK 426
Cdd:cd14173   69 FEEEDK---------FYLVFEKMRGGSILSHIHRRR--HFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPN 137
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 427 Q---VKIGDFGLVTSLKNDGKRTRSK--------GTLRYMSPEQISSQD-----YGKEVDLYALGLILAELL 482
Cdd:cd14173  138 QvspVKICDFDLGSGIKLNSDCSPIStpelltpcGSAEYMAPEVVEAFNeeasiYDKRCDLWSLGVILYIML 209
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
267-482 1.07e-10

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: 63.19  E-value: 1.07e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER---EVKALAKLDhvnivhyngcwdgvdydPETSDDYLES 343
Cdd:cd14227   17 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILKNHPSYARQgqiEVSILARLS-----------------TESADDYNFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 SDYDPENSKNSSrsktkCLFIQMEfcdKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd14227   80 RAYECFQHKNHT-----CLVFEML---EQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLV 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 424 DTK----QVKIGDFGLVTSLKNDGKRTRSKgTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14227  152 DPSrqpyRVKVIDFGSASHVSKAVCSTYLQ-SRYYRAPEIILGLPFCEAIDMWSLGCVIAELF 213
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
266-482 1.25e-10

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 63.15  E-value: 1.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKyNNEKAEREVKALAKLDHVNIVHYNGCWdgvdydpetsddyLESSD 345
Cdd:cd05627    3 DFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILR-KADMLEKEQVAHIRAERDILVEADGAW-------------VVKMF 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YDPENSKNssrsktkcLFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDT 425
Cdd:cd05627   69 YSFQDKRN--------LYLIMEFLPGGDMMTLLMKK--DTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAK 138
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQVKIGDFGLVTSLKN------------------------------DGKRTRSK------GTLRYMSPEQISSQDYGKEV 469
Cdd:cd05627  139 GHVKLSDFGLCTGLKKahrtefyrnlthnppsdfsfqnmnskrkaeTWKKNRRQlaystvGTPDYIAPEVFMQTGYNKLC 218
                        250
                 ....*....|...
gi 525343631 470 DLYALGLILAELL 482
Cdd:cd05627  219 DWWSLGVIMYEML 231
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
362-488 1.44e-10

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: 62.36  E-value: 1.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIenrRGEKLDKVLALELFEQITKGVDYIHSK-----------KLIHRDLKPSNIFLVDTKQVKI 430
Cdd:cd14140   68 LWLITAFHDKGSLTDYL---KGNIVSWNELCHIAETMARGLSYLHEDvprckgeghkpAIAHRDFKSKNVLLKNDLTAVL 144
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 431 GDFGLVTSL---KNDGKRTRSKGTLRYMSPEQIS-----SQDYGKEVDLYALGLILAELLHVCDTA 488
Cdd:cd14140  145 ADFGLAVRFepgKPPGDTHGQVGTRRYMAPEVLEgainfQRDSFLRIDMYAMGLVLWELVSRCKAA 210
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
362-550 1.72e-10

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 62.01  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKN 441
Cdd:cd05071   78 IYIVTEYMSKGSLLDFLKGEMGKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIED 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 442 DGKRTR--SKGTLRYMSPEQISSQDYGKEVDLYALGLILAELlhvcdtafeTSKFFTDLRDGIISDIFDKKEKTLLQKLL 519
Cdd:cd05071  158 NEYTARqgAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTEL---------TTKGRVPYPGMVNREVLDQVERGYRMPCP 228
                        170       180       190
                 ....*....|....*....|....*....|.
gi 525343631 520 SKKPEdrpNTSEILrtLTVWKKSPEknERHT 550
Cdd:cd05071  229 PECPE---SLHDLM--CQCWRKEPE--ERPT 252
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
270-482 2.08e-10

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: 61.95  E-value: 2.08e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDG----KTYVIKRVK-YNNEKA----EREVKALAKLDHVNIVhyngCWDGVDYDPETSD-- 338
Cdd:cd05090   10 MEELGECAFGKIYKGHLYLPGmdhaQLVAIKTLKdYNNPQQwnefQQEASLMTELHHPNIV----CLLGVVTQEQPVCml 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 -DYLESSDYDPENSKNSSRSKTKClfiqmEFCDKGTLEQwienrrgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKP 417
Cdd:cd05090   86 fEFMNQGDLHEFLIMRSPHSDVGC-----SSDEDGTVKS--------SLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAA 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 525343631 418 SNIFLVDTKQVKIGDFGLVTSL-KNDGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05090  153 RNILVGEQLHVKISDLGLSREIySSDYYRVQNKSLLpiRWMPPEAIMYGKFSSDSDIWSFGVVLWEIF 220
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
357-536 2.09e-10

Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. IGF-1R is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the ligand (IGF-1 or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, which stimulates downstream kinase activities and biological function. IGF-1R signaling is important in the differentiation, growth, and survival of normal cells. In cancer cells, where it is frequently overexpressed, IGF-1R is implicated in proliferation, the suppression of apoptosis, invasion, and metastasis. IGF-1R is being developed as a therapeutic target in cancer treatment. The IGF-1R subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 61.59  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 357 SKTKCLFIQMEFCDKGTLEQWIENRRGEK----------LDKVLalELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK 426
Cdd:cd05062   79 SQGQPTLVIMELMTRGDLKSYLRSLRPEMennpvqappsLKKMI--QMAGEIADGMAYLNANKFVHRDLAARNCMVAEDF 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 427 QVKIGDFGLVTSL-KNDGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETSKFFTDLRDGII 503
Cdd:cd05062  157 TVKIGDFGMTRDIyETDYYRKGGKGLLpvRWMSPESLKDGVFTTYSDVWSFGVVLWEIATLAEQPYQGMSNEQVLRFVME 236
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 525343631 504 SDIFDKKEK------TLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd05062  237 GGLLDKPDNcpdmlfELMRMCWQYNPKMRPSFLEIISSI 275
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
100-161 2.38e-10

double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; The family includes EIF2AK2 and adenosine deaminase domain-containing proteins, ADAD1 and ADAD2. EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. ADAD1 (also called testis nuclear RNA-binding protein (TENR)) and ADAD2 (also called testis nuclear RNA-binding protein-like (TENRL)) are phylogenetically related to a family of adenosine deaminases involved in RNA editing. ADAD1 plays an essential function in spermatid morphogenesis. It may be involved in testis-specific nuclear post-transcriptional processes such as heterogeneous nuclear RNA (hnRNA) packaging, alternative splicing, or nuclear/cytoplasmic transport of mRNAs. ADAD2 is a double-stranded RNA binding protein with unclear biological function. Members of this group contains varying numbers of double-stranded RNA binding motifs (DSRMs). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380704  Cd Length: 67  Bit Score: 56.51  E-value: 2.38e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 525343631 100 NYIGLINRIAQKKRLTVNYEQCASGVHGPEGFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLA 161
Cdd:cd19875    2 NPVSALNEYCQKRGLSLEFVDVSVGPDHCPGFTASATIDGIVFASATGTSKKEAKRAAAKLA 63
DSRM smart00358
Double-stranded RNA binding motif;
14-59 2.41e-10

Double-stranded RNA binding motif;


Pssm-ID: 214634 [Multi-domain]  Cd Length: 67  Bit Score: 56.50  E-value: 2.41e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 525343631    14 LNTYRQKQGVVLKYQELPNSGPPHDRRFTFRVIIDEREFPEGEGRS 59
Cdd:smart00358   5 LQELAQKRKLPPEYELVKEEGPDHAPRFTVTVKVGGKRTGEGEGSS 50
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
273-482 3.21e-10

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: 60.94  E-value: 3.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIK---RVKYNNEKAEREVKALAKLDHVNIVHYngcwdgvdydpetsddylessdydpe 349
Cdd:cd14662    8 IGSGNFGVARLMRNKETKELVAVKyieRGLKIDENVQREIINHRSLRHPNIIRF-------------------------- 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 350 nsKNSSRSKTKcLFIQMEFCDKGTLEQWIENRRGEKLDKvlALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVD--TKQ 427
Cdd:cd14662   62 --KEVVLTPTH-LAIVMEYAAGGELFERICNAGRFSEDE--ARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGspAPR 136
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 428 VKIGDFGLVTSLKNDGKRTRSKGTLRYMSPEQISSQDY-GKEVDLYALGLILAELL 482
Cdd:cd14662  137 LKICDFGYSKSSVLHSQPKSTVGTPAYIAPEVLSRKEYdGKVADVWSCGVTLYVML 192
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
397-482 4.14e-10

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: 61.05  E-value: 4.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSK-KLIHRDLKPSNIFL-VDTKQVKIGDFGlvTSLKNDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYAL 474
Cdd:cd14136  127 QVLQGLDYLHTKcGIIHTDIKPENVLLcISKIEVKIADLG--NACWTDKHFTEDIQTRQYRSPEVILGAGYGTPADIWST 204

                 ....*...
gi 525343631 475 GLILAELL 482
Cdd:cd14136  205 ACMAFELA 212
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
362-482 4.39e-10

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: 61.28  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKN 441
Cdd:cd05588   71 LFFVIEFVNGGDLMFHMQRQR--RLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLR 148
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 525343631 442 DGKRTRS-KGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05588  149 PGDTTSTfCGTPNYIAPEILRGEDYGFSVDWWALGVLMFEML 190
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
303-534 4.54e-10

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: 60.80  E-value: 4.54e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 303 EKAEREVKALAKLDHVNIVHYNGCwdgvdydpetsddyLESSdydpensKNSSRSKTKCLFIQME--FCDKGTLEQWIEN 380
Cdd:cd14011   47 ELLKRGVKQLTRLRHPRILTVQHP--------------LEES-------RESLAFATEPVFASLAnvLGERDNMPSPPPE 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 381 RRGEKLDKVLALELFEQITKGVDYIH-SKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDGK-RTRSKG-------- 450
Cdd:cd14011  106 LQDYKLYDVEIKYGLLQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDqFPYFREydpnlppl 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 451 ---TLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDTAFETS-------KFFTDLRDGIIS--DIFDKKEKTLLQKL 518
Cdd:cd14011  186 aqpNLNYLAPEYILSKTCDPASDMFSLGVLIYAIYNKGKPLFDCVnnllsykKNSNQLRQLSLSllEKVPEELRDHVKTL 265
                        250
                 ....*....|....*.
gi 525343631 519 LSKKPEDRPNTSEILR 534
Cdd:cd14011  266 LNVTPEVRPDAEQLSK 281
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
273-482 5.25e-10

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


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 60.44  E-value: 5.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAK-----HRIDGKTYVIKRVKYNNEKAE----REVKALAKLDHVNIVHYNGCWdgVDYDPetsddyles 343
Cdd:cd05093   13 LGEGAFGKVFLAEcynlcPEQDKILVAVKTLKDASDNARkdfhREAELLTNLQHEHIVKFYGVC--VEGDP--------- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 sdydpensknssrsktkcLFIQMEFCDKGTLEQWI-----------ENRRGEKLDKVLALELFEQITKGVDYIHSKKLIH 412
Cdd:cd05093   82 ------------------LIMVFEYMKHGDLNKFLrahgpdavlmaEGNRPAELTQSQMLHIAQQIAAGMVYLASQHFVH 143
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 413 RDLKPSNIFLVDTKQVKIGDFGLVTSL-KNDGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05093  144 RDLATRNCLVGENLLVKIGDFGMSRDVySTDYYRVGGHTMLpiRWMPPESIMYRKFTTESDVWSLGVVLWEIF 216
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
273-482 5.41e-10

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


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 60.41  E-value: 5.41e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAK-----HRIDGKTYVIKRVKYNNEKA----EREVKALAKLDHVNIVHYNG-CWDGvdyDPETSD-DYL 341
Cdd:cd05094   13 LGEGAFGKVFLAEcynlsPTKDKMLVAVKTLKDPTLAArkdfQREAELLTNLQHDHIVKFYGvCGDG---DPLIMVfEYM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 342 ESSDYDPensknssrsktkclFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIF 421
Cdd:cd05094   90 KHGDLNK--------------FLRAHGPDAMILVDGQPRQAKGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCL 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 422 LVDTKQVKIGDFGLVTSL-KNDGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05094  156 VGANLLVKIGDFGMSRDVySTDYYRVGGHTMLpiRWMPPESIMYRKFTTESDVWSFGVILWEIF 219
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
266-520 5.44e-10

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 61.15  E-value: 5.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDG----------KTYVIKRVKYNNEKAERevKALAKLDHVNIVHYNGCWDGVDYdpe 335
Cdd:PTZ00426  31 DFNFIRTLGTGSFGRVILATYKNEDfppvaikrfeKSKIIKQKQVDHVFSER--KILNYINHPFCVNLYGSFKDESY--- 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 336 tsddylessdydpensknssrsktkcLFIQMEFCDKGTLEQWIenRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDL 415
Cdd:PTZ00426 106 --------------------------LYLVLEFVIGGEFFTFL--RRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 416 KPSNIFLVDTKQVKIGDFGLVTSLknDGKRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVCDT--AFETSK 493
Cdd:PTZ00426 158 KPENLLLDKDGFIKMTDFGFAKVV--DTRTYTLCGTPEYIAPEILLNVGHGKAADWWTLGIFIYEILVGCPPfyANEPLL 235
                        250       260
                 ....*....|....*....|....*....
gi 525343631 494 FFTDLRDGII--SDIFDKKEKTLLQKLLS 520
Cdd:PTZ00426 236 IYQKILEGIIyfPKFLDNNCKHLMKKLLS 264
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
270-481 5.63e-10

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: 60.73  E-value: 5.63e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDGKTYVIKRVKynNEKA-----EREVKALAKLDHvnivhyngcwdgvDYDPETSDDYLESS 344
Cdd:cd14212    4 LDLLGQGTFGQVVKCQDLKTNKLVAVKVLK--NKPAyfrqaMLEIAILTLLNT-------------KYDPEDKHHIVRLL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 DYDPENSKnssrsktkcLFIQMEFCDKGTLEQWIENR-RGEKLDkvLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd14212   69 DHFMHHGH---------LCIVFELLGVNLYELLKQNQfRGLSLQ--LIRKFLQQLLDALSVLKDARIIHCDLKPENILLV 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 424 --DTKQVKIGDFGlvtSLKNDGKRTRSKGTLR-YMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd14212  138 nlDSPEIKLIDFG---SACFENYTLYTYIQSRfYRSPEVLLGLPYSTAIDMWSLGCIAAEL 195
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
273-482 5.77e-10

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: 60.00  E-value: 5.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQV---FKAKHRIDGKTYVIKRVKYNNEKAE----REVKALAKLDHVNIVHYNgcwdgvdydpetsdDYLESSD 345
Cdd:cd14163    8 IGEGTYSKVkeaFSKKHQRKVAIKIIDKSGGPEEFIQrflpRELQIVERLDHKNIIHVY--------------EMLESAD 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YDpensknssrsktkcLFIQMEFCDKGTLEQWIENrrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIfLVDT 425
Cdd:cd14163   74 GK--------------IYLVMELAEDGDVFDCVLH--GGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENA-LLQG 136
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQVKIGDFGLVTSLKNDGKRTRSK--GTLRYMSPEQISSQDY-GKEVDLYALGLILAELL 482
Cdd:cd14163  137 FTLKLTDFGFAKQLPKGGRELSQTfcGSTAYAAPEVLQGVPHdSRKGDIWSMGVVLYVML 196
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
362-482 6.06e-10

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: 60.08  E-value: 6.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 362 LFIQMEFCDKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKN 441
Cdd:cd05070   78 IYIVTEYMSKGSLLDFLKDGEGRALKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIED 157
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 525343631 442 DGKRTR--SKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05070  158 NEYTARqgAKFPIKWTAPEAALYGRFTIKSDVWSFGILLTELV 200
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
273-485 6.13e-10

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: 60.22  E-value: 6.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAErEVKALAKLDHVNIVHYNGcwdGVDYDPETSddylessdydpensk 352
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKVRLEVFRAE-ELMACAGLTSPRVVPLYG---AVREGPWVN--------------- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 353 nssrsktkclfIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL-VDTKQVKIG 431
Cdd:cd13991   75 -----------IFMDLKEGGSLGQLIKEQ--GCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLsSDGSDAFLC 141
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 432 DFGLVTSLKNDGKRTRS------KGTLRYMSPEQISSQDYGKEVDLYALGLILAELLHVC 485
Cdd:cd13991  142 DFGHAECLDPDGLGKSLftgdyiPGTETHMAPEVVLGKPCDAKVDVWSSCCMMLHMLNGC 201
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
270-537 6.44e-10

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: 60.43  E-value: 6.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQV---------------FKAKHRIDGKTYV-IKRVKYNNEKA-----EREVKALAKLDHVNIVHYNG-Cw 327
Cdd:cd05051   10 VEKLGEGQFGEVhlceanglsdltsddFIGNDNKDEPVLVaVKMLRPDASKNaredfLKEVKIMSQLKDPNIVRLLGvC- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 328 dgvdydpeTSDDylessdydPensknssrsktkcLFIQMEFCDKGTLEQWIENRRGEKLDKVLALELF----------EQ 397
Cdd:cd05051   89 --------TRDE--------P-------------LCMIVEYMENGDLNQFLQKHEAETQGASATNSKTlsygtllymaTQ 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 398 ITKGVDYIHSKKLIHRDLKPSNIfLVDTK-QVKIGDFGLVTSL-KNDGKRTRSKGTL--RYMSPEQISSQDYGKEVDLYA 473
Cdd:cd05051  140 IASGMKYLESLNFVHRDLATRNC-LVGPNyTIKIADFGMSRNLySGDYYRIEGRAVLpiRWMAWESILLGKFTTKSDVWA 218
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 474 LGLILAELLHVC-DTAFE----------TSKFFTDLRDGII--------SDIFDkkektLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd05051  219 FGVTLWEILTLCkEQPYEhltdeqvienAGEFFRDDGMEVYlsrppncpKEIYE-----LMLECWRRDEEDRPTFREIHL 293

                 ...
gi 525343631 535 TLT 537
Cdd:cd05051  294 FLQ 296
DSRM_ADAD1 cd19905
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) ...
105-161 6.46e-10

double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) and similar proteins; ADAD1 (also known as testis nuclear RNA-binding protein (TENR)) is phylogenetically related to a family of adenosine deaminases involved in RNA editing. It plays an essential function in spermatid morphogenesis. It may be involved in testis-specific nuclear post-transcriptional processes such as heterogeneous nuclear RNA (hnRNA) packaging, alternative splicing, or nuclear/cytoplasmic transport of mRNAs. ADAD1 contains a double-stranded RNA binding motif (DSRM) and a C-terminal adenosine-deaminase (editase) domain. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380734  Cd Length: 69  Bit Score: 55.35  E-value: 6.46e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 525343631 105 INRIAQKKRLTVNYEQCA--SGVHGPEgFHYKCKMGQKEYSIGTGSTKQEAKQLAAKLA 161
Cdd:cd19905    7 LHEYAQMTRLKLSFKETVttGNVAGPY-FAFCAVVDGIEYPTGVGKTKKEAKANAAKIA 64
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
381-549 6.99e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 61.45  E-value: 6.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 381 RRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKndGKRTRS-----KGTLRYM 455
Cdd:PHA03211 252 ARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACFAR--GSWSTPfhygiAGTVDTN 329
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 456 SPEQISSQDYGKEVDLYALGLILAEllhvcdTAFETSKFFTdlrdgiisdifdkkektllqklLSKKPEDRPNTSEILRT 535
Cdd:PHA03211 330 APEVLAGDPYTPSVDIWSAGLVIFE------AAVHTASLFS----------------------ASRGDERRPYDAQILRI 381
                        170
                 ....*....|....
gi 525343631 536 LTVWKKSPEKNERH 549
Cdd:PHA03211 382 IRQAQVHVDEFPQH 395
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
273-434 7.25e-10

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: 57.07  E-value: 7.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNN----EKAEREVKALAKLD--HVNIVHYngcwdgvdYDPETSDDYLessdy 346
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGDDVNneegEDLESEMDILRRLKglELNIPKV--------LVTEDVDGPN----- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 347 dpensknssrsktkclFIQMEFCDKGTLEQWIEnrrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTK 426
Cdd:cd13968   68 ----------------ILLMELVKGGTLIAYTQ---EEELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDG 128

                 ....*...
gi 525343631 427 QVKIGDFG 434
Cdd:cd13968  129 NVKLIDFG 136
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
267-482 7.42e-10

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: 60.43  E-value: 7.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER---EVKALAKLDHvnivhyngcwdgvdydpETSDDYLES 343
Cdd:cd14229    2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILKNHPSYARQgqiEVGILARLSN-----------------ENADEFNFV 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 SDYDPENSKNSSrsktkCLFIQMefcdkgtLEQ----WIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSN 419
Cdd:cd14229   65 RAYECFQHRNHT-----CLVFEM-------LEQnlydFLKQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPEN 132
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 420 IFLVD----TKQVKIGDFGLVTSLKNDGKRTRSKGTLrYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14229  133 IMLVDpvrqPYRVKVIDFGSASHVSKTVCSTYLQSRY-YRAPEIILGLPFCEAIDMWSLGCVIAELF 198
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
282-536 7.66e-10

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


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 59.87  E-value: 7.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 282 FKAKHRIDGKTYVIKRVKYN----NEKAEREVKALAKLDHVNIVHYNGcwdGVDYDPETSddylessdydpensknssrs 357
Cdd:cd14045   22 FTQTGIYDGRTVAIKKIAKKsftlSKRIRKEVKQVRELDHPNLCKFIG---GCIEVPNVA-------------------- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 358 ktkclfIQMEFCDKGTLEQWIENRRgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVT 437
Cdd:cd14045   79 ------IITEYCPKGSLNDVLLNED-IPLNWGFRFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 438 SLKNDGKRT----RSKGTLRYMSPEQISSQDY--GKEVDLYALGLILAELLHVCDTAFETSKFFTD-----LRDGIISDI 506
Cdd:cd14045  152 YRKEDGSENasgyQQRLMQVYLPPENHSNTDTepTQATDVYSYAIILLEIATRNDPVPEDDYSLDEawcppLPELISGKT 231
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 525343631 507 FDK-----KEKTLLQKLLSKKPEDRPNTSEILRTL 536
Cdd:cd14045  232 ENScpcpaDYVELIRRCRKNNPAQRPTFEQIKKTL 266
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
266-526 7.84e-10

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 60.01  E-value: 7.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVF---KAKHRIDGKTYVIKRVK----------YNNEKAEREVkalakLDHVNivhyngcwdgvdy 332
Cdd:cd05613    1 NFELLKVLGTGAYGKVFlvrKVSGHDAGKLYAMKVLKkativqkaktAEHTRTERQV-----LEHIR------------- 62
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 333 dpetSDDYLESSDYdpensknSSRSKTKcLFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIH 412
Cdd:cd05613   63 ----QSPFLVTLHY-------AFQTDTK-LHLILDYINGGELFTHLSQR--ERFTENEVQIYIGEIVLALEHLHKLGIIY 128
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 413 RDLKPSNIFLVDTKQVKIGDFGLVTS-LKNDGKRTRSK-GTLRYMSPEQISSQDYG--KEVDLYALGLILAELLHvcdta 488
Cdd:cd05613  129 RDIKLENILLDSSGHVVLTDFGLSKEfLLDENERAYSFcGTIEYMAPEIVRGGDSGhdKAVDWWSLGVLMYELLT----- 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 525343631 489 fETSKFFTDLRDGIISDIFD---KKE-----------KTLLQKLLSKKPEDR 526
Cdd:cd05613  204 -GASPFTVDGEKNSQAEISRrilKSEppypqemsalaKDIIQRLLMKDPKKR 254
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
265-481 8.05e-10

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: 59.51  E-value: 8.05e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 265 MDFKEIELI---GSGGFG--QVFKAKHRIDGKTYVIKRVKYNNEKAEREVKALAKLDHVNIVHYNG-Cwdgvdydpetsd 338
Cdd:cd05113    1 IDPKDLTFLkelGTGQFGvvKYGKWRGQYDVAIKMIKEGSMSEDEFIEEAKVMMNLSHEKLVQLYGvC------------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 dylessdydpensknssrSKTKCLFIQMEFCDKGTLEQWIENRrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd05113   69 ------------------TKQRPIFIITEYMANGCLLNYLREM-RKRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAAR 129
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631 419 NIFLVDTKQVKIGDFGLVTSLKNDgKRTRSKGT---LRYMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd05113  130 NCLVNDQGVVKVSDFGLSRYVLDD-EYTSSVGSkfpVRWSPPEVLMYSKFSSKSDVWAFGVLMWEV 194
DSRM_EIF2AK2-like cd19875
double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 ...
11-64 8.65e-10

double-stranded RNA binding motif of eukaryotic translation initiation factor 2-alpha kinase 2 (EIF2AK2) and similar proteins; The family includes EIF2AK2 and adenosine deaminase domain-containing proteins, ADAD1 and ADAD2. EIF2AK2 (EC 2.7.11.1/EC 2.7.10.2; also known as interferon-induced, double-stranded RNA-activated protein kinase, eIF-2A protein kinase 2, interferon-inducible RNA-dependent protein kinase, P1/eIF-2A protein kinase, protein kinase RNA-activated (PKR), protein kinase R, tyrosine-protein kinase EIF2AK2, or p68 kinase) acts as an IFN-induced dsRNA-dependent serine/threonine-protein kinase which plays a key role in the innate immune response to viral infection and is also involved in the regulation of signal transduction, apoptosis, cell proliferation and differentiation. ADAD1 (also called testis nuclear RNA-binding protein (TENR)) and ADAD2 (also called testis nuclear RNA-binding protein-like (TENRL)) are phylogenetically related to a family of adenosine deaminases involved in RNA editing. ADAD1 plays an essential function in spermatid morphogenesis. It may be involved in testis-specific nuclear post-transcriptional processes such as heterogeneous nuclear RNA (hnRNA) packaging, alternative splicing, or nuclear/cytoplasmic transport of mRNAs. ADAD2 is a double-stranded RNA binding protein with unclear biological function. Members of this group contains varying numbers of double-stranded RNA binding motifs (DSRMs). DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380704  Cd Length: 67  Bit Score: 54.97  E-value: 8.65e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 525343631  11 MEELNTYRQKQGVVLKYQELPnSGPPHDRRFTFRVIIDEREFPEGEGRSKKEAK 64
Cdd:cd19875    4 VSALNEYCQKRGLSLEFVDVS-VGPDHCPGFTASATIDGIVFASATGTSKKEAK 56
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
269-482 1.19e-09

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


Pssm-ID: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 59.55  E-value: 1.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 269 EIELIGSGGFGQVFKAKHRiDGKTYV-IKRVKYNNEKAEREVKALakLDHVNIVH-----YNGCWDGVDYDPETsddyle 342
Cdd:cd14026    1 DLRYLSRGAFGTVSRARHA-DWRVTVaIKCLKLDSPVGDSERNCL--LKEAEILHkarfsYILPILGICNEPEF------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 ssdydpensknssrsktkcLFIQMEFCDKGTLEQWIeNRRGEKLDKV--LALELFEQITKGVDYIH--SKKLIHRDLKPS 418
Cdd:cd14026   72 -------------------LGIVTEYMTNGSLNELL-HEKDIYPDVAwpLRLRILYEIALGVNYLHnmSPPLLHHDLKTQ 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 419 NIFLVDTKQVKIGDFGL----VTSLKNDGKRTRSK--GTLRYMSPEQIS-SQDYGKEV--DLYALGLILAELL 482
Cdd:cd14026  132 NILLDGEFHVKIADFGLskwrQLSISQSRSSKSAPegGTIIYMPPEEYEpSQKRRASVkhDIYSYAIIMWEVL 204
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
381-527 1.69e-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: 58.66  E-value: 1.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 381 RRGEKLDKVLALELfeQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVtslKNDGKRTRS-KGTLRYMSPEQ 459
Cdd:cd13975   96 KAGLSLEERLQIAL--DVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFC---KPEAMMSGSiVGTPIHMAPEL 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 460 ISSQdYGKEVDLYALGLIlaeLLHVCD------TAFETSK----FFTDLRDGIISD---IFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd13975  171 FSGK-YDNSVDVYAFGIL---FWYLCAghvklpEAFEQCAskdhLWNNVRKGVRPErlpVFDEECWNLMEACWSGDPSQR 246

                 .
gi 525343631 527 P 527
Cdd:cd13975  247 P 247
PTKc_Aatyk2 cd05086
Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs ...
270-537 2.49e-09

Catalytic domain of the Protein Tyrosine Kinase, Apoptosis-associated tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk2 is a member of the Aatyk subfamily of proteins, which are receptor kinases containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk2 is also called lemur tyrosine kinase 2 (Lmtk2) or brain-enriched kinase (Brek). It is expressed at high levels in early postnatal brain, and has been shown to play a role in nerve growth factor (NGF) signaling. Studies with knockout mice reveal that Aatyk2 is essential for late stage spermatogenesis. Although it is classified as a PTK based on sequence similarity and the phylogenetic tree, Aatyk2 has been functionally characterized as a serine/threonine kinase. The Aatyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270669 [Multi-domain]  Cd Length: 271  Bit Score: 58.34  E-value: 2.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAK-HRIDGKTYVIkrVKynnekaerEVKALAkldhvnivhyngcwdgvdyDPETSDDYLESSD-YD 347
Cdd:cd05086    2 IQEIGNGWFGKVLLGEiYTGTSVARVV--VK--------ELKASA-------------------NPKEQDDFLQQGEpYY 52
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 PENSKNSSRSKTKCL-----FIQMEFCDKGTLEQWIENRRgEKL----DKVLALELFEQITKGVDYIHSKKLIHRDLKPS 418
Cdd:cd05086   53 ILQHPNILQCVGQCVeaipyLLVFEFCDLGDLKTYLANQQ-EKLrgdsQIMLLQRMACEIAAGLAHMHKHNFLHSDLALR 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 419 NIFLVDTKQVKIGDFGL-VTSLKNDGKRTRSK--GTLRYMSPEQISSQ-------DYGKEVDLYALGLILAELLhvcDTA 488
Cdd:cd05086  132 NCYLTSDLTVKVGDYGIgFSRYKEDYIETDDKkyAPLRWTAPELVTSFqdgllaaEQTKYSNIWSLGVTLWELF---ENA 208
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 525343631 489 FETSKFFTDLRdgIISDIFDKKEKTLLQKLLSK---------------KPEDRPNTSEILRTLT 537
Cdd:cd05086  209 AQPYSDLSDRE--VLNHVIKERQVKLFKPHLEQpysdrwyevlqfcwlSPEKRPTAEEVHRLLT 270
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
267-482 2.71e-09

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: 58.95  E-value: 2.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 267 FKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER---EVKALAKLDhvnivhyngcwdgvdydPETSDDYLES 343
Cdd:cd14228   17 YEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILKNHPSYARQgqiEVSILSRLS-----------------SENADEYNFV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 344 SDYDPENSKNSSrsktkCLFIQMEfcdKGTLEQWIENRRGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLV 423
Cdd:cd14228   80 RSYECFQHKNHT-----CLVFEML---EQNLYDFLKQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLV 151
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 424 D----TKQVKIGDFGLVTSLKNDGKRTRSKgTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd14228  152 DpvrqPYRVKVIDFGSASHVSKAVCSTYLQ-SRYYRAPEIILGLPFCEAIDMWSLGCVIAELF 213
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
362-482 2.76e-09

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


Pssm-ID: 274846 [Multi-domain]  Cd Length: 1266  Bit Score: 60.24  E-value: 2.76e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631   362 LFIQMEFCDKGTLEQWIENrrgeklDKVLALE----LFEQITKGVDYIHSKKLIHRDLKPSNIFLV---DTKQVKIGDFG 434
Cdd:TIGR03903   54 LFAVFEYVPGRTLREVLAA------DGALPAGetgrLMLQVLDALACAHNQGIVHRDLKPQNIMVSqtgVRPHAKVLDFG 127
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 525343631   435 LVTSLKNDGKRTRSK--------GTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:TIGR03903  128 IGTLLPGVRDADVATltrttevlGTPTYCAPEQLRGEPVTPNSDLYAWGLIFLECL 183
PTKc_Aatyk cd05042
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs ...
366-537 3.37e-09

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Aatyk subfamily is also referred to as the lemur tyrosine kinase (Lmtk) subfamily. It consists of Aatyk1 (Lmtk1), Aatyk2 (Lmtk2, Brek), Aatyk3 (Lmtk3), and similar proteins. Aatyk proteins are mostly receptor PTKs (RTKs) containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. Aatyk1 does not contain a transmembrane segment and is a cytoplasmic (or nonreceptor) kinase. Aatyk proteins are classified as PTKs based on overall sequence similarity and the phylogenetic tree. However, analysis of catalytic residues suggests that Aatyk proteins may be multispecific kinases, functioning also as serine/threonine kinases. They are involved in neural differentiation, nerve growth factor (NGF) signaling, apoptosis, and spermatogenesis. The Aatyk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270638 [Multi-domain]  Cd Length: 269  Bit Score: 57.98  E-value: 3.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 366 MEFCDKGTLEQWIENRRGEKL---DKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTS-LKN 441
Cdd:cd05042   74 MEFCDLGDLKAYLRSEREHERgdsDTRTLQRMACEVAAGLAHLHKLNFVHSDLALRNCLLTSDLTVKIGDYGLAHSrYKE 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 442 DGKRTRSKG--TLRYMSPEQISS-------QDYGKEVDLYALGLILAELLhvcDTAFETSKFFTDLR--DGIISDIFDKK 510
Cdd:cd05042  154 DYIETDDKLwfPLRWTAPELVTEfhdrllvVDQTKYSNIWSLGVTLWELF---ENGAQPYSNLSDLDvlAQVVREQDTKL 230
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 525343631 511 EKTLLQKLLSKK-----------PEDRPNTSEILRTLT 537
Cdd:cd05042  231 PKPQLELPYSDRwyevlqfcwlsPEQRPAAEDVHLLLT 268
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
266-526 3.81e-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: 58.53  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER-EVKALAKLDHVNIVHYNGCwdgvdydpetsdDYLESS 344
Cdd:cd05633    6 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgETLALNERIMLSLVSTGDC------------PFIVCM 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 345 DYdpensknSSRSKTKCLFIqMEFCDKGTLEQWIENRR--GEKLDKVLALElfeqITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd05633   74 TY-------AFHTPDKLCFI-LDLMNGGDLHYHLSQHGvfSEKEMRFYATE----IILGLEHMHNRFVVYRDLKPANILL 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 423 VDTKQVKIGDFGLVTSLKNDgKRTRSKGTLRYMSPEQISS-QDYGKEVDLYALGLILAELL--------HVCDTAFETSK 493
Cdd:cd05633  142 DEHGHVRISDLGLACDFSKK-KPHASVGTHGYMAPEVLQKgTAYDSSADWFSLGCMLFKLLrghspfrqHKTKDKHEIDR 220
                        250       260       270
                 ....*....|....*....|....*....|...
gi 525343631 494 fFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05633  221 -MTLTVNVELPDSFSPELKSLLEGLLQRDVSKR 252
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
266-482 4.05e-09

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: 58.14  E-value: 4.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAER-EVKALAKLDHVNIVHYNGCWDGV--DYDPETSD---- 338
Cdd:cd14223    1 DFSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQgETLALNERIMLSLVSTGDCPFIVcmSYAFHTPDklsf 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 339 --DYLESSDYDPENSKNSSRSKTKCLFIQMEfcdkgtleqwienrrgekldkvlalelfeqITKGVDYIHSKKLIHRDLK 416
Cdd:cd14223   81 ilDLMNGGDLHYHLSQHGVFSEAEMRFYAAE------------------------------IILGLEHMHSRFVVYRDLK 130
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 525343631 417 PSNIFLVDTKQVKIGDFGLVTSLKNDgKRTRSKGTLRYMSPEQISSQ-DYGKEVDLYALGLILAELL 482
Cdd:cd14223  131 PANILLDEFGHVRISDLGLACDFSKK-KPHASVGTHGYMAPEVLQKGvAYDSSADWFSLGCMLFKLL 196
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
266-482 4.25e-09

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 58.51  E-value: 4.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 266 DFKEIELIGSGGFGQVFKAKHRIDGKTYVIKRVKyNNEKAEREVKALAKLDHVNIVHYNGCWdgvdydpetsddyLESSD 345
Cdd:cd05628    2 DFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILR-KADMLEKEQVGHIRAERDILVEADSLW-------------VVKMF 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YDPENSKNssrsktkcLFIQMEFCDKGTLEQWIENRrgEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDT 425
Cdd:cd05628   68 YSFQDKLN--------LYLIMEFLPGGDMMTLLMKK--DTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSK 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 426 KQVKIGDFGLVTSLKN------------------------------DGKRTRSK------GTLRYMSPEQISSQDYGKEV 469
Cdd:cd05628  138 GHVKLSDFGLCTGLKKahrtefyrnlnhslpsdftfqnmnskrkaeTWKRNRRQlafstvGTPDYIAPEVFMQTGYNKLC 217
                        250
                 ....*....|...
gi 525343631 470 DLYALGLILAELL 482
Cdd:cd05628  218 DWWSLGVIMYEML 230
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
370-535 4.45e-09

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: 57.05  E-value: 4.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 370 DKGTLEQWIENRRgeKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKNDG---KRT 446
Cdd:cd13976   67 DHGDLHSYVRSRK--RLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLESLEDAVILEGeddSLS 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 447 RSKGTLRYMSPEQISSQDY--GKEVDLYALGLILAELLhVCDTAF---ETSKFFTDLRDG--IISDIFDKKEKTLLQKLL 519
Cdd:cd13976  145 DKHGCPAYVSPEILNSGATysGKAADVWSLGVILYTML-VGRYPFhdsEPASLFAKIRRGqfAIPETLSPRARCLIRSLL 223
                        170
                 ....*....|....*.
gi 525343631 520 SKKPEDRPNTSEILRT 535
Cdd:cd13976  224 RREPSERLTAEDILLH 239
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
273-526 4.93e-09

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: 57.97  E-value: 4.93e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 273 IGSGGFGQVFKAKHRIDGKTYVIKRVKYNNEKAEREVKAlaKLDHVNIVHYNGCWD-----GVDYDPETSDDYLESSDYD 347
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKEVAH--TIGERNILVRTALDEspfivGLKFSFQTPTDLYLVTDYM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 348 PENSknssrsktkcLFIQMEFcdkgtleqwiENRRGEKLDKVLALELfeqiTKGVDYIHSKKLIHRDLKPSNIFLVDTKQ 427
Cdd:cd05586   79 SGGE----------LFWHLQK----------EGRFSEDRAKFYIAEL----VLALEHLHKNDIVYRDLKPENILLDANGH 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 428 VKIGDFGLVTSLKNDGKRTRS-KGTLRYMSPE-QISSQDYGKEVDLYALGLILAELlhVCD----TAFETSKFFTDLRDG 501
Cdd:cd05586  135 IALCDFGLSKADLTDNKTTNTfCGTTEYLAPEvLLDEKGYTKMVDFWSLGVLVFEM--CCGwspfYAEDTQQMYRNIAFG 212
                        250       260
                 ....*....|....*....|....*...
gi 525343631 502 II---SDIFDKKEKTLLQKLLSKKPEDR 526
Cdd:cd05586  213 KVrfpKDVLSDEGRSFVKGLLNRNPKHR 240
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
268-482 5.71e-09

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: 57.03  E-value: 5.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 268 KEIELIGSGGFGQVFKAkhRIDGKTYV-IKRVK---YNNEKAEREVKALAKLDHVNIVH-YNGCwdgvdydpetsddyle 342
Cdd:cd05068   11 KLLRKLGSGQFGEVWEG--LWNNTTPVaVKTLKpgtMDPEDFLREAQIMKKLRHPKLIQlYAVC---------------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 343 sSDYDPensknssrsktkcLFIQMEFCDKGTLEQWIENRrGEKLDKVLALELFEQITKGVDYIHSKKLIHRDLKPSNIFL 422
Cdd:cd05068   73 -TLEEP-------------IYIITELMKHGSLLEYLQGK-GRSLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLV 137
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 423 VDTKQVKIGDFGLVTSLKNDG---KRTRSKGTLRYMSPEQISSQDYGKEVDLYALGLILAELL 482
Cdd:cd05068  138 GENNICKVADFGLARVIKVEDeyeAREGAKFPIKWTAPEAANYNRFSIKSDVWSFGILLTEIV 200
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
397-534 5.96e-09

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


Pssm-ID: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 57.10  E-value: 5.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSLKND-----GKRTRSKGTLRYMSPEQISSQDYGKEVDL 471
Cdd:cd05058  106 QVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDIYDKeyysvHNHTGAKLPVKWMALESLQTQKFTTKSDV 185
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 525343631 472 YALGLILAELL--------HVcdTAFETSKFFTDLRDGIISDIFDKKEKTLLQKLLSKKPEDRPNTSEILR 534
Cdd:cd05058  186 WSFGVLLWELMtrgappypDV--DSFDITVYLLQGRRLLQPEYCPDPLYEVMLSCWHPKPEMRPTFSELVS 254
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
270-481 8.35e-09

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: 57.33  E-value: 8.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 270 IELIGSGGFGQVFKAKHRIDgKTYV----IKRVKYNNEKAEREVKALAKLDHvnivhyngcwdgvdydpetsddylessd 345
Cdd:cd14226   18 DSLIGKGSFGQVVKAYDHVE-QEWVaikiIKNKKAFLNQAQIEVRLLELMNK---------------------------- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 YDPENSKNSSRSKTK-------CL---FIQMEFCD--KGTleqwieNRRGEKLDkvLALELFEQITKGVDYIHSKKL--I 411
Cdd:cd14226   69 HDTENKYYIVRLKRHfmfrnhlCLvfeLLSYNLYDllRNT------NFRGVSLN--LTRKFAQQLCTALLFLSTPELsiI 140
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631 412 HRDLKPSNIFLVDTK--QVKIGDFGLVTSLkndGKRTRSKGTLR-YMSPEQISSQDYGKEVDLYALGLILAEL 481
Cdd:cd14226  141 HCDLKPENILLCNPKrsAIKIIDFGSSCQL---GQRIYQYIQSRfYRSPEVLLGLPYDLAIDMWSLGCILVEM 210
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
271-488 8.99e-09

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: 56.97  E-value: 8.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 271 ELIGSGGFGQVFKAK---HRIDGKTYVIK-RVKYNNEkaeREVKALAKLDHVNIVHYNGCWD-GVDYDPEtsddylessd 345
Cdd:cd14141    1 EIKARGRFGCVWKAQllnEYVAVKIFPIQdKLSWQNE---YEIYSLPGMKHENILQFIGAEKrGTNLDVD---------- 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 346 ydpensknssrsktkcLFIQMEFCDKGTLEQWIenrrgeKLDKVLALEL---FEQITKGVDYIHSK----------KLIH 412
Cdd:cd14141   68 ----------------LWLITAFHEKGSLTDYL------KANVVSWNELchiAQTMARGLAYLHEDipglkdghkpAIAH 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 413 RDLKPSNIFLVDTKQVKIGDFGLVTSL---KNDGKRTRSKGTLRYMSPEQIS-----SQDYGKEVDLYALGLILAELLHV 484
Cdd:cd14141  126 RDIKSKNVLLKNNLTACIADFGLALKFeagKSAGDTHGQVGTRRYMAPEVLEgainfQRDAFLRIDMYAMGLVLWELASR 205

                 ....
gi 525343631 485 CDTA 488
Cdd:cd14141  206 CTAS 209
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
397-501 9.22e-09

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: 56.69  E-value: 9.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 525343631 397 QITKGVDYIHSKKLIHRDLKPSNIFLVDTKQVKIGDFGLVTSL---------KNDGKrtrskgTLRYMSPEQISSQDYGK 467
Cdd:cd05043  124 QIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLfpmdyhclgDNENR------PIKWMSLESLVNKEYSS 197
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 525343631 468 EVDLYALGLILAELLHVCDTAFETSKFF---TDLRDG 501
Cdd:cd05043  198 ASDVWSFGVLLWELMTLGQTPYVEIDPFemaAYLKDG 234
DSRM_ADAD1 cd19905
double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) ...
14-86 6.11e-04

double-stranded RNA binding motif of adenosine deaminase domain-containing protein 1 (ADAD1) and similar proteins; ADAD1 (also known as testis nuclear RNA-binding protein (TENR)) is phylogenetically related to a family of adenosine deaminases involved in RNA editing. It plays an essential function in spermatid morphogenesis. It may be involved in testis-specific nuclear post-transcriptional processes such as heterogeneous nuclear RNA (hnRNA) packaging, alternative splicing, or nuclear/cytoplasmic transport of mRNAs. ADAD1 contains a double-stranded RNA binding motif (DSRM) and a C-terminal adenosine-deaminase (editase) domain. DSRM is not sequence specific, but highly specific for dsRNAs of various origin and structure.


Pssm-ID: 380734  Cd Length: 69  Bit Score: 38.40  E-value: 6.11e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 525343631  14 LNTYRQKQGVVLKYQELPNSGPPHDRRFTFRVIIDEREFPEGEGRSKKEAKNaaaklaveilNKEKKAVSPLL 86
Cdd:cd19905    7 LHEYAQMTRLKLSFKETVTTGNVAGPYFAFCAVVDGIEYPTGVGKTKKEAKA----------NAAKIALDELL 69
dsrm pfam00035
Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training ...
13-64 2.09e-03

Double-stranded RNA binding motif; Sequences gathered for seed by HMM_iterative_training Putative motif shared by proteins that bind to dsRNA. At least some DSRM proteins seem to bind to specific RNA targets. Exemplified by Staufen, which is involved in localization of at least five different mRNAs in the early Drosophila embryo. Also by interferon-induced protein kinase in humans, which is part of the cellular response to dsRNA.


Pssm-ID: 425434 [Multi-domain]  Cd Length: 66  Bit Score: 36.82  E-value: 2.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 525343631   13 ELNTYRQKQGVVLKYQELPNSGPPHDRRFTFRVIIDEREFPEGEGRSKKEAK 64
Cdd:pfam00035   4 LLQEYAQKNGKPPPYEYVSEEGPPHSPKFTVTVKVDGKLYGSGTGSSKKEAE 55
 
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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