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Conserved domains on  [gi|145309300|ref|NP_112557|]
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cyclin-dependent kinase 13 isoform 2 [Homo sapiens]

Protein Classification

cyclin-dependent kinase( domain architecture ID 10167630)

cyclin-dependent kinase (CDK) is a serine/threonine-protein kinase that catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; similar to CDK12 that phosphorylates the C-terminal domain (CTD) of the large subunit of RNA polymerase II (POLR2A), thereby acting as a key regulator of transcription elongation

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
697-998 0e+00

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: 659.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  697 WGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKED 776
Cdd:cd07864     1 WGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLKEIVTDKQD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 ALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd07864    81 ALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPA 936
Cdd:cd07864   161 GLARLYNSEESRPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCPA 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  937 VWPDVIKLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd07864   241 VWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
 
Name Accession Description Interval E-value
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
697-998 0e+00

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: 659.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  697 WGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKED 776
Cdd:cd07864     1 WGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLKEIVTDKQD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 ALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd07864    81 ALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPA 936
Cdd:cd07864   161 GLARLYNSEESRPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCPA 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  937 VWPDVIKLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd07864   241 VWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
705-994 4.82e-89

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 289.82  E-value: 4.82e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300    705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgFPITAIREIKILRQLTHQSIINMKEIVTDKEDaldfkkdk 784
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK-DRERILREIKILKKLKHPNIVRLYDVFEDEDK-------- 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300    785 gaFYLVFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYS 863
Cdd:smart00220   72 --LYLVMEYCEGgDLFDLLKKR-GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLD 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300    864 SEESrpYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQelaQLELISRICGSPCPAVWPDVIK 943
Cdd:smart00220  149 PGEK--LTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDD---QLLELFKKIGKPKPPFPPPEWD 222
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|.
gi 145309300    944 lpyfntmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:smart00220  223 -----------------------ISPEAKDLIRKLLVKDPEKRLTAEEALQ 250
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
702-1002 3.43e-79

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 263.22  E-value: 3.43e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVtdkedaldfK 781
Cdd:PLN00009    1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVV---------H 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDKgAFYLVFEYMDHDLMGLLESGlVHFNENH--IKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR-GQIKLADFGL 858
Cdd:PLN00009   72 SEK-RLYLVFEYLDLDLKKHMDSS-PDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRtNALKLADFGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYSSEeSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVW 938
Cdd:PLN00009  150 ARAFGIP-VRTFTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETW 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  939 PDVIKLPYFNTMKPKkqYRRKLREEFV-FIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVE 1002
Cdd:PLN00009  229 PGVTSLPDYKSAFPK--WPPKDLATVVpTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKDLG 291
Pkinase pfam00069
Protein kinase domain;
705-998 2.20e-55

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 192.07  E-value: 2.20e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300   705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDaldfkkdk 784
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDN-------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300   785 gaFYLVFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKknflhrdikcsnillnnrgqikladfglarlys 863
Cdd:pfam00069   73 --LYLVLEYVEGgSLFDLLSEK-GAFSEREAKFIMKQILEGLESGSS--------------------------------- 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300   864 seesrpYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELIsricgspcpavwpdvIK 943
Cdd:pfam00069  117 ------LTTFVGTPWYMAPE-VLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELI---------------ID 174
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 145309300   944 LPYFNTMKPKKqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:pfam00069  175 QPYAFPELPSN------------LSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
702-1193 2.32e-46

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 174.82  E-value: 2.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLD-----NEKEGFpitaIREIKILRQLTHQSIINMkeivtdked 776
Cdd:COG0515     6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPElaadpEARERF----RREARALARLNHPNIVRV--------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 aLDFKKDKGAFYLVFEYMD-HDLMGLLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLAD 855
Cdd:COG0515    73 -YDVGEEDGRPYLVMEYVEgESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLID 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  856 FGLARLYSSEESRPYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANqelAQLELISRICGSPCP 935
Cdd:COG0515   151 FGIARALGGATLTQTGTVVGTPGYMAPEQARG-EPVDPRSDVYSLGVTLYELLTGRPPFDGD---SPAELLRAHLREPPP 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  936 AVwpdviklpyfntmkpkkqyrRKLREEfvfIPAAALDLFDYMLALDPSKRCTAEQALQCEfLRDVEPSKMPPPDLPLWQ 1015
Cdd:COG0515   227 PP--------------------SELRPD---LPPALDAIVLRALAKDPEERYQSAAELAAA-LRAVLRSLAAAAAAAAAA 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300 1016 DC--HELWSKKRRRQKQMGMTDDVSTIKAPRKDLSLGLDDSRTNTPQGVLPSSQLKSQGSSNVAPGEKQTDPSTPQQESS 1093
Cdd:COG0515   283 AAaaAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAA 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300 1094 KPLGGIQPSSQTIQPKVETDAAQAAVQSAFAVLLTQLIKAQQSKQKDVLLEERENGSGHEASLQLRPPPEPSTPVSGQDD 1173
Cdd:COG0515   363 AAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAA 442
                         490       500
                  ....*....|....*....|
gi 145309300 1174 LIQHQDMRILELTPEPDRPR 1193
Cdd:COG0515   443 RLLAAAAAAAAAAAAAPLLA 462
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
707-915 1.36e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 101.03  E-value: 1.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  707 IIGIIGEGTYGQVYKARDKDTGEMVALKKVRLD-NEKEGFpiTA--IREIKILRQLTHQSIINMkeivtdkedaLDFKKD 783
Cdd:NF033483   11 IGERIGRGGMAEVYLAKDTRLDRDVAVKVLRPDlARDPEF--VArfRREAQSAASLSHPNIVSV----------YDVGED 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMD-HDLMGLL-ESGLVHFNEnhIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL 861
Cdd:NF033483   79 GGIPYIVMEYVDgRTLKDYIrEHGPLSPEE--AVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARA 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  862 ySSEESRPYTNKVI-TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQ 915
Cdd:NF033483  157 -LSSTTMTQTNSVLgTVHYLSPEQARG-GTVDARSDIYSLGIVLYEMLTGRPPFD 209
 
Name Accession Description Interval E-value
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
697-998 0e+00

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: 659.19  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  697 WGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKED 776
Cdd:cd07864     1 WGKRCVDKFDIIGIIGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAIREIKILRQLNHRSVVNLKEIVTDKQD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 ALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd07864    81 ALDFKKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADF 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPA 936
Cdd:cd07864   161 GLARLYNSEESRPYTNKVITLWYRPPELLLGEERYGPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRLCGSPCPA 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  937 VWPDVIKLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd07864   241 VWPDVIKLPYFNTMKPKKQYRRRLREEFSFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
705-997 1.09e-177

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: 529.83  E-value: 1.09e-177
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEdaldFKKDK 784
Cdd:cd07840     1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPITAIREIKLLQKLDHPNVVRLKEIVTSKG----SAKYK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSS 864
Cdd:cd07840    77 GSIYMVFEYMDHDLTGLLDNPEVKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGLARPYTK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  865 EESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKL 944
Cdd:cd07840   157 ENNADYTNRVITLWYRPPELLLGATRYGPEVDMWSVGCILAELFTGKPIFQGKTELEQLEKIFELCGSPTEENWPGVSDL 236
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  945 PYFNTMKPKKQYRRKLREEFV-FIPAAALDLFDYMLALDPSKRCTAEQALQCEF 997
Cdd:cd07840   237 PWFENLKPKKPYKRRLREVFKnVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
705-994 4.93e-127

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: 395.31  E-value: 4.93e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdk 784
Cdd:cd07829     1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALKKIRLDNEEEGIPSTALREISLLKELKHPNIVKLLDVIHTEN--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSS 864
Cdd:cd07829    72 -KLYLVFEYCDQDLKKYLDKRPGPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGLARAFGI 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  865 EeSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKL 944
Cdd:cd07829   151 P-LRTYTHEVVTLWYRAPEILLGSKHYSTAVDIWSVGCIFAELITGKPLFPGDSEIDQLFKIFQILGTPTEESWPGVTKL 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 145309300  945 PYFNtMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd07829   230 PDYK-PTFPKWPKNDLEKVLPRLDPEGIDLLSKMLQYNPAKRISAKEALK 278
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
702-997 9.85e-126

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: 392.89  E-value: 9.85e-126
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKedALDFK 781
Cdd:cd07865    11 VSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKEGFPITALREIKILQLLKHENVVNLIEICRTK--ATPYN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL 861
Cdd:cd07865    89 RYKGSIYLVFEFCEHDLAGLLSNKNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARA 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  862 YS-SEESRP--YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVW 938
Cdd:cd07865   169 FSlAKNSQPnrYTNRVVTLWYRPPELLLGERDYGPPIDMWGAGCIMAEMWTRSPIMQGNTEQHQLTLISQLCGSITPEVW 248
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  939 PDVIKLPYFNTMK-PKKQYRR-KLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEF 997
Cdd:cd07865   249 PGVDKLELFKKMElPQGQKRKvKERLKPYVKDPYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
700-997 3.37e-119

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: 374.64  E-value: 3.37e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  700 RCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKedald 779
Cdd:cd07843     2 RSVDEYEKLNRIEEGTYGVVYRARDKKTGEIVALKKLKMEKEKEGFPITSLREINILLKLQHPNIVTVKEVVVGS----- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fKKDKgaFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd07843    77 -NLDK--IYMVMEYVEHDLKSLMETMKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGLA 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RLYSSEeSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWP 939
Cdd:cd07843   154 REYGSP-LKPYTQLVVTLWYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGKSEIDQLNKIFKLLGTPTEKIWP 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  940 DVIKLPYFNTMKPKKQYRRKLREEF--VFIPAAALDLFDYMLALDPSKRCTAEQALQCEF 997
Cdd:cd07843   233 GFSELPGAKKKTFTKYPYNQLRKKFpaLSLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
702-997 7.43e-118

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: 371.65  E-value: 7.43e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDalDFK 781
Cdd:cd07866     7 LRDYEILGKLGEGTFGEVYKARQIKTGRVVALKKILMHNEKDGFPITALREIKILKKLKHPNVVPLIDMAVERPD--KSK 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL 861
Cdd:cd07866    85 RKRGSVYMVTPYMDHDLSGLLENPSVKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFGLARP 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  862 Y----------SSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICG 931
Cdd:cd07866   165 YdgpppnpkggGGGGTRKYTNLVVTRWYRPPELLLGERRYTTAVDIWGIGCVFAEMFTRRPILQGKSDIDQLHLIFKLCG 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  932 SPCPAVWPDVIKLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEF 997
Cdd:cd07866   245 TPTEETWPGWRSLPGCEGVHSFTNYPRTLEERFGKLGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
700-1007 2.53e-110

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: 350.90  E-value: 2.53e-110
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  700 RCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKedALD 779
Cdd:cd07845     4 RSVTEFEKLNRIGEGTYGIVYRARDTTSGEIVALKKVRMDNERDGIPISSLREITLLLNLRHPNIVELKEVVVGK--HLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkkdkgAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd07845    82 ------SIFLVMEYCEQDLASLLDNMPTPFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RLYSSEeSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWP 939
Cdd:cd07845   156 RTYGLP-AKPMTPKVVTLWYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSEIEQLDLIIQLLGTPNESIWP 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  940 DVIKLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRD----VEPSKMP 1007
Cdd:cd07845   235 GFSDLPLVGKFTLPKQPYNNLKHKFPWLSEAGLRLLNFLLMYDPKKRATAEEALESSYFKEkplpCEPEMMP 306
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
704-1012 1.18e-104

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: 334.93  E-value: 1.18e-104
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKE---GFPITAIREIKILRQLTHQSIInmkeivtdkeDALDF 780
Cdd:cd07841     1 RYEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKLGERKEakdGINFTALREIKLLQELKHPNII----------GLLDV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 KKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR 860
Cdd:cd07841    71 FGHKSNINLVFEFMETDLEKVIKDKSIVLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLAR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 LYSSEeSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPD 940
Cdd:cd07841   151 SFGSP-NRKMTHQVVTRWYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVPFLPGDSDIDQLGKIFEALGTPTEENWPG 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  941 VIKLPYFNTMKPKKQYrrKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRdVEPSKMPPPDLP 1012
Cdd:cd07841   230 VTSLPDYVEFKPFPPT--PLKQIFPAASDDALDLLQRLLTLNPNKRITARQALEHPYFS-NDPAPTPPSQLP 298
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
711-994 5.53e-94

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: 304.60  E-value: 5.53e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDkEDALdfkkdkgafYLV 790
Cdd:cd07835     7 IGEGTYGVVYKARDKLTGEIVALKKIRLETEDEGVPSTAIREISLLKELNHPNIVRLLDVVHS-ENKL---------YLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHDLMGLLES-GLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEeSRP 869
Cdd:cd07835    77 FEFLDLDLKKYMDSsPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFGVP-VRT 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  870 YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPYFNT 949
Cdd:cd07835   156 YTHEVVTLWYRAPEILLGSKHYSTPVDIWSVGCIFAEMVTRRPLFPGDSEIDQLFRIFRTLGTPDEDVWPGVTSLPDYKP 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 145309300  950 MKPKKQyRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd07835   236 TFPKWA-RQDLSKVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQ 279
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
705-994 4.82e-89

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 289.82  E-value: 4.82e-89
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300    705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgFPITAIREIKILRQLTHQSIINMKEIVTDKEDaldfkkdk 784
Cdd:smart00220    1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIKK-DRERILREIKILKKLKHPNIVRLYDVFEDEDK-------- 71
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300    785 gaFYLVFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYS 863
Cdd:smart00220   72 --LYLVMEYCEGgDLFDLLKKR-GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLD 148
                           170       180       190       200       210       220       230       240
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300    864 SEESrpYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQelaQLELISRICGSPCPAVWPDVIK 943
Cdd:smart00220  149 PGEK--LTTFVGTPEYMAPEVLLG-KGYGKAVDIWSLGVILYELLTGKPPFPGDD---QLLELFKKIGKPKPPFPPPEWD 222
                           250       260       270       280       290
                    ....*....|....*....|....*....|....*....|....*....|.
gi 145309300    944 lpyfntmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:smart00220  223 -----------------------ISPEAKDLIRKLLVKDPEKRLTAEEALQ 250
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
704-998 5.54e-88

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: 288.07  E-value: 5.54e-88
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQL-THQSIINMKEIVTDKEDaldfkk 782
Cdd:cd07832     1 RYKILGRIGEGAHGIVFKAKDRETGETVALKKVALRKLEGGIPNQALREIKALQACqGHPYVVKLRDVFPHGTG------ 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgaFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd07832    75 ----FVLVFEYMLSSLSEVLRDEERPLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLF 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVI 942
Cdd:cd07832   151 SEEDPRLYSHQVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGENDIEQLAIVLRTLGTPNEKTWPELT 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  943 KLPYFNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd07832   231 SLPDYNKITFPESKGIRLEEIFPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
705-998 1.33e-84

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: 278.39  E-value: 1.33e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLT---HQSIINMKEIVTDKEDALDFK 781
Cdd:cd07838     1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKVRVPLSEEGIPLSTIREIALLKQLEsfeHPNVVRLLDVCHGPRTDRELK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgaFYLVFEYMDHDLMGLLE----SGLvhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG 857
Cdd:cd07838    81 -----LTLVFEHVDQDLATYLDkcpkPGL---PPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARLYSSEESRpyTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAV 937
Cdd:cd07838   153 LARIYSFEMAL--TSVVVTLWYRAPEVLLQSS-YATPVDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDVIGLPSEEE 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  938 WPDVIKLpyfntmkPKKQYRRKLREEFV-FIP---AAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd07838   230 WPRNSAL-------PRSSFPSYTPRPFKsFVPeidEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
705-997 3.93e-83

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: 274.00  E-value: 3.93e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMkeivtdkedaLDFKKDK 784
Cdd:cd07860     2 FQKVEKIGEGTYGVVYKARNKLTGEVVALKKIRLDTETEGVPSTAIREISLLKELNHPNIVKL----------LDVIHTE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVFEYMDHDLMGLLESGLVH-FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYS 863
Cdd:cd07860    72 NKLYLVFEFLHQDLKKFMDASALTgIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEeSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIK 943
Cdd:cd07860   152 VP-VRTYTHEVVTLWYRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDSEIDQLFRIFRTLGTPDEVVWPGVTS 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  944 LPYFNTMKPKkqYRRKLREEFV-FIPAAALDLFDYMLALDPSKRCTAEQALQCEF 997
Cdd:cd07860   231 MPDYKPSFPK--WARQDFSKVVpPLDEDGRDLLSQMLHYDPNKRISAKAALAHPF 283
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
704-994 7.14e-83

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: 274.55  E-value: 7.14e-83
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKD--TGEMVALKKVRLDNEK-EGFPITAIREIKILRQLTHQSIINMKEIVTDKEDaldf 780
Cdd:cd07842     1 KYEIEGCIGRGTYGRVYKAKRKNgkDGKEYAIKKFKGDKEQyTGISQSACREIALLRELKHENVVSLVEVFLEHAD---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdkGAFYLVFEYMDHDLMGLL----ESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL----NNRGQIK 852
Cdd:cd07842    77 ----KSVYLLFDYAEHDLWQIIkfhrQAKRVSIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVK 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFGLARLYSSEESRPYT-NK-VITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQE---------LA 921
Cdd:cd07842   153 IGDLGLARLFNAPLKPLADlDPvVVTIWYRAPELLLGARHYTKAIDIWAIGCIFAELLTLEPIFKGREAkikksnpfqRD 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  922 QLELISRICGSPCPAVWPDVIKLPYFNTMKPKKQYRR-------KLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd07842   233 QLERIFEVLGTPTEKDWPDIKKMPEYDTLKSDTKASTypnsllaKWMHKHKKPDSQGFDLLRKLLEYDPTKRITAEEALE 312
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
711-994 5.95e-82

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: 270.89  E-value: 5.95e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEkEGFPITAIREIKILRQLTHQSIINMKEIVtDKEDALdfkkdkgafYLV 790
Cdd:cd07836     8 LGEGTYATVYKGRNRTTGEIVALKEIHLDAE-EGTPSTAIREISLMKELKHENIVRLHDVI-HTENKL---------MLV 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHDLMGLLESGLVH--FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESR 868
Cdd:cd07836    77 FEYMDKDLKKYMDTHGVRgaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGIPVNT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  869 pYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPYFN 948
Cdd:cd07836   157 -FSNEVVTLWYRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNNEDQLLKIFRIMGTPTESTWPGISQLPEYK 235
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 145309300  949 TMKPKKQyRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd07836   236 PTFPRYP-PQDLQQLFPHADPLGIDLLHRLLQLNPELRISAHDALQ 280
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
704-994 7.19e-82

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: 270.46  E-value: 7.19e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIV-TDKEdaldfkk 782
Cdd:cd07839     1 KYEKLEKIGEGTYGTVFKAKNRETHEIVALKRVRLDDDDEGVPSSALREICLLKELKHKNIVRLYDVLhSDKK------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgaFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd07839    74 ----LTLVFEYCDQDLKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSeESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTK-KPIFQANQELAQLELISRICGSPCPAVWPDV 941
Cdd:cd07839   150 GI-PVRCYSAEVVTLWYRPPDVLFGAKLYSTSIDMWSAGCIFAELANAgRPLFPGNDVDDQLKRIFRLLGTPTEESWPGV 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  942 IKLPYFntmKPKKQYRRKLREEFVF--IPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd07839   229 SKLPDY---KPYPMYPATTSLVNVVpkLNSTGRDLLQNLLVCNPVQRISAEEALQ 280
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
704-1017 6.04e-81

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: 269.78  E-value: 6.04e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRL--DNekegfPITA---IREIKILRQLTHQSIINMKEIVTDkEDAL 778
Cdd:cd07834     1 RYELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNvfDD-----LIDAkriLREIKILRHLKHENIIGLLDILRP-PSPE 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 DFKKdkgaFYLVFEYMDHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd07834    75 EFND----VYIVTELMETDLHKVIKSP-QPLTDDHIQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYSSEESRPY-TNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAV 937
Cdd:cd07834   150 ARGVDPDEDKGFlTEYVVTRWYRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDYIDQLNLIVEVLGTPSEED 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  938 WPDVIKLPYFNTMKPKKQYRRKLREEFV-FIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDV-----EPSKMPPPDL 1011
Cdd:cd07834   230 LKFISSEKARNYLKSLPKKPKKPLSEVFpGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLhdpedEPVAKPPFDF 309

                  ....*.
gi 145309300 1012 PLWQDC 1017
Cdd:cd07834   310 PFFDDE 315
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
705-994 6.49e-81

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


Pssm-ID: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 267.86  E-value: 6.49e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVrldneKEGFP----ITAIREIKILRQLT-HQSIINMKEIVtdkedald 779
Cdd:cd07830     1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKM-----KKKFYsweeCMNLREVKSLRKLNeHPNIVKLKEVF-------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkKDKGAFYLVFEYMDHDLMGLLES-GLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd07830    68 --RENDELYFVFEYMEGNLYQLMKDrKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGL 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARlySSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVW 938
Cdd:cd07830   146 AR--EIRSRPPYTDYVSTRWYRAPEILLRSTSYSSPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKICSVLGTPTKQDW 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  939 PDVIKLPY-----FNTMKPKKQYRrklreefvFIP---AAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd07830   224 PEGYKLASklgfrFPQFAPTSLHQ--------LIPnasPEAIDLIKDMLRWDPKKRPTASQALQ 279
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
704-993 6.90e-81

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: 267.75  E-value: 6.90e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTdKEDALdfkkd 783
Cdd:cd07861     1 DYTKIEKIGEGTYGVVYKGRNKKTGQIVAMKKIRLESEEEGVPSTAIREISLLKELQHPNIVCLEDVLM-QENRL----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgafYLVFEYMDHDLMGLLES--GLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL 861
Cdd:cd07861    75 ----YLVFEFLSMDLKKYLDSlpKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARA 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  862 YSSEeSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDV 941
Cdd:cd07861   151 FGIP-VRVYTHEVVTLWYRAPEVLLGSPRYSTPVDIWSIGTIFAEMATKKPLFHGDSEIDQLFRIFRILGTPTEDIWPGV 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 145309300  942 IKLPYFNTMKPKKQyRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQAL 993
Cdd:cd07861   230 TSLPDYKNTFPKWK-KGSLRTAVKNLDEDGLDLLEKMLIYDPAKRISAKKAL 280
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
708-998 8.15e-81

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: 267.71  E-value: 8.15e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  708 IGIIGEGTYGQVYKARDKDTGEMVALKKVRLdNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAF 787
Cdd:cd07844     5 LDKLGEGSYATVYKGRSKLTGQLVALKEIRL-EHEEGAPFTAIREASLLKDLKHANIVTLHDIIHTKK----------TL 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLySSEES 867
Cdd:cd07844    74 TLVFEYLDTDLKQYMDDCGGGLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARA-KSVPS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  868 RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQE-LAQLELISRICGSPCPAVWPDVIKLPY 946
Cdd:cd07844   153 KTYSNEVVTLWYRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGSTDvEDQLHKIFRVLGTPTEETWPGVSSNPE 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  947 FNTMKPKKQYRRKLREEF--VFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd07844   233 FKPYSFPFYPPRPLINHAprLDRIPHGEELALKFLQYEPKKRISAAEAMKHPYF 286
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
703-994 1.14e-80

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: 267.26  E-value: 1.14e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIvtdkedaldFKK 782
Cdd:cd07833     1 NKYEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEA---------FRR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dKGAFYLVFEYMDHDLMGLLE---SGLvhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd07833    72 -KGRLYLVFEYVERTLLELLEaspGGL---PPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWP 939
Cdd:cd07833   148 RALTARPASPLTDYVATRWYRAPELLVGDTNYGKPVDVWAIGCIMAELLDGEPLFPGDSDIDQLYLIQKCLGPLPPSHQE 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  940 DVIKLPYFNTMKPKKQYRRKLREE--FVFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd07833   228 LFSSNPRFAGVAFPEPSQPESLERryPGKVSSPALDFLKACLRMDPKERLTCDELLQ 284
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
705-998 1.80e-79

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: 262.17  E-value: 1.80e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEkegFPITAIREIKILRQLT----HQSIINMKEIVTDKEDaldf 780
Cdd:cd05118     1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIKNDFR---HPKAALREIKLLKHLNdvegHPNIVKLLDVFEHRGG---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdkGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN-RGQIKLADFGLA 859
Cdd:cd05118    74 ----NHLCLVFELMGMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLeLGQLKLADFGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RLYSSeesRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPcpavwp 939
Cdd:cd05118   150 RSFTS---PPYTPYVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRLLGTP------ 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  940 dviklpyfntmkpkkqyrrklreefvfipaAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd05118   221 ------------------------------EALDLLSKMLKYDPAKRITASQALAHPYF 249
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
702-1002 3.43e-79

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 263.22  E-value: 3.43e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVtdkedaldfK 781
Cdd:PLN00009    1 MDQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVV---------H 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDKgAFYLVFEYMDHDLMGLLESGlVHFNENH--IKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR-GQIKLADFGL 858
Cdd:PLN00009   72 SEK-RLYLVFEYLDLDLKKHMDSS-PDFAKNPrlIKTYLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRtNALKLADFGL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYSSEeSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVW 938
Cdd:PLN00009  150 ARAFGIP-VRTFTHEVVTLWYRAPEILLGSRHYSTPVDIWSVGCIFAEMVNQKPLFPGDSEIDELFKIFRILGTPNEETW 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  939 PDVIKLPYFNTMKPKkqYRRKLREEFV-FIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVE 1002
Cdd:PLN00009  229 PGVTSLPDYKSAFPK--WPPKDLATVVpTLEPAGVDLLSKMLRLDPSKRITARAALEHEYFKDLG 291
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
711-1013 1.10e-78

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 263.55  E-value: 1.10e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKE------------GFPITAIREIKILRQLTHQSIInmkeivtdkeDAL 778
Cdd:PTZ00024   17 LGEGTYGKVEKAYDTLTGKIVAIKKVKIIEISNdvtkdrqlvgmcGIHFTTLRELKIMNEIKHENIM----------GLV 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 DFKKDKGAFYLVFEYMDHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:PTZ00024   87 DVYVEGDFINLVMDIMASDLKKVVDRK-IRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFGL 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLY-------------SSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLEL 925
Cdd:PTZ00024  166 ARRYgyppysdtlskdeTMQRREEMTSKVVTLWYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGENEIDQLGR 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  926 ISRICGSPCPAVWPDVIKLPY---FNTMKPKkqyrrKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRdVE 1002
Cdd:PTZ00024  246 IFELLGTPNEDNWPQAKKLPLyteFTPRKPK-----DLKTIFPNASDDAIDLLQSLLKLNPLERISAKEALKHEYFK-SD 319
                         330
                  ....*....|.
gi 145309300 1003 PSKMPPPDLPL 1013
Cdd:PTZ00024  320 PLPCDPSQLPF 330
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
695-1013 6.58e-74

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: 249.78  E-value: 6.58e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  695 IDwgKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKV------RLDNEKegfpitAIREIKILRQLT-HQSIINM 767
Cdd:cd07852     1 ID--KHILRRYEILKKLGKGAYGIVWKAIDKKTGEVVALKKIfdafrnATDAQR------TFREIMFLQELNdHPNIIKL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  768 KEIVTDKEDaldfkKDkgaFYLVFEYMDHDLMGLLESGLVhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN 847
Cdd:cd07852    73 LNVIRAEND-----KD---IYLVFEYMETDLHAVIRANIL--EDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNS 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  848 RGQIKLADFGLARLYSSEESRPY----TNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQL 923
Cdd:cd07852   143 DCRVKLADFGLARSLSQLEEDDEnpvlTDYVATRWYRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGTSTLNQL 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  924 ELISRICGSPCPavwPDV--IKLPYFNTMKPKKQYRRK--LREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLR 999
Cdd:cd07852   223 EKIIEVIGRPSA---EDIesIQSPFAATMLESLPPSRPksLDELFPKASPDALDLLKKLLVFNPNKRLTAEEALRHPYVA 299
                         330
                  ....*....|....*....
gi 145309300 1000 DV-----EPSKMPPPDLPL 1013
Cdd:cd07852   300 QFhnpadEPSLPGPIVIPL 318
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
703-994 1.22e-71

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: 241.51  E-value: 1.22e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPIT---AIREIKILRQLTHQSIINMKEIvtdkedald 779
Cdd:cd07847     1 EKYEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFV---ESEDDPVIkkiALREIRMLKQLKHPNLVNLIEV--------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FKKdKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd07847    69 FRR-KRKLHLVFEYCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFA 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RLYSSEESRpYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWP 939
Cdd:cd07847   148 RILTGPGDD-YTDYVATRWYRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQPLWPGKSDVDQLYLIRKTLGDLIPRHQQ 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  940 DVIKLPYFNTMK-PKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd07847   227 IFSTNQFFKGLSiPEPETREPLESKFPNISSPALSFLKGCLQMDPTERLSCEELLE 282
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
711-1010 4.85e-71

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: 240.29  E-value: 4.85e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEkEGFPITAIREIKILRQLTHQSIINMKEIV-TDKedaldfkkdkgAFYL 789
Cdd:cd07873    10 LGEGTYATVYKGRSKLTDNLVALKEIRLEHE-EGAPCTAIREVSLLKDLKHANIVTLHDIIhTEK-----------SLTL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLySSEESRP 869
Cdd:cd07873    78 VFEYLDKDLKQYLDDCGNSINMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARA-KSIPTKT 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  870 YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPYFNT 949
Cdd:cd07873   157 YSNEVVTLWYRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTVEEQLHFIFRILGTPTEETWPGILSNEEFKS 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  950 MKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKMPPPD 1010
Cdd:cd07873   237 YNYPKYRADALHNHAPRLDSDGADLLSKLLQFEGRKRISAEEAMKHPYFHSLGERIHKLPD 297
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
708-994 1.74e-70

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: 238.37  E-value: 1.74e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  708 IGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEkEGFPITAIREIKILRQLTHQSIINMKEIV-TDKedaldfkkdkgA 786
Cdd:cd07871    10 LDKLGEGTYATVFKGRSKLTENLVALKEIRLEHE-EGAPCTAIREVSLLKNLKHANIVTLHDIIhTER-----------C 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLySSEE 866
Cdd:cd07871    78 LTLVFEYLDSDLKQYLDNCGNLMSMHNVKIFMFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARA-KSVP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  867 SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPY 946
Cdd:cd07871   157 TKTYSNEVVTLWYRPPDVLLGSTEYSTPIDMWGVGCILYEMATGRPMFPGSTVKEELHLIFRLLGTPTEETWPGVTSNEE 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 145309300  947 FNTMKpKKQYR-RKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd07871   237 FRSYL-FPQYRaQPLINHAPRLDTDGIDLLSSLLLYETKSRISAEAALR 284
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
703-994 1.50e-69

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: 235.88  E-value: 1.50e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLThQSIINMKEIVTDKEDaldfKK 782
Cdd:cd07837     1 DAYEKLEKIGEGTYGKVYKARDKNTGKLVALKKTRLEMEEEGVPSTALREVSLLQMLS-QSIYIVRLLDVEHVE----EN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFYLVFEYMDHDLMGLLESglvHFNENH-------IKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN-RGQIKLA 854
Cdd:cd07837    76 GKPLLYLVFEYLDTDLKKFIDS---YGRGPHnplpaktIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKqKGLLKIA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  855 DFGLARLYSSEeSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPC 934
Cdd:cd07837   153 DLGLGRAFTIP-IKSYTHEIVTLWYRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSELQQLLHIFRLLGTPN 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  935 PAVWPDVIKLP---YFNTMKPKkqyrrKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd07837   232 EEVWPGVSKLRdwhEYPQWKPQ-----DLSRAVPDLEPEGVDLLTKMLAYDPAKRISAKAALQ 289
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
704-1012 3.75e-69

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: 236.11  E-value: 3.75e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVR--LDNEKEGfpITAIREIKILRQLTHQSIINMKEIVTdkedaldfK 781
Cdd:cd07858     6 KYVPIKPIGRGAYGIVCSAKNSETNEKVAIKKIAnaFDNRIDA--KRTLREIKLLRHLDHENVIAIKDIMP--------P 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDKGAF---YLVFEYMDHDLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd07858    76 PHREAFndvYIVYELMDTDLHQIIRSSQT-LSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLySSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSpcpavw 938
Cdd:cd07858   155 ART-TSEKGDFMTEYVVTRWYRAPELLLNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKDYVHQLKLITELLGS------ 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  939 PDVIKLPYFNTMKPKK-------QYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDV-EPSKMPPPD 1010
Cdd:cd07858   228 PSEEDLGFIRNEKARRyirslpyTPRQSFARLFPHANPLAIDLLEKMLVFDPSKRITVEEALAHPYLASLhDPSDEPVCQ 307

                  ..
gi 145309300 1011 LP 1012
Cdd:cd07858   308 TP 309
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
703-997 1.04e-68

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: 233.08  E-value: 1.04e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIvtdkedaldFKK 782
Cdd:cd07846     1 EKYENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKMVKKIAMREIKMLKQLRHENLVNLIEV---------FRR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKgAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR-L 861
Cdd:cd07846    72 KK-RWYLVFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARtL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  862 YSSEESrpYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDV 941
Cdd:cd07846   151 AAPGEV--YTDYVATRWYRAPELLVGDTKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDIDQLYHIIKCLGNLIPRHQELF 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  942 IKLPYFNTMK-PKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEF 997
Cdd:cd07846   229 QKNPLFAGVRlPEVKEVEPLERRYPKLSGVVIDLAKKCLHIDPDKRPSCSELLHHEF 285
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
704-1001 2.66e-68

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: 232.01  E-value: 2.66e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLD-NEKEgfpitaiREIKILRQLTHQSIINMKEIVTDKEDaldfKK 782
Cdd:cd14137     5 SYTIEKVIGSGSFGVVYQAKLLETGEVVAIKKVLQDkRYKN-------RELQIMRRLKHPNIVKLKYFFYSSGE----KK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFYLVFEYMDHDLMGLLesglVHFNEN-------HIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR-GQIKLA 854
Cdd:cd14137    74 DEVYLNLVMEYMPETLYRVI----RHYSKNkqtipiiYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDPEtGVLKLC 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  855 DFGLA-RLYSSEESRPYtnkVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSP 933
Cdd:cd14137   150 DFGSAkRLVPGEPNVSY---ICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGESSVDQLVEIIKVLGTP 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  934 CpavwPDVIKlpyfnTMKPKK------QYRRKLREEF--VFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDV 1001
Cdd:cd14137   227 T----REQIK-----AMNPNYtefkfpQIKPHPWEKVfpKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFFDEL 293
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
704-998 2.47e-67

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: 229.08  E-value: 2.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLT---HQSIINMKEIV----TDKED 776
Cdd:cd07863     1 QYEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRVQTNEDGLPLSTVREVALLKRLEafdHPNIVRLMDVCatsrTDRET 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 ALDfkkdkgafyLVFEYMDHDLMGLLES----GLvhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIK 852
Cdd:cd07863    81 KVT---------LVFEHVDQDLRTYLDKvpppGL---PAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFGLARLYSSEESrpYTNKVITLWYRPPELLLGEERYTPaIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGS 932
Cdd:cd07863   149 LADFGLARIYSCQMA--LTPVVVTLWYRAPEVLLQSTYATP-VDMWSVGCIFAEMFRRKPLFCGNSEADQLGKIFDLIGL 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  933 PCPAVWPDVIKLPYFNtMKPKKQyrRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd07863   226 PPEDDWPRDVTLPRGA-FSPRGP--RPVQSVVPEIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
703-998 5.47e-67

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: 229.88  E-value: 5.47e-67
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRlDNEKEGFPITAIREIKILRQLTHQSIINMKEIVtdKEDALDFKK 782
Cdd:cd07849     5 PRYQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKIS-PFEHQTYCLRTLREIKILLRFKHENIIGILDIQ--RPPTFESFK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DkgaFYLVFEYMDHDLMGLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd07849    82 D---VYIVQELMETDLYKLIKTQ--HLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLARIA 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEE--SRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSP------- 933
Cdd:cd07849   157 DPEHdhTGFLTEYVATRWYRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGKDYLHQLNLILGILGTPsqedlnc 236
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  934 -CPAVWPDVIK-LPYFNTMKPKKQYRRklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd07849   237 iISLKARNYIKsLPFKPKVPWNKLFPN--------ADPKALDLLDKMLTFNPHKRITVEEALAHPYL 295
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
703-1010 4.61e-66

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: 227.25  E-value: 4.61e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKV--RLDNekegfPITA---IREIKILRQLTHQSIINMKEIVTDKEDA 777
Cdd:cd07855     5 DRYEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIpnAFDV-----VTTAkrtLRELKILRHFKHDNIIAIRDILRPKVPY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 LDFKKdkgaFYLVFEYMDHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG 857
Cdd:cd07855    80 ADFKD----VYVVLDLMESDLHHIIHSD-QPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARLYSS---EESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPC 934
Cdd:cd07855   155 MARGLCTspeEHKYFMTEYVATRWYRAPELMLSLPEYTQAIDMWSVGCIFAEMLGRRQLFPGKNYVHQLQLILTVLGTPS 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  935 PAVwpdviklpyFNTMKPKKQYR------RKLREEF-VFIPAA---ALDLFDYMLALDPSKRCTAEQALQCEFLR----- 999
Cdd:cd07855   235 QAV---------INAIGADRVRRyiqnlpNKQPVPWeTLYPKAdqqALDLLSQMLRFDPSERITVAEALQHPFLAkyhdp 305
                         330
                  ....*....|.
gi 145309300 1000 DVEPSKMPPPD 1010
Cdd:cd07855   306 DDEPDCAPPFD 316
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
711-1003 3.52e-63

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: 217.94  E-value: 3.52e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEkEGFPITAIREIKILRQLTHQSIINMKEIV-TDKedaldfkkdkgAFYL 789
Cdd:cd07872    14 LGEGTYATVFKGRSKLTENLVALKEIRLEHE-EGAPCTAIREVSLLKDLKHANIVTLHDIVhTDK-----------SLTL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLySSEESRP 869
Cdd:cd07872    82 VFEYLDKDLKQYMDDCGNIMSMHNVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARA-KSVPTKT 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  870 YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPYFNT 949
Cdd:cd07872   161 YSNEVVTLWYRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTVEDELHLIFRLLGTPTEETWPGISSNDEFKN 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  950 MKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEP 1003
Cdd:cd07872   241 YNFPKYKPQPLINHAPRLDTEGIELLTKFLQYESKKRISAEEAMKHAYFRSLGT 294
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
705-994 1.87e-62

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: 214.83  E-value: 1.87e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVrldneKEGF----PITAIREIKILRQLT-HQSIINMKEIVTDKEdald 779
Cdd:cd07831     1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCM-----KKHFksleQVNNLREIQALRRLSpHPNILRLIEVLFDRK---- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkkdKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNrGQIKLADFGLA 859
Cdd:cd07831    72 ----TGRLALVFELMDMNLYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-DILKLADFGSC 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 R-LYSSEesrPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVW 938
Cdd:cd07831   147 RgIYSKP---PYTEYISTRWYRAPECLLTDGYYGPKMDIWAVGCVFFEILSLFPLFPGTNELDQIAKIHDVLGTPDAEVL 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  939 PDVIKLPYFNTMKPKKQyRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd07831   224 KKFRKSRHMNYNFPSKK-GTGLRKLLPNASAEGLDLLKKLLAYDPDERITAKQALR 278
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
711-993 6.50e-62

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: 213.67  E-value: 6.50e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEkEGFPITAIREIKILRQLTHQSIINMKEIVTDKEdALDFkkdkgafylV 790
Cdd:cd07870     8 LGEGSYATVYKGISRINGQLVALKVISMKTE-EGVPFTAIREASLLKGLKHANIVLLHDIIHTKE-TLTF---------V 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHDL---MGLLESGLVHFNenhIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARlYSSEES 867
Cdd:cd07870    77 FEYMHTDLaqyMIQHPGGLHPYN---VRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLAR-AKSIPS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  868 RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQE-LAQLELISRICGSPCPAVWPDVIKLPY 946
Cdd:cd07870   153 QTYSSEVVTLWYRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPGVSDvFEQLEKIWTVLGVPTEDTWPGVSKLPN 232
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 145309300  947 FNT---MKPKKQYRRKLREEFVFIPAAAlDLFDYMLALDPSKRCTAEQAL 993
Cdd:cd07870   233 YKPewfLPCKPQQLRVVWKRLSRPPKAE-DLASQMLMMFPKDRISAQDAL 281
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
703-993 1.80e-60

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: 209.47  E-value: 1.80e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIvtdkedaldFKK 782
Cdd:cd07848     1 NKFEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEA---------FRR 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd07848    72 -RGKLYLVFEYVEKNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEESRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGsPCPavwPDVI 942
Cdd:cd07848   151 SEGSNANYTEYVATRWYRSPELLLGAP-YGKAVDMWSVGCILGELSDGQPLFPGESEIDQLFTIQKVLG-PLP---AEQM 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  943 KL----PYFNTMK-PKKQYRRKLREEFV-FIPAAALDLFDYMLALDPSKRCTAEQAL 993
Cdd:cd07848   226 KLfysnPRFHGLRfPAVNHPQSLERRYLgILSGVLLDLMKNLLKLNPTDRYLTEQCL 282
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
703-999 2.60e-60

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: 211.00  E-value: 2.60e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKK 782
Cdd:cd07851    15 DRYQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASSLEDFQD 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgaFYLVFEYMDHDLMGLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd07851    95 ----VYLVTHLMGADLNNIVKCQ--KLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHT 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEesrpYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVwpdVI 942
Cdd:cd07851   169 DDE----MTGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGKTLFPGSDHIDQLKRIMNLVGTPDEEL---LK 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  943 KLP------YFNTMkPKKQyRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLR 999
Cdd:cd07851   242 KISsesarnYIQSL-PQMP-KKDFKEVFSGANPLAIDLLEKMLVLDPDKRITAAEALAHPYLA 302
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
711-994 1.55e-59

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: 203.66  E-value: 1.55e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgFPITAIREIKILRQLTHQSIINMkeivtdkedaLDFKKDKGAFYLV 790
Cdd:cd00180     1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKK-LLEELLREIEILKKLNHPNIVKL----------YDVFETENFLYLV 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRP 869
Cdd:cd00180    70 MEYCEGgSLKDLLKENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  870 YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisricgspcpavwpdviklpyfnt 949
Cdd:cd00180   150 KTTGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL------------------------------------------ 187
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 145309300  950 mkpkkqyrrklrEEFVfipaaalDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd00180   188 ------------EELK-------DLIRRMLQYDPKKRPSAKELLE 213
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
704-994 4.43e-59

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: 205.65  E-value: 4.43e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARD-KDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLT---HQSIINMKEIVT----DKE 775
Cdd:cd07862     2 QYECVAEIGEGAYGKVFKARDlKNGGRFVALKRVRVQTGEEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVCTvsrtDRE 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  776 DALDfkkdkgafyLVFEYMDHDLMGLLES----GLvhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQI 851
Cdd:cd07862    82 TKLT---------LVFEHVDQDLTTYLDKvpepGV---PTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  852 KLADFGLARLYSSEESrpYTNKVITLWYRPPELLLGEERYTPaIDVWSCGCILGELFTKKPIFQANQELAQLELISRICG 931
Cdd:cd07862   150 KLADFGLARIYSFQMA--LTSVVVTLWYRAPEVLLQSSYATP-VDLWSVGCIFAEMFRRKPLFRGSSDVDQLGKILDVIG 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  932 SPCPAVWPDVIKLPYfNTMKPKKQyrrKLREEFV-FIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd07862   227 LPGEEDWPRDVALPR-QAFHSKSA---QPIEKFVtDIDELGKDLLLKCLTFNPAKRISAYSALS 286
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
705-1007 4.22e-58

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: 204.17  E-value: 4.22e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDT--GEMVALKKVRLDNEKEGFPITAIREIKILRQL-THQSIINM--KEIVTDkeDALD 779
Cdd:cd07857     2 YELIKELGQGAYGIVCSARNAETseEETVAIKKITNVFSKKILAKRALRELKLLRHFrGHKNITCLydMDIVFP--GNFN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkkdkgAFYLVFEYMDHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd07857    80 ------ELYLYEELMEADLHQIIRSG-QPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGLA 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RLYSS--EESRPY-TNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSP--- 933
Cdd:cd07857   153 RGFSEnpGENAGFmTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGKDYVDQLNQILQVLGTPdee 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  934 ------CPAVWPDVIKLPYfntmKPKKQYRRKlreeFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDV-EPSKM 1006
Cdd:cd07857   233 tlsrigSPKAQNYIRSLPN----IPKKPFESI----FPNANPLALDLLEKLLAFDPTKRISVEEALEHPYLAIWhDPDDE 304

                  .
gi 145309300 1007 P 1007
Cdd:cd07857   305 P 305
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
703-1003 1.44e-57

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: 201.46  E-value: 1.44e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLdNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEdaldfkk 782
Cdd:cd07869     5 DSYEKLEKLGEGSYATVYKGKSKVNGKLVALKVIRL-QEEEGTPFTAIREASLLKGLKHANIVLLHDIIHTKE------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLy 862
Cdd:cd07869    77 ---TLTLVFEYVHTDLCQYMDKHPGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARA- 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELA-QLELISRICGSPCPAVWPDV 941
Cdd:cd07869   153 KSVPSHTYSNEVVTLWYRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQdQLERIFLVLGTPNEDTWPGV 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  942 IKLPYFNTMKPKKQYRRKLREEFVFIPAA--ALDLFDYMLALDPSKRCTAEQALQCEFLRDVEP 1003
Cdd:cd07869   233 HSLPHFKPERFTLYSPKNLRQAWNKLSYVnhAEDLASKLLQCFPKNRLSAQAALSHEYFSDLPP 296
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
704-1011 5.24e-57

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: 201.16  E-value: 5.24e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTdKEDALDFKKd 783
Cdd:cd07859     1 RYKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIML-PPSRREFKD- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgaFYLVFEYMDHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYS 863
Cdd:cd07859    79 ---IYVVFELMESDLHQVIKAN-DDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARVAF 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEESRP--YTNKVITLWYRPPELLlGE--ERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWP 939
Cdd:cd07859   155 NDTPTAifWTDYVATRWYRAPELC-GSffSKYTPAIDIWSIGCIFAEVLTGKPLFPGKNVVHQLDLITDLLGTPSPETIS 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  940 DVIKLP---YFNTMKPKKQyrRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLR-----DVEPSKMPPPDL 1011
Cdd:cd07859   234 RVRNEKarrYLSSMRKKQP--VPFSQKFPNADPLALRLLERLLAFDPKDRPTAEEALADPYFKglakvEREPSAQPITKL 311
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
704-994 1.38e-55

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


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 193.89  E-value: 1.38e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVtdkedaldfkKD 783
Cdd:cd14003     1 NYELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVI----------ET 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDH-DLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd14003    71 ENKIYLVMEYASGgELFDYIVN-NGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 sSEESRPYTnKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGspcpavwpdvi 942
Cdd:cd14003   150 -RGGSLLKT-FCGTPAYAAPEVLLGRKYDGPKADVWSLGVILYAM---------------------LTG----------- 195
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  943 KLPYFNTMKPKKqYRRKLREEF---VFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14003   196 YLPFDDDNDSKL-FRKILKGKYpipSHLSPDARDLIRRMLVVDPSKRITIEEILN 249
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
711-1000 1.84e-55

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: 196.92  E-value: 1.84e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgfPITAIREIKILRQLTHQSIINMKEIV----TDKEDALDFKKDKGA 786
Cdd:cd07854    13 LGCGSNGLVFSAVDSDCDKRVAVKKIVLTDPQS--VKHALREIKIIRRLDHDNIVKVYEVLgpsgSDLTEDVGSLTELNS 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDHDLMGLLESGLVhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQI-KLADFGLARLYSSE 865
Cdd:cd07854    91 VYIVQEYMETDLANVLEQGPL--SEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLVlKIGDFGLARIVDPH 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  866 ESRP--YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRicgsPCPAVWPD--- 940
Cdd:cd07854   169 YSHKgyLSEGLVTKWYRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAHELEQMQLILE----SVPVVREEdrn 244
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  941 --VIKLPYFnTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRD 1000
Cdd:cd07854   245 elLNVIPSF-VRNDGGEPRRPLRDLLPGVNPEALDFLEQILTFNPMDRLTAEEALMHPYMSC 305
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
704-994 2.08e-55

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: 193.83  E-value: 2.08e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEivtdkedalDFKkD 783
Cdd:cd08215     1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYE---------SFE-E 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDH-DLMGLLE---SGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd08215    71 NGKLCIVMEYADGgDLAQKIKkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGIS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RLYSSEESrpYTNKVI-TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQelaQLELISRICGSPCPAVw 938
Cdd:cd08215   151 KVLESTTD--LAKTVVgTPYYLSPELCEN-KPYNYKSDIWALGCVLYELCTLKHPFEANN---LPALVYKIVKGQYPPI- 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  939 pdviklpyfntmkpKKQYRRKLReefvfipaaalDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd08215   224 --------------PSQYSSELR-----------DLVNSMLQKDPEKRPSANEILS 254
Pkinase pfam00069
Protein kinase domain;
705-998 2.20e-55

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 192.07  E-value: 2.20e-55
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300   705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDaldfkkdk 784
Cdd:pfam00069    1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDN-------- 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300   785 gaFYLVFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKknflhrdikcsnillnnrgqikladfglarlys 863
Cdd:pfam00069   73 --LYLVLEYVEGgSLFDLLSEK-GAFSEREAKFIMKQILEGLESGSS--------------------------------- 116
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300   864 seesrpYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELIsricgspcpavwpdvIK 943
Cdd:pfam00069  117 ------LTTFVGTPWYMAPE-VLGGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYELI---------------ID 174
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 145309300   944 LPYFNTMKPKKqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:pfam00069  175 QPYAFPELPSN------------LSEEAKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
710-998 5.10e-54

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


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 189.65  E-value: 5.10e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFpITAI-REIKILRQLTHQSIINMkeivtdkedaLDFKKDKGAFY 788
Cdd:cd06606     7 LLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEE-LEALeREIRILSSLKHPNIVRY----------LGTERTENTLN 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDH-DLMGLLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEES 867
Cdd:cd06606    76 IFLEYVPGgSLASLLKKFG-KLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIAT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  868 RPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFT-KKPIFQANQELAQLELISRICGSPCpavwpdvikLP 945
Cdd:cd06606   155 GEGTKSLRgTPYWMAPEVIRGEG-YGRAADIWSLGCTVIEMATgKPPWSELGNPVAALFKIGSSGEPPP---------IP 224
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 145309300  946 yfntmkpkkqyrrklreefVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd06606   225 -------------------EHLSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
711-1019 1.14e-52

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: 188.96  E-value: 1.14e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKdkgaFYLV 790
Cdd:cd07879    23 VGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGDEFQD----FYLV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHDL---MGLlesglvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEes 867
Cdd:cd07879    99 MPYMQTDLqkiMGH------PLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADAE-- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  868 rpYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVwpdVIKLPYF 947
Cdd:cd07879   171 --MTGYVVTRWYRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKDYLDQLTQILKVTGVPGPEF---VQKLEDK 245
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  948 NTMKPKKQYRRKLREEF-VFIPAA---ALDLFDYMLALDPSKRCTAEQALQCEF---LRDVEPSKMPPPdlplWQDCHE 1019
Cdd:cd07879   246 AAKSYIKSLPKYPRKDFsTLFPKAspqAVDLLEKMLELDVDKRLTATEALEHPYfdsFRDADEETEQQP----YDDSLE 320
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
711-1009 1.22e-52

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: 189.01  E-value: 1.22e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKdkgaFYLV 790
Cdd:cd07880    23 VGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLDRFHD----FYLV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHDLMGLLEsgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEesrpY 870
Cdd:cd07880    99 MPFMGTDLGKLMK--HEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDSE----M 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  871 TNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIKLPYFNTM 950
Cdd:cd07880   173 TGYVVTRWYRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGHDHLDQLMEIMKVTGTPSKEFVQKLQSEDAKNYV 252
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  951 KPKKQYRRK-LREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEF---LRDVEPSKMPPP 1009
Cdd:cd07880   253 KKLPRFRKKdFRSLLPNANPLAVNVLEKMLVLDAESRITAAEALAHPYfeeFHDPEDETEAPP 315
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
704-997 1.95e-51

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: 182.29  E-value: 1.95e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDaldfkkd 783
Cdd:cd05117     1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKN------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgaFYLVFEYM------DHdlmgLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR---GQIKLA 854
Cdd:cd05117    74 ---LYLVMELCtggelfDR----IVKKG--SFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKdpdSPIKII 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  855 DFGLARLYssEESRPYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQElaqLELISRICgspc 934
Cdd:cd05117   145 DFGLAKIF--EEGEKLKTVCGTPYYVAPEVLKG-KGYGKKCDIWSLGVILYILLCGYPPFYGETE---QELFEKIL---- 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  935 pavwpdviklpyfntmkpKKQYRRKlREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEF 997
Cdd:cd05117   215 ------------------KGKYSFD-SPEWKNVSEEAKDLIKRLLVVDPKKRLTAAEALNHPW 258
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
705-998 1.05e-50

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: 181.97  E-value: 1.05e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldNEKEgFPITAIREIKILRQLTH------QSIINMKeivtdkeDAL 778
Cdd:cd14210    15 YEVLSVLGKGSFGQVVKCLDHKTGQLVAIKIIR--NKKR-FHQQALVEVKILKHLNDndpddkHNIVRYK-------DSF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 DFKkdkGAFYLVFEYMDHDLMGLLES-GLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL--NNRGQIKLAD 855
Cdd:cd14210    85 IFR---GHLCIVFELLSINLYELLKSnNFQGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLkqPSKSSIKVID 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  856 FGLA-----RLYSSEESRpytnkvitlWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRIC 930
Cdd:cd14210   162 FGSScfegeKVYTYIQSR---------FYRAPEVILGLP-YDTAIDMWSLGCILAELYTGYPLFPGENEEEQLACIMEVL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  931 GSP-------CPAVWPDVIKL--PYFNTMKPKKQYR---RKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14210   232 GVPpkslidkASRRKKFFDSNgkPRPTTNSKGKKRRpgsKSLAQVLKCDDPSFLDFLKKCLRWDPSERMTPEEALQHPWI 311
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
704-998 9.52e-50

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: 177.39  E-value: 9.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPItaIREIKILRQLTHQSIINMKEIVTDKEDAldfkkd 783
Cdd:cd05122     1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESI--LNEIAILKKCKHPNIVKYYGSYLKKDEL------ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgafYLVFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd05122    73 ----WIVMEFCSGgSLKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQL 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEESRpyTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRI--CGSPCPAVWPD 940
Cdd:cd05122   149 SDGKTR--NTFVGTPYWMAPEVIQG-KPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNgpPGLRNPKKWSK 225
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  941 viklpyfntmkpkkqyrrklreEFVfipaaalDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd05122   226 ----------------------EFK-------DFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
684-997 1.11e-49

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: 178.89  E-value: 1.11e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  684 GPRYGETKEKDIDWGKrcVDKFDIIGIIGEGTYGQVYKARDKDTGEMVA---LKKVRLDNEKegfpitaiREIKILRQLT 760
Cdd:cd14132     1 PPEYWDYENLNVEWGS--QDDYEIIRKIGRGKYSEVFEGINIGNNEKVVikvLKPVKKKKIK--------REIKILQNLR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  761 -HQSIINMKEIVTDKedaldfkkDKGAFYLVFEYMDH-DLMGLLESglvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDI 838
Cdd:cd14132    71 gGPNIVKLLDVVKDP--------QSKTPSLIFEYVNNtDFKTLYPT----LTDYDIRYYMYELLKALDYCHSKGIMHRDV 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  839 KCSNILLN-NRGQIKLADFGLARLYSSeeSRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKK-PIFQA 916
Cdd:cd14132   139 KPHNIMIDhEKRKLRLIDWGLAEFYHP--GQEYNVRVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRKePFFHG 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  917 NQELAQLELISRICGSpcpavwpDV---------IKLP-YFNTMKPKkqYRRKLREEFV------FIPAAALDLFDYMLA 980
Cdd:cd14132   217 HDNYDQLVKIAKVLGT-------DDlyayldkygIELPpRLNDILGR--HSKKPWERFVnsenqhLVTPEALDLLDKLLR 287
                         330
                  ....*....|....*..
gi 145309300  981 LDPSKRCTAEQALQCEF 997
Cdd:cd14132   288 YDHQERITAKEAMQHPY 304
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
711-994 3.09e-49

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: 177.95  E-value: 3.09e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEM--VALKKVrldnEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDAldfkkdkgAFY 788
Cdd:cd07867    10 VGRGTYGHVYKAKRKDGKDEkeYALKQI----EGTGISMSACREIALLRELKHPNVIALQKVFLSHSDR--------KVW 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDHDLMGLLE--------SGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL----NNRGQIKLADF 856
Cdd:cd07867    78 LLFDYAEHDLWHIIKfhraskanKKPMQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADM 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSEeSRPYTN---KVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQE---------LAQLE 924
Cdd:cd07867   158 GFARLFNSP-LKPLADldpVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEdiktsnpfhHDQLD 236
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  925 LISRICGSPCPAVWPDVIKLPYFNTMkpKKQYRR---------KLREEFVFIP-AAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd07867   237 RIFSVMGFPADKDWEDIRKMPEYPTL--QKDFRRttyanssliKYMEKHKVKPdSKVFLLLQKLLTMDPTKRITSEQALQ 314
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
705-999 3.24e-49

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: 175.74  E-value: 3.24e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALK-----KVRLDNEKEGFpitaIREIKILRQLTHQSIINMkeivtdkedaLD 779
Cdd:cd14007     2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKvisksQLQKSGLEHQL----RREIEIQSHLRHPNILRL----------YG 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FKKDKGAFYLVFEYMDH-DLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd14007    68 YFEDKKRIYLILEYAPNgELYKELKK-QKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGW 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARlySSEESRPYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQElaqlelisricgspcpavw 938
Cdd:cd14007   147 SV--HAPSNRRKT-FCGTLDYLPPEMVEGKE-YDYKVDIWSLGVLCYELLVGKPPFESKSH------------------- 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  939 pdviklpyfntmkpKKQYRRKLREEFVF---IPAAALDLFDYMLALDPSKRCTAEQALQCEFLR 999
Cdd:cd14007   204 --------------QETYKRIQNVDIKFpssVSPEAKDLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
699-994 6.99e-49

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: 177.56  E-value: 6.99e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  699 KRCVDKFDIIGI-IGEGTYGQVYKARDKDTGEM--VALKKVrldnEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKE 775
Cdd:cd07868    12 ERVEDLFEYEGCkVGRGTYGHVYKAKRKDGKDDkdYALKQI----EGTGISMSACREIALLRELKHPNVISLQKVFLSHA 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  776 DAldfkkdkgAFYLVFEYMDHDLMGLLE--------SGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL-- 845
Cdd:cd07868    88 DR--------KVWLLFDYAEHDLWHIIKfhraskanKKPVQLPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmg 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  846 --NNRGQIKLADFGLARLYSSEeSRPYTN---KVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQE- 919
Cdd:cd07868   160 egPERGRVKIADMGFARLFNSP-LKPLADldpVVVTFWYRAPELLLGARHYTKAIDIWAIGCIFAELLTSEPIFHCRQEd 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  920 --------LAQLELISRICGSPCPAVWPDVIKLPYFNTMkpKKQYRR---------KLREEFVFIP-AAALDLFDYMLAL 981
Cdd:cd07868   239 iktsnpyhHDQLDRIFNVMGFPADKDWEDIKKMPEHSTL--MKDFRRntytncsliKYMEKHKVKPdSKAFHLLQKLLTM 316
                         330
                  ....*....|...
gi 145309300  982 DPSKRCTAEQALQ 994
Cdd:cd07868   317 DPIKRITSEQAMQ 329
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
711-1000 1.30e-48

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: 178.01  E-value: 1.30e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKV-----RLDNEKEGFpitaiREIKILRQLTHQSIINMKEIVtdKEDALDFKKDkg 785
Cdd:cd07853     8 IGYGAFGVVWSVTDPRDGKRVALKKMpnvfqNLVSCKRVF-----RELKMLCFFKHDNVLSALDIL--QPPHIDPFEE-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 aFYLVFEYMDHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSE 865
Cdd:cd07853    79 -IYVVTELMQSDLHKIIVSP-QPLSSDHVKVFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPD 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  866 ESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCpavwpdviklp 945
Cdd:cd07853   157 ESKHMTQEVVTQYYRAPEILMGSRHYTSAVDIWSVGCIFAELLGRRILFQAQSPIQQLDLITDLLGTPS----------- 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  946 yFNTMKPKKQ------YRRKLREE------FVFIPAA--ALDLFDYMLALDPSKRCTAEQALQCEFLRD 1000
Cdd:cd07853   226 -LEAMRSACEgarahiLRGPHKPPslpvlyTLSSQATheAVHLLCRMLVFDPDKRISAADALAHPYLDE 293
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
711-998 6.01e-48

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: 174.68  E-value: 6.01e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEI-VTDKEDaldfkkdkgaFYL 789
Cdd:cd07856    18 VGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIfISPLED----------IYF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDHDLMGLLESGLVHfnENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEesrp 869
Cdd:cd07856    88 VTELLGTDLHRLLTSRPLE--KQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQ---- 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  870 YTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPcPAvwpDVIK-LPYFN 948
Cdd:cd07856   162 MTGYVSTRYYRAPEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGKDHVNQFSIITELLGTP-PD---DVINtICSEN 237
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  949 TMK-----PKKQyRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd07856   238 TLRfvqslPKRE-RVPFSEKFKNADPDAIDLLEKMLVFDPKKRISAAEALAHPYL 291
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
702-1193 2.32e-46

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 174.82  E-value: 2.32e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLD-----NEKEGFpitaIREIKILRQLTHQSIINMkeivtdked 776
Cdd:COG0515     6 LGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLRPElaadpEARERF----RREARALARLNHPNIVRV--------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 aLDFKKDKGAFYLVFEYMD-HDLMGLLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLAD 855
Cdd:COG0515    73 -YDVGEEDGRPYLVMEYVEgESLADLLRRRG-PLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLID 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  856 FGLARLYSSEESRPYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANqelAQLELISRICGSPCP 935
Cdd:COG0515   151 FGIARALGGATLTQTGTVVGTPGYMAPEQARG-EPVDPRSDVYSLGVTLYELLTGRPPFDGD---SPAELLRAHLREPPP 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  936 AVwpdviklpyfntmkpkkqyrRKLREEfvfIPAAALDLFDYMLALDPSKRCTAEQALQCEfLRDVEPSKMPPPDLPLWQ 1015
Cdd:COG0515   227 PP--------------------SELRPD---LPPALDAIVLRALAKDPEERYQSAAELAAA-LRAVLRSLAAAAAAAAAA 282
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300 1016 DC--HELWSKKRRRQKQMGMTDDVSTIKAPRKDLSLGLDDSRTNTPQGVLPSSQLKSQGSSNVAPGEKQTDPSTPQQESS 1093
Cdd:COG0515   283 AAaaAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAPAAAAAAAAAAAALAAAAAAAAAAAAAALLAAAAALAAAA 362
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300 1094 KPLGGIQPSSQTIQPKVETDAAQAAVQSAFAVLLTQLIKAQQSKQKDVLLEERENGSGHEASLQLRPPPEPSTPVSGQDD 1173
Cdd:COG0515   363 AAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAALAAAAAAAAAAAAAAAAAAAAAA 442
                         490       500
                  ....*....|....*....|
gi 145309300 1174 LIQHQDMRILELTPEPDRPR 1193
Cdd:COG0515   443 RLLAAAAAAAAAAAAAPLLA 462
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
704-994 2.73e-46

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: 167.72  E-value: 2.73e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLD--NEKEGFPITAirEIKILRQLTHQSIINMKEIVTDKEDALdfk 781
Cdd:cd08217     1 DYEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGkmSEKEKQQLVS--EVNILRELKHPNIVRYYDRIVDRANTT--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgaFYLVFEYMDH-DLMGLLESGLVH---FNENHIKSFMRQLMEGLDYCHKKN-----FLHRDIKCSNILLNNRGQIK 852
Cdd:cd08217    76 -----LYIVMEYCEGgDLAQLIKKCKKEnqyIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFGLARLYSSEESRPYTNkVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANQelaQLELISRICGS 932
Cdd:cd08217   151 LGDFGLARVLSHDSSFAKTY-VGTPYYMSPELLN-EQSYDEKSDIWSLGCLIYELCALHPPFQAAN---QLELAKKIKEG 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  933 PCPAvwpdvikLPYfntmkpkkQYRRKLREefvfipaaaldLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd08217   226 KFPR-------IPS--------RYSSELNE-----------VIKSMLNVDPDKRPSVEELLQ 261
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
704-994 3.39e-46

Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes many bacterial eukaryotic-type STKs including Staphylococcus aureus PknB (also called PrkC or Stk1), Bacillus subtilis PrkC, and Mycobacterium tuberculosis Pkn proteins (PknB, PknD, PknE, PknF, PknL, and PknH), among others. S. aureus PknB is the only eukaryotic-type STK present in this species, although many microorganisms encode for several such proteins. It is important for the survival and pathogenesis of S. aureus as it is involved in the regulation of purine and pyrimidine biosynthesis, cell wall metabolism, autolysis, virulence, and antibiotic resistance. M. tuberculosis PknB is essential for growth and it acts on diverse substrates including proteins involved in peptidoglycan synthesis, cell division, transcription, stress responses, and metabolic regulation. B. subtilis PrkC is located at the inner membrane of endospores and functions to trigger spore germination. Bacterial STKs in this subfamily show varied domain architectures. The well-characterized members such as S. aureus and M. tuberculosis PknB, and B. subtilis PrkC, contain an N-terminal cytosolic kinase domain, a transmembrane (TM) segment, and mutliple C-terminal extracellular PASTA domains. The PknB subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 167.38  E-value: 3.39e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDN-EKEGFPITAIREIKILRQLTHQSIINMkeivtdkedaLDFKK 782
Cdd:cd14014     1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELaEDEEFRERFLREARALARLSHPNIVRV----------YDVGE 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFYLVFEYMD----HDLMGllESGLVHFNEnhIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd14014    71 DDGRPYIVMEYVEggslADLLR--ERGPLPPRE--ALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLySSEESRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAqleLISRICGSPCPAV 937
Cdd:cd14014   147 ARA-LGDSGLTQTGSVLgTPAYMAPEQARGGP-VDPRSDIYSLGVVLYELLTGRPPFDGDSPAA---VLAKHLQEAPPPP 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  938 WPDVIKlpyfntmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKR-CTAEQALQ 994
Cdd:cd14014   222 SPLNPD-----------------------VPPALDAIILRALAKDPEERpQSAAELLA 256
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
703-1007 8.10e-46

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: 169.06  E-value: 8.10e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKK 782
Cdd:cd07877    17 ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFTPARSLEEFND 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgaFYLVFEYMDHDLMGLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARlY 862
Cdd:cd07877    97 ----VYLVTHLMGADLNNIVKCQ--KLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLAR-H 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEESRPYtnkVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVwpdVI 942
Cdd:cd07877   170 TDDEMTGY---VATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGTDHIDQLKLILRLVGTPGAEL---LK 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  943 KLP------YFNTMKpkkqYRRKLREEFVFIPA--AALDLFDYMLALDPSKRCTAEQALQCEFLR-----DVEPSKMP 1007
Cdd:cd07877   244 KISsesarnYIQSLT----QMPKMNFANVFIGAnpLAVDLLEKMLVLDSDKRITAAQALAHAYFAqyhdpDDEPVADP 317
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
705-998 4.88e-45

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: 163.98  E-value: 4.88e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldNEKEgFPITAIREIKILRQLT------HQSIINMKEIVTDKEDAL 778
Cdd:cd14133     1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKIIK--NNKD-YLDQSLDEIRLLELLNkkdkadKYHIVRLKDVFYFKNHLC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 dfkkdkgafyLVFEYMDHDLMGLLESGLVH-FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL--NNRGQIKLAD 855
Cdd:cd14133    78 ----------IVFELLSQNLYEFLKQNKFQyLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIKIID 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  856 FGLA-----RLYSSEESRpytnkvitlWYRPPELLLGEeRYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRIC 930
Cdd:cd14133   148 FGSScfltqRLYSYIQSR---------YYRAPEVILGL-PYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTI 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  931 GSPcpavwpdviklPYFNTMKPKKQyrrklREEFVfipaaalDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14133   218 GIP-----------PAHMLDQGKAD-----DELFV-------DFLKKLLEIDPKERPTASQALSHPWL 262
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
704-998 7.05e-45

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: 163.15  E-value: 7.05e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGfpiTAIREIKILRQLTHQSIINMkeivtdkedaLDFKKD 783
Cdd:cd06614     1 LYKNLEKIGEGASGEVYKATDRATGKEVAIKKMRLRKQNKE---LIINEILIMKECKHPNIVDY----------YDSYLV 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd06614    68 GDELWVVMEYMDGgSLTDIITQNPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEESRPYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGSPcpavwpdvi 942
Cdd:cd06614   148 TKEKSKRNS-VVGTPYWMAPEVIKRKD-YGPKVDIWSLGIMCIEM---------------------AEGEP--------- 195
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  943 klPYFN----------TMK--PKKQYRRKLREEFvfipaaaLDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd06614   196 --PYLEepplralfliTTKgiPPLKNPEKWSPEF-------KDFLNKCLVKDPEKRPSAEELLQHPFL 254
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
703-998 7.26e-45

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: 163.19  E-value: 7.26e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKV--RLDNEKEgfpITAIR-EIKILRQLTHQSIINMKE-IVTDKEdal 778
Cdd:cd14002     1 ENYHVLELIGEGSFGKVYKGRRKYTGQVVALKFIpkRGKSEKE---LRNLRqEIEILRKLNHPNIIEMLDsFETKKE--- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 dfkkdkgaFYLVFEYMDHDLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd14002    75 --------FVVVTEYAQGELFQILEDDGT-LPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGF 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYSSeesrpytNKVI------TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQelaQLELISRICGS 932
Cdd:cd14002   146 ARAMSC-------NTLVltsikgTPLYMAPE-LVQEQPYDHTADLWSLGCILYELFVGQPPFYTNS---IYQLVQMIVKD 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  933 PCPavWPDviklpyfnTMKPkkqyrrklreEFVfipaaalDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14002   215 PVK--WPS--------NMSP----------EFK-------SFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
711-993 7.18e-44

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: 163.30  E-value: 7.18e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKdkgaFYLV 790
Cdd:cd07878    23 VGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFTPATSIENFNE----VYLV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHDLMGLLEsgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEesrpY 870
Cdd:cd07878    99 TNLMGADLNNIVK--CQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDE----M 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  871 TNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVIK---LPYF 947
Cdd:cd07878   173 TGYVATRWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGNDYIDQLKRIMEVVGTPSPEVLKKISSehaRKYI 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 145309300  948 NTMKPKKQyrRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQAL 993
Cdd:cd07878   253 QSLPHMPQ--QDLKKIFRGANPLAIDLLEKMLVLDSDKRISASEAL 296
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
705-999 3.57e-43

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: 158.52  E-value: 3.57e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgFPITAIREIKILRQLTHQSIINMKEivtdkedALDfkkDK 784
Cdd:cd06623     3 LERVKVLGQGSSGVVYKVRHKPTGKIYALKKIHVDGDEE-FRKQLLRELKTLRSCESPYVVKCYG-------AFY---KE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVFEYMDhdlMGLLESGL---VHFNENHIKSFMRQLMEGLDYCH-KKNFLHRDIKCSNILLNNRGQIKLADFGLAR 860
Cdd:cd06623    72 GEISIVLEYMD---GGSLADLLkkvGKIPEPVLAYIARQILKGLDYLHtKRHIIHRDIKPSNLLINSKGEVKIADFGISK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 lySSEESRPYTNK-VITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAvWP 939
Cdd:cd06623   149 --VLENTLDQCNTfVGTVTYMSPERIQGES-YSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAICDGPPPS-LP 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  940 DVIKLPYFntmkpkkqyrrklrEEFVfipaaaldlfDYMLALDPSKRCTAEQALQCEFLR 999
Cdd:cd06623   225 AEEFSPEF--------------RDFI----------SACLQKDPKKRPSAAELLQHPFIK 260
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
711-941 2.81e-41

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: 152.76  E-value: 2.81e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFpITAIR-EIKILRQLTHQSIInmKEIvtdkedalDFKKDKGAFYL 789
Cdd:cd06627     8 IGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSD-LKSVMgEIDLLKKLNHPNIV--KYI--------GSVKTKDSLYI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDhdlMGLLESGLV---HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA-RLYSSE 865
Cdd:cd06627    77 ILEYVE---NGSLASIIKkfgKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVAtKLNEVE 153
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  866 ESrpyTNKVI-TLWYRPPELLLGEERYTpAIDVWSCGCILGELFTKKPIFqanQELAQLELISRICGSPCPAVWPDV 941
Cdd:cd06627   154 KD---ENSVVgTPYWMAPEVIEMSGVTT-ASDIWSVGCTVIELLTGNPPY---YDLQPMAALFRIVQDDHPPLPENI 223
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
711-998 3.48e-40

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: 150.01  E-value: 3.48e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEGF--------PITAI-REIKILRQLTHQSIINMKEIVTD-KEDA 777
Cdd:cd14008     1 LGRGSFGKVKLALDTETGQLYAIKifnKSRLRKRREGKndrgkiknALDDVrREIAIMKKLDHPNIVRLYEVIDDpESDK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 LdfkkdkgafYLVFEYMDH-DLMGLLE-SGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLAD 855
Cdd:cd14008    81 L---------YLVLEYCEGgPVMELDSgDRVPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  856 FGLARLYSSEESRpYTNKVITLWYRPPELLLGEERY--TPAIDVWSCGCILGELFTKKPIFQANQElaqLELISRICGSP 933
Cdd:cd14008   152 FGVSEMFEDGNDT-LQKTAGTPAFLAPELCDGDSKTysGKAADIWALGVTLYCLVFGRLPFNGDNI---LELYEAIQNQN 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  934 CPAVWPDVIklpyfntmkpkkqyrrklREEFVfipaaalDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14008   228 DEFPIPPEL------------------SPELK-------DLLRRMLEKDPEKRITLKEIKEHPWV 267
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
710-909 3.11e-39

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 146.91  E-value: 3.11e-39
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300    710 IIGEGTYGQVYKAR----DKDTGEMVALKKVRLD---NEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEdaldfkk 782
Cdd:smart00219    6 KLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLKEDaseQQIEEF----LREARIMRKLDHPNVVKLLGVCTEEE------- 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300    783 dkgAFYLVFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR- 860
Cdd:smart00219   75 ---PLYIVMEYMEGgDLLSYLRKNRPKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRd 151
                           170       180       190       200
                    ....*....|....*....|....*....|....*....|....*....
gi 145309300    861 LYSSEESRPYTNKVITLWYrPPELLLgEERYTPAIDVWSCGCILGELFT 909
Cdd:smart00219  152 LYDDDYYRKRGGKLPIRWM-APESLK-EGKFTSKSDVWSFGVLLWEIFT 198
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
707-998 2.44e-38

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: 144.63  E-value: 2.44e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  707 IIGI-IGEGTYGQVYKA--RDKDTGEMVALK----KVRLDNEKEGF-PitaiREIKILRQLTHQSIINMKEIVtdkedal 778
Cdd:cd14080     3 RLGKtIGEGSYSKVKLAeyTKSGLKEKVACKiidkKKAPKDFLEKFlP----RELEILRKLRHPNIIQVYSIF------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 dfkKDKGAFYLVFEYMDH-DLMG-LLESGLVHfnENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd14080    72 ---ERGSKVFIFMEYAEHgDLLEyIQKRGALS--ESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSEE----SRPYTNkviTLWYRPPELLLGEErYTPAI-DVWSCGCIlgeLFTkkpifqanqelaqlelisRICG 931
Cdd:cd14080   147 GFARLCPDDDgdvlSKTFCG---SAAYAAPEILQGIP-YDPKKyDIWSLGVI---LYI------------------MLCG 201
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  932 SpcpavwpdvikLPyFNTMKPKKQYRRKLREEFVF------IPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14080   202 S-----------MP-FDDSNIKKMLKDQQNRKVRFpssvkkLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
711-998 3.18e-38

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: 144.08  E-value: 3.18e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEkEGFPITAI----REIKILRQLTHQSIInmKEIVTDKEDAldfkkdkgA 786
Cdd:cd06632     8 LGSGSFGSVYEGFNGDTGDFFAVKEVSLVDD-DKKSRESVkqleQEIALLSKLRHPNIV--QYYGTEREED--------N 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDhdlMGLLESgLVH----FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARlY 862
Cdd:cd06632    77 LYIFLEYVP---GGSIHK-LLQrygaFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAK-H 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFqanQELAQLELISRICGSPCPAVWPDvi 942
Cdd:cd06632   152 VEAFSFAKSFKGSPYWMAPEVIMQKNSGYGLAVDIWSLGCTVLEMATGKPPW---SQYEGVAAIFKIGNSGELPPIPD-- 226
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  943 klpyfnTMKPKKQyrrklreEFVFIpaaaldlfdyMLALDPSKRCTAEQALQCEFL 998
Cdd:cd06632   227 ------HLSPDAK-------DFIRL----------CLQRDPEDRPTASQLLEHPFV 259
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
710-909 5.21e-38

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: 143.46  E-value: 5.21e-38
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300    710 IIGEGTYGQVYKAR----DKDTGEMVALKKVRLD---NEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEdaldfkk 782
Cdd:smart00221    6 KLGEGAFGEVYKGTlkgkGDGKEVEVAVKTLKEDaseQQIEEF----LREARIMRKLDHPNIVKLLGVCTEEE------- 74
                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300    783 dkgAFYLVFEYMDH-DLMG-LLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR 860
Cdd:smart00221   75 ---PLMIVMEYMPGgDLLDyLRKNRPKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSR 151
                           170       180       190       200       210
                    ....*....|....*....|....*....|....*....|....*....|
gi 145309300    861 -LYSSEESRPYTNKVITLWYrPPELLLgEERYTPAIDVWSCGCILGELFT 909
Cdd:smart00221  152 dLYDDDYYKVKGGKLPIRWM-APESLK-EGKFTSKSDVWSFGVLLWEIFT 199
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
711-943 5.65e-38

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: 143.06  E-value: 5.65e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKdtGEMVALKKVRLDNE----KEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDaldfkkdkga 786
Cdd:cd13999     1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDndelLKEF----RREVSILSKLRHPNIVQFIGACLSPPP---------- 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSE 865
Cdd:cd13999    65 LCIVTEYMPGgSLYDLLHKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNST 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  866 ESRpYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFqanQELAQLELISRICGS----PCPAVWPDV 941
Cdd:cd13999   145 TEK-MTGVVGTPRWMAPEVLRG-EPYTEKADVYSFGIVLWELLTGEVPF---KELSPIQIAAAVVQKglrpPIPPDCPPE 219

                  ..
gi 145309300  942 IK 943
Cdd:cd13999   220 LS 221
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
704-994 5.92e-38

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: 143.77  E-value: 5.92e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALK-----KVRL-DNEKEGFPitaiREIKILRQLTHQSIINMKEIVTDKEDa 777
Cdd:cd14098     1 KYQIIDRLGSGTFAEVKKAVEVETGKMRAIKqivkrKVAGnDKNLQLFQ----REINILKSLEHPGIVRLIDWYEDDQH- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 ldfkkdkgaFYLVFEYMDH-DLMG-LLESGLVhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ--IKL 853
Cdd:cd14098    76 ---------IYLVMEYVEGgDLMDfIMAWGAI--PEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPviVKI 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  854 ADFGLARLYsseesrpYTNKVI-----TLWYRPPELLLGEER-----YTPAIDVWSCGCILGELFTKKPIFQANQELAQL 923
Cdd:cd14098   145 SDFGLAKVI-------HTGTFLvtfcgTMAYLAPEILMSKEQnlqggYSNLVDMWSVGCLVYVMLTGALPFDGSSQLPVE 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  924 ELISRicGSPCpavwpdviklpyfntMKPKKQYRrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14098   218 KRIRK--GRYT---------------QPPLVDFN---------ISEEAIDFILRLLDVDPEKRMTAAQALD 262
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
707-998 8.23e-38

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: 145.47  E-value: 8.23e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  707 IIGIIGEGTYGQVYKARDKDTGEMVALKKVRldNEKEGFPiTAIREIKILRQLthqsiiNMKeivTDKEDA------LDF 780
Cdd:cd14212     3 VLDLLGQGTFGQVVKCQDLKTNKLVAVKVLK--NKPAYFR-QAMLEIAILTLL------NTK---YDPEDKhhivrlLDH 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 KKDKGAFYLVFEYMDHDLMGLLESglvhfNENH------IKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR--GQIK 852
Cdd:cd14212    71 FMHHGHLCIVFELLGVNLYELLKQ-----NQFRglslqlIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLdsPEIK 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFGLA-----RLYSSEESRpytnkvitlWYRPPELLLGEeRYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELIS 927
Cdd:cd14212   146 LIDFGSAcfenyTLYTYIQSR---------FYRSPEVLLGL-PYSTAIDMWSLGCIAAELFLGLPLFPGNSEYNQLSRII 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  928 RICGSP----------------------CPAVW----------------------------PDVI-KLPYFNTMKPKKQY 956
Cdd:cd14212   216 EMLGMPpdwmlekgkntnkffkkvaksgGRSTYrlktpeefeaenncklepgkryfkyktlEDIImNYPMKKSKKEQIDK 295
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 145309300  957 RRKLREEFVfipaaalDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14212   296 EMETRLAFI-------DFLKGLLEYDPKKRWTPDQALNHPFI 330
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
705-998 1.28e-37

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: 142.40  E-value: 1.28e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgfPItaIREIKILRQLTHQSIInmkeivtdkedaldfkKDK 784
Cdd:cd06612     5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPVEEDLQ--EI--IKEISILKQCDSPYIV----------------KYY 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFY------LVFEYMD----HDLMGLLESGLvhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLA 854
Cdd:cd06612    65 GSYFkntdlwIVMEYCGagsvSDIMKITNKTL---TEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  855 DFGLARlySSEESRPYTNKVI-TLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPifqANQELAQLELISRICGSP 933
Cdd:cd06612   142 DFGVSG--QLTDTMAKRNTVIgTPFWMAPEVIQ-EIGYNNKADIWSLGITAIEMAEGKP---PYSDIHPMRAIFMIPNKP 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  934 CPavwpdviklpyfnTMKPKKQYrrklREEFVfipaaalDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd06612   216 PP-------------TLSDPEKW----SPEFN-------DFVKKCLVKDPEERPSAIQLLQHPFI 256
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
698-999 2.04e-37

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: 144.38  E-value: 2.04e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  698 GKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKeDA 777
Cdd:cd14226     8 GEKWMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIK---NKKAFLNQAQIEVRLLELMNKHDTENKYYIVRLK-RH 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 LDFKkdkGAFYLVFEYMDHDLMGLLESglVHFNE---NHIKSFMRQLMEGLDYCHKK--NFLHRDIKCSNILLNN--RGQ 850
Cdd:cd14226    84 FMFR---NHLCLVFELLSYNLYDLLRN--TNFRGvslNLTRKFAQQLCTALLFLSTPelSIIHCDLKPENILLCNpkRSA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  851 IKLADFGLA-----RLYSSEESRpytnkvitlWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLEL 925
Cdd:cd14226   159 IKIIDFGSScqlgqRIYQYIQSR---------FYRSPEVLLGLP-YDLAIDMWSLGCILVEMHTGEPLFSGANEVDQMNK 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  926 ISRICGSPcPAVWPD--------VIKLP----YFNTMKPKKQYR----RKLRE---------------EFVFIPAAALDL 974
Cdd:cd14226   229 IVEVLGMP-PVHMLDqapkarkfFEKLPdgtyYLKKTKDGKKYKppgsRKLHEilgvetggpggrragEPGHTVEDYLKF 307
                         330       340
                  ....*....|....*....|....*...
gi 145309300  975 FDY---MLALDPSKRCTAEQALQCEFLR 999
Cdd:cd14226   308 KDLilrMLDYDPKTRITPAEALQHSFFK 335
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
703-998 2.30e-37

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


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 141.59  E-value: 2.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDT-------GEMVALKKVRLDNEkegfPITAIREIKILRQLTHQS-IINMKEIVTDK 774
Cdd:cd14019     1 NKYRIIEKIGEGTFSSVYKAEDKLHdlydrnkGRLVALKHIYPTSS----PSRILNELECLERLGGSNnVSGLITAFRNE 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  775 EDALdfkkdkgafyLVFEYMDHDlmgllesglvHFNEN-------HIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN 847
Cdd:cd14019    77 DQVV----------AVLPYIEHD----------DFRDFyrkmsltDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNR 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  848 R-GQIKLADFGLARLYSSEESRPyTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTK-KPIFQANQELAQLEL 925
Cdd:cd14019   137 EtGKGVLVDFGLAQREEDRPEQR-APRAGTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGrFPFFFSSDDIDALAE 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  926 ISRICGSpcpavwpdviklpyfntmkpkkqyrrklreefvfipAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14019   216 IATIFGS------------------------------------DEAYDLLDKLLELDPSKRITAEEALKHPFF 252
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
705-990 2.54e-37

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: 142.35  E-value: 2.54e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEGFpiTAIREIKILRQLTHQSIINMkeivtdkedALDFK 781
Cdd:cd05581     3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKvldKRHIIKEKKVK--YVTIEKEVLSRLAHPGIVKL---------YYTFQ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kDKGAFYLVFEYMDH-DLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR 860
Cdd:cd05581    72 -DESKLYFVLEYAPNgDLLEYIRK-YGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAK 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 LYSSEESrPYTNK-----------------VITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQL 923
Cdd:cd05581   150 VLGPDSS-PESTKgdadsqiaynqaraasfVGTAEYVSPE-LLNEKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTF 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  924 ELISRICgspcpAVWPDviklpyfntmkpkkqyrrklreefvFIPAAALDLFDYMLALDPSKRCTAE 990
Cdd:cd05581   228 QKIVKLE-----YEFPE-------------------------NFPPDAKDLIQKLLVLDPSKRLGVN 264
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
711-917 5.45e-37

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: 140.34  E-value: 5.45e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPI-TAIREIKILRQLTHQSIINMKeivtdkedaLDFKkDKGAFYL 789
Cdd:cd05123     1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVeHTLNERNILERVNHPFIVKLH---------YAFQ-TEEKLYL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESR 868
Cdd:cd05123    71 VLDYVPGgELFSHLSK-EGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDR 149
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 145309300  869 PYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQAN 917
Cdd:cd05123   150 TYT-FCGTPEYLAPEVLLGKG-YGKAVDWWSLGVLLYEMLTGKPPFYAE 196
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
704-998 2.33e-36

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


Pssm-ID: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 141.38  E-value: 2.33e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPITAIREIKILRQLTHQ------SIINMKEIVTdkeda 777
Cdd:cd14225    44 RYEILEVIGKGSFGQVVKALDHKTNEHVAIKIIR---NKKRFHHQALVEVKILDALRRKdrdnshNVIHMKEYFY----- 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 ldFKKDkgaFYLVFEYMDHDLMGLLE-SGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ--IKLA 854
Cdd:cd14225   116 --FRNH---LCITFELLGMNLYELIKkNNFQGFSLSLIRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQssIKVI 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  855 DFGlarlySS--EESRPYTnKVITLWYRPPELLLGEeRYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGS 932
Cdd:cd14225   191 DFG-----SScyEHQRVYT-YIQSRFYRSPEVILGL-PYSMAIDMWSLGCILAELYTGYPLFPGENEVEQLACIMEVLGL 263
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  933 PCPAVWPDVIKLPYF--------NTMKPKKQYRRKLREEFVFIPAAALDLF-DYM---LALDPSKRCTAEQALQCEFL 998
Cdd:cd14225   264 PPPELIENAQRRRLFfdskgnprCITNSKGKKRRPNSKDLASALKTSDPLFlDFIrrcLEWDPSKRMTPDEALQHEWI 341
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
703-999 4.20e-36

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: 138.53  E-value: 4.20e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgfPITAI-REIKILRQLTHQSIINMKEIVTDkedalDFK 781
Cdd:cd06609     1 ELFTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAED--EIEDIqQEIQFLSQCDSPYITKYYGSFLK-----GSK 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgaFYLVFEYMDH-DLMGLLESGLvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR 860
Cdd:cd06609    74 -----LWIIMEYCGGgSVLDLLKPGP--LDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 LYSSEESRPYTNkVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPifqANQELAQLELISRICGSPCPAVwpd 940
Cdd:cd06609   147 QLTSTMSKRNTF-VGTPFWMAPEVIKQSG-YDEKADIWSLGITAIELAKGEP---PLSDLHPMRVLFLIPKNNPPSL--- 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  941 viklpyfntmkPKKQYRRKLReEFVfipAAALDlfdymlaLDPSKRCTAEQALQCEFLR 999
Cdd:cd06609   219 -----------EGNKFSKPFK-DFV---ELCLN-------KDPKERPSAKELLKHKFIK 255
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
711-998 7.86e-36

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 137.30  E-value: 7.86e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDN-EKEGFPITAIREIKILRQLTHQSIINMKeivtdkedalDFKKDKGAFYL 789
Cdd:cd14099     9 LGKGGFAKCYEVTDMSTGKVYAGKVVPKSSlTKPKQREKLKSEIKIHRSLKHPNIVKFH----------DCFEDEENVYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESR 868
Cdd:cd14099    79 LLELCSNgSLMELLKRR-KALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYDGER 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  869 PYT-----NkvitlwYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQAnqelaqlelisricgspcpavwPDVik 943
Cdd:cd14099   158 KKTlcgtpN------YIAPEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFET----------------------SDV-- 207
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  944 lpyfntmkpKKQYRRKLREEFVF-----IPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14099   208 ---------KETYKRIKKNEYSFpshlsISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
711-940 7.87e-36

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: 137.24  E-value: 7.87e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300   711 IGEGTYGQVYKAR----DKDTGEMVALKKVR---LDNEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDAldfkkd 783
Cdd:pfam07714    7 LGEGAFGEVYKGTlkgeGENTKIKVAVKTLKegaDEEEREDF----LEEASIMKKLDHPNIVKLLGVCTQGEPL------ 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300   784 kgafYLVFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR-L 861
Cdd:pfam07714   77 ----YIVTEYMPGgDLLDFLRKHKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSRdI 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300   862 YSSEESRPYTNKVITL-WYrPPELLLgEERYTPAIDVWSCGCILGELFT--KKPIFQ-ANQELaqLELISRICGSPCPAV 937
Cdd:pfam07714  153 YDDDYYRKRGGGKLPIkWM-APESLK-DGKFTSKSDVWSFGVLLWEIFTlgEQPYPGmSNEEV--LEFLEDGYRLPQPEN 228

                   ...
gi 145309300   938 WPD 940
Cdd:pfam07714  229 CPD 231
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
710-909 9.91e-36

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: 137.29  E-value: 9.91e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKAR---DKDTGEMVALKKVRLD---NEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDaldfkkd 783
Cdd:cd00192     2 KLGEGAFGEVYKGKlkgGDGKTVDVAVKTLKEDaseSERKDF----LKEARVMKKLGHPNVVRLLGVCTEEEP------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgaFYLVFEYMDH-DLMGLLESGLVHFNENHIK--------SFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLA 854
Cdd:cd00192    71 ---LYLVMEYMEGgDLLDFLRKSRPVFPSPEPStlslkdllSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKIS 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  855 DFGLARLYSSEESrpYTN----KVITLWYrPPELLLgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd00192   148 DFGLSRDIYDDDY--YRKktggKLPIRWM-APESLK-DGIFTSKSDVWSFGVLLWEIFT 202
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
711-1009 1.71e-35

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: 138.70  E-value: 1.71e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKdkgaFYLV 790
Cdd:cd07850     8 IGSGAQGIVCAAYDTVTGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKSLEEFQD----VYLV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHDLMGLLESGLVHfneNHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSE-ESRP 869
Cdd:cd07850    84 MELMDANLCQVIQMDLDH---ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSfMMTP 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  870 YtnkVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCP----AVWPDViklP 945
Cdd:cd07850   161 Y---VVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMIRGTVLFPGTDHIDQWNKIIEQLGTPSDefmsRLQPTV---R 233
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  946 YFNTMKPKKQYR--RKLREEFVFIPAA----------ALDLFDYMLALDPSKRCTAEQALQCEFLR---DVEPSKMPPP 1009
Cdd:cd07850   234 NYVENRPKYAGYsfEELFPDVLFPPDSeehnklkasqARDLLSKMLVIDPEKRISVDDALQHPYINvwyDPSEVEAPPP 312
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
711-944 1.87e-35

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: 135.81  E-value: 1.87e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLD--NEK--EGFpitaIREIKILRQLTHQSIINMkeivtdkedaLDFKKDKGA 786
Cdd:cd14009     1 IGRGSFATVWKGRHKQTGEVVAIKEISRKklNKKlqENL----ESEIAILKSIKHPNIVRL----------YDVQKTEDF 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMD-HDLmglleSGLVH----FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG---QIKLADFGL 858
Cdd:cd14009    67 IYLVLEYCAgGDL-----SQYIRkrgrLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGddpVLKIADFGF 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARlysseeSRPYTNKVITL----WYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISR----IC 930
Cdd:cd14009   142 AR------SLQPASMAETLcgspLYMAPEILQF-QKYDAKADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERsdavIP 214
                         250
                  ....*....|....
gi 145309300  931 GSPCPAVWPDVIKL 944
Cdd:cd14009   215 FPIAAQLSPDCKDL 228
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
705-991 3.30e-35

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: 135.54  E-value: 3.30e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMkeivtdkedaLDFKKDK 784
Cdd:cd14069     3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRF----------YGHRREG 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYS 863
Cdd:cd14069    73 EFQYLFLEYASGgELFDKIEPD-VGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFR 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SE-ESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCIL-----GELFTKKPIfQANQElaqlelisricgspcpav 937
Cdd:cd14069   152 YKgKERLLNKMCGTLPYVAPELLAKKKYRAEPVDVWSCGIVLfamlaGELPWDQPS-DSCQE------------------ 212
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  938 wpdviklpYFNTMKPKKQYRRKLREefvfIPAAALDLFDYMLALDPSKRCTAEQ 991
Cdd:cd14069   213 --------YSDWKENKKTYLTPWKK----IDTAALSLLRKILTENPNKRITIED 254
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
710-1011 4.81e-35

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 140.17  E-value: 4.81e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDnekegfPITAIREIKILRQLTHQSIINMKEIVTDKEdaldFKKDKGAFYL 789
Cdd:PTZ00036   73 IIGNGSFGVVYEAICIDTSEKVAIKKVLQD------PQYKNRELLIMKNLNHINIIFLKDYYYTEC----FKKNEKNIFL 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 --VFEYMDHDLMGLLEsglvHFNENH-------IKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ-IKLADFGLA 859
Cdd:PTZ00036  143 nvVMEFIPQTVHKYMK----HYARNNhalplflVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSA 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 R-LYSSEESRPYtnkVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCpavw 938
Cdd:PTZ00036  219 KnLLAGQRSVSY---ICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVLGTPT---- 291
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  939 PDVIKL--PYFNTMKPKKQYRRKLREEF-VFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDV-EPS-KMPP----- 1008
Cdd:PTZ00036  292 EDQLKEmnPNYADIKFPDVKPKDLKKVFpKGTPDDAINFISQFLKYEPLKRLNPIEALADPFFDDLrDPCiKLPKyidkl 371

                  ...
gi 145309300 1009 PDL 1011
Cdd:PTZ00036  372 PDL 374
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
705-994 7.27e-35

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: 134.46  E-value: 7.27e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKedaldfkkdk 784
Cdd:cd08529     2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDK---------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVFEYMDH-DLMGLLESGLVH-FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd08529    72 GKLNIVMEYAENgDLHSLIKSQRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKIL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEESRPYTnKVITLWYRPPELLlgEER-YTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAvwpdv 941
Cdd:cd08529   152 SDTTNFAQT-IVGTPYYLSPELC--EDKpYNEKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPPISA----- 223
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 145309300  942 iklpyfntmkpkkQYRRKLreefvfipaaaLDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd08529   224 -------------SYSQDL-----------SQLIDSCLTKDYRQRPDTTELLR 252
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
711-986 9.48e-35

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: 134.65  E-value: 9.48e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKV------------RLDNEKEgfpitaireikILRQLTHQSIINMKEIVTDKEDal 778
Cdd:cd05579     1 ISRGAYGRVYLAKKKSTGDLYAIKVIkkrdmirknqvdSVLAERN-----------ILSQAQNPFVVKLYYSFQGKKN-- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 dfkkdkgaFYLVFEYMDH-DLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG 857
Cdd:cd05579    68 --------LYLVMEYLPGgDLYSLLEN-VGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFG 138
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARLYSSEESRPY-------------TNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQElaqL 923
Cdd:cd05579   139 LSKVGLVRRQIKLsiqkksngapekeDRRIVgTPDYLAPEILLGQG-HGKTVDWWSLGVILYEFLVGIPPFHAETP---E 214
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  924 ELISRICGSPCPavWPdviklpyfntmkpkkqyrrklreEFVFIPAAALDLFDYMLALDPSKR 986
Cdd:cd05579   215 EIFQNILNGKIE--WP-----------------------EDPEVSDEAKDLISKLLTPDPEKR 252
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
703-998 1.67e-34

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 135.77  E-value: 1.67e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRlDNEK--EgfpiTAIREIKILRQLTHQ------SIINMKeivtdk 774
Cdd:cd14134    12 NRYKILRLLGEGTFGKVLECWDRKRKRYVAVKIIR-NVEKyrE----AAKIEIDVLETLAEKdpngksHCVQLR------ 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  775 eDALDFkkdKGAFYLVFEymdhdLMG------LLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN- 847
Cdd:cd14134    81 -DWFDY---RGHMCIVFE-----LLGpslydfLKKNNYGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDs 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  848 ------------------RGQIKLADFGLARLysseESRPYTNKVITLWYRPPELLLGEERYTPAiDVWSCGCILGELFT 909
Cdd:cd14134   152 dyvkvynpkkkrqirvpkSTDIKLIDFGSATF----DDEYHSSIVSTRHYRAPEVILGLGWSYPC-DVWSIGCILVELYT 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  910 KKPIFQANQELAQLELISRICGsPCPAVW----PDVIKLPYFNTMK-------PKKQYRRKLREEFVFIPAAA------- 971
Cdd:cd14134   227 GELLFQTHDNLEHLAMMERILG-PLPKRMirraKKGAKYFYFYHGRldwpegsSSGRSIKRVCKPLKRLMLLVdpehrll 305
                         330       340
                  ....*....|....*....|....*..
gi 145309300  972 LDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14134   306 FDLIRKMLEYDPSKRITAKEALKHPFF 332
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
702-998 3.90e-34

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: 132.81  E-value: 3.90e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIGIIGEGTYGQVYKARDKDTGEMVALK--KVRLDNEKEgfpITAirEIKILRQLT-HQSIIN-----MKEIVTD 773
Cdd:cd06608     5 AGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKimDIIEDEEEE---IKL--EINILRKFSnHPNIATfygafIKKDPPG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  774 KEDALdfkkdkgafYLVFEYMDH----DLM-GLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR 848
Cdd:cd06608    80 GDDQL---------WLVMEYCGGgsvtDLVkGLRKKG-KRLKEEWIAYILRETLRGLAYLHENKVIHRDIKGQNILLTEE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  849 GQIKLADFGLARLYSSEESRpyTNKVI-TLWYRPPELLLGEERYTPAI----DVWSCGCILGELFTKKPIFQANQELAQL 923
Cdd:cd06608   150 AEVKLVDFGVSAQLDSTLGR--RNTFIgTPYWMAPEVIACDQQPDASYdarcDVWSLGITAIELADGKPPLCDMHPMRAL 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  924 ELISRicgSPCPavwpdviklpyfnTMKPKKQYRRKLREefvFIPAAaldlfdymLALDPSKRCTAEQALQCEFL 998
Cdd:cd06608   228 FKIPR---NPPP-------------TLKSPEKWSKEFND---FISEC--------LIKNYEQRPFTEELLEHPFI 275
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
698-996 4.48e-34

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: 132.80  E-value: 4.48e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  698 GKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLdNEKEGFPITAIREIKILRQLTHqsiinmKEIVT----- 772
Cdd:cd13996     1 NSRYLNDFEEIELLGSGGFGSVYKVRNKVDGVTYAIKKIRL-TEKSSASEKVLREVKALAKLNH------PNIVRyytaw 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  773 DKEDALdfkkdkgafYLVFEYMD-HDLMGLLESGLVHFNENH--IKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR- 848
Cdd:cd13996    74 VEEPPL---------YIQMELCEgGTLRDWIDRRNSSSKNDRklALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDd 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  849 GQIKLADFGLARLYSS--EESRP-----------YTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKkpiFQ 915
Cdd:cd13996   145 LQVKIGDFGLATSIGNqkRELNNlnnnnngntsnNSVGIGTPLYASPEQLDGEN-YNEKADIYSLGIILFEMLHP---FK 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  916 ANQElaqlelisRIcgspcpavwpdviklpyfNTMKPKKQYrrKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQC 995
Cdd:cd13996   221 TAME--------RS------------------TILTDLRNG--ILPESFKAKHPKEADLIQSLLSKNPEERPSAEQLLRS 272

                  .
gi 145309300  996 E 996
Cdd:cd13996   273 L 273
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
710-998 4.81e-34

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: 132.27  E-value: 4.81e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDN------EKEGFPITAI-REIKILRQLTHQSIINMkeivtdkedaLDFKK 782
Cdd:cd06628     7 LIGSGSFGSVYLGMNASSGELMAVKQVELPSvsaenkDRKKSMLDALqREIALLRELQHENIVQY----------LGSSS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR-- 860
Cdd:cd06628    77 DANHLNIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKkl 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 -----LYSSEESRPYTNKviTLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFqanQELAQLELISRICGSPCP 935
Cdd:cd06628   157 eanslSTKNNGARPSLQG--SVFWMAPE-VVKQTSYTRKADIWSLGCLVVEMLTGTHPF---PDCTQMQAIFKIGENASP 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  936 AVWPDviklpyfntmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd06628   231 TIPSN--------------------------ISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
711-1011 5.01e-34

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: 135.16  E-value: 5.01e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKdkgaFYLV 790
Cdd:cd07876    29 IGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLEEFQD----VYLV 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHDLMGLLESGLVHfneNHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSE-ESRP 869
Cdd:cd07876   105 MELMDANLCQVIHMELDH---ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNfMMTP 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  870 YtnkVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPC--------PAVWPDV 941
Cdd:cd07876   182 Y---VVTRYYRAPEVILG-MGYKENVDIWSVGCIMGELVKGSVIFQGTDHIDQWNKVIEQLGTPSaefmnrlqPTVRNYV 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  942 IKLPYFNTMK----------PKKQYRRKLREefvfipAAALDLFDYMLALDPSKRCTAEQALQCEFLR---DVEPSKMPP 1008
Cdd:cd07876   258 ENRPQYPGISfeelfpdwifPSESERDKLKT------SQARDLLSKMLVIDPDKRISVDEALRHPYITvwyDPAEAEAPP 331

                  ...
gi 145309300 1009 PDL 1011
Cdd:cd07876   332 PQI 334
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
704-991 9.79e-34

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: 130.97  E-value: 9.79e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAI-REIKILRQLTHQSIINMKEIVTDKEDALdfkk 782
Cdd:cd14073     2 RYELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIEDEQDMVRIrREIEIMSSLNHPHIIRIYEVFENKDKIV---- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgafyLVFEYMDH-DLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL 861
Cdd:cd14073    78 ------IVMEYASGgELYDYISERRR-LPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  862 YSSeesrpytNKVITLW-----YRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRicgspcpa 936
Cdd:cd14073   151 YSK-------DKLLQTFcgsplYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISS-------- 215
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  937 vwpdviklpyfntmkpkKQYRRKLReefvfiPAAALDLFDYMLALDPSKRCTAEQ 991
Cdd:cd14073   216 -----------------GDYREPTQ------PSDASGLIRWMLTVNPKRRATIED 247
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
704-919 1.30e-33

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: 131.32  E-value: 1.30e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLD--NEKEGFPI---TAIREIKILRQLT-HQSIINMKEIVTDKEda 777
Cdd:cd13993     1 RYQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSgpNSKDGNDFqklPQLREIDLHRRVSrHPNIITLHDVFETEV-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 ldfkkdkgAFYLVFEYMDH-DLM-GLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR-GQIKLA 854
Cdd:cd13993    79 --------AIYIVLEYCPNgDLFeAITENRIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLC 150
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  855 DFGLArlysSEESRPYTNKVITLWYRPPELL-----LGEERYTPAIDVWSCG-CILGELFTKKPIFQANQE 919
Cdd:cd13993   151 DFGLA----TTEKISMDFGVGSEFYMAPECFdevgrSLKGYPCAAGDIWSLGiILLNLTFGRNPWKIASES 217
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
710-998 4.16e-33

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: 129.73  E-value: 4.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRL-DNEKEGFPITAiREIKILRQLTHQSIInmkeivtdKEDALDFKKDKgaFY 788
Cdd:cd06626     7 KIGEGTFGKVYTAVNLDTGELMAMKEIRFqDNDPKTIKEIA-DEMKVLEGLDHPNLV--------RYYGVEVHREE--VY 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDH-DLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEES 867
Cdd:cd06626    76 IFMEYCQEgTLEELLRHGRI-LDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  868 RPYTNK----VITLWYRPPELLLGEER--YTPAIDVWSCGCILGELFT-KKPIFQANQELAqleLISRIcGSPCPAVWPD 940
Cdd:cd06626   155 TMAPGEvnslVGTPAYMAPEVITGNKGegHGRAADIWSLGCVVLEMATgKRPWSELDNEWA---IMYHV-GMGHKPPIPD 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  941 VIKLpyfntmkpkkqyrrklreefvfiPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd06626   231 SLQL-----------------------SPEGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
711-998 4.65e-33

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: 129.35  E-value: 4.65e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMV--ALKKVR--LDNEKEG-FPITAIREIKILRQLTHQSIINmkeivtdkedALD-FKKDK 784
Cdd:cd13994     1 IGKGATSVVRIVTKKNPRSGVlyAVKEYRrrDDESKRKdYVKRLTSEYIISSKLHHPNIVK----------VLDlCQDLH 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVFEYMDH-DLMGLLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA--RL 861
Cdd:cd13994    71 GKWCLVMEYCPGgDLFTLIEKAD-SLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAevFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  862 YSSEESRPYTNKVI-TLWYRPPELLLGEErYTP-AIDVWSCGCILGELFTKKPIFqanqelaqlelisRIcgspcpAVWP 939
Cdd:cd13994   150 MPAEKESPMSAGLCgSEPYMAPEVFTSGS-YDGrAVDVWSCGIVLFALFTGRFPW-------------RS------AKKS 209
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  940 DVIKLPYfntMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd13994   210 DSAYKAY---EKSGDFTNGPYEPIENLLPSECRRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
711-1011 5.87e-33

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: 131.75  E-value: 5.87e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKdkgaFYLV 790
Cdd:cd07874    25 IGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLEEFQD----VYLV 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHDLMGLLESGLVHfneNHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARlySSEESRPY 870
Cdd:cd07874   101 MELMDANLCQVIQMELDH---ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR--TAGTSFMM 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  871 TNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCP----AVWPDV----- 941
Cdd:cd07874   176 TPYVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLGTPCPefmkKLQPTVrnyve 254
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  942 -------IKLP--YFNTMKPKKQYRRKLReefvfiPAAALDLFDYMLALDPSKRCTAEQALQCEFLR---DVEPSKMPPP 1009
Cdd:cd07874   255 nrpkyagLTFPklFPDSLFPADSEHNKLK------ASQARDLLSKMLVIDPAKRISVDEALQHPYINvwyDPAEVEAPPP 328

                  ..
gi 145309300 1010 DL 1011
Cdd:cd07874   329 QI 330
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
704-994 1.10e-32

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: 128.16  E-value: 1.10e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLdnekegFPITA-------IREIKILRQLTHQSIINMkeivtdked 776
Cdd:cd08224     1 NYEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQI------FEMMDakarqdcLKEIDLLQQLNHPNIIKY--------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 aLDFKKDKGAFYLVFEYMDH-DLMGLLE---SGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIK 852
Cdd:cd08224    66 -LASFIENNELNIVLELADAgDLSRLIKhfkKQKRLIPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVK 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFGLARLYSSEESRPYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFT-KKPIFQANQELAQL-ELISRIC 930
Cdd:cd08224   145 LGDLGLGRFFSSKTTAAHS-LVGTPYYMSPERIREQG-YDFKSDIWSLGCLLYEMAAlQSPFYGEKMNLYSLcKKIEKCE 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  931 GSPCPAvwpdviklpyfntmkpkKQYRRKLReefvfipaaalDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd08224   223 YPPLPA-----------------DLYSQELR-----------DLVAACIQPDPEKRPDISYVLD 258
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
710-998 1.18e-32

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: 128.65  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRL-------DNEKEGFPITAIR-EIKILRQLTHQSIINMkeivtdkedaLDFK 781
Cdd:cd06629     8 LIGKGTYGRVYLAMNATTGEMLAVKQVELpktssdrADSRQKTVVDALKsEIDTLKDLDHPNIVQY----------LGFE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR- 860
Cdd:cd06629    78 ETEDYFSIFLEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGISKk 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 ---LYSSEESrpyTNKVITLWYRPPELLLGEER-YTPAIDVWSCGCILGELFT-KKPIFQANQELAQLELISRICGSPCP 935
Cdd:cd06629   158 sddIYGNNGA---TSMQGSVFWMAPEVIHSQGQgYSAKVDIWSLGCVVLEMLAgRRPWSDDEAIAAMFKLGNKRSAPPVP 234
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  936 avwPDVIklpyfntmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd06629   235 ---EDVN------------------------LSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
703-994 2.84e-32

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: 127.51  E-value: 2.84e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKV---------RLDNEKegfPITAIREIKILRQLTHQSIINMKEIVtD 773
Cdd:cd14084     6 KKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIInkrkftigsRREINK---PRNIETEIEILKKLSHPCIIKIEDFF-D 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  774 KEDAldfkkdkgaFYLVFEYMDH-DLMGLLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ-- 850
Cdd:cd14084    82 AEDD---------YYIVLELMEGgELFDRVVSNK-RLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEec 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  851 -IKLADFGLARLysSEESRPYTNKVITLWYRPPELLL--GEERYTPAIDVWSCGCILGELFTKKPIFqaNQELAQLELIS 927
Cdd:cd14084   152 lIKITDFGLSKI--LGETSLMKTLCGTPTYLAPEVLRsfGTEGYTRAVDCWSLGVILFICLSGYPPF--SEEYTQMSLKE 227
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  928 RIcgspcpavwpdviklpyfntmkpkkqyrrkLREEFVFIPAA-------ALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14084   228 QI------------------------------LSGKYTFIPKAwknvseeAKDLVKKMLVVDPSRRPSIEEALE 271
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
705-998 3.39e-32

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: 127.33  E-value: 3.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDtGEMVALKKVRLDN----EKEGFpitaIREIKILRQLTHQS-IINMKEI-VTDKEDAL 778
Cdd:cd14131     3 YEILKQLGKGGSSKVYKVLNPK-KKIYALKRVDLEGadeqTLQSY----KNEIELLKKLKGSDrIIQLYDYeVTDEDDYL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 dfkkdkgafYLVFEYMDHDLMGLLESGLVH-FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNrGQIKLADFG 857
Cdd:cd14131    78 ---------YMVMECGEIDLATILKKKRPKpIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK-GRLKLIDFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARLYSSEEsrpyTN-----KVITLWYRPPELLL-------GEERY--TPAIDVWSCGCILGELFTKKPIFQANQElaQL 923
Cdd:cd14131   148 IAKAIQNDT----TSivrdsQVGTLNYMSPEAIKdtsasgeGKPKSkiGRPSDVWSLGCILYQMVYGKTPFQHITN--PI 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  924 ELISRICGsPCPAV-WPDViklpyfntmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14131   222 AKLQAIID-PNHEIeFPDI-------------------------PNPDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
704-997 3.51e-32

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: 3.51e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDnEKEGFPITAiREIKILRQLTHQSIINMKeivtdkedALDFKKD 783
Cdd:cd06613     1 DYELIQRIGSGTYGDVYKARNIATGELAAVKVIKLE-PGDDFEIIQ-QEISMLKECRHPNIVAYF--------GSYLRRD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KgaFYLVFEYMD----HDLMGLLEsglvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL- 858
Cdd:cd06613    71 K--LWIVMEYCGggslQDIYQVTG----PLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGVs 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYSSEESRpytNKVI-TLWYRPPELLLGEER--YTPAIDVWSCG--CI-LGELftKKPIFQANQELAqLELISRICGS 932
Cdd:cd06613   145 AQLTATIAKR---KSFIgTPYWMAPEVAAVERKggYDGKCDIWALGitAIeLAEL--QPPMFDLHPMRA-LFLIPKSNFD 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  933 PcpavwpdviklpyfntmkPKKQYRRKLREEFV-FIPAAaldlfdymLALDPSKRCTAEQALQCEF 997
Cdd:cd06613   219 P------------------PKLKDKEKWSPDFHdFIKKC--------LTKNPKKRPTATKLLQHPF 258
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
705-994 4.89e-32

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: 125.97  E-value: 4.89e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKegfpITAI-REIKILRQLTHQSIINMKEiVTDKEDALdf 780
Cdd:cd14071     2 YDIERTIGKGNFAVVKLARHRITKTEVAIKiidKSQLDEEN----LKKIyREVQIMKMLNHPHIIKLYQ-VMETKDML-- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdkgafYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR 860
Cdd:cd14071    75 -------YLVTEYASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 LYSSEEsrpytnkVITLW-----YRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQAN--QELAQLELISRicgsp 933
Cdd:cd14071   148 FFKPGE-------LLKTWcgsppYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGALPFDGStlQTLRDRVLSGR----- 215
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  934 cpavwpdvIKLPYFNTMKPKKQYRRklreefvfipaaaldlfdyMLALDPSKRCTAEQALQ 994
Cdd:cd14071   216 --------FRIPFFMSTDCEHLIRR-------------------MLVLDPSKRLTIEQIKK 249
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
710-998 5.09e-32

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: 126.70  E-value: 5.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRL------DNEKEGFPITAIREIKILRQLT-HQSIINMKeivtdkedalDFKK 782
Cdd:cd14093    10 ILGRGVSSTVRRCIEKETGQEFAVKIIDItgekssENEAEELREATRREIEILRQVSgHPNIIELH----------DVFE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFYLVFEYMDH-DLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA-R 860
Cdd:cd14093    80 SPTFIFLVFELCRKgELFDYLTE-VVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFAtR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 LYSSEESRpytNKVITLWYRPPELL-----LGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELIsricgspcp 935
Cdd:cd14093   159 LDEGEKLR---ELCGTPGYLAPEVLkcsmyDNAPGYGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNI--------- 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  936 avwpdviklpyfntMKPKKQYRrklREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14093   227 --------------MEGKYEFG---SPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
711-1012 5.32e-32

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: 129.39  E-value: 5.32e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKdkgaFYLV 790
Cdd:cd07875    32 IGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVFTPQKSLEEFQD----VYIV 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHDLMGLLESGLVHfneNHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARlySSEESRPY 870
Cdd:cd07875   108 MELMDANLCQVIQMELDH---ERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLAR--TAGTSFMM 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  871 TNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDV---IKLPYF 947
Cdd:cd07875   183 TPYVVTRYYRAPEVILGMG-YKENVDIWSVGCIMGEMIKGGVLFPGTDHIDQWNKVIEQLGTPCPEFMKKLqptVRTYVE 261
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  948 NTMKPKKQYRRKLREEFVFiPA----------AALDLFDYMLALDPSKRCTAEQALQCEFLR---DVEPSKMPPPDLP 1012
Cdd:cd07875   262 NRPKYAGYSFEKLFPDVLF-PAdsehnklkasQARDLLSKMLVIDASKRISVDEALQHPYINvwyDPSEAEAPPPKIP 338
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
705-939 9.57e-32

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: 125.58  E-value: 9.57e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRL----DNEKEgfpiTAIREIKILRQLTHQSIINMKEIVtdkedaLDF 780
Cdd:cd08530     2 FKVLKKLGKGSYGSVYKVKRLSDNQVYALKEVNLgslsQKERE----DSVNEIRLLASVNHPNIIRYKEAF------LDG 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 KKdkgaFYLVFEYMD-HDLMGLLESGLVH---FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd08530    72 NR----LCIVMEYAPfGDLSKLISKRKKKrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSEESRPYTNkviTLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQAN--QELAQlelisRICGSPC 934
Cdd:cd08530   148 GISKVLKKNLAKTQIG---TPLYAAPEVWKGRP-YDYKSDIWSLGCLLYEMATFRPPFEARtmQELRY-----KVCRGKF 218

                  ....*
gi 145309300  935 PAVWP 939
Cdd:cd08530   219 PPIPP 223
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
711-998 1.38e-31

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 125.06  E-value: 1.38e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKV-RLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDaldfkkdkgaFYL 789
Cdd:cd14081     9 LGKGQTGLVKLAKHCVTGQKVAIKIVnKEKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKY----------LYL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYM-DHDLMG-LLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLysSEES 867
Cdd:cd14081    79 VLEYVsGGELFDyLVKKG--RLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASL--QPEG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  868 RPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQaNQELAQLelisricgspcpavwpdviklpyF 947
Cdd:cd14081   155 SLLETSCGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFD-DDNLRQL-----------------------L 210
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  948 NTMKpkkqyrrklREEFV---FIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14081   211 EKVK---------RGVFHiphFISPDAQDLLRRMLEVNPEKRITIEEIKKHPWF 255
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
711-998 2.64e-31

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: 124.48  E-value: 2.64e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKV--------RLDNEKEGFPITA-----IREIKILRQLTHQSIINMKEIVTDKEda 777
Cdd:cd14077     9 IGAGSMGKVKLAKHIRTGEKCAIKIIprasnaglKKEREKRLEKEISrdirtIREAALSSLLNHPHICRLRDFLRTPN-- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 ldfkkdkgAFYLVFEYMDHDLMglLESGLVH--FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLAD 855
Cdd:cd14077    87 --------HYYMLFEYVDGGQL--LDYIISHgkLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIID 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  856 FGLARLYSSEES-RPYTNkviTLWYRPPELLLGeERYT-PAIDVWSCGCILGELFTKKPIFQaNQELAQLEliSRIcgsp 933
Cdd:cd14077   157 FGLSNLYDPRRLlRTFCG---SLYFAAPELLQA-QPYTgPEVDVWSFGVVLYVLVCGKVPFD-DENMPALH--AKI---- 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  934 cpavwpdviklpyfntMKPKKQYRRKLREEfvfipaaALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14077   226 ----------------KKGKVEYPSYLSSE-------CKSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
704-998 5.15e-31

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


Pssm-ID: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 125.03  E-value: 5.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTG-EMVALKKVRlDNEKegFPITAIREIKILRQLTHqsiinmkeivTDKEDA----- 777
Cdd:cd14135     1 RYRVYGYLGKGVFSNVVRARDLARGnQEVAIKIIR-NNEL--MHKAGLKELEILKKLND----------ADPDDKkhcir 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 -LDFKKDKGAFYLVFEYMDHDLMGLL--ESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLN-NRGQIKL 853
Cdd:cd14135    68 lLRHFEHKNHLCLVFESLSMNLREVLkkYGKNVGLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNeKKNTLKL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  854 ADFGLARLYSSEESRPYtnkVITLWYRPPELLLGEeRYTPAIDVWSCGCILGELFTKKPIFQA---NQEL---------- 920
Cdd:cd14135   148 CDFGSASDIGENEITPY---LVSRFYRAPEIILGL-PYDYPIDMWSVGCTLYELYTGKILFPGktnNHMLklmmdlkgkf 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  921 ----------------AQLELISR----ICGSPcpavwpdVIKLPYFNtmKPKKQYRRKLRE-----EFVFIPAAAL-DL 974
Cdd:cd14135   224 pkkmlrkgqfkdqhfdENLNFIYRevdkVTKKE-------VRRVMSDI--KPTKDLKTLLIGkqrlpDEDRKKLLQLkDL 294
                         330       340
                  ....*....|....*....|....
gi 145309300  975 FDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14135   295 LDKCLMLDPEKRITPNEALQHPFI 318
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
703-1006 7.34e-31

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: 123.70  E-value: 7.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRL--DNEKEGFpitaIREIKILRQLTHQSIINMKEIVtdkedaldF 780
Cdd:cd06611     5 DIWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIesEEELEDF----MVEIDILSECKHPNIVGLYEAY--------F 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 KKDKgaFYLVFEYMD----HDLMGLLESGLvhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd06611    73 YENK--LWILIEFCDggalDSIMLELERGL---TEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSEESRPYTNkVITLWYRPPELLLGE----ERYTPAIDVWSCGCILGELFTKKPifqANQELAQLELISRICGS 932
Cdd:cd06611   148 GVSAKNKSTLQKRDTF-IGTPYWMAPEVVACEtfkdNPYDYKADIWSLGITLIELAQMEP---PHHELNPMRVLLKILKS 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  933 PCPavwpdviklpyfnTMKPKKQYRRKLReefvfipaaalDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKM 1006
Cdd:cd06611   224 EPP-------------TLDQPSKWSSSFN-----------DFLKSCLVKDPDDRPTAAELLKHPFVSDQSDNKA 273
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
704-935 1.26e-30

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


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 125.63  E-value: 1.26e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldNEKEgFPITAIREIKILRQLTHQSIINMKEIVtdkeDALDFKKD 783
Cdd:cd14224    66 RYEVLKVIGKGSFGQVVKAYDHKTHQHVALKMVR--NEKR-FHRQAAEEIRILEHLKKQDKDNTMNVI----HMLESFTF 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDHDLMGLLE-SGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ--IKLADFGLA- 859
Cdd:cd14224   139 RNHICMTFELLSMNLYELIKkNKFQGFSLQLVRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFGSSc 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 ----RLYSSEESRpytnkvitlWYRPPELLLGEeRYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCP 935
Cdd:cd14224   219 yehqRIYTYIQSR---------FYRAPEVILGA-RYGMPIDMWSFGCILAELLTGYPLFPGEDEGDQLACMIELLGMPPQ 288
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
710-998 1.44e-30

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: 122.52  E-value: 1.44e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITaiREIKILRQLTHQSIInmKEIVTDKEDAldfkkdkgaFYL 789
Cdd:cd06624    15 VLGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLH--EEIALHSRLSHKNIV--QYLGSVSEDG---------FFK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFeyMDH----DLMGLLES--GLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN-RGQIKLADFG----L 858
Cdd:cd06624    82 IF--MEQvpggSLSALLRSkwGPLKDNENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFGtskrL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLysseesRPYTNKVI-TLWYRPPELL-LGEERYTPAIDVWSCGCILGELFTKKPIFqanqelaqLELisricGSPCPA 936
Cdd:cd06624   160 AGI------NPCTETFTgTLQYMAPEVIdKGQRGYGPPADIWSLGCTIIEMATGKPPF--------IEL-----GEPQAA 220
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  937 VWpdviKLPYFNTMKPkkqyrrklreefvfIP----AAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd06624   221 MF----KVGMFKIHPE--------------IPeslsEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
704-936 1.62e-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: 122.00  E-value: 1.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPiTAIREIKILRQLTHQSIINMKEivtdkedalDFKKD 783
Cdd:cd08219     1 QYNVLRVVGEGSFGRALLVQHVNSDQKYAMKEIRLPKSSSAVE-DSRKEAVLLAKMKHPNIVAFKE---------SFEAD 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kGAFYLVFEYMDH-DLMGL--LESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR 860
Cdd:cd08219    71 -GHLYIVMEYCDGgDLMQKikLQRGKL-FPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSAR 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  861 LYSSEESRPYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANqelAQLELISRICG---SPCPA 936
Cdd:cd08219   149 LLTSPGAYACT-YVGTPYYVPPEIWENMP-YNNKSDIWSLGCILYELCTLKHPFQAN---SWKNLILKVCQgsyKPLPS 222
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
710-912 2.32e-30

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: 121.69  E-value: 2.32e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNE-----KEgfpITAI-REIKILRQLTHQSIINMkeivtdkedaLDFKKD 783
Cdd:cd06625     7 LLGQGAFGQVYLCYDADTGRELAVKQVEIDPInteasKE---VKALeCEIQLLKNLQHERIVQY----------YGCLQD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMdhdlmgllESGLVH--------FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLAD 855
Cdd:cd06625    74 EKSLSIFMEYM--------PGGSVKdeikaygaLTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGD 145
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  856 FGLARLYSSEESRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKP 912
Cdd:cd06625   146 FGASKRLQTICSSTGMKSVTgTPYWMSPEVINGEG-YGRKADIWSVGCTVVEMLTTKP 202
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
704-917 3.18e-30

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: 121.02  E-value: 3.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKV----RLDNEKEGfpiTAIREIKILRQLTHQSIINMKEIvtdkedald 779
Cdd:cd06607     2 IFEDLREIGHGSFGAVYYARNKRTSEVVAIKKMsysgKQSTEKWQ---DIIKEVKFLRQLRHPNTIEYKGC--------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FKKDKGAfYLVFEYMDHDLMGLLEsglVH---FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd06607    70 YLREHTA-WLVMEYCLGSASDIVE---VHkkpLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADF 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  857 GLARLYSseesrPYTNKVITLWYRPPELLLG--EERYTPAIDVWSCG--CI-LGElfTKKPIFQAN 917
Cdd:cd06607   146 GSASLVC-----PANSFVGTPYWMAPEVILAmdEGQYDGKVDVWSLGitCIeLAE--RKPPLFNMN 204
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
704-994 5.49e-30

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 120.20  E-value: 5.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKvrLDNE---KEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDaldf 780
Cdd:cd14663     1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKI--IDKEqvaREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTK---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdkgaFYLVFEYMDHdlmGLLESGLV---HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG 857
Cdd:cd14663    75 ------IFFVMELVTG---GELFSKIAkngRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARLysSEESRPYT---NKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQAnqelaqlelisricgspc 934
Cdd:cd14663   146 LSAL--SEQFRQDGllhTTCGTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFDD------------------ 205
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  935 pavwPDVIKLpyfntmkpkkqYRRKLREEFVF---IPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14663   206 ----ENLMAL-----------YRKIMKGEFEYprwFSPGAKSLIKRILDPNPSTRITVEQIMA 253
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
711-903 6.29e-30

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: 119.68  E-value: 6.29e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALK--KVRLDNEKEgfpitAIREIKILRQLTHQSIINMKEIVTDKEDALdfkkdkgafy 788
Cdd:cd14006     1 LGRGRFGVVKRCIEKATGREFAAKfiPKRDKKKEA-----VLREISILNQLQHPRIIQLHEAYESPTELV---------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDHdlmGLLESGLVH---FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG--QIKLADFGLARLYS 863
Cdd:cd14006    66 LILELCSG---GELLDRLAErgsLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLARKLN 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 145309300  864 SEESRpytnKVI--TLWYRPPELLLGEErYTPAIDVWSCGCI 903
Cdd:cd14006   143 PGEEL----KEIfgTPEFVAPEIVNGEP-VSLATDMWSIGVL 179
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
704-930 6.51e-30

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: 120.06  E-value: 6.51e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDN----EKEGfpitAIREIKILRQLTHQSIINMkeivtdkedaLD 779
Cdd:cd08225     1 RYEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKmpvkEKEA----SKKEVILLAKMKHPNIVTF----------FA 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FKKDKGAFYLVFEYMDH-DLMGLL--ESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQI-KLAD 855
Cdd:cd08225    67 SFQENGRLFIVMEYCDGgDLMKRInrQRG-VLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGD 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  856 FGLARLYSSEESRPYTNkVITLWYRPPELLlgEER-YTPAIDVWSCGCILGELFTKKPIFQANQeLAQLELisRIC 930
Cdd:cd08225   146 FGIARQLNDSMELAYTC-VGTPYYLSPEIC--QNRpYNNKTDIWSLGCVLYELCTLKHPFEGNN-LHQLVL--KIC 215
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
711-947 6.81e-30

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: 120.09  E-value: 6.81e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAI-REIKILRQLTHQSIINMKE-IVTDKEdaldfkkdkgaFY 788
Cdd:cd14162     8 LGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKFLpREIEVIKGLKHPNLICFYEaIETTSR-----------VY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARlyssEES 867
Cdd:cd14162    77 IIMELAENgDLLDYIRKN-GALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFAR----GVM 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  868 RPYTNKVI-------TLWYRPPELLLGEErYTPAI-DVWSCGCIL-----GEL-------------FTKKPIFQANQELA 921
Cdd:cd14162   152 KTKDGKPKlsetycgSYAYASPEILRGIP-YDPFLsDIWSMGVVLytmvyGRLpfddsnlkvllkqVQRRVVFPKNPTVS 230
                         250       260       270
                  ....*....|....*....|....*....|
gi 145309300  922 Q--LELISRICgSPCP--AVWPDVIKLPYF 947
Cdd:cd14162   231 EecKDLILRML-SPVKkrITIEEIKRDPWF 259
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
711-996 1.05e-29

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: 119.28  E-value: 1.05e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVA---LKKVRL-------DNEKegfpitaiREIKILRQLTHQSIINMKEIVTDKEdaldf 780
Cdd:cd14119     1 LGEGSYGKVKEVLDTETLCRRAvkiLKKRKLrripngeANVK--------REIQILRRLNHRNVIKLVDVLYNEE----- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdKGAFYLVFEYMDHDLMGLL-ESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd14119    68 ---KQKLYMVMEYCVGGLQEMLdSAPDKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 rlyssEESRPY------TNKVITLWYRPPELLLGEERYTP-AIDVWSCGCILGELFTKK-PIFQANqelaQLELISRIcg 931
Cdd:cd14119   145 -----EALDLFaeddtcTTSQGSPAFQPPEIANGQDSFSGfKVDIWSAGVTLYNMTTGKyPFEGDN----IYKLFENI-- 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  932 SPCPAVWPDViklpyfntmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCE 996
Cdd:cd14119   214 GKGEYTIPDD-------------------------VDPDLQDLLRGMLEKDPEKRFTIEQIRQHP 253
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
711-997 2.62e-29

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: 118.55  E-value: 2.62e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVrldnEKEGFPITAiREIKILRQLTHQSIInmkeivtdkedaldfkkdkgAFY-- 788
Cdd:cd14010     8 IGRGKHSVVYKGRRKGTIEFVAIKCV----DKSKRPEVL-NEVRLTHELKHPNVL--------------------KFYew 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 --------LVFEY-MDHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd14010    63 yetsnhlwLVVEYcTGGDLETLLRQD-GNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLA 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RL-----------YSSEESRPYTNKVITL----WYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANqelAQLE 924
Cdd:cd14010   142 RRegeilkelfgqFSDEGNVNKVSKKQAKrgtpYYMAPELFQGGV-HSFASDLWALGCVLYEMFTGKPPFVAE---SFTE 217
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  925 LISRICGSPCPAvwpdviklpyfntmkPKKQYRRKLREEFVfipaaalDLFDYMLALDPSKRCTAEQALQCEF 997
Cdd:cd14010   218 LVEKILNEDPPP---------------PPPKVSSKPSPDFK-------SLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
701-929 3.88e-29

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: 118.14  E-value: 3.88e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  701 CVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLdnEKEGFPITAIREIKILRQLTHQSIINMkeivtdkeda 777
Cdd:cd14116     3 ALEDFEIGRPLGKGKFGNVYLAREKQSKFILALKvlfKAQL--EKAGVEHQLRREVEIQSHLRHPNILRL---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 LDFKKDKGAFYLVFEYMDH-DLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd14116    71 YGYFHDATRVYLILEYAPLgTVYRELQK-LSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADF 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  857 GLArLYSSEESRpyTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRI 929
Cdd:cd14116   150 GWS-VHAPSSRR--TTLCGTLDYLPPEMIEG-RMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRV 218
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
704-904 4.12e-29

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: 117.75  E-value: 4.12e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKdTGEMVALKKVRLDNEKEGFPITAIR-EIKILRQLTHQSIINMKEIVTDKEDALdfkk 782
Cdd:cd14161     4 RYEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIKDEQDLLHIRrEIEIMSSLNHPHIISVYEVFENSSKIV---- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgafyLVFEYMDH-DLMGLLeSGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL 861
Cdd:cd14161    79 ------IVMEYASRgDLYDYI-SERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNL 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 145309300  862 YSSEES-RPYTNKVItlwYRPPELLLGEERYTPAIDVWSCGCIL 904
Cdd:cd14161   152 YNQDKFlQTYCGSPL---YASPEIVNGRPYIGPEVDSWSLGVLL 192
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
711-991 6.36e-29

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: 117.00  E-value: 6.36e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDK-DTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKeivtdkedalDFKKDKGAFYL 789
Cdd:cd14121     3 LGSGTYATVYKAYRKsGAREVVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELK----------DFQWDEEHIYL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLmglleSGLVHFN----ENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ--IKLADFGLARlY 862
Cdd:cd14121    73 IMEYCSGgDL-----SRFIRSRrtlpESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNpvLKLADFGFAQ-H 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEESRPYTNKVITLwYRPPELLLGeERYTPAIDVWSCGCILGE-LFTKKPIfqANQELAQLELisRICGSpcpavwpDV 941
Cdd:cd14121   147 LKPNDEAHSLRGSPL-YMAPEMILK-KKYDARVDLWSVGVILYEcLFGRAPF--ASRSFEELEE--KIRSS-------KP 213
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 145309300  942 IKLPyfntmkpkkqyrrklreEFVFIPAAALDLFDYMLALDPSKRCTAEQ 991
Cdd:cd14121   214 IEIP-----------------TRPELSADCRDLLLRLLQRDPDRRISFEE 246
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
707-994 7.83e-29

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: 116.98  E-value: 7.83e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  707 IIG-IIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEGFPITaiREIKILRQLTHQSIINMKEIVTDKEDaldfkk 782
Cdd:cd14079     5 ILGkTLGVGSFGKVKLAEHELTGHKVAVKilnRQKIKSLDMEEKIR--REIQILKLFRHPHIIRLYEVIETPTD------ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgaFYLVFEYM------DHdlmgLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd14079    77 ----IFMVMEYVsggelfDY----IVQKG--RLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSEE----SRPYTNkvitlwYRPPELLLGEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGS 932
Cdd:cd14079   147 GLSNIMRDGEflktSCGSPN------YAAPEVISGKLYAGPEVDVWSCGVILYAL---------------------LCGS 199
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  933 pcpavwpdvikLPYFNTMKPkkQYRRKLREEFVFIP----AAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14079   200 -----------LPFDDEHIP--NLFKKIKSGIYTIPshlsPGARDLIKRMLVVDPLKRITIPEIRQ 252
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
704-994 8.78e-29

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: 117.04  E-value: 8.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVrlDNEK-EGFPITAIREIKILRQLTHQSIINM-KEIVTDKEdaldfk 781
Cdd:cd14095     1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKII--DKAKcKGKEHMIENEVAILRRVKHPNIVQLiEEYDTDTE------ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgaFYLVFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG----QIKLADF 856
Cdd:cd14095    73 -----LYLVMELVKGgDLFDAITSS-TKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEdgskSLKLADF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLArlysSEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQA---NQElaqlELISRI--CG 931
Cdd:cd14095   147 GLA----TEVKEPLFTVCGTPTYVAPE-ILAETGYGLKVDIWAAGVITYILLCGFPPFRSpdrDQE----ELFDLIlaGE 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  932 SPCPAvwpdviklPYFNTmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14095   218 FEFLS--------PYWDN-----------------ISDSAKDLISRMLVVDPEKRYSAGQVLD 255
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
696-998 9.39e-29

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: 117.38  E-value: 9.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  696 DW--GKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEK------EGFPITAIREIKILRQLT-HQSIIN 766
Cdd:cd14181     1 DWagAKEFYQKYDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEVTAERlspeqlEEVRSSTLKEIHILRQVSgHPSIIT 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  767 MkeivtdkedaLDFKKDKGAFYLVFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL 845
Cdd:cd14181    81 L----------IDSYESSTFIFLVFDLMRRgELFDYLTEK-VTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  846 NNRGQIKLADFGLA-RLYSSEESRPYTNkviTLWYRPPELL---LGE--ERYTPAIDVWSCGCILGELFTKKPIFQANQE 919
Cdd:cd14181   150 DDQLHIKLSDFGFScHLEPGEKLRELCG---TPGYLAPEILkcsMDEthPGYGKEVDLWACGVILFTLLAGSPPFWHRRQ 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  920 LAQLELISR---ICGSPcpaVWPDviklpYFNTMKpkkqyrrklreefvfipaaalDLFDYMLALDPSKRCTAEQALQCE 996
Cdd:cd14181   227 MLMLRMIMEgryQFSSP---EWDD-----RSSTVK---------------------DLISRLLVVDPEIRLTAEQALQHP 277

                  ..
gi 145309300  997 FL 998
Cdd:cd14181   278 FF 279
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
703-914 1.26e-28

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: 118.93  E-value: 1.26e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldneKEgfpitaireikilrqlthqSIINMKEIVTDKE--DALDF 780
Cdd:cd05573     1 DDFEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILR----KS-------------------DMLKREQIAHVRAerDILAD 57
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 KK------------DKGAFYLVFEYM-DHDLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN 847
Cdd:cd05573    58 ADspwivrlhyafqDEDHLYLVMEYMpGGDLMNLLIKYDV-FPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDA 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  848 RGQIKLADFGLA-RLYSSEESRPYTNKVITLW---------------------------YRPPELLLGEErYTPAIDVWS 899
Cdd:cd05573   137 DGHIKLADFGLCtKMNKSGDRESYLNDSVNTLfqdnvlarrrphkqrrvraysavgtpdYIAPEVLRGTG-YGPECDWWS 215
                         250
                  ....*....|....*
gi 145309300  900 CGCILGELFTKKPIF 914
Cdd:cd05573   216 LGVILYEMLYGFPPF 230
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
705-986 1.63e-28

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 116.20  E-value: 1.63e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEGFPItaIREIKILRQLTHQSIINMKEIVTDKEDaldfk 781
Cdd:cd05578     2 FQILRVIGKGSFGKVCIVQKKDTKKMFAMKymnKQKCIEKDSVRNV--LNELEILQELEHPFLVNLWYSFQDEED----- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgaFYLVFEYMdhdLMGLLE---SGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd05578    75 -----MYMVVDLL---LGGDLRyhlQQKVKFSEETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNI 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYssEESRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGE-LFTKKPIfqanqelaqlelisricgspcpav 937
Cdd:cd05578   147 ATKL--TDGTLATSTSGTKPYMAPEVFMRAG-YSFAVDWWSLGVTAYEmLRGKRPY------------------------ 199
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 145309300  938 wpdviklpYFNTMKPKKQYRRKLREEFVFIPAA----ALDLFDYMLALDPSKR 986
Cdd:cd05578   200 --------EIHSRTSIEEIRAKFETASVLYPAGwseeAIDLINKLLERDPQKR 244
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
704-993 1.68e-28

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: 115.99  E-value: 1.68e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEivtdkedalDFKKD 783
Cdd:cd08220     1 KYEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYE---------SFLED 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KgAFYLVFEYMDHDLMG--LLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQI-KLADFGLAR 860
Cdd:cd08220    72 K-ALMIVMEYAPGGTLFeyIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISK 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 LYSSEeSRPYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQAnqelAQLelisricgspcPAVwpd 940
Cdd:cd08220   151 ILSSK-SKAYT-VVGTPCYISPELCEGKP-YNQKSDIWALGCVLYELASLKRAFEA----ANL-----------PAL--- 209
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 145309300  941 VIKLPYFNTMKPKKQYRRKLREefvfipaaaldLFDYMLALDPSKRCTAEQAL 993
Cdd:cd08220   210 VLKIMRGTFAPISDRYSEELRH-----------LILSMLHLDPNKRPTLSEIM 251
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
703-1002 1.86e-28

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: 117.26  E-value: 1.86e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLD--NEKEGFPITAI-REIKILRQLTHQSIINMKEIVTDKedald 779
Cdd:cd14094     3 DVYELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAkfTSSPGLSTEDLkREASICHMLKHPHIVELLETYSSD----- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkkdkGAFYLVFEYMD-----HDLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL---NNRGQI 851
Cdd:cd14094    78 -----GMLYMVFEFMDgadlcFEIVKRADAGFV-YSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  852 KLADFGLARLYSSEESRPyTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQlELISRICG 931
Cdd:cd14094   152 KLGGFGVAIQLGESGLVA-GGRVGTPHFMAPE-VVKREPYGKPVDVWGCGVILFILLSGCLPFYGTKERLF-EGIIKGKY 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  932 SPCPAVWPDviklpyfntmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVE 1002
Cdd:cd14094   229 KMNPRQWSH--------------------------ISESAKDLVRRMLMLDPAERITVYEALNHPWIKERD 273
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
711-1006 2.04e-28

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: 117.45  E-value: 2.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKV----RLDNEKEGfpiTAIREIKILRQLTHQSIINMKEIvtdkedaldFKKDKGA 786
Cdd:cd06633    29 IGHGSFGAVYFATNSHTNEVVAIKKMsysgKQTNEKWQ---DIIKEVKFLQQLKHPNTIEYKGC---------YLKDHTA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 fYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGlarlySSEE 866
Cdd:cd06633    97 -WLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG-----SASI 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  867 SRPYTNKVITLWYRPPELLLG--EERYTPAIDVWSCGCILGELFTKKP-IFQANqelaQLELISRICGSPCPAV----WP 939
Cdd:cd06633   171 ASPANSFVGTPYWMAPEVILAmdEGQYDGKVDIWSLGITCIELAERKPpLFNMN----AMSALYHIAQNDSPTLqsneWT 246
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  940 DviklpyfntmkpkkQYRRklreeFVfipaaaldlfDYMLALDPSKRCTAEQALQCEFLRDVEPSKM 1006
Cdd:cd06633   247 D--------------SFRG-----FV----------DYCLQKIPQERPSSAELLRHDFVRRERPPRV 284
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
703-998 3.01e-28

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: 116.91  E-value: 3.01e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDnekEGFPITAIREIKILRQlthqsIINMKEIVTDKE---DALD 779
Cdd:cd14136    10 GRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSA---QHYTEAALDEIKLLKC-----VREADPKDPGREhvvQLLD 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FKKDKGAF----YLVFEYMDHDLMGLLEsglvHFNE-----NHIKSFMRQLMEGLDYCHKK-NFLHRDIKCSNILLN-NR 848
Cdd:cd14136    82 DFKHTGPNgthvCMVFEVLGPNLLKLIK----RYNYrgiplPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCiSK 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  849 GQIKLADFGLARLYsseeSRPYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQ---------E 919
Cdd:cd14136   158 IEVKIADLGNACWT----DKHFTEDIQTRQYRSPEVILG-AGYGTPADIWSTACMAFELATGDYLFDPHSgedysrdedH 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  920 LAQL-ELISRIcgspcpavwPDVIKL------PYFNTMKPKKQYRR--------KLREEFVFIPAAALDLFD---YMLAL 981
Cdd:cd14136   233 LALIiELLGRI---------PRSIILsgkysrEFFNRKGELRHISKlkpwpledVLVEKYKWSKEEAKEFASfllPMLEY 303
                         330
                  ....*....|....*..
gi 145309300  982 DPSKRCTAEQALQCEFL 998
Cdd:cd14136   304 DPEKRATAAQCLQHPWL 320
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
703-997 4.30e-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: 115.15  E-value: 4.30e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPiTAIREIKILRQLTHQSIINMKEIVTDKEDaldfkk 782
Cdd:cd06610     1 DDYELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQTSMD-ELRKEIQAMSQCNHPNVVSYYTSFVVGDE------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgaFYLVFEYMD----HDLM--GLLESGlvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd06610    74 ----LWLVMPLLSggslLDIMksSYPRGG---LDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GL-ARLYSSEESRPYTNKVI--TLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFqanQELAQLELISRICGSP 933
Cdd:cd06610   147 GVsASLATGGDRTRKVRKTFvgTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPY---SKYPPMKVLMLTLQND 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  934 CPavwpdviKLPyfnTMKPKKQYRRKLReefvfipaaalDLFDYMLALDPSKRCTAEQALQCEF 997
Cdd:cd06610   224 PP-------SLE---TGADYKKYSKSFR-----------KMISLCLQKDPSKRPTAEELLKHKF 266
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
710-962 9.16e-28

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: 114.06  E-value: 9.16e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRL----DNEKEGFPITAIREIKILRQLTHQSIINMkeivtdkedaLDFKKDKG 785
Cdd:cd06630     7 LLGTGAFSSCYQARDVKTGTLMAVKQVSFcrnsSSEQEEVVEAIREEIRMMARLNHPNIVRM----------LGATQHKS 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 AFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ-IKLADFGLARLYSS 864
Cdd:cd06630    77 HFNIFVEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGQrLRIADFGAAARLAS 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  865 EESRP--YTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDV 941
Cdd:cd06630   157 KGTGAgeFQGQLLgTIAFMAPEVLRGEQ-YGRSCDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATTPPPIPEH 235
                         250       260
                  ....*....|....*....|....*
gi 145309300  942 IKLPY----FNTMKPKKQYRRKLRE 962
Cdd:cd06630   236 LSPGLrdvtLRCLELQPEDRPPARE 260
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
711-995 1.27e-27

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: 113.57  E-value: 1.27e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEK-EGFpitaIREIKILRQL-THQSIINMKEIVTDKEDaldfkkdkgafY 788
Cdd:cd13987     1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPSTKlKDF----LREYNISLELsVHPHIIKTYDVAFETED-----------Y 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEyMDHDLMGLL------ESGLvhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL--NNRGQIKLADFGLAR 860
Cdd:cd13987    66 YVFA-QEYAPYGDLfsiippQVGL---PEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfdKDCRRVKLCDFGLTR 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 LYSSeesrpyTNKVITLW--YRPPEL--LLGEERYT--PAIDVWSCGCILGELFTKKPIFQAnqelaqlelisriCGSPC 934
Cdd:cd13987   142 RVGS------TVKRVSGTipYTAPEVceAKKNEGFVvdPSIDVWAFGVLLFCCLTGNFPWEK-------------ADSDD 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  935 PAVWPDVIKLPYFNTMKPkKQYRRklreefvFIPaAALDLFDYMLALDPSKRCTAEQALQC 995
Cdd:cd13987   203 QFYEEFVRWQKRKNTAVP-SQWRR-------FTP-KALRMFKKLLAPEPERRCSIKEVFKY 254
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
711-994 1.36e-27

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: 113.91  E-value: 1.36e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDtGEMVALKKVRLDNEKEGFPiTAIREIKILRQLTHQSIINMkeivtdkedaLDFKKDKGAFYLV 790
Cdd:cd14066     1 IGSGGFGTVYKGVLEN-GTVVAVKRLNEMNCAASKK-EFLTELEMLGRLRHPNLVRL----------LGYCLESDEKLLV 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHdlmGLLESglvHFNENH---------IKSFMRQLMEGLDYCHKKNFL---HRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd14066    69 YEYMPN---GSLED---RLHCHKgspplpwpqRLKIAKGIARGLEYLHEECPPpiiHGDIKSSNILLDEDFEPKLTDFGL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYSSEESRPYTNKVI-TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAV 937
Cdd:cd14066   143 ARLIPPSESVSKTSAVKgTIGYLAPEYIRT-GRVSTKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVEWVESKGKEE 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  938 WPDVIklpyfntmkpkkqyRRKLREEFVFIPAAALDLFDymLAL-----DPSKRCTAEQALQ 994
Cdd:cd14066   222 LEDIL--------------DKRLVDDDGVEEEEVEALLR--LALlctrsDPSLRPSMKEVVQ 267
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
705-944 2.07e-27

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: 113.37  E-value: 2.07e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTG-EMVALKKVRLDN--------EKEGFPITAIREIKILR-QLTHQSIINMKEIVTDk 774
Cdd:cd08528     2 YAVLELLGSGAFGCVYKVRKKSNGqTLLALKEINMTNpafgrteqERDKSVGDIISEVNIIKeQLRHPNIVRYYKTFLE- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  775 EDALdfkkdkgafYLVFEYMDHDLMGLLESGL----VHFNENHIKSFMRQLMEGLDYCHK-KNFLHRDIKCSNILLNNRG 849
Cdd:cd08528    81 NDRL---------YIVMELIEGAPLGEHFSSLkeknEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDD 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  850 QIKLADFGLARLYSSEESRpYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELA-------- 921
Cdd:cd08528   152 KVTITDFGLAKQKGPESSK-MTSVVGTILYSCPEIVQNEP-YGEKADIWALGCILYQMCTLQPPFYSTNMLTlatkivea 229
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 145309300  922 ------------QLELISRICGSPCPAVWPDVIKL 944
Cdd:cd08528   230 eyeplpegmysdDITFVIRSCLTPDPEARPDIVEV 264
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
711-998 5.64e-27

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: 111.75  E-value: 5.64e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARD---KDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAF 787
Cdd:cd08222     8 LGSGNFGTVYLVSDlkaTADEELKVLKEISVGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKE----------SF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEY-----MDHDLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNrGQIKLADFGLARLY 862
Cdd:cd08222    78 CIVTEYceggdLDDKISEYKKSGTT-IDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKN-NVIKVGDFGISRIL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 --SSEESRPYTNkviTLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAqleLISRICGSPCPAVwPD 940
Cdd:cd08222   156 mgTSDLATTFTG---TPYYMSPEVLKHEG-YNSKSDIWSLGCILYEMCCLKHAFDGQNLLS---VMYKIVEGETPSL-PD 227
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  941 viklpyfntmkpkkQYRRKLReefvfipaaalDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd08222   228 --------------KYSKELN-----------AIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
704-916 8.05e-27

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: 111.06  E-value: 8.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEivtdkedalDFKkD 783
Cdd:cd08218     1 KYVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQE---------SFE-E 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDH-DLMGLLESGL-VHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL 861
Cdd:cd08218    71 NGNLYIVMDYCDGgDLYKRINAQRgVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARV 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  862 YSS--EESRPYTNkviTLWYRPPELLlgEER-YTPAIDVWSCGCILGELFTKKPIFQA 916
Cdd:cd08218   151 LNStvELARTCIG---TPYYLSPEIC--ENKpYNNKSDIWALGCVLYEMCTLKHAFEA 203
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
705-993 8.75e-27

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


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 112.14  E-value: 8.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARD-KDTGEMVALKKVRL-----DNEKEGFPITAIREIKILRQLTHQSIINMkeivtdkedaL 778
Cdd:cd14096     3 YRLINKIGEGAFSNVYKAVPlRNTGKPVAIKVVRKadlssDNLKGSSRANILKEVQIMKRLSHPNIVKL----------L 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 DFKKDKGAFYLVFEYMD-----HDLMGLlesglVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLN------- 846
Cdd:cd14096    73 DFQESDEYYYIVLELADggeifHQIVRL-----TYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLFEpipfips 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  847 --------------------------NRGQIKLADFGLARLYSSEESRPYTNkviTLWYRPPElLLGEERYTPAIDVWSC 900
Cdd:cd14096   148 ivklrkadddetkvdegefipgvgggGIGIVKLADFGLSKQVWDSNTKTPCG---TVGYTAPE-VVKDERYSKKVDMWAL 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  901 GCILGELftkkpifqanqelaqlelisrICGSPcpavwpdviklPYFNtmKPKKQYRRK-LREEFVF-------IPAAAL 972
Cdd:cd14096   224 GCVLYTL---------------------LCGFP-----------PFYD--ESIETLTEKiSRGDYTFlspwwdeISKSAK 269
                         330       340
                  ....*....|....*....|.
gi 145309300  973 DLFDYMLALDPSKRCTAEQAL 993
Cdd:cd14096   270 DLISHLLTVDPAKRYDIDEFL 290
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
711-919 9.03e-27

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: 111.16  E-value: 9.03e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKE-GFPITAIREIKILRQLTHQSIINMkeivtdkedaldFK--KDKGAF 787
Cdd:cd05572     1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQtRQQEHIFSEKEILEECNSPFIVKL------------YRtfKDKKYL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMD-HDLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR-LYSSE 865
Cdd:cd05572    69 YMLMEYCLgGELWTILRD-RGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKkLGSGR 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  866 esRPYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQE 919
Cdd:cd05572   148 --KTWT-FCGTPEYVAPEIILNKG-YDFSVDYWSLGILLYELLTGRPPFGGDDE 197
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
704-909 9.39e-27

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: 111.16  E-value: 9.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIgiIGEGTYGQVYKARDKDTGEMVALKKVRLD----NEKEGFpitaIREIKILRQLTHQSIINMkeivtdkedaLD 779
Cdd:cd13983     4 KFNEV--LGRGSFKTVYRAFDTEEGIEVAWNEIKLRklpkAERQRF----KQEIEILKSLKHPNIIKF----------YD 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 --FKKDKGAFYLVFEYMdhdlmgllESG--------LVHFNENHIKSFMRQLMEGLDYCHKKN--FLHRDIKCSNILLN- 846
Cdd:cd13983    68 swESKSKKEVIFITELM--------TSGtlkqylkrFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINg 139
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  847 NRGQIKLADFGLARLysSEESRPYTnkVI-TLWYRPPELLlgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd13983   140 NTGEVKIGDLGLATL--LRQSFAKS--VIgTPEFMAPEMY--EEHYDEKVDIYAFGMCLLEMAT 197
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
710-998 1.12e-26

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: 111.10  E-value: 1.12e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVrlDNEKEGFPITAI--REIKILRQLTHQSIINMKEIvtdkedaldFKKDKgAF 787
Cdd:cd14097     8 KLGQGSFGVVIEATHKETQTKWAIKKI--NREKAGSSAVKLleREVDILKHVNHAHIIHLEEV---------FETPK-RM 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN-------RGQIKLADFGLAR 860
Cdd:cd14097    76 YLVMELCEDGELKELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSsiidnndKLNIKVTDFGLSV 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 LYSSEESRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPD 940
Cdd:cd14097   156 QKYGLGEDMLQETCGTPIYMAPEVISAHG-YSQQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSVWQS 234
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  941 viklpyfntmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14097   235 --------------------------VSDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
703-1006 3.40e-26

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKs are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. There are several types of CaMKs including CaMKI, CaMKII, and CaMKIV. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. CaMKII is a signaling molecule that translates upstream calcium and reactive oxygen species (ROS) signals into downstream responses that play important roles in synaptic function and cardiovascular physiology. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 110.20  E-value: 3.40e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRL------DNEKegfpitAIREIKILRQLTHQSIINMKEIVTDKed 776
Cdd:cd14086     1 DEYDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTkklsarDHQK------LEREARICRLLKHPNIVRLHDSISEE-- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 aldfkkdkGAFYLVFEYMDHdlmGLLESGLV---HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ--- 850
Cdd:cd14086    73 --------GFHYLVFDLVTG---GELFEDIVareFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKgaa 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  851 IKLADFGLArLYSSEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIF--QANQELAQlelisr 928
Cdd:cd14086   142 VKLADFGLA-IEVQGDQQAWFGFAGTPGYLSPE-VLRKDPYGKPVDIWACGVILYILLVGYPPFwdEDQHRLYA------ 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  929 icgspcpavwpdVIKLPYFNTMKPkkqyrrklreEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL--RDVEPSKM 1006
Cdd:cd14086   214 ------------QIKAGAYDYPSP----------EWDTVTPEAKDLINQMLTVNPAKRITAAEALKHPWIcqRDRVASMV 271
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
711-998 3.93e-26

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: 108.85  E-value: 3.93e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALK--KVRLDNEKEgfpiTAIREIKILRQLTHQSIINMKeivtdkeDALDFKKDkgaFY 788
Cdd:cd14103     1 LGRGKFGTVYRCVEKATGKELAAKfiKCRKAKDRE----DVRNEIEIMNQLRHPRLLQLY-------DAFETPRE---MV 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYM----------DHDLmgllesglvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR--GQIKLADF 856
Cdd:cd14103    67 LVMEYVaggelfervvDDDF---------ELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRtgNQIKIIDF 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSEESRpytnKVItlwYRPPELLLGE----ERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRicgs 932
Cdd:cd14103   138 GLARKYDPDKKL----KVL---FGTPEFVAPEvvnyEPISYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTR---- 206
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  933 pcpAVWpdviklpYFNTmkpkkqyrrklrEEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14103   207 ---AKW-------DFDD------------EAFDDISDEAKDFISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
704-994 4.17e-26

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: 109.15  E-value: 4.17e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEdaldfkkd 783
Cdd:cd14072     1 NYRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEK-------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgAFYLVFEY------MDHdlmgLLESGLVHFNENHIKsfMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG 857
Cdd:cd14072    73 --TLYLVMEYasggevFDY----LVAHGRMKEKEARAK--FRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LarlysSEESRPyTNKVITLW----YRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQAnQELAqlELISRIcgsp 933
Cdd:cd14072   145 F-----SNEFTP-GNKLDTFCgsppYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDG-QNLK--ELRERV---- 211
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  934 cpavwpdviklpyfntmkpkkqYRRKLREEFvFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14072   212 ----------------------LRGKYRIPF-YMSTDCENLLKKFLVLNPSKRGTLEQIMK 249
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
705-994 4.21e-26

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 109.04  E-value: 4.21e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEGFPITAIREIKILRqltHQSIINMKEiVTDKEDALdfk 781
Cdd:cd14074     5 YDLEETLGRGHFAVVKLARHVFTGEKVAVKvidKTKLDDVSKAHLFQEVRCMKLVQ---HPNVVRLYE-VIDTQTKL--- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgafYLVFEYMD----HDLMGLLESGLvhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL-NNRGQIKLADF 856
Cdd:cd14074    78 ------YLILELGDggdmYDYIMKHENGL---NEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDF 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSEEsrpytnKVIT----LWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFqanQELAQLELISRICGs 932
Cdd:cd14074   149 GFSNKFQPGE------KLETscgsLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPF---QEANDSETLTMIMD- 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  933 pCPAVWPDviklpyfntmkpkkqyrrklreefvFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14074   219 -CKYTVPA-------------------------HVSPECKDLIRRMLIRDPKKRASLEEIEN 254
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
702-1008 7.36e-26

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: 108.80  E-value: 7.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKV-RLDNEKEGFPITAIREIKILRQLTHQSIINMkeivtdkedaLDF 780
Cdd:cd14117     5 IDDFDIGRPLGKGKFGNVYLAREKQSKFIVALKVLfKSQIEKEGVEHQLRREIEIQSHLRHPNILRL----------YNY 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 KKDKGAFYLVFEYMDHDLM--GLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd14117    75 FHDRKRIYLILEYAPRGELykELQKHG--RFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGW 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYSSEESRPYTNkviTLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANqelAQLELISRIcgspcpaVW 938
Cdd:cd14117   153 SVHAPSLRRRTMCG---TLDYLPPEMIEGRT-HDEKVDLWCIGVLCYELLVGMPPFESA---SHTETYRRI-------VK 218
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  939 PDViKLPyfntmkpkkqyrrklreefVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKMPP 1008
Cdd:cd14117   219 VDL-KFP-------------------PFLSDGSRDLISKLLRYHPSERLPLKGVMEHPWVKANSRRVLPP 268
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
705-996 7.68e-26

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: 109.00  E-value: 7.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPiTAIREIKILRQLTHQSIINMKEIVTDKEDaldfkkdk 784
Cdd:cd14046     8 FEELQVLGKGAFGQVVKVRNKLDGRYYAIKKIKLRSESKNNS-RILREVMLLSRLNHQHVVRYYQAWIERAN-------- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gaFYLVFEYMD-HDLMGLLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA---- 859
Cdd:cd14046    79 --LYIQMEYCEkSTLRDLIDSGL-FQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLAtsnk 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 -----------RLYSSE--ESRPYTNKVITLWYRPPELLLGEER-YTPAIDVWSCGCILGEL-FTKKPIFQANQELAQLE 924
Cdd:cd14046   156 lnvelatqdinKSTSAAlgSSGDLTGNVGTALYVAPEVQSGTKStYNEKVDMYSLGIIFFEMcYPFSTGMERVQILTALR 235
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  925 LISricgspcpavwpdvIKLP-YFNTMKPKKQYRrklreefvfipaaaldLFDYMLALDPSKRCTAEQALQCE 996
Cdd:cd14046   236 SVS--------------IEFPpDFDDNKHSKQAK----------------LIRWLLNHDPAKRPSAQELLKSE 278
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
689-1005 9.20e-26

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: 108.97  E-value: 9.20e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  689 ETKEKDIDWGkrcvDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgfPITAIREIKILRQLTHQSIINMk 768
Cdd:cd06644     2 EHVRRDLDPN----EVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEEE--LEDYMVEIEILATCNHPYIVKL- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  769 eivtdkedaLDFKKDKGAFYLVFEYMD----HDLMGLLESGLvhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNIL 844
Cdd:cd06644    75 ---------LGAFYWDGKLWIMIEFCPggavDAIMLELDRGL---TEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  845 LNNRGQIKLADFGL-ARLYSSEESRpyTNKVITLWYRPPELLLGEER----YTPAIDVWSCGCILGELFTKKPifqANQE 919
Cdd:cd06644   143 LTLDGDIKLADFGVsAKNVKTLQRR--DSFIGTPYWMAPEVVMCETMkdtpYDYKADIWSLGITLIEMAQIEP---PHHE 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  920 LAQLELISRICGSPCPAVwpdviklpyfntMKPKKQyrrklreefvfipaaALDLFDYM-LALD--PSKRCTAEQALQCE 996
Cdd:cd06644   218 LNPMRVLLKIAKSEPPTL------------SQPSKW---------------SMEFRDFLkTALDkhPETRPSAAQLLEHP 270

                  ....*....
gi 145309300  997 FLRDVEPSK 1005
Cdd:cd06644   271 FVSSVTSNR 279
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
707-998 9.54e-26

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


Pssm-ID: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 108.33  E-value: 9.54e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  707 IIGI-IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGF-----PitaiREIKILRQLTHQSIINMKEIvtdkedaldF 780
Cdd:cd14165     4 ILGInLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFvekflP----RELEILARLNHKSIIKTYEI---------F 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 KKDKGAFYLVFEY-MDHDLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd14165    71 ETSDGKVYIVMELgVQGDLLEFIKLRGA-LPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFS 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 R-LYSSEESRPYTNKVI--TLWYRPPELLLGEErYTPAI-DVWSCGCILGELftkkpifqanqelaqlelisrICGSpcp 935
Cdd:cd14165   150 KrCLRDENGRIVLSKTFcgSAAYAAPEVLQGIP-YDPRIyDIWSLGVILYIM---------------------VCGS--- 204
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  936 avwpdvikLPYfNTMKPKKQYRRKLREEFVFIPAAAL-----DLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14165   205 --------MPY-DDSNVKKMLKIQKEHRVRFPRSKNLtseckDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
711-999 9.87e-26

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: 108.09  E-value: 9.87e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPItaIREIKILRQLTHQSIINMKE--IVTDKedaldfkkdkgaFY 788
Cdd:cd06647    15 IGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKELI--INEILVMRENKNPNIVNYLDsyLVGDE------------LW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYmdhdLMGLLESGLVH---FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSE 865
Cdd:cd06647    81 VVMEY----LAGGSLTDVVTetcMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPE 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  866 ESRpYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISricgspcpavwpdviklp 945
Cdd:cd06647   157 QSK-RSTMVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA------------------ 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  946 yfNTMKPKKQYRRKLREEFvfipaaaLDLFDYMLALDPSKRCTAEQALQCEFLR 999
Cdd:cd06647   217 --TNGTPELQNPEKLSAIF-------RDFLNRCLEMDVEKRGSAKELLQHPFLK 261
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
710-999 1.63e-25

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: 107.95  E-value: 1.63e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKegFPITAI-REIKILRQLTHQSIINmkeIVTDKEDALdfkkdKG-AF 787
Cdd:cd06917     8 LVGRGSYGAVYRGYHVKTGRVVALKVLNLDTDD--DDVSDIqKEVALLSQLKLGQPKN---IIKYYGSYL-----KGpSL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDH-DLMGLLESGLVhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEE 866
Cdd:cd06917    78 WIIMDYCEGgSIRTLMRAGPI--AERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNS 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  867 SRPYTnKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFqANQELAQleLISRICGSPCPAVwpdviklpy 946
Cdd:cd06917   156 SKRST-FVGTPYWMAPEVITEGKYYDTKADIWSLGITTYEMATGNPPY-SDVDALR--AVMLIPKSKPPRL--------- 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 145309300  947 fntmkPKKQYRRKLReEFVfipAAALDlfdymlaLDPSKRCTAEQALQCEFLR 999
Cdd:cd06917   223 -----EGNGYSPLLK-EFV---AACLD-------EEPKDRLSADELLKSKWIK 259
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
705-991 1.94e-25

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: 107.58  E-value: 1.94e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKegfpitAIREIKILRQLTHQSIINMKEIVTDKEDALD--FKK 782
Cdd:cd14047     8 FKEIELIGSGGFGQVFKAKHRIDGKTYAIKRVKLNNEK------AEREVKALAKLDHPNIVRYNGCWDGFDYDPEtsSSN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKG-AFYLVFEYMDHDLMGLLESGLVHFNENHIKSFM-----RQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd14047    82 SSRsKTKCLFIQMEFCEKGTLESWIEKRNGEKLDKVLaleifEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDF 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLarLYSSEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTkkpIFQANQELAQlelisricgspcpa 936
Cdd:cd14047   162 GL--VTSLKNDGKRTKSKGTLSYMSPE-QISSQDYGKEVDIYALGLILFELLH---VCDSAFEKSK-------------- 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  937 VWPDViklpyfntmkpkkqYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQ 991
Cdd:cd14047   222 FWTDL--------------RNGILPDIFDKRYKIEKTIIKKMLSKKPEDRPNASE 262
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
711-909 2.56e-25

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: 107.47  E-value: 2.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKAR----DKDTGEMVALKKVRLD---NEKEGFPitaiREIKILRQLTHQSIINMKEIVTdkedaldfKKD 783
Cdd:cd05038    12 LGEGHFGSVELCRydplGDNTGEQVAVKSLQPSgeeQHMSDFK----REIEILRTLDHEYIVKYKGVCE--------SPG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYmdhdlmglLESG-LVHFNENH--------IKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLA 854
Cdd:cd05038    80 RRSLRLIMEY--------LPSGsLRDYLQRHrdqidlkrLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKIS 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  855 DFGLARLYSSEESRPYTNK---VITLWYRPPEllLGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05038   152 DFGLAKVLPEDKEYYYVKEpgeSPIFWYAPEC--LRESRFSSASDVWSFGVTLYELFT 207
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
711-1003 3.37e-25

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: 107.03  E-value: 3.37e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgfPITAIREIKIlrqltHQSIINMKEIVTDKEDALDFKKDKGAFYLV 790
Cdd:cd13985     8 LGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQ--LRVAIKEIEI-----MKRLCGHPNIVQYYDSAILSSEGRKEVLLL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHDLMGLLESGL-VHFNENHIKSFMRQLMEGLDYCHKKN--FLHRDIKCSNILLNNRGQIKLADFGLArlysSEES 867
Cdd:cd13985    81 MEYCPGSLVDILEKSPpSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSA----TTEH 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  868 RPYT------------NKVITLWYRPPEL--LLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELaqlelisricgsp 933
Cdd:cd13985   157 YPLEraeevniieeeiQKNTTPMYRAPEMidLYSKKPIGEKADIWALGCLLYKLCFFKLPFDESSKL------------- 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  934 cpAVWPDVIKLPYFNTmkpkkqYRRKLReefvfipaaalDLFDYMLALDPSKRCTAEQALQceFLRDVEP 1003
Cdd:cd13985   224 --AIVAGKYSIPEQPR------YSPELH-----------DLIRHMLTPDPAERPDIFQVIN--IITKDTK 272
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
711-989 3.74e-25

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


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 106.41  E-value: 3.74e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNekegfpITAIREIKILRQlthQSIINMKEIVTDKEDALDFKKDKGAF-YL 789
Cdd:cd05611     4 ISKGAFGSVYLAKKRSTGDYFAIKVLKKSD------MIAKNQVTNVKA---ERAIMMIQGESPYVAKLYYSFQSKDYlYL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLysSEESRP 869
Cdd:cd05611    75 VMEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRN--GLEKRH 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  870 YTNKVITLWYRPPELLLGEERyTPAIDVWSCGCILGELFTKKPIFQANQELAQLELI-SRICGspcpavWPDviklpyfn 948
Cdd:cd05611   153 NKKFVGTPDYLAPETILGVGD-DKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNIlSRRIN------WPE-------- 217
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 145309300  949 tmkpkkqyrrklrEEFVFIPAAALDLFDYMLALDPSKRCTA 989
Cdd:cd05611   218 -------------EVKEFCSPEAVDLINRLLCMDPAKRLGA 245
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
708-1000 4.47e-25

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: 107.39  E-value: 4.47e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  708 IGIIGEGTYGQVYKARDKDTGEMVALKKV--RLDnekegfpitAIREIKILRQLT-HQSIINMKEIvtdkedaldfKKDK 784
Cdd:cd14092    11 EEALGDGSFSVCRKCVHKKTGQEFAVKIVsrRLD---------TSREVQLLRLCQgHPNIVKLHEV----------FQDE 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVFEYmdhdLMG--LLE--SGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL---NNRGQIKLADFG 857
Cdd:cd14092    72 LHTYLVMEL----LRGgeLLEriRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFG 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARLysSEESRPYTNKVITLWYRPPELL---LGEERYTPAIDVWSCGCILGELFTKKPIFQA-NQELAQLELISRICgsp 933
Cdd:cd14092   148 FARL--KPENQPLKTPCFTLPYAAPEVLkqaLSTQGYDESCDLWSLGVILYTMLSGQVPFQSpSRNESAAEIMKRIK--- 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  934 cpavwpdviklpyfntmkpkkqyrrklREEFVF-------IPAAALDLFDYMLALDPSKRCTAEQALQCEFLRD 1000
Cdd:cd14092   223 ---------------------------SGDFSFdgeewknVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQG 269
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
705-994 5.50e-25

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: 105.80  E-value: 5.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEGFPitaiREIKILRQLTHQSIINMKEIV-TDKEdaldf 780
Cdd:cd14185     2 YEIGRTIGDGNFAVVKECRHWNENQEYAMKiidKSKLKGKEDMIE----SEILIIKSLSHPNIVKLFEVYeTEKE----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdkgaFYLVFEYMDH-DLM-GLLESglVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ----IKLA 854
Cdd:cd14185    73 ------IYLILEYVRGgDLFdAIIES--VKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDksttLKLA 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  855 DFGLARLYsseeSRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQAnQELAQLELIsricgspc 934
Cdd:cd14185   145 DFGLAKYV----TGPIFTVCGTPTYVAPE-ILSEKGYGLEVDMWAAGVILYILLCGFPPFRS-PERDQEELF-------- 210
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  935 pavwpDVIKLPYFNTMKPKKQYrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14185   211 -----QIIQLGHYEFLPPYWDN----------ISEAAKDLISRLLVVDPEKRYTAKQVLQ 255
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
710-939 9.13e-25

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: 105.51  E-value: 9.13e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNE--KEGFPITAIR-EIKILRQLTHQSIINMKEIVTD-KEDALDFkkdkg 785
Cdd:cd06652     9 LLGQGAFGRVYLCYDADTGRELAVKQVQFDPEspETSKEVNALEcEIQLLKNLLHERIVQYYGCLRDpQERTLSI----- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 afylvfeYMDHDLMGLLESGLVHF---NENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA-RL 861
Cdd:cd06652    84 -------FMEYMPGGSIKDQLKSYgalTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASkRL 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  862 YSSEESRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFqanQELAQLELISRICGSPCPAVWP 939
Cdd:cd06652   157 QTICLSGTGMKSVTgTPYWMSPEVISGEG-YGRKADIWSVGCTVVEMLTEKPPW---AEFEAMAAIFKIATQPTNPQLP 231
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
704-994 1.16e-24

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: 104.78  E-value: 1.16e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALK-----KVRLD---NEKEGFPITAirEIKILRQL---THQSIINMkeivt 772
Cdd:cd14004     1 DYTILKEMGEGAYGQVNLAIYKSKGKEVVIKfifkeRILVDtwvRDRKLGTVPL--EIHILDTLnkrSHPNIVKL----- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  773 dkedaLDFKKDKGAFYLVFEymDH----DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR 848
Cdd:cd14004    74 -----LDFFEDDEFYYLVME--KHgsgmDLFDFIERK-PNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGN 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  849 GQIKLADFGLARLYsseESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELftkkpIFQANqelaqlelisr 928
Cdd:cd14004   146 GTIKLIDFGSAAYI---KSGPFDTFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTL-----VFKEN----------- 206
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  929 icgspcpavwpdviklPYFN---TMKPKKQYRRKLREEfvfipaaALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14004   207 ----------------PFYNieeILEADLRIPYAVSED-------LIDLISRMLNRDVGDRPTIEELLT 252
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
711-917 1.18e-24

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: 106.67  E-value: 1.18e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKV----RLDNEKEGfpiTAIREIKILRQLTHQSIINMKEIVTDKEDAldfkkdkga 786
Cdd:cd06635    33 IGHGSFGAVYFARDVRTSEVVAIKKMsysgKQSNEKWQ---DIIKEVKFLQRIKHPNSIEYKGCYLREHTA--------- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 fYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSsee 866
Cdd:cd06635   101 -WLVMEYCLGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIAS--- 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  867 srPYTNKVITLWYRPPELLLG--EERYTPAIDVWSCGCILGELFTKK-PIFQAN 917
Cdd:cd06635   177 --PANSFVGTPYWMAPEVILAmdEGQYDGKVDVWSLGITCIELAERKpPLFNMN 228
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
711-999 1.35e-24

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


Pssm-ID: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 104.83  E-value: 1.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKvrLDNEKEGFPITAIREIKILRQLTHQSIINM--KEIVTDKedaldfkkdkgaFY 788
Cdd:cd06648    15 IGEGSTGIVCIATDKSTGRQVAVKK--MDLRKQQRRELLFNEVVIMRDYQHPNIVEMysSYLVGDE------------LW 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDHdlmGLLESGLVH--FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEE 866
Cdd:cd06648    81 VVMEFLEG---GALTDIVTHtrMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQVSKEV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  867 SRpYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPifqanqelaqlelisricgspcpavwpdviklPY 946
Cdd:cd06648   158 PR-RKSLVGTPYWMAPE-VISRLPYGTEVDIWSLGIMVIEMVDGEP--------------------------------PY 203
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  947 FNtmKPKKQYRRKLREE-------FVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLR 999
Cdd:cd06648   204 FN--EPPLQAMKRIRDNeppklknLHKVSPRLRSFLDRMLVRDPAQRATAAELLNHPFLA 261
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
710-912 1.57e-24

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: 105.09  E-value: 1.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRL-----DNEKEGFPITAIREIKILRQLTHQSIINMKEIvtdkedaldFKKDK 784
Cdd:cd13990     7 LLGKGGFSEVYKAFDLVEQRYVACKIHQLnkdwsEEKKQNYIKHALREYEIHKSLDHPRIVKLYDV---------FEIDT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVFEYMD-HDLMGLL-ESGLVhfNENHIKSFMRQLMEGLDYC--HKKNFLHRDIKCSNILLNNR---GQIKLADFG 857
Cdd:cd13990    78 DSFCTVLEYCDgNDLDFYLkQHKSI--PEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLHSGnvsGEIKITDFG 155
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  858 LARLySSEESRPYTNKVI------TLWYRPPE-LLLGEE--RYTPAIDVWSCGCILGE-LFTKKP 912
Cdd:cd13990   156 LSKI-MDDESYNSDGMELtsqgagTYWYLPPEcFVVGKTppKISSKVDVWSVGVIFYQmLYGRKP 219
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
703-917 3.22e-24

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: 103.40  E-value: 3.22e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKV-RLDNEKEGFPITAIREIKILRQLTHQSIINMkeivtdkedaLDFK 781
Cdd:cd14186     1 EDFKVLNLLGKGSFACVYRARSLHTGLEVAIKMIdKKAMQKAGMVQRVRNEVEIHCQLKHPSILEL----------YNYF 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDKGAFYLVFEyMDHDlmGLLESGLVH----FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG 857
Cdd:cd14186    71 EDSNYVYLVLE-MCHN--GEMSRYLKNrkkpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFG 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARLYSSEESRPYTnKVITLWYRPPELLLGEERYTPAiDVWSCGCILGELFTKKPIFQAN 917
Cdd:cd14186   148 LATQLKMPHEKHFT-MCGTPNYISPEIATRSAHGLES-DVWSLGCMFYTLLVGRPPFDTD 205
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
705-1011 3.33e-24

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: 106.65  E-value: 3.33e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldneKegfpitaiREIKILRQLTHqsIINMKEIVT-DKEDAL----- 778
Cdd:cd05600    13 FQILTQVGQGGYGSVFLARKKDTGEICALKIMK----K--------KVLFKLNEVNH--VLTERDILTtTNSPWLvklly 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 DFKkDKGAFYLVFEYM-DHDLMGLL-ESGLVHfnENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd05600    79 AFQ-DPENVYLAMEYVpGGDFRTLLnNSGILS--EEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDF 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLAR---------------------------------LYSS--EESRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSC 900
Cdd:cd05600   156 GLASgtlspkkiesmkirleevkntafleltakerrnIYRAmrKEDQNYANSVVgSPDYMAPEVLRGEG-YDLTVDYWSL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  901 GCILGELFTKKPIFqanqelaqlelisriCGSPCPAVWpdvIKLPYFNTM--KPKKQyrrKLREEFvFIPAAALDLFDYM 978
Cdd:cd05600   235 GCILFECLVGFPPF---------------SGSTPNETW---ANLYHWKKTlqRPVYT---DPDLEF-NLSDEAWDLITKL 292
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|..
gi 145309300  979 LAlDPSKR-CTAEQALQCEFLRDV------EPSKmPP--PDL 1011
Cdd:cd05600   293 IT-DPQDRlQSPEQIKNHPFFKNIdwdrlrEGSK-PPfiPEL 332
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
698-998 3.36e-24

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


Pssm-ID: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 105.48  E-value: 3.36e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  698 GKRCVDKFDIIGIIGEGTYGQVYKARDKDTGE-MVALKKVR-LDNEKEGfpitAIREIKILRQLTHQSIINmKEIVTDKE 775
Cdd:cd14214     8 GDWLQERYEIVGDLGEGTFGKVVECLDHARGKsQVALKIIRnVGKYREA----ARLEINVLKKIKEKDKEN-KFLCVLMS 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  776 DALDFKkdkGAFYLVFEYMDHDLMGLL-ESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN------- 847
Cdd:cd14214    83 DWFNFH---GHMCIAFELLGKNTFEFLkENNFQPYPLPHIRHMAYQLCHALKFLHENQLTHTDLKPENILFVNsefdtly 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  848 ------------RGQIKLADFGLARLysseESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQ 915
Cdd:cd14214   160 nesksceeksvkNTSIRVADFGSATF----DHEHHTTIVATRHYRPPEVIL-ELGWAQPCDVWSLGCILFEYYRGFTLFQ 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  916 ANQELAQLELISRICGsPCPA-VWPDVIKLPYF------------------NTMKPKKQYRRKLREEFVFIpaaaLDLFD 976
Cdd:cd14214   235 THENREHLVMMEKILG-PIPShMIHRTRKQKYFykgslvwdenssdgryvsENCKPLMSYMLGDSLEHTQL----FDLLR 309
                         330       340
                  ....*....|....*....|..
gi 145309300  977 YMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14214   310 RMLEFDPALRITLKEALLHPFF 331
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
705-998 4.04e-24

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: 103.29  E-value: 4.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEivtdkedalDFKKDK 784
Cdd:cd08223     2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKE---------SFEGED 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVfeymdhdlMGLLESGLVH----------FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLA 854
Cdd:cd08223    73 GFLYIV--------MGFCEGGDLYtrlkeqkgvlLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVG 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  855 DFGLARLYSSEESRPyTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAqleLISRICGSPC 934
Cdd:cd08223   145 DLGIARVLESSSDMA-TTLIGTPYYMSPE-LFSNKPYNHKSDVWALGCCVYEMATLKHAFNAKDMNS---LVYKILEGKL 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  935 PAvwpdvikLPyfntmkpkKQYRRKLreefvfipaaaLDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd08223   220 PP-------MP--------KQYSPEL-----------GELIKAMLHQDPEKRPSVKRILRQPYI 257
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
703-936 4.51e-24

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: 103.58  E-value: 4.51e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLD-NEKEGFPItaIREIKILRQLTHQSIInmkeivtdkedalDFK 781
Cdd:cd06605     1 DDLEYLGELGEGNGGVVSKVRHRPSGQIMAVKVIRLEiDEALQKQI--LRELDVLHKCNSPYIV-------------GFY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 K---DKGAFYLVFEYMDHdlmGLLESGL--VHFNENHIKSFM-RQLMEGLDYCHKK-NFLHRDIKCSNILLNNRGQIKLA 854
Cdd:cd06605    66 GafySEGDISICMEYMDG---GSLDKILkeVGRIPERILGKIaVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLC 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  855 DFGLarlySSE--ESRPYTNkVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKK---PIFQANQELAQLELISRI 929
Cdd:cd06605   143 DFGV----SGQlvDSLAKTF-VGTRSYMAPERISGGK-YTVKSDIWSLGLSLVELATGRfpyPPPNAKPSMMIFELLSYI 216

                  ....*..
gi 145309300  930 CGSPCPA 936
Cdd:cd06605   217 VDEPPPL 223
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
703-1005 6.04e-24

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 103.66  E-value: 6.04e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgFPITAIREIKILRQLTHQSIINMKEIVTDKEDaldfkk 782
Cdd:cd06621     1 DKIVELSSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPD-VQKQILRELEINKSCASPYIVKYYGAFLDEQD------ 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkGAFYLVFEYMD----HDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd06621    74 --SSIGIAMEYCEggslDSIYKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYSSEESRPYTNkviTLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQAN--QELAQLELISRICGSPCPa 936
Cdd:cd06621   152 SGELVNSLAGTFTG---TSYYMAPERIQGGP-YSITSDVWSLGLTLLEVAQNRFPFPPEgePPLGPIELLSYIVNMPNP- 226
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  937 vwpdviklpyfnTMKPKKQYRRKLREEFVfipaaalDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSK 1005
Cdd:cd06621   227 ------------ELKDEPENGIKWSESFK-------DFIEKCLEKDGTRRPGPWQMLAHPWIKAQEKKK 276
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
710-988 7.03e-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: 103.21  E-value: 7.03e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQV---YKARDKDTGEMVALKKVRLdNEKEGF------------------PITAI-REIKILRQLTHQSIINM 767
Cdd:cd14118     1 EIGKGSYGIVklaYNEEDNTLYAMKILSKKKL-LKQAGFfrrppprrkpgalgkpldPLDRVyREIAILKKLDHPNVVKL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  768 KEIVTD-KEDALdfkkdkgafYLVFEymdhdlmgLLESGLVH-------FNENHIKSFMRQLMEGLDYCHKKNFLHRDIK 839
Cdd:cd14118    80 VEVLDDpNEDNL---------YMVFE--------LVDKGAVMevptdnpLSEETARSYFRDIVLGIEYLHYQKIIHRDIK 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  840 CSNILLNNRGQIKLADFGLARLYSSEESRpYTNKVITLWYRPPELLLGEERYTP--AIDVWSCGCILGELFTKKPIFQAN 917
Cdd:cd14118   143 PSNLLLGDDGHVKIADFGVSNEFEGDDAL-LSSTAGTPAFMAPEALSESRKKFSgkALDIWAMGVTLYCFVFGRCPFEDD 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  918 QELAQLELISRicgspcpavwpDVIKLPyfntmkpkkqyrrklrEEFVFIPAAAlDLFDYMLALDPSKRCT 988
Cdd:cd14118   222 HILGLHEKIKT-----------DPVVFP----------------DDPVVSEQLK-DLILRMLDKNPSERIT 264
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
710-940 8.48e-24

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: 102.80  E-value: 8.48e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLD--NEKEGFPITAIR-EIKILRQLTHQSIINMKEIVTDKEDaldfKKdkga 786
Cdd:cd06653     9 LLGRGAFGEVYLCYDADTGRELAVKQVPFDpdSQETSKEVNALEcEIQLLKNLRHDRIVQYYGCLRDPEE----KK---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDHdlmGLLESGLVHF---NENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA-RLY 862
Cdd:cd06653    81 LSIFVEYMPG---GSVKDQLKAYgalTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRIQ 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  863 SSEESRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQlelISRICGSPCPAVWPD 940
Cdd:cd06653   158 TICMSGTGIKSVTgTPYWMSPEVISGEG-YGRKADVWSVACTVVEMLTEKPPWAEYEAMAA---IFKIATQPTKPQLPD 232
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
710-923 8.80e-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: 102.78  E-value: 8.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEM-VALKKVRLDNEKEGFPITAiREIKILRQLTHQSIINMkeivtdkedaLDFKKDKGAFY 788
Cdd:cd14202     9 LIGHGAFAVVFKGRHKEKHDLeVAVKCINKKNLAKSQTLLG-KEIKILKELKHENIVAL----------YDFQEIANSVY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDH-DLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG---------QIKLADFGL 858
Cdd:cd14202    78 LVMEYCNGgDLADYLHT-MRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSYSGgrksnpnniRIKIADFGF 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  859 ARLYSSeesrpyTNKVITL----WYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQAN--QELAQL 923
Cdd:cd14202   157 ARYLQN------NMMAATLcgspMYMAPEVIM-SQHYDAKADLWSIGTIIYQCLTGKAPFQASspQDLRLF 220
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
708-998 9.54e-24

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: 102.12  E-value: 9.54e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  708 IGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMkeivtdkedaLDFKKDKGAF 787
Cdd:cd08221     5 VRVLGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITY----------YNHFLDGESL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMD----HDLMGLLESGLvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYS 863
Cdd:cd08221    75 FIEMEYCNggnlHDKIAQQKNQL--FPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLD 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SeESRPYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQELaqlelisRICGSPCPAVWPDVIk 943
Cdd:cd08221   153 S-ESSMAESIVGTPYYMSPELVQG-VKYNFKSDIWAVGCVLYELLTLKRTFDATNPL-------RLAVKIVQGEYEDID- 222
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  944 lpyfntmkpkKQYRRKLREefvfipaaaldLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd08221   223 ----------EQYSEEIIQ-----------LVHDCLHQDPEDRPTAEELLERPLL 256
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
711-923 1.69e-23

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: 101.29  E-value: 1.69e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKD-TGEMVALKKVRLDNEKEGFPITAiREIKILRQLTHQSIINMkeivtdkedaLDFKKDKGAFYL 789
Cdd:cd14120     1 IGHGAFAVVFKGRHRKkPDLPVAIKCITKKNLSKSQNLLG-KEIKILKELSHENVVAL----------LDCQETSSSVYL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG---------QIKLADFGLA 859
Cdd:cd14120    70 VMEYCNGgDLADYLQAKGT-LSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIADFGFA 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RLYSSEEsrpytnKVITL----WYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQAN--QELAQL 923
Cdd:cd14120   149 RFLQDGM------MAATLcgspMYMAPEVIMSLQ-YDAKADLWSIGTIVYQCLTGKAPFQAQtpQELKAF 211
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
705-935 1.87e-23

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


Pssm-ID: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 103.30  E-value: 1.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKvrLDNEKEGFPITAIrEIKILRQLTHQSiinmkeivTDKED---ALDFK 781
Cdd:cd14211     1 YEVLEFLGRGTFGQVVKCWKRGTNEIVAIKI--LKNHPSYARQGQI-EVSILSRLSQEN--------ADEFNfvrAYECF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDKGAFYLVFEYMDHDLMGLL-ESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG----QIKLADF 856
Cdd:cd14211    70 QHKNHTCLVFEMLEQNLYDFLkQNKFSPLPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVrqpyRVKVIDF 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  857 GLARLYSSEESRPYTNkviTLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCP 935
Cdd:cd14211   150 GSASHVSKAVCSTYLQ---SRYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGSSEYDQIRYISQTQGLPAE 224
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
711-917 2.15e-23

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: 102.41  E-value: 2.15e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKV----RLDNEKEGfpiTAIREIKILRQLTHQSIINMKEIVTDKEDAldfkkdkga 786
Cdd:cd06634    23 IGHGSFGAVYFARDVRNNEVVAIKKMsysgKQSNEKWQ---DIIKEVKFLQKLRHPNTIEYRGCYLREHTA--------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 fYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSsee 866
Cdd:cd06634    91 -WLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMA--- 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  867 srPYTNKVITLWYRPPELLLG--EERYTPAIDVWSCGCILGELFTKK-PIFQAN 917
Cdd:cd06634   167 --PANSFVGTPYWMAPEVILAmdEGQYDGKVDVWSLGITCIELAERKpPLFNMN 218
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
703-937 3.53e-23

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: 101.26  E-value: 3.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKV--RLDNEKEGFPItairEIKILRQLTHQSIINMKeivtdkeDALDF 780
Cdd:cd06643     5 DFWEIVGELGDGAFGKVYKAQNKETGILAAAKVIdtKSEEELEDYMV----EIDILASCDHPNIVKLL-------DAFYY 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 KKDkgaFYLVFEYMD----HDLMGLLESGLVhfnENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd06643    74 ENN---LWILIEFCAggavDAVMLELERPLT---EPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADF 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLarlySSEESRPYTNK---VITLWYRPPELLLGEER----YTPAIDVWSCGCILGELFTKKPifqANQELAQLELISRI 929
Cdd:cd06643   148 GV----SAKNTRTLQRRdsfIGTPYWMAPEVVMCETSkdrpYDYKADVWSLGVTLIEMAQIEP---PHHELNPMRVLLKI 220

                  ....*...
gi 145309300  930 CGSPCPAV 937
Cdd:cd06643   221 AKSEPPTL 228
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
703-914 4.28e-23

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: 101.92  E-value: 4.28e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDN--EKEgfPITAIR-EIKILRQLTHQSIINMKEIVTDKEDald 779
Cdd:cd05599     1 EDFEPLKVIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEmlEKE--QVAHVRaERDILAEADNPWVVKLYYSFQDEEN--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkkdkgaFYLVFEYMDH-DLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd05599    76 -------LYLIMEFLPGgDMMTLLMKKDT-LTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGL 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  859 ------ARL-YSSeesrpytnkVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIF 914
Cdd:cd05599   148 ctglkkSHLaYST---------VGTPDYIAPEVFL-QKGYGKECDWWSLGVIMYEMLIGYPPF 200
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
711-909 7.10e-23

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: 100.48  E-value: 7.10e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKAR----DKDTGEMVALKKVRLDNEK--EGFPitaiREIKILRQLTHQSIINMKEIVtdkedaldFKKDK 784
Cdd:cd14205    12 LGKGNFGSVEMCRydplQDNTGEVVAVKKLQHSTEEhlRDFE----REIEILKSLQHDNIVKYKGVC--------YSAGR 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYs 863
Cdd:cd14205    80 RNLRLIMEYLPYgSLRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVL- 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEESRPYTNK----VITLWYRPPELLlgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd14205   159 PQDKEYYKVKepgeSPIFWYAPESLT--ESKFSVASDVWSFGVVLYELFT 206
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
711-909 7.19e-23

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: 100.39  E-value: 7.19e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQV----YKARDKDTGEMVALKKvrLDNEKEGFPITAI-REIKILRQLTHQSIINMKEIVTDKEDAldfkkdkg 785
Cdd:cd05079    12 LGEGHFGKVelcrYDPEGDNTGEQVAVKS--LKPESGGNHIADLkKEIEILRNLYHENIVKYKGICTEDGGN-------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 AFYLVFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSS 864
Cdd:cd05079    82 GIKLIMEFLPSgSLKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIET 161
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 145309300  865 EESRpYTNK----VITLWYrPPELLLGEERYTpAIDVWSCGCILGELFT 909
Cdd:cd05079   162 DKEY-YTVKddldSPVFWY-APECLIQSKFYI-ASDVWSFGVTLYELLT 207
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
704-994 7.57e-23

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: 99.62  E-value: 7.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIR----EIKILRQ---LTHQSIINMkeivtdked 776
Cdd:cd14005     1 QYEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRVTEWAMINGPVpvplEIALLLKaskPGVPGVIRL--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 aLDFKKDKGAFYLVFEYMD--HDLMGLL-ESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLN-NRGQIK 852
Cdd:cd14005    72 -LDWYERPDGFLLIMERPEpcQDLFDFItERG--ALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVK 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFGLARLYsseESRPYTNKVITLWYRPPELLLgEERY--TPAIdVWSCGCILGELftkkpifqanqelaqlelisrIC 930
Cdd:cd14005   149 LIDFGCGALL---KDSVYTDFDGTRVYSPPEWIR-HGRYhgRPAT-VWSLGILLYDM---------------------LC 202
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  931 GspcpavwpdviKLPYFNT---MKPKKQYRRKLREEfvfipaaALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14005   203 G-----------DIPFENDeqiLRGNVLFRPRLSKE-------CCDLISRCLQFDPSKRPSLEQILS 251
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
703-994 7.74e-23

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


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 99.75  E-value: 7.74e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEgfpiTAIREIKILRQLTHQSIINMKEIVtdkedald 779
Cdd:cd14083     3 DKYEFKEVLGTGAFSEVVLAEDKATGKLVAIKcidKKALKGKED----SLENEIAVLRKIKHPNIVQLLDIY-------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkKDKGAFYLVF------EYMDHdlmgLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNIL---LNNRGQ 850
Cdd:cd14083    71 --ESKSHLYLVMelvtggELFDR----IVEKG--SYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSK 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  851 IKLADFGLARLyssEESRPYTNKVITLWYRPPELLlGEERYTPAIDVWSCGcilgelftkkpifqanqelaqleLISRI- 929
Cdd:cd14083   143 IMISDFGLSKM---EDSGVMSTACGTPGYVAPEVL-AQKPYGKAVDCWSIG-----------------------VISYIl 195
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  930 -CGSPcpavwpdviklPYFNTMKPKkQYRRKLREEFVF-------IPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14083   196 lCGYP-----------PFYDENDSK-LFAQILKAEYEFdspywddISDSAKDFIRHLMEKDPNKRYTCEQALE 256
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
704-892 1.03e-22

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: 99.45  E-value: 1.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPitaiREIKILRQLthQSIINMKEIvtdkedaLDFKKD 783
Cdd:cd14016     1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIKIEKKDSKHPQLE----YEAKVYKLL--QGGPGIPRL-------YWFGQE 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL---NNRGQIKLADFGLAR 860
Cdd:cd14016    68 GDYNVMVMDLLGPSLEDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMglgKNSNKVYLIDFGLAK 147
                         170       180       190
                  ....*....|....*....|....*....|..
gi 145309300  861 LYSSeesrPYTNKVITlwYRPPELLLGEERYT 892
Cdd:cd14016   148 KYRD----PRTGKHIP--YREGKSLTGTARYA 173
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
711-993 2.84e-22

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: 97.84  E-value: 2.84e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKvrLDNEKEGFPITAI-REIKILRQLTHQSIINMKEIV-TDKEdaldfkkdkgaFY 788
Cdd:cd14078    11 IGSGGFAKVKLATHILTGEKVAIKI--MDKKALGDDLPRVkTEIEALKNLSHQHICRLYHVIeTDNK-----------IF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDHdlmGLLESGLV---HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL-ARLYSS 864
Cdd:cd14078    78 MVLEYCPG---GELFDYIVakdRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLcAKPKGG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  865 EESRPYTNkVITLWYRPPELLLGEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGSpcpavwpdvikL 944
Cdd:cd14078   155 MDHHLETC-CGSPAYAAPELIQGKPYIGSEADVWSMGVLLYAL---------------------LCGF-----------L 201
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 145309300  945 PY--FNTMKPKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQAL 993
Cdd:cd14078   202 PFddDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQVDPKKRITVKELL 252
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
711-1008 3.16e-22

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: 99.03  E-value: 3.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPItaIREIKILRQLTHQSIINMkeivtdkedaLDFKKDKGAFYLV 790
Cdd:cd06654    28 IGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKELI--INEILVMRENKNPNIVNY----------LDSYLVGDELWVV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHdlmGLLESGLVH--FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESR 868
Cdd:cd06654    96 MEYLAG---GSLTDVVTEtcMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSK 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  869 PYTnKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISricgspcpavwpdviklpyfN 948
Cdd:cd06654   173 RST-MVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMIEGEPPYLNENPLRALYLIA--------------------T 230
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  949 TMKPKKQYRRKLREEFvfipaaaLDLFDYMLALDPSKRCTAEQALQCEFLRDVEP-SKMPP 1008
Cdd:cd06654   231 NGTPELQNPEKLSAIF-------RDFLNRCLEMDVEKRGSAKELLQHQFLKIAKPlSSLTP 284
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
708-1009 4.35e-22

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 99.51  E-value: 4.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  708 IGIIGEGTYGQVYKARDKDTGEMVALKkVRLDNEKEGFPITAIREIKILRQLTHQSIINMKeivtdkedalDFKKDKGAF 787
Cdd:PLN00034   79 VNRIGSGAGGTVYKVIHRPTGRLYALK-VIYGNHEDTVRRQICREIEILRDVNHPNVVKCH----------DMFDHNGEI 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDHdlmGLLESGLVHfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYsSEES 867
Cdd:PLN00034  148 QVLLEFMDG---GSLEGTHIA-DEQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRIL-AQTM 222
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  868 RPYTNKVITLWYRPPELL---LGEERYTP-AIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWPDVik 943
Cdd:PLN00034  223 DPCNSSVGTIAYMSPERIntdLNHGAYDGyAGDIWSLGVSILEFYLGRFPFGVGRQGDWASLMCAICMSQPPEAPATA-- 300
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  944 lpyfntmkpKKQYRrklreefvfipaaalDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSK----------MPPP 1009
Cdd:PLN00034  301 ---------SREFR---------------HFISCCLQREPAKRWSAMQLLQHPFILRAQPGQgqggpnlhqlLPPP 352
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
703-994 5.19e-22

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: 97.97  E-value: 5.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPItairEIKILRQLTHQSIINMKEIVTDKEDaldfkk 782
Cdd:cd14085     3 DFFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDKKIVRT----EIGVLLRLSHPNIIKLKEIFETPTE------ 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgaFYLVFEYMDHDLM--GLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ---IKLADFG 857
Cdd:cd14085    73 ----ISLVLELVTGGELfdRIVEKG--YYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARLYSSEesrpYTNKVI--TLWYRPPELLLGEErYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGSPcp 935
Cdd:cd14085   147 LSKIVDQQ----VTMKTVcgTPGYCAPEILRGCA-YGPEVDMWSVGVITYIL---------------------LCGFE-- 198
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  936 avwpdviklPYFNTMKPKKQYRRKLREEFVFI-------PAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14085   199 ---------PFYDERGDQYMFKRILNCDYDFVspwwddvSLNAKDLVKKLIVLDPKKRLTTQQALQ 255
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
711-1012 7.51e-22

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: 97.21  E-value: 7.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKV---RLdnEKEGFPITAIREIKILRQLTHQSIINMkeivtdkedALDFKKdKGAF 787
Cdd:cd05577     1 LGRGGFGEVCACQVKATGKMYACKKLdkkRI--KKKKGETMALNEKIILEKVSSPFIVSL---------AYAFET-KDKL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDH-DL-MGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSse 865
Cdd:cd05577    69 CLVLTLMNGgDLkYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFK-- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  866 ESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRIcgspcpaVWPDVIKLP 945
Cdd:cd05577   147 GGKKIKGRVGTHGYMAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRR-------TLEMAVEYP 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  946 YFNTmkpkkqyrrklreefvfipAAALDLFDYMLALDPSKRC-----TAEQALQCEFLRD-----VEPSKMPPPDLP 1012
Cdd:cd05577   220 DSFS-------------------PEARSLCEGLLQKDPERRLgcrggSADEVKEHPFFRSlnwqrLEAGMLEPPFVP 277
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
703-999 8.32e-22

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 96.91  E-value: 8.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLD-------NEKEGFPITAIREIKILRQLT-HQSIINMKeivtdk 774
Cdd:cd14182     3 EKYEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITgggsfspEEVQELREATLKEIDILRKVSgHPNIIQLK------ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  775 edalDFKKDKGAFYLVFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKL 853
Cdd:cd14182    77 ----DTYETNTFFFLVFDLMKKgELFDYLTEK-VTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  854 ADFGLA-RLYSSEESRPYTNkviTLWYRPPELLL-----GEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELI- 926
Cdd:cd14182   152 TDFGFScQLDPGEKLREVCG---TPGYLAPEIIEcsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIm 228
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  927 --SRICGSPcpaVWPDviklpYFNTMKpkkqyrrklreefvfipaaalDLFDYMLALDPSKRCTAEQALQCEFLR 999
Cdd:cd14182   229 sgNYQFGSP---EWDD-----RSDTVK---------------------DLISRFLVVQPQKRYTAEEALAHPFFQ 274
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
705-1004 8.42e-22

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


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 97.37  E-value: 8.42e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITaiREIKILRQLTHQSIINMKeivtdkedalDFKKDK 784
Cdd:cd14166     5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLE--NEIAVLKRIKHENIVTLE----------DIYEST 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVFEYMDHDLM--GLLESGLvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL---NNRGQIKLADFGLA 859
Cdd:cd14166    73 THYYLVMQLVSGGELfdRILERGV--YTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RLyssEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAVWP 939
Cdd:cd14166   151 KM---EQNGIMSTACGTPGYVAPE-VLAQKPYSKAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGYYEFESPFWD 226
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  940 DviklpyfntmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCEFL-------RDVEPS 1004
Cdd:cd14166   227 D--------------------------ISESAKDFIRHLLEKNPSKRYTCEKALSHPWIigntalhRDIYPS 272
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
708-910 8.97e-22

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: 97.28  E-value: 8.97e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  708 IGIIGEGTYGQV----YKARDKDTGEMVALKKVRLDN---EKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDAldf 780
Cdd:cd05080     9 IRDLGEGHFGKVslycYDPTNDGTGEMVAVKALKADCgpqHRSGW----KQEIDILKTLYHENIVKYKGCCSEQGGK--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdkgAFYLVFEYMDhdlMGLLESGLVHFNEN--HIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd05080    82 -----SLQLIMEYVP---LGSLRDYLPKHSIGlaQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGL 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  859 ARLYSSEE-----SRPYTNKVitLWYRPPelLLGEERYTPAIDVWSCGCILGELFTK 910
Cdd:cd05080   154 AKAVPEGHeyyrvREDGDSPV--FWYAPE--CLKEYKFYYASDVWSFGVTLYELLTH 206
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
711-904 9.31e-22

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 96.60  E-value: 9.31e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVrldnEKEGFPITAI-----REIKILRQLTHQSIINMKEIVTDKEdaldfkkdkG 785
Cdd:cd14163     8 IGEGTYSKVKEAFSKKHQRKVAIKII----DKSGGPEEFIqrflpRELQIVERLDHKNIIHVYEMLESAD---------G 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 AFYLVFEYM-DHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRgQIKLADFGLARLY-- 862
Cdd:cd14163    75 KIYLVMELAeDGDVFDCVLHG-GPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-TLKLTDFGFAKQLpk 152
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 145309300  863 -SSEESRPYTNKVItlwYRPPELLLGEERYTPAIDVWSCGCIL 904
Cdd:cd14163   153 gGRELSQTFCGSTA---YAAPEVLQGVPHDSRKGDIWSMGVVL 192
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
703-994 1.03e-21

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: 96.64  E-value: 1.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRlDNEKEGFPITAIREIKILRQLTHQSIINMKEIVtdkedaldfkK 782
Cdd:cd14167     3 DIYDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIA-KKALEGKETSIENEIAVLHKIKHPNIVALDDIY----------E 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFYLVFEYMDHDLM--GLLESGLvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNIL---LNNRGQIKLADFG 857
Cdd:cd14167    72 SGGHLYLIMQLVSGGELfdRIVEKGF--YTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFG 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARLYSSeeSRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGSPcpav 937
Cdd:cd14167   150 LSKIEGS--GSVMSTACGTPGYVAPE-VLAQKPYSKAVDCWSIGVIAYIL---------------------LCGYP---- 201
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  938 wpdviklPYFNTmKPKKQYRRKLREEFVF-------IPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14167   202 -------PFYDE-NDAKLFEQILKAEYEFdspywddISDSAKDFIQHLMEKDPEKRFTCEQALQ 257
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
711-1008 1.11e-21

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: 97.10  E-value: 1.11e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPItaIREIKILRQLTHQSIINMkeivtdkedaLDFKKDKGAFYLV 790
Cdd:cd06656    27 IGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKELI--INEILVMRENKNPNIVNY----------LDSYLVGDELWVV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHdlmGLLESGLVH--FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESR 868
Cdd:cd06656    95 MEYLAG---GSLTDVVTEtcMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQITPEQSK 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  869 PYTnKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISricgspcpavwpdviklpyfN 948
Cdd:cd06656   172 RST-MVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA--------------------T 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  949 TMKPKKQYRRKLREEFvfipaaaLDLFDYMLALDPSKRCTAEQALQCEFLRDVEP-SKMPP 1008
Cdd:cd06656   230 NGTPELQNPERLSAVF-------RDFLNRCLEMDVDRRGSAKELLQHPFLKLAKPlSSLTP 283
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
711-951 1.33e-21

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: 95.81  E-value: 1.33e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEmVALKKVrldneKEG--FPITAIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAFY 788
Cdd:cd05034     3 LGAGQFGEVWMGVWNGTTK-VAVKTL-----KPGtmSPEAFLQEAQIMKKLRHDKLVQLYAVCSDEE----------PIY 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDH-DLMGLLESGL-VHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL----- 861
Cdd:cd05034    67 IVTELMSKgSLLDYLRTGEgRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLiedde 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  862 YSSEESRPYTNKvitlWYRPPELLLGeeRYTPAIDVWSCGCILGELFTKKPI---FQANQE-LAQLELISRIcgsPCPAV 937
Cdd:cd05034   147 YTAREGAKFPIK----WTAPEAALYG--RFTIKSDVWSFGILLYEIVTYGRVpypGMTNREvLEQVERGYRM---PKPPG 217
                         250
                  ....*....|....
gi 145309300  938 WPDviklPYFNTMK 951
Cdd:cd05034   218 CPD----ELYDIML 227
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
707-915 1.36e-21

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 101.03  E-value: 1.36e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  707 IIGIIGEGTYGQVYKARDKDTGEMVALKKVRLD-NEKEGFpiTA--IREIKILRQLTHQSIINMkeivtdkedaLDFKKD 783
Cdd:NF033483   11 IGERIGRGGMAEVYLAKDTRLDRDVAVKVLRPDlARDPEF--VArfRREAQSAASLSHPNIVSV----------YDVGED 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMD-HDLMGLL-ESGLVHFNEnhIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL 861
Cdd:NF033483   79 GGIPYIVMEYVDgRTLKDYIrEHGPLSPEE--AVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARA 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  862 ySSEESRPYTNKVI-TLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQ 915
Cdd:NF033483  157 -LSSTTMTQTNSVLgTVHYLSPEQARG-GTVDARSDIYSLGIVLYEMLTGRPPFD 209
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
711-910 1.45e-21

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: 95.59  E-value: 1.45e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLD---NEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAF 787
Cdd:cd05041     3 IGRGNFGDVYRGVLKPDNTEVAVKTCRETlppDLKRKF----LQEARILKQYDHPNIVKLIGVCVQKQ----------PI 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARlysSEE 866
Cdd:cd05041    69 MIVMELVPGgSLLTFLRKKGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSR---EEE 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 145309300  867 SRPYT-----NKVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFTK 910
Cdd:cd05041   146 DGEYTvsdglKQIPIKWTAPEALNYG--RYTSESDVWSFGILLWEIFSL 192
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
703-926 1.57e-21

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: 96.49  E-value: 1.57e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKK------VRLDNEKEgfpitAIREIKILRQLTHQSIINMkeivtdked 776
Cdd:cd05580     1 DDFEFLKTLGTGSFGRVRLVKHKDSGKYYALKIlkkakiIKLKQVEH-----VLNEKRILSEVRHPFIVNL--------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 aLDFKKDKGAFYLVFEYMD-HDLMGLL-ESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLA 854
Cdd:cd05580    67 -LGSFQDDRNLYMVMEYVPgGELFSLLrRSG--RFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKIT 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  855 DFGLARLYsseESRPYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELI 926
Cdd:cd05580   144 DFGFAKRV---KDRTYT-LCGTPEYLAPEIILSKG-HGKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKI 210
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
711-931 1.60e-21

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: 95.98  E-value: 1.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMkeivtdkedaLDFKKDKGAFYLV 790
Cdd:cd13978     1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPL----------LGVCVERRSLGLV 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDH-DLMGLLESGL------VHFNenhiksFMRQLMEGLDYCH--KKNFLHRDIKCSNILLNNRGQIKLADFGLARL 861
Cdd:cd13978    71 MEYMENgSLKSLLEREIqdvpwsLRFR------IIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKL 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  862 Y----SSEESRPYTNKVITLWYRPPELL-LGEERYTPAIDVWSCGCILGELFTKKPIFqANQELAQLELISRICG 931
Cdd:cd13978   145 GmksiSANRRRGTENLGGTPIYMAPEAFdDFNKKPTSKSDVYSFAIVIWAVLTRKEPF-ENAINPLLIMQIVSKG 218
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
700-908 1.86e-21

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: 96.42  E-value: 1.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  700 RCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSI--------------- 764
Cdd:cd14049     3 RYLNEFEEIARLGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIvgyhtawmehvqlml 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  765 -INMKEIVTDKEDALDFKKDKGAFYlVFEYMDHDLMGLlesglvhfneNHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNI 843
Cdd:cd14049    83 yIQMQLCELSLWDWIVERNKRPCEE-EFKSAPYTPVDV----------DVTTKILQQLLEGVTYIHSMGIVHRDLKPRNI 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  844 LLNNRG-QIKLADFGLA-----------RLYSSEESRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELF 908
Cdd:cd14049   152 FLHGSDiHVRIGDFGLAcpdilqdgndsTTMSRLNGLTHTSGVGTCLYAAPEQLEGSH-YDFKSDMYSIGVILLELF 227
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
711-1008 1.96e-21

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: 96.33  E-value: 1.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPItaIREIKILRQLTHQSIINMkeivtdkedaLDFKKDKGAFYLV 790
Cdd:cd06655    27 IGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKELI--INEILVMKELKNPNIVNF----------LDSFLVGDELFVV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHdlmGLLESGLVH--FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESR 868
Cdd:cd06655    95 MEYLAG---GSLTDVVTEtcMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQITPEQSK 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  869 PYTnKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISricgspcpavwpdviklpyfN 948
Cdd:cd06655   172 RST-MVGTPYWMAPEVVT-RKAYGPKVDIWSLGIMAIEMVEGEPPYLNENPLRALYLIA--------------------T 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  949 TMKPKKQYRRKLREEFvfipaaaLDLFDYMLALDPSKRCTAEQALQCEFLRDVEP-SKMPP 1008
Cdd:cd06655   230 NGTPELQNPEKLSPIF-------RDFLNRCLEMDVEKRGSAKELLQHPFLKLAKPlSSLTP 283
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
705-1020 2.09e-21

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: 96.16  E-value: 2.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVrldnEKEGFPITaiREIKIL-RQLTHQSIINMKEIVtdkedaldfkKD 783
Cdd:cd14091     2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKII----DKSKRDPS--EEIEILlRYGQHPNIITLRDVY----------DD 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDhdlmG--LLESGLV--HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ----IKLAD 855
Cdd:cd14091    66 GNSVYLVTELLR----GgeLLDRILRqkFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGdpesLRICD 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  856 FGLARLYSSEES---RP-YT-NKVitlwyrPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRIc 930
Cdd:cd14091   142 FGFAKQLRAENGllmTPcYTaNFV------APE-VLKKQGYDAACDIWSLGVLLYTMLAGYTPFASGPNDTPEVILARI- 213
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  931 GSpcpavwpDVIKL--PYFNTmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRdvEPSKMPP 1008
Cdd:cd14091   214 GS-------GKIDLsgGNWDH-----------------VSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIR--NRDSLPQ 267
                         330
                  ....*....|..
gi 145309300 1009 PDLPLWQDCHEL 1020
Cdd:cd14091   268 RQLTDPQDAALV 279
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
710-986 3.43e-21

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: 96.10  E-value: 3.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPIT-AIREIKILRQLTHQSIINMKeivtdkedaLDFKKdKGAFY 788
Cdd:cd05585     1 VIGKGSFGKVMQVRKKDTSRIYALKTIRKAHIVSRSEVThTLAERTVLAQVDCPFIVPLK---------FSFQS-PEKLY 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDHDLM--GLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEE 866
Cdd:cd05585    71 LVLAFINGGELfhHLQREG--RFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLNMKDD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  867 SRpyTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPifqanqelaqlelisricgspcpavwpdviklP 945
Cdd:cd05585   149 DK--TNTFCgTPEYLAPELLLGHG-YTKAVDWWTLGVLLYEMLTGLP--------------------------------P 193
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 145309300  946 YFNTMKPkKQYRRKLREEFVF---IPAAALDLFDYMLALDPSKR 986
Cdd:cd05585   194 FYDENTN-EMYRKILQEPLRFpdgFDRDAKDLLIGLLNRDPTKR 236
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
705-993 4.12e-21

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: 94.37  E-value: 4.12e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKK----VRLDNEKEgfpiTAIREIKILRQLTHQSiiNMKEIVTDKEDAldf 780
Cdd:cd13997     2 FHELEQIGSGSFSEVFKVRSKVDGCLYAVKKskkpFRGPKERA----RALREVEAHAALGQHP--NIVRYYSSWEEG--- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdkGAFYLVFEYMD-HDLMGLLE--SGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG 857
Cdd:cd13997    73 ----GHLYIQMELCEnGSLQDALEelSPISKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFG 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LA-RLYSS---EESRPYtnkvitlwYRPPELLLGEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGSP 933
Cdd:cd13997   149 LAtRLETSgdvEEGDSR--------YLAPELLNENYTHLPKADIFSLGVTVYEA---------------------ATGEP 199
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  934 CPAvwpdviklpyfntmkpKKQYRRKLRE-EFVFIPAAAL-----DLFDYMLALDPSKRCTAEQAL 993
Cdd:cd13997   200 LPR----------------NGQQWQQLRQgKLPLPPGLVLsqeltRLLKVMLDPDPTRRPTADQLL 249
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
705-962 5.50e-21

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: 94.32  E-value: 5.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVR----LDNEKEGfpiTAIREIKILRQLTHQSIIN-MKEIVTDKEdald 779
Cdd:cd08228     4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQifemMDAKARQ---DCVKEIDLLKQLNHPNVIKyLDSFIEDNE---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkkdkgaFYLVFEYMDhdlMGLLESGLVHFN-------ENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIK 852
Cdd:cd08228    77 -------LNIVLELAD---AGDLSQMIKYFKkqkrlipERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFGLARLYSSEESRPYTnKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQeLAQLELISRICGS 932
Cdd:cd08228   147 LGDLGLGRFFSSKTTAAHS-LVGTPYYMSPE-RIHENGYNFKSDIWSLGCLLYEMAALQSPFYGDK-MNLFSLCQKIEQC 223
                         250       260       270
                  ....*....|....*....|....*....|
gi 145309300  933 PCPAVwpdviklpyfntmkPKKQYRRKLRE 962
Cdd:cd08228   224 DYPPL--------------PTEHYSEKLRE 239
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
699-930 7.48e-21

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: 94.49  E-value: 7.48e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  699 KRCVDKFDIIGII------GEGTYGQVYKARDKDTgeMVALKK------VRLDNEKEGFPitaiREIKILRQLTHQSIIN 766
Cdd:cd14158     5 KNMTNNFDERPISvggnklGEGGFGVVFKGYINDK--NVAVKKlaamvdISTEDLTKQFE----QEIQVMAKCQHENLVE 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  767 MkeivtdkedaLDFKKDKGAFYLVFEYMDHdlmGLLESGLVHFNEN-----HIKSFMRQ-LMEGLDYCHKKNFLHRDIKC 840
Cdd:cd14158    79 L----------LGYSCDGPQLCLVYTYMPN---GSLLDRLACLNDTpplswHMRCKIAQgTANGINYLHENNHIHRDIKS 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  841 SNILLNNRGQIKLADFGLARLYSSEESRPYTNKVI-TLWYRPPELLLGEerYTPAIDVWSCGCILGELFTKKPIFQANQE 919
Cdd:cd14158   146 ANILLDETFVPKISDFGLARASEKFSQTIMTERIVgTTAYMAPEALRGE--ITPKSDIFSFGVVLLEIITGLPPVDENRD 223
                         250
                  ....*....|..
gi 145309300  920 LAQL-ELISRIC 930
Cdd:cd14158   224 PQLLlDIKEEIE 235
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
705-1012 8.52e-21

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: 95.46  E-value: 8.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVR----LDNEKEGFPItaiREIKILRQLTHQSIINMKEIVTDKEDaldf 780
Cdd:cd05601     3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKksetLAQEEVSFFE---EERDIMAKANSPWITKLQYAFQDSEN---- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdkgaFYLVFEYM-DHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG-L 858
Cdd:cd05601    76 ------LYLVMEYHpGGDLLSLLSRYDDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGsA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYSSEESRPyTNKVITLWYRPPELLLGEER-----YTPAIDVWSCGCILGELFTKKPIFQAnqelaqlelisricgsp 933
Cdd:cd05601   150 AKLSSDKTVTS-KMPVGTPDYIAPEVLTSMNGgskgtYGVECDWWSLGIVAYEMLYGKTPFTE----------------- 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  934 cpavwpDVIKLPYFNTMkpkkQYRRKLR-EEFVFIPAAALDLFDYMLAlDPSKRCTAEQALQCEFLRDVEPSK---MPPP 1009
Cdd:cd05601   212 ------DTVIKTYSNIM----NFKKFLKfPEDPKVSESAVDLIKGLLT-DAKERLGYEGLCCHPFFSGIDWNNlrqTVPP 280

                  ...
gi 145309300 1010 DLP 1012
Cdd:cd05601   281 FVP 283
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
711-936 9.47e-21

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: 93.98  E-value: 9.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEM-----VALKKVRLDNE---KEGFPitaiREIKILRQLTHQSIINMKEIVTDKEdaldfkk 782
Cdd:cd05048    13 LGEGAFGKVYKGELLGPSSEesaisVAIKTLKENASpktQQDFR----REAELMSDLQHPNIVCLLGVCTKEQ------- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgAFYLVFEYMDH-DLMGLL------ESGLVHFNENHIKSFMR---------QLMEGLDYCHKKNFLHRDIKCSNILLN 846
Cdd:cd05048    82 ---PQCMLFEYMAHgDLHEFLvrhsphSDVGVSSDDDGTASSLDqsdflhiaiQIAAGMEYLSSHHYVHRDLAARNCLVG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  847 NRGQIKLADFGLARL-YSSEESRPYTNKVITLWYRPPE-LLLGeeRYTPAIDVWSCGCILGELFT--KKPIFQ-ANQELa 921
Cdd:cd05048   159 DGLTVKISDFGLSRDiYSSDYYRVQSKSLLPVRWMPPEaILYG--KFTTESDVWSFGVVLWEIFSygLQPYYGySNQEV- 235
                         250
                  ....*....|....*....
gi 145309300  922 qLELI-SRI---CGSPCPA 936
Cdd:cd05048   236 -IEMIrSRQllpCPEDCPA 253
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
711-912 1.08e-20

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: 93.32  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFpitaIREIKILRQLTHQSIINMKEIVTdkedaldfkKDkGAFYLV 790
Cdd:cd14065     1 LGKGFFGEVYKVTHRETGKVMVMKELKRFDEQRSF----LKEVKLMRRLSHPNILRFIGVCV---------KD-NKLNFI 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMD-HDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL--NNRGQ-IKLADFGLARLYSSEE 866
Cdd:cd14065    67 TEYVNgGTLEELLKSMDEQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreANRGRnAVVADFGLAREMPDEK 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 145309300  867 SR-PYTNKVITL----WYRPPELLLGEErYTPAIDVWSCGCILGELFTKKP 912
Cdd:cd14065   147 TKkPDRKKRLTVvgspYWMAPEMLRGES-YDEKVDVFSFGIVLCEIIGRVP 196
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
707-991 1.09e-20

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: 94.04  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  707 IIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDnEKEGFPITAIREIKILRQLTHQSIINMKeivtdkedaldfkkdkGA 786
Cdd:cd06620     9 TLKDLGAGNGGSVSKVLHIPTGTIMAKKVIHID-AKSSVRKQILRELQILHECHSPYIVSFY----------------GA 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FY-------LVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKK-NFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd06620    72 FLnennniiICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGV 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 arlysseeSRPYTNKVI-----TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQ--------LEL 925
Cdd:cd06620   152 --------SGELINSIAdtfvgTSTYMSPERIQGGK-YSVKSDVWSLGLSIIELALGEFPFAGSNDDDDgyngpmgiLDL 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  926 ISRICGSPCPavwpdviKLPyfntmkpkkqyrrklrEEFVFiPAAALDLFDYMLALDPSKRCTAEQ 991
Cdd:cd06620   223 LQRIVNEPPP-------RLP----------------KDRIF-PKDLRDFVDRCLLKDPRERPSPQL 264
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
703-998 1.21e-20

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: 93.42  E-value: 1.21e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITaiREIKILRQLTHQSIINMkeivtdkEDALDfkk 782
Cdd:cd14114     2 DHYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVR--KEIQIMNQLHHPKLINL-------HDAFE--- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFYLVFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR--GQIKLADFGLA 859
Cdd:cd14114    70 DDNEMVLILEFLSGgELFERIAAEHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKrsNEVKLIDFGLA 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RLYSSEESRPYTNKviTLWYRPPELLLGEE--RYTpaiDVWSCGCILGELFTKKPIFQANQELAQLELISRicgspCPAV 937
Cdd:cd14114   150 THLDPKESVKVTTG--TAEFAAPEIVEREPvgFYT---DMWAVGVLSYVLLSGLSPFAGENDDETLRNVKS-----CDWN 219
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  938 WPDviklpyfntmkpkkqyrrklrEEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14114   220 FDD---------------------SAFSGISEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
703-998 1.27e-20

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: 93.17  E-value: 1.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPI--TAIREIKILRQLTHQSIINMKEI-VTDKEDALD 779
Cdd:cd14088     1 DRYDLGQVIKTEEFCEIFRAKDKTTGKLYTCKKFL---KRDGRKVrkAAKNEINILKMVKHPNILQLVDVfETRKEYFIF 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FKKDKGAfyLVFEYmdhdlmgLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR---GQIKLADF 856
Cdd:cd14088    78 LELATGR--EVFDW-------ILDQG--YYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYNRlknSKIVISDF 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSEESRPYTnkviTLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLElisricgspcpa 936
Cdd:cd14088   147 HLAKLENGLIKEPCG----TPEYLAPE-VVGRQRYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYE------------ 209
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  937 vwpdviklpyfntMKPKKQYRRKLREEFVF-------IPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14088   210 -------------NHDKNLFRKILAGDYEFdspywddISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
711-939 1.54e-20

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: 92.67  E-value: 1.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKardkdtGEMVALKKVRLDNEKEGF--PITAIREIKILRQLTHQSIINMKEIVTDKedaldfkkdkgAFY 788
Cdd:cd14203     3 LGQGCFGEVWM------GTWNGTTKVAIKTLKPGTmsPEAFLEEAQIMKKLRHDKLVQLYAVVSEE-----------PIY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDH-DLMGLLESGLVHFNE-NHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEE 866
Cdd:cd14203    66 IVTEFMSKgSLLDFLKDGEGKYLKlPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNE 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  867 SRPYTN-KVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFTKKPI---FQANQELaqLELISRICGSPCPAVWP 939
Cdd:cd14203   146 YTARQGaKFPIKWTAPEAALYG--RFTIKSDVWSFGILLTELVTKGRVpypGMNNREV--LEQVERGYRMPCPPGCP 218
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
710-904 1.59e-20

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: 92.86  E-value: 1.59e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVrldnEKEGFPITAIR----EIKILRQLTHQSIINMKEIVTDKEDAldfkkdkg 785
Cdd:cd14082    10 VLGSGQFGIVYGGKHRKTGRDVAIKVI----DKLRFPTKQESqlrnEVAILQQLSHPGVVNLECMFETPERV-------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 afYLVFEYMDHDLMGL-LESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG---QIKLADFGLARL 861
Cdd:cd14082    78 --FVVMEKLHGDMLEMiLSSEKGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGFARI 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 145309300  862 YSSEESRpyTNKVITLWYRPPELLLgEERYTPAIDVWSCGCIL 904
Cdd:cd14082   156 IGEKSFR--RSVVGTPAYLAPEVLR-NKGYNRSLDMWSVGVII 195
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
711-904 1.64e-20

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


Pssm-ID: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 92.62  E-value: 1.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKV-RLDNEKEGFPITAIREIKILRQLTHQSIINMKEIvtdkedaldFKKDKGAFYL 789
Cdd:cd14164     8 IGEGSFSKVKLATSQKYCCKVAIKIVdRRRASPDFVQKFLPRELSILRRVNHPNIVQMFEC---------IEVANGRLYI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDHDLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG-QIKLADFGLARLYSS--EE 866
Cdd:cd14164    79 VMEAAATDLLQKIQE-VHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDrKIKIADFGFARFVEDypEL 157
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 145309300  867 SRPYTNkviTLWYRPPELLLGEERYTPAIDVWSCGCIL 904
Cdd:cd14164   158 STTFCG---SRAYTPPEVILGTPYDPKKYDVWSLGVVL 192
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
711-914 1.70e-20

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: 92.50  E-value: 1.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDtgEMVALKKVRLDNEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAFYLV 790
Cdd:cd14058     1 VGRGSFGVVCKARWRN--QIVAVKIIESESEKKAF----EVEVRQLSRVDHPNIIKLYGACSNQK----------PVCLV 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDH-DLMGLLES--GLVHFNENHIKSFMRQLMEGLDYCHK---KNFLHRDIKCSNILLNNRGQ-IKLADFGLArlys 863
Cdd:cd14058    65 MEYAEGgSLYNVLHGkePKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTvLKICDFGTA---- 140
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 145309300  864 SEESRPYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIF 914
Cdd:cd14058   141 CDISTHMTNNKGSAAWMAPEVFEG-SKYSEKCDVFSWGIILWEVITRRKPF 190
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
707-935 1.75e-20

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: 93.30  E-value: 1.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  707 IIGIIGEGTYGQVYKA--------RDKDTGEMVALKKVRLDNEKEGFPitaiREIKILRQLTHQSIINMKEIVTDKedal 778
Cdd:cd05049     9 LKRELGEGAFGKVFLGecynlepeQDKMLVAVKTLKDASSPDARKDFE----REAELLTNLQHENIVKFYGVCTEG---- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 dfkkdkGAFYLVFEYMDH-DLMGLLESG------LVHFNENHIKSFMRQLME-------GLDYCHKKNFLHRDIKCSNIL 844
Cdd:cd05049    81 ------DPLLMVFEYMEHgDLNKFLRSHgpdaafLASEDSAPGELTLSQLLHiavqiasGMVYLASQHFVHRDLATRNCL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  845 LNNRGQIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT--KKPIFQ-ANQEL 920
Cdd:cd05049   155 VGTNLVVKIGDFGMSRdIYSTDYYRVGGHTMLPIRWMPPESIL-YRKFTTESDVWSFGVVLWEIFTygKQPWFQlSNTEV 233
                         250
                  ....*....|....*..
gi 145309300  921 AQLELISRICGSP--CP 935
Cdd:cd05049   234 IECITQGRLLQRPrtCP 250
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
710-998 1.87e-20

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: 92.68  E-value: 1.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALK-----KVRLDNEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDaldfkkdk 784
Cdd:cd14189     8 LLGKGGFARCYEMTDLATNKTYAVKviphsRVAKPHQREKI----VNEIELHRDLHHKHVVKFSHHFEDAEN-------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gaFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL-ARLYS 863
Cdd:cd14189    76 --IYIFLELCSRKSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLaARLEP 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEESRpytnKVI--TLWYRPPELLLgEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGSPcPavwpdv 941
Cdd:cd14189   154 PEQRK----KTIcgTPNYLAPEVLL-RQGHGPESDVWSLGCVMYTL---------------------LCGNP-P------ 200
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  942 iklpyFNTMKPKKQYRRKLREEFV---FIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14189   201 -----FETLDLKETYRCIKQVKYTlpaSLSLPARHLLAGILKRNPGDRLTLDQILEHEFF 255
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
703-994 2.30e-20

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: 92.55  E-value: 2.30e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVA---LKKVRLDNEKEGFPITAI-REIKILRQLTHQSIINMKEIVTDKEDAL 778
Cdd:cd14105     5 DFYDIGEELGSGQFAVVKKCREKSTGLEYAakfIKKRRSKASRRGVSREDIeREVSILRQVLHPNIITLHDVFENKTDVV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 dfkkdkgafyLVFEYMD----HDLMGLLESglvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG----Q 850
Cdd:cd14105    85 ----------LILELVAggelFDFLAEKES----LSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  851 IKLADFGLArlYSSEESRPYTNKVITLWYRPPELLLGEERYTPAiDVWSCGCILGELFTKKPIFQANQELAQLELISric 930
Cdd:cd14105   151 IKLIDFGLA--HKIEDGNEFKNIFGTPEFVAPEIVNYEPLGLEA-DMWSIGVITYILLSGASPFLGDTKQETLANIT--- 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  931 gspcpAVWPDVIKLPYFNTMKPKKQYRRKLreefvfipaaaldlfdymLALDPSKRCTAEQALQ 994
Cdd:cd14105   225 -----AVNYDFDDEYFSNTSELAKDFIRQL------------------LVKDPRKRMTIQESLR 265
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
705-994 2.67e-20

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: 92.74  E-value: 2.67e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRL---DNEKEgfpitAIREIKILRQLTHQSIINMKE--IVTDKEdald 779
Cdd:cd13986     2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKKILChskEDVKE-----AMREIENYRLFNHPNILRLLDsqIVKEAG---- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkkDKGAFYLVFEYMDH-DLMGLLESGLVH---FNENHIKSFMRQLMEGLDYCHK---KNFLHRDIKCSNILLNNRGQIK 852
Cdd:cd13986    73 ---GKKEVYLLLPYYKRgSLQDEIERRLVKgtfFPEDRILHIFLGICRGLKAMHEpelVPYAHRDIKPGNVLLSEDDEPI 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFG---LARLY--SSEESRP---YTNKVITLWYRPPEL--LLGEERYTPAIDVWSCGCILGEL-FTKKP---IFQANQ 918
Cdd:cd13986   150 LMDLGsmnPARIEieGRREALAlqdWAAEHCTMPYRAPELfdVKSHCTIDEKTDIWSLGCTLYALmYGESPferIFQKGD 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  919 ELAQlelisricgspcpAVWPDVIKLPyfntmkPKKQYrrklreefvfiPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd13986   230 SLAL-------------AVLSGNYSFP------DNSRY-----------SEELHQLVKSMLVVNPAERPSIDDLLS 275
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
710-923 2.91e-20

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: 92.45  E-value: 2.91e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNE--KEGFPITAIR-EIKILRQLTHQSIINMKEIVTDKEDAldfkkdkgA 786
Cdd:cd06651    14 LLGQGAFGRVYLCYDVDTGRELAAKQVQFDPEspETSKEVSALEcEIQLLKNLQHERIVQYYGCLRDRAEK--------T 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA-RLYSSE 865
Cdd:cd06651    86 LTIFMEYMPGGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASkRLQTIC 165
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  866 ESRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQL 923
Cdd:cd06651   166 MSGTGIRSVTgTPYWMSPEVISGEG-YGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAI 223
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
703-994 2.99e-20

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 92.86  E-value: 2.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIG-IIGEGTYGQVYKARDKDTGEMVALKKVrldNEKEGFPITAI-REIKILRQLT-HQSIINMKEivtdkedald 779
Cdd:cd14090     1 DLYKLTGeLLGEGAYASVQTCINLYTGKEYAVKII---EKHPGHSRSRVfREVETLHQCQgHPNILQLIE---------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FKKDKGAFYLVFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQI---KLAD 855
Cdd:cd14090    68 YFEDDERFYLVFEKMRGgPLLSHIEKR-VHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKVspvKICD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  856 FGLAR--LYSSEESRPYT-----NKVITLWYRPPELL---LGEE-RYTPAIDVWSCGCILGELFTKKPIFQANqelaqle 924
Cdd:cd14090   147 FDLGSgiKLSSTSMTPVTtpellTPVGSAEYMAPEVVdafVGEAlSYDKRCDLWSLGVILYIMLCGYPPFYGR------- 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  925 lisriCGSPCPavW------PDVIKLPYFNTMKPKKQYRRKlreEFVFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14090   220 -----CGEDCG--WdrgeacQDCQELLFHSIQEGEYEFPEK---EWSHISAEAKDLISHLLVRDASQRYTAEQVLQ 285
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
710-995 3.45e-20

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


Pssm-ID: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 91.97  E-value: 3.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKkVRLDNEKegfpitAIREIKI-LRQLTHQSIINMKEIVTDKedaldFKKDKgAFY 788
Cdd:cd14089     8 VLGLGINGKVLECFHKKTGEKFALK-VLRDNPK------ARREVELhWRASGCPHIVRIIDVYENT-----YQGRK-CLL 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDHdlmGLL-----ESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG---QIKLADFGLAR 860
Cdd:cd14089    75 VVMECMEG---GELfsriqERADSAFTEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSSKGpnaILKLTDFGFAK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 LysSEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAqlelISricgspcpavwPD 940
Cdd:cd14089   152 E--TTTKKSLQTPCYTPYYVAPE-VLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLA----IS-----------PG 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  941 viklpyfntMKpkkqyrRKLR--------EEFVFIPAAALDLFDYMLALDPSKRCTAEQALQC 995
Cdd:cd14089   214 ---------MK------KRIRngqyefpnPEWSNVSEEAKDLIRGLLKTDPSERLTIEEVMNH 261
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
704-998 3.82e-20

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


Pssm-ID: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 93.38  E-value: 3.82e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKD-TGEMVALKKVR-LDNEKEGfpitAIREIKILRQLTHQSIINMKEIVtdkeDALDFK 781
Cdd:cd14213    13 RYEIVDTLGEGAFGKVVECIDHKmGGMHVAVKIVKnVDRYREA----ARSEIQVLEHLNTTDPNSTFRCV----QMLEWF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDKGAFYLVFEymdhdLMGLL------ESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNIL----------- 844
Cdd:cd14213    85 DHHGHVCIVFE-----LLGLStydfikENSFLPFPIDHIRNMAYQICKSVNFLHHNKLTHTDLKPENILfvqsdyvvkyn 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  845 ---------LNNRgQIKLADFGLARlYSSEEsrpYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQ 915
Cdd:cd14213   160 pkmkrdertLKNP-DIKVVDFGSAT-YDDEH---HSTLVSTRHYRAPEVIL-ALGWSQPCDVWSIGCILIEYYLGFTVFQ 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  916 ANQELAQLELISRICGsPCPA-VWPDVIKLPYFN------------------TMKPKKQYR--RKLREEFVFipaaalDL 974
Cdd:cd14213   234 THDSKEHLAMMERILG-PLPKhMIQKTRKRKYFHhdqldwdehssagryvrrRCKPLKEFMlsQDVDHEQLF------DL 306
                         330       340
                  ....*....|....*....|....
gi 145309300  975 FDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14213   307 IQKMLEYDPAKRITLDEALKHPFF 330
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
711-998 4.08e-20

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 92.74  E-value: 4.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKvrLDNEKEGFPITAIREIKILRQLTHQSIINM-KEIVTDKEdaldfkkdkgaFYL 789
Cdd:cd06659    29 IGEGSTGVVCIAREKHSGRQVAVKM--MDLRKQQRRELLFNEVVIMRDYQHPNVVEMyKSYLVGEE-----------LWV 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRp 869
Cdd:cd06659    96 LMEYLQGGALTDIVSQ-TRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQISKDVPK- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  870 YTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANqelAQLELISRICGSPCPavwpdviKLPYFNT 949
Cdd:cd06659   174 RKSLVGTPYWMAPEVIS-RCPYGTEVDIWSLGIMVIEMVDGEPPYFSD---SPVQAMKRLRDSPPP-------KLKNSHK 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 145309300  950 MKPkkqyrrKLReefvfipaaalDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd06659   243 ASP------VLR-----------DFLERMLVRDPQERATAQELLDHPFL 274
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
703-912 5.16e-20

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: 92.36  E-value: 5.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVR----LDNEKEGfpitairEIKILRQL-THQSIInmkeivtdKEDA 777
Cdd:cd06639    22 DTWDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDpisdVDEEIEA-------EYNILRSLpNHPNVV--------KFYG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 LDFKKDK---GAFYLVFEYMD----HDLM-GLLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG 849
Cdd:cd06639    87 MFYKADQyvgGQLWLVLELCNggsvTELVkGLLKCGQ-RLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEG 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  850 QIKLADFGLARLYSSEESRPYTNkVITLWYRPPELLLGEERYTPA----IDVWSCGCILGELFTKKP 912
Cdd:cd06639   166 GVKLVDFGVSAQLTSARLRRNTS-VGTPFWMAPEVIACEQQYDYSydarCDVWSLGITAIELADGDP 231
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
703-926 5.19e-20

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: 92.08  E-value: 5.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKvrLDNEKegfpitaireIKILRQLTHqsIINMKEIVtdkeDALDFK- 781
Cdd:cd14209     1 DDFDRIKTLGTGSFGRVMLVRHKETGNYYAMKI--LDKQK----------VVKLKQVEH--TLNEKRIL----QAINFPf 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 --------KDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKL 853
Cdd:cd14209    63 lvkleysfKDNSNLYMVMEYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKV 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  854 ADFGLARLYsseESRPYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELI 926
Cdd:cd14209   143 TDFGFAKRV---KGRTWT-LCGTPEYLAPEIILSKG-YNKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKI 210
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
710-967 8.29e-20

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: 91.19  E-value: 8.29e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGE---MVALKKVR---LDNEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDALdfkkd 783
Cdd:cd05063    12 VIGAGEFGEVFRGILKMPGRkevAVAIKTLKpgyTEKQRQDF----LSEASIMGQFSHHNIIRLEGVVTKFKPAM----- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgafyLVFEYMDHdlmGLLESGLV----HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd05063    83 -----IITEYMEN---GALDKYLRdhdgEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RLYSSEESRPYTN---KVITLWYRPPEllLGEERYTPAIDVWSCGCILGEL--FTKKPIFQ-ANQELaqLELISRICGSP 933
Cdd:cd05063   155 RVLEDDPEGTYTTsggKIPIRWTAPEA--IAYRKFTSASDVWSFGIVMWEVmsFGERPYWDmSNHEV--MKAINDGFRLP 230
                         250       260       270
                  ....*....|....*....|....*....|....
gi 145309300  934 CPAVWPDVIklpyFNTMKPKKQYRRKLREEFVFI 967
Cdd:cd05063   231 APMDCPSAV----YQLMLQCWQQDRARRPRFVDI 260
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
705-998 8.60e-20

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: 90.86  E-value: 8.60e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDnEKEGFPITAiREIKILRQLTHQSIINMKEIVTDKEDaldfkkdk 784
Cdd:cd06646    11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLE-PGDDFSLIQ-QEIFMVKECKHCNIVAYFGSYLSREK-------- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gaFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSS 864
Cdd:cd06646    81 --LWICMEYCGGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  865 EESRpYTNKVITLWYRPPELLLGEER--YTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPcpavwpdvi 942
Cdd:cd06646   159 TIAK-RKSFIGTPYWMAPEVAAVEKNggYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMSKSNFQP--------- 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  943 klpyfntmkPKKQYRRKLREEF-VFIPAAaldlfdymLALDPSKRCTAEQALQCEFL 998
Cdd:cd06646   229 ---------PKLKDKTKWSSTFhNFVKIS--------LTKNPKKRPTAERLLTHLFV 268
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
704-904 9.37e-20

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: 90.43  E-value: 9.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPITAIREIKILRQLTHQSIINMKE-IVTDKEDALDFKK 782
Cdd:cd14665     1 RYELVKDIGSGNFGVARLMRDKQTKELVAVKYIE---RGEKIDENVQREIINHRSLRHPNIVRFKEvILTPTHLAIVMEY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAfyLVFEYmdhdlmgLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG--QIKLADFGLAR 860
Cdd:cd14665    78 AAGG--ELFER-------ICNAG--RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSK 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 145309300  861 lYSSEESRPYTNkVITLWYRPPELLLGEERYTPAIDVWSCGCIL 904
Cdd:cd14665   147 -SSVLHSQPKST-VGTPAYIAPEVLLKKEYDGKIADVWSCGVTL 188
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
707-986 1.03e-19

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: 90.62  E-value: 1.03e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  707 IIG-IIGEGTYGQV-----YKARDKDTGEMVALKKVRLDNEKEGFPITAI-REIKILRQLTHQSIINMkeivtdkedaLD 779
Cdd:cd14076     4 ILGrTLGEGEFGKVklgwpLPKANHRSGVQVAIKLIRRDTQQENCQTSKImREINILKGLTHPNIVRL----------LD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FKKDKGAFYLVFEYMDHDlmGLLESGLVH--FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG 857
Cdd:cd14076    74 VLKTKKYIGIVLEFVSGG--ELFDYILARrrLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARLYSSEESRPYTNKVITLWYRPPELLLGEERYT-PAIDVWSCGCILGELFTKKPIFQANQELAQLELISR----ICGS 932
Cdd:cd14076   152 FANTFDHFNGDLMSTSCGSPCYAAPELVVSDSMYAgRKADIWSCGVILYAMLAGYLPFDDDPHNPNGDNVPRlyryICNT 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  933 PcpavwpdvIKLPYFNTMKPKkqyrrklreefvfipaaalDLFDYMLALDPSKR 986
Cdd:cd14076   232 P--------LIFPEYVTPKAR-------------------DLLRRILVPNPRKR 258
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
703-937 1.18e-19

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: 90.84  E-value: 1.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVR----LDNEKEGfpitairEIKILRQLT-HQSIINMKEIVTDKEda 777
Cdd:cd06638    18 DTWEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDpihdIDEEIEA-------EYNILKALSdHPNVVKFYGMYYKKD-- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 ldfKKDKGAFYLVFEYMD----HDLM-GLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIK 852
Cdd:cd06638    89 ---VKNGDQLWLVLELCNggsvTDLVkGFLKRG-ERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVK 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFGLARLYSSEESRPYTNkVITLWYRPPELLLGEER----YTPAIDVWSCGCILGELFTKKPIFqanQELAQLELISR 928
Cdd:cd06638   165 LVDFGVSAQLTSTRLRRNTS-VGTPFWMAPEVIACEQQldstYDARCDVWSLGITAIELGDGDPPL---ADLHPMRALFK 240

                  ....*....
gi 145309300  929 ICGSPCPAV 937
Cdd:cd06638   241 IPRNPPPTL 249
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
705-907 1.37e-19

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: 90.06  E-value: 1.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKilrqlTHqsiinmkEIVTDKEDALDFKK-- 782
Cdd:cd14050     3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVE-----RH-------EKLGEHPNCVRFIKaw 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 -DKGAFYLVFEYMDHDLMGLLEsGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL--- 858
Cdd:cd14050    71 eEKGILYIQTELCDTSLQQYCE-ETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLvve 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 145309300  859 ---ARLYSSEESRPYtnkvitlwYRPPELLLGeeRYTPAIDVWSCGCILGEL 907
Cdd:cd14050   150 ldkEDIHDAQEGDPR--------YMAPELLQG--SFTKAADIFSLGITILEL 191
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
711-1003 1.45e-19

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 90.87  E-value: 1.45e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKvrLDNEKEGFPITAIREIKILRQLTHQSIINMKE--IVTDKedaldfkkdkgaFY 788
Cdd:cd06658    30 IGEGSTGIVCIATEKHTGKQVAVKK--MDLRKQQRRELLFNEVVIMRDYHHENVVDMYNsyLVGDE------------LW 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDHdlmGLLESGLVH--FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEE 866
Cdd:cd06658    96 VVMEFLEG---GALTDIVTHtrMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEV 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  867 SRpYTNKVITLWYRPPELLlGEERYTPAIDVWSCGCILGELFTKKPifqanqelaqlelisricgspcpavwpdviklPY 946
Cdd:cd06658   173 PK-RKSLVGTPYWMAPEVI-SRLPYGTEVDIWSLGIMVIEMIDGEP--------------------------------PY 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  947 FNtmKPKKQYRRKLRE-------EFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEP 1003
Cdd:cd06658   219 FN--EPPLQAMRRIRDnlpprvkDSHKVSSVLRGFLDLMLVREPSQRATAQELLQHPFLKLAGP 280
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
708-909 2.09e-19

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: 90.34  E-value: 2.09e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  708 IGIIGEGTYGQV----YKARDKDTGEMVALKKVRLDNEKEGFPITaiREIKILRQLTHQSIINMKEIVtdkedaldFKKD 783
Cdd:cd05081     9 ISQLGKGNFGSVelcrYDPLGDNTGALVAVKQLQHSGPDQQRDFQ--REIQILKALHSDFIVKYRGVS--------YGPG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYM-DHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd05081    79 RRSLRLVMEYLpSGCLRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLL 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 145309300  863 SSEES-----RPYTNKVitLWYRPPEllLGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05081   159 PLDKDyyvvrEPGQSPI--FWYAPES--LSDNIFSRQSDVWSFGVVLYELFT 206
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
711-994 2.63e-19

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: 89.72  E-value: 2.63e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRL-----DNEKEgfpitAIREIKILRQ-LTHQSIINMKEIVTDKEDALdfkkdk 784
Cdd:cd14106    16 LGRGKFAVVRKCIHKETGKEYAAKFLRKrrrgqDCRNE-----ILHEIAVLELcKDCPRVVNLHEVYETRSELI------ 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gafyLVFEYMDHdlmGLLESGLV---HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLN---NRGQIKLADFGL 858
Cdd:cd14106    85 ----LILELAAG---GELQTLLDeeeCLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTsefPLGDIKLCDFGI 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYS-SEESRPYtnkVITLWYRPPELLlgeeRYTP---AIDVWSCGCILGELFTKKPIFQANQELAQLELISRicgspC 934
Cdd:cd14106   158 SRVIGeGEEIREI---LGTPDYVAPEIL----SYEPislATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQ-----C 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  935 PAVWPDviklpyfntmkpkkqyrrklrEEFVFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14106   226 NLDFPE---------------------ELFKDVSPLAIDFIKRLLVKDPEKRLTAKECLE 264
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
703-914 2.91e-19

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: 89.80  E-value: 2.91e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKK------VRLDNEKEgfpitAIREIKILRQLTHQSIINMkeivtdked 776
Cdd:cd05612     1 DDFERIKTIGTGTFGRVHLVRDRISEHYYALKVmaipevIRLKQEQH-----VHNEKRVLKEVSHPFIIRL--------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 aLDFKKDKGAFYLVFEYM-DHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLAD 855
Cdd:cd05612    67 -FWTEHDQRFLYMLMEYVpGGELFSYLRNS-GRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTD 144
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  856 FGLARLYSseeSRPYTnKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIF 914
Cdd:cd05612   145 FGFAKKLR---DRTWT-LCGTPEYLAPE-VIQSKGHNKAVDWWALGILIYEMLVGYPPF 198
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
707-919 3.04e-19

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: 89.35  E-value: 3.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  707 IIGIIGEGTYGQVYKARDKDTGE---MVALKKVRL---DNEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDALdf 780
Cdd:cd05033     8 IEKVIGGGEFGEVCSGSLKLPGKkeiDVAIKTLKSgysDKQRLDF----LTEASIMGQFDHPNVIRLEGVVTKSRPVM-- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdkgafyLVFEYMDHdlmGLLESGLVH----FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd05033    82 --------IVTEYMEN---GSLDKFLREndgkFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDF 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  857 GLARLYSSEESRPYTN--KVITLWYRPPEllLGEERYTPAIDVWSCGCILGEL--FTKKPIFQ-ANQE 919
Cdd:cd05033   151 GLSRRLEDSEATYTTKggKIPIRWTAPEA--IAYRKFTSASDVWSFGIVMWEVmsYGERPYWDmSNQD 216
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
703-998 3.04e-19

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: 89.33  E-value: 3.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDnEKEGFPITAiREIKILRQLTHQSIINMKeivtdkedALDFKK 782
Cdd:cd06645    11 EDFELIQRIGSGTYGDVYKARNVNTGELAAIKVIKLE-PGEDFAVVQ-QEIIMMKDCKHSNIVAYF--------GSYLRR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKgaFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd06645    81 DK--LWICMEFCGGGSLQDIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEESRpYTNKVITLWYRPPELLLGEER--YTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPcpavwpd 940
Cdd:cd06645   159 TATIAK-RKSFIGTPYWMAPEVAAVERKggYNQLCDIWAVGITAIELAELQPPMFDLHPMRALFLMTKSNFQP------- 230
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  941 viklpyfntmkPKKQYRRKLREEFVFIPAAAldlfdymLALDPSKRCTAEQALQCEFL 998
Cdd:cd06645   231 -----------PKLKDKMKWSNSFHHFVKMA-------LTKNPKKRPTAEKLLQHPFV 270
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
711-907 3.95e-19

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 88.86  E-value: 3.95e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKK-VRLDNEKEGfpiTAIREIKILRQLTHQSIINMKEIVTdKEDALDFkkdkgafyl 789
Cdd:cd14221     1 LGKGCFGQAIKVTHRETGEVMVMKElIRFDEETQR---TFLKEVKVMRCLEHPNVLKFIGVLY-KDKRLNF--------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESR 868
Cdd:cd14221    68 ITEYIKGgTLRGIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMVDEKTQ 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 145309300  869 P--------------YTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGEL 907
Cdd:cd14221   148 PeglrslkkpdrkkrYT-VVGNPYWMAPEMINGRS-YDEKVDVFSFGIVLCEI 198
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
711-919 4.10e-19

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 89.25  E-value: 4.10e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKA--------RDKDTGEMVALKKVRlDNEKEGFPitaiREIKILRQLTHQSIINMKEIVTDKEDALdfkk 782
Cdd:cd05092    13 LGEGAFGKVFLAechnllpeQDKMLVAVKALKEAT-ESARQDFQ----REAELLTVLQHQHIVRFYGVCTEGEPLI---- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgafyLVFEYMDH-DLMGLLES--------------GLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN 847
Cdd:cd05092    84 ------MVFEYMRHgDLNRFLRShgpdakildggegqAPGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQ 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  848 RGQIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT--KKPIFQ-ANQE 919
Cdd:cd05092   158 GLVVKIGDFGMSRdIYSTDYYRVGGRTMLPIRWMPPESIL-YRKFTTESDIWSFGVVLWEIFTygKQPWYQlSNTE 232
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
711-998 4.33e-19

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: 89.34  E-value: 4.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDnEKEGFPITAIREIKILRQLTHQSIInmkeivtdKEDALDFKKDKgaFYLV 790
Cdd:cd06640    12 IGKGSFGEVFKGIDNRTQQVVAIKIIDLE-EAEDEIEDIQQEITVLSQCDSPYVT--------KYYGSYLKGTK--LWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDH-DLMGLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRP 869
Cdd:cd06640    81 MEYLGGgSALDLLRAG--PFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKR 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  870 YTNKVITLWYRPPelLLGEERYTPAIDVWSCGCILGELFTKKPifqANQELAQLELISRICGSPCPAVWPDviklpyfnt 949
Cdd:cd06640   159 NTFVGTPFWMAPE--VIQQSAYDSKADIWSLGITAIELAKGEP---PNSDMHPMRVLFLIPKNNPPTLVGD--------- 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 145309300  950 mkpkkqYRRKLREefvFIPAAaldlfdymLALDPSKRCTAEQALQCEFL 998
Cdd:cd06640   225 ------FSKPFKE---FIDAC--------LNKDPSFRPTAKELLKHKFI 256
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
703-946 5.32e-19

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: 90.07  E-value: 5.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKkvrldnekegfpitAIREIKILR--QLTHqsIINMKEIVTDKEDALDF 780
Cdd:cd05598     1 SMFEKIKTIGVGAFGEVSLVRKKDTNALYAMK--------------TLRKKDVLKrnQVAH--VKAERDILAEADNEWVV 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 K-----KDKGAFYLVFEYM-DHDLMGLL-ESGLvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKL 853
Cdd:cd05598    65 KlyysfQDKENLYFVMDYIpGGDLMSLLiKKGI--FEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  854 ADFGLARLYS-SEESRPYTNK--VITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANQEL-AQLELISri 929
Cdd:cd05598   143 TDFGLCTGFRwTHDSKYYLAHslVGTPNYIAPEVLL-RTGYTQLCDWWSVGVILYEMLVGQPPFLAQTPAeTQLKVIN-- 219
                         250
                  ....*....|....*..
gi 145309300  930 cgspcpavWPDVIKLPY 946
Cdd:cd05598   220 --------WRTTLKIPH 228
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
710-917 5.76e-19

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: 88.53  E-value: 5.76e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARD-KDTGEMVALKKVRLDNEKEGfPITAIREIKILRQLTHQSIINMkeivtdkedaLDFKKDKGAFY 788
Cdd:cd14201    13 LVGHGAFAVVFKGRHrKKTDWEVAIKSINKKNLSKS-QILLGKEIKILKELQHENIVAL----------YDVQEMPNSVF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDH-DLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG---------QIKLADFGL 858
Cdd:cd14201    82 LVMEYCNGgDLADYLQAKGT-LSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASrkkssvsgiRIKIADFGF 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 AR-LYSSEESRPYTNKVItlwYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQAN 917
Cdd:cd14201   161 ARyLQSNMMAATLCGSPM---YMAPEVIM-SQHYDAKADLWSIGTVIYQCLVGKPPFQAN 216
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
703-903 6.70e-19

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


Pssm-ID: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 87.97  E-value: 6.70e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDK--DTGEMVALKKVRLDNEKEgfpiTAIREIKILRQLTHQSIINMkeivtdkedaLDF 780
Cdd:cd14112     3 GRFSFGSEIFRGRFSVIVKAVDSttETDAHCAVKIFEVSDEAS----EAVREFESLRTLQHENVQRL----------IAA 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 KKDKGAFYLVFEYMDHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG--QIKLADFGL 858
Cdd:cd14112    69 FKPSNFAYLVMEKLQEDVFTRFSSN-DYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRswQVKLVDFGR 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 145309300  859 ARLYSSEESRPytNKVITLWyRPPELLLGEERYTPAIDVWSCGCI 903
Cdd:cd14112   148 AQKVSKLGKVP--VDGDTDW-ASPEFHNPETPITVQSDIWGLGVL 189
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
723-1001 8.22e-19

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 91.62  E-value: 8.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  723 RDKDTGEMVALKKVRLDNEKEGfpITAIREIKILRQLTHQSIINMKEivtdkedalDFKKDKgAFYLVFEY-MDHDLMGL 801
Cdd:PTZ00267   88 RGSDPKEKVVAKFVMLNDERQA--AYARSELHCLAACDHFGIVKHFD---------DFKSDD-KLLLIMEYgSGGDLNKQ 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  802 LESGL---VHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRPYTNKVI-TL 877
Cdd:PTZ00267  156 IKQRLkehLPFQEYEVGLLFYQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASSFCgTP 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  878 WYRPPELLlGEERYTPAIDVWSCGCILGELFTKKPIFQ--ANQELAQLELISRICGSPCPAVwpdviklpyfNTMKPkkq 955
Cdd:PTZ00267  236 YYLAPELW-ERKRYSKKADMWSLGVILYELLTLHRPFKgpSQREIMQQVLYGKYDPFPCPVS----------SGMKA--- 301
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 145309300  956 yrrklreefvfipaaaldLFDYMLALDPSKRCTAEQALQCEFLRDV 1001
Cdd:PTZ00267  302 ------------------LLDPLLSKNPALRPTTQQLLHTEFLKYV 329
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
703-940 8.69e-19

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 88.96  E-value: 8.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRL-----DNEKEGFPITAIREIKILRQLTHQSIINMKEIvtdkeda 777
Cdd:cd14041     6 DRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLnknwrDEKKENYHKHACREYRIHKELDHPRIVKLYDY------- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 ldFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCH--KKNFLHRDIKCSNILLNNR---GQIK 852
Cdd:cd14041    79 --FSLDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNeiKPPIIHYDLKPGNILLVNGtacGEIK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFGLARL-----YSSEESRPYTNK-VITLWYRPPE-LLLGEE--RYTPAIDVWSCGCILGE-LFTKKPI--FQANQEL 920
Cdd:cd14041   157 ITDFGLSKImdddsYNSVDGMELTSQgAGTYWYLPPEcFVVGKEppKISNKVDVWSVGVIFYQcLYGRKPFghNQSQQDI 236
                         250       260
                  ....*....|....*....|...
gi 145309300  921 AQLELI---SRICGSPCPAVWPD 940
Cdd:cd14041   237 LQENTIlkaTEVQFPPKPVVTPE 259
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
705-1016 1.01e-18

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: 89.21  E-value: 1.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVY---KARDKDTGEMVALKKVR----LDNEK-------EGFPITAIREIKILRQLTHQsiinmkei 770
Cdd:cd05614     2 FELLKVLGTGAYGKVFlvrKVSGHDANKLYAMKVLRkaalVQKAKtvehtrtERNVLEHVRQSPFLVTLHYA-------- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  771 vtdkedaldFKKDkGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ 850
Cdd:cd05614    74 ---------FQTD-AKLHLILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGH 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  851 IKLADFGLARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQEL-AQLELISRI 929
Cdd:cd05614   144 VVLTDFGLSKEFLTEEKERTYSFCGTIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFTLEGEKnTQSEVSRRI 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  930 --CGSPCPAvwpdviklpyfntmkpkkqyrrklreefvFIPAAALDLFDYMLALDPSKRC-----TAEQALQCEFLRDVE 1002
Cdd:cd05614   224 lkCDPPFPS-----------------------------FIGPVARDLLQKLLCKDPKKRLgagpqGAQEIKEHPFFKGLD 274
                         330
                  ....*....|....*....
gi 145309300 1003 PS-----KMPPPDLPLWQD 1016
Cdd:cd05614   275 WEalalrKVNPPFRPSIRS 293
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
711-907 1.03e-18

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: 89.17  E-value: 1.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKV--RLDNEKEGFPITaIREIKIL-RQLTHQS--IINMKeivtdkedaLDFKKDKg 785
Cdd:cd05586     1 IGKGTFGQVYQVRKKDTRRIYAMKVLskKVIVAKKEVAHT-IGERNILvRTALDESpfIVGLK---------FSFQTPT- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 AFYLVFEYMDHdlmGLLESGLVH---FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARly 862
Cdd:cd05586    70 DLYLVTDYMSG---GELFWHLQKegrFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSK-- 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 145309300  863 SSEESRPYTNKVI-TLWYRPPELLLGEERYTPAIDVWSCGCILGEL 907
Cdd:cd05586   145 ADLTDNKTTNTFCgTTEYLAPEVLLDEKGYTKMVDFWSLGVLVFEM 190
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
705-963 1.07e-18

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: 88.93  E-value: 1.07e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPITAIREIKILRQLThqsiinmkeivTDKEDALDFKKDK 784
Cdd:cd14229     2 YEVLDFLGRGTFGQVVKCWKRGTNEIVAVKILK---NHPSYARQGQIEVGILARLS-----------NENADEFNFVRAY 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFY------LVFEYMDHDLMGLL-ESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL----NNRGQIKL 853
Cdd:cd14229    68 ECFQhrnhtcLVFEMLEQNLYDFLkQNKFSPLPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLvdpvRQPYRVKV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  854 ADFGLARLYSSEESRPYTNkviTLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSP 933
Cdd:cd14229   148 IDFGSASHVSKTVCSTYLQ---SRYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGALEYDQIRYISQTQGLP 223
                         250       260       270
                  ....*....|....*....|....*....|...
gi 145309300  934 CPAVWPDVIKLPYF---NTMKPKKQYRRKLREE 963
Cdd:cd14229   224 GEQLLNVGTKTSRFfcrETDAPYSSWRLKTLEE 256
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
696-998 1.12e-18

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


Pssm-ID: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 88.92  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  696 DWGKrcvDKFDIIGIIGEGTYGQVYKARD-KDTGEMVALKKVRldnEKEGFPITAIREIKILRQLTHQSIINmKEIVTDK 774
Cdd:cd14215     8 DWLQ---ERYEIVSTLGEGTFGRVVQCIDhRRGGARVALKIIK---NVEKYKEAARLEINVLEKINEKDPEN-KNLCVQM 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  775 EDALDFKkdkGAFYLVFEYMDHDLMGLL-ESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG---- 849
Cdd:cd14215    81 FDWFDYH---GHMCISFELLGLSTFDFLkENNYLPYPIHQVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDyelt 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  850 ---------------QIKLADFGLARLysseESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIF 914
Cdd:cd14215   158 ynlekkrdersvkstAIRVVDFGSATF----DHEHHSTIVSTRHYRAPEVIL-ELGWSQPCDVWSIGCIIFEYYVGFTLF 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  915 QANQELAQLELISRICGsPCPA-VWPDVIKLPYF---------NT---------MKPKKQYRRKLREEFvfipAAALDLF 975
Cdd:cd14215   233 QTHDNREHLAMMERILG-PIPSrMIRKTRKQKYFyhgrldwdeNTsagryvrenCKPLRRYLTSEAEEH----HQLFDLI 307
                         330       340
                  ....*....|....*....|...
gi 145309300  976 DYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14215   308 ESMLEYEPSKRLTLAAALKHPFF 330
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
711-940 1.29e-18

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: 87.46  E-value: 1.29e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEmVALKKVRLDN-EKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAFYL 789
Cdd:cd05068    16 LGSGQFGEVWEGLWNNTTP-VAVKTLKPGTmDPEDF----LREAQIMKKLRHPKLIQLYAVCTLEE----------PIYI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDHdlmgllESGLVHFNENHIKSFMRQLME-------GLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd05068    81 ITELMKH------GSLLEYLQGKGRSLQLPQLIDmaaqvasGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSE---ESRPYTNKVITlWYRPPELLLgeERYTPAIDVWSCGCILGELFTKK----PIFQANQELAQLELISRIcgsPCP 935
Cdd:cd05068   155 KVEdeyEAREGAKFPIK-WTAPEAANY--NRFSIKSDVWSFGILLTEIVTYGripyPGMTNAEVLQQVERGYRM---PCP 228

                  ....*
gi 145309300  936 AVWPD 940
Cdd:cd05068   229 PNCPP 233
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
711-999 1.71e-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: 87.37  E-value: 1.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVA---LKKVRLDNEKEGFPITAI-REIKILRQLTHQSIINMKEIVTDKEDALdfkkdkga 786
Cdd:cd14195    13 LGSGQFAIVRKCREKGTGKEYAakfIKKRRLSSSRRGVSREEIeREVNILREIQHPNIITLHDIFENKTDVV-------- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 fyLVFEYMD----HDLMGLLESglvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG----QIKLADFGL 858
Cdd:cd14195    85 --LILELVSggelFDFLAEKES----LTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpnpRIKLIDFGI 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ArlYSSEESRPYTNKVITLWYRPPELLlgeeRYTP---AIDVWSCGCILGELFTKKPIFQANQELAQLELISricgspcp 935
Cdd:cd14195   159 A--HKIEAGNEFKNIFGTPEFVAPEIV----NYEPlglEADMWSIGVITYILLSGASPFLGETKQETLTNIS-------- 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  936 AVWPDVIKLPYFNTMKPKKQYRRKLreefvfipaaaldlfdymLALDPSKRCTAEQALQCEFLR 999
Cdd:cd14195   225 AVNYDFDEEYFSNTSELAKDFIRRL------------------LVKDPKKRMTIAQSLEHSWIK 270
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
710-903 1.75e-18

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: 86.89  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITaiREIKILRQLTHQSIINMKeivtdkeDALDFKKDkgaFYL 789
Cdd:cd14193    11 ILGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVK--NEIEVMNQLNHANLIQLY-------DAFESRND---IVL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR--GQIKLADFGLARLYSSEE 866
Cdd:cd14193    79 VMEYVDGgELFDRIIDENYNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSReaNQVKIIDFGLARRYKPRE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 145309300  867 SrpytnkvITLWYRPPELLLGE----ERYTPAIDVWSCGCI 903
Cdd:cd14193   159 K-------LRVNFGTPEFLAPEvvnyEFVSFPTDMWSLGVI 192
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
712-903 1.83e-18

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: 86.80  E-value: 1.83e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  712 GEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGfpiTAIREIKILRQLTHQSIINMKEI-VTDKedaldfkkdkgafYLV 790
Cdd:cd14111    12 ARGRFGVIRRCRENATGKNFPAKIVPYQAEEKQ---GVLQEYEILKSLHHERIMALHEAyITPR-------------YLV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 F--EYMDHD--LMGLLESglVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEE 866
Cdd:cd14111    76 LiaEFCSGKelLHSLIDR--FRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLS 153
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 145309300  867 SRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCI 903
Cdd:cd14111   154 LRQLGRRTGTLEYMAPEMVKGEP-VGPPADIWSIGVL 189
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
703-1012 1.89e-18

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: 88.10  E-value: 1.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDN-EKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEdaldfk 781
Cdd:cd05632     2 NTFRQYRVLGKGGFGEVCACQVRATGKMYACKRLEKKRiKKRKGESMALNEKQILEKVNSQFVVNLAYAYETKD------ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgAFYLVFEYMDH-DL-MGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd05632    76 ----ALCLVLTIMNGgDLkFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLA 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 rlYSSEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRicgspcpavwp 939
Cdd:cd05632   152 --VKIPEGESIRGRVGTVGYMAPE-VLNNQRYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDR----------- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  940 dviklpyfNTMKPKKQYRRKLREEfvfipaaALDLFDYMLALDPSKR--CTAEQALQCE---FLRDV-----EPSKMPPP 1009
Cdd:cd05632   218 --------RVLETEEVYSAKFSEE-------AKSICKMLLTKDPKQRlgCQEEGAGEVKrhpFFRNMnfkrlEAGMLDPP 282

                  ...
gi 145309300 1010 DLP 1012
Cdd:cd05632   283 FVP 285
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
710-998 1.90e-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: 87.11  E-value: 1.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARdKDTGEMVALKKVRLDN------EKEGFPITaiREIKILRQLTHQSIINMkeIVTDKEDALdfkkd 783
Cdd:cd06631     8 VLGKGAYGTVYCGL-TSTGQLIAVKQVELDTsdkekaEKEYEKLQ--EEVDLLKTLKHVNIVGY--LGTCLEDNV----- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgafylVFEYMDHDLMGLLESGLVHF---NENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR 860
Cdd:cd06631    78 ------VSIFMEFVPGGSIASILARFgalEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGCAK 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 LYSSEESRPYTNKVI-----TLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISricgspcp 935
Cdd:cd06631   152 RLCINLSSGSQSQLLksmrgTPYWMAPEVIN-ETGHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIG-------- 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  936 avwpdviklpyfNTMKPKKQyrrkLREEFvfiPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd06631   223 ------------SGRKPVPR----LPDKF---SPEARDFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
703-903 2.02e-18

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: 86.93  E-value: 2.02e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVA---LKKVRLDNEKEGFPITAI-REIKILRQLTHQSIINMKEIVTDKEDAL 778
Cdd:cd14196     5 DFYDIGEELGSGQFAIVKKCREKSTGLEYAakfIKKRQSRASRRGVSREEIeREVSILRQVLHPNIITLHDVYENRTDVV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 dfkkdkgafyLVFEYMD----HDLMGLLESglvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG----Q 850
Cdd:cd14196    85 ----------LILELVSggelFDFLAQKES----LSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipH 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  851 IKLADFGLArlYSSEESRPYTNKVITLWYRPPELLlgeeRYTP---AIDVWSCGCI 903
Cdd:cd14196   151 IKLIDFGLA--HEIEDGVEFKNIFGTPEFVAPEIV----NYEPlglEADMWSIGVI 200
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
710-1012 2.23e-18

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: 87.36  E-value: 2.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDN-EKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAFY 788
Cdd:cd05631     7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRiKKRKGEAMALNEKRILEKVNSRFVVSLAYAYETKD----------ALC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDH-DL-MGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLArlYSSEE 866
Cdd:cd05631    77 LVLTIMNGgDLkFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLA--VQIPE 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  867 SRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRicgspcpavwpdviklpy 946
Cdd:cd05631   155 GETVRGRVGTVGYMAPE-VINNEKYTFSPDWWGLGCLIYEMIQGQSPFRKRKERVKREEVDR------------------ 215
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  947 fNTMKPKKQYRRKLREEfvfipaaALDLFDYMLALDPSKR--CTAEQALQCEF--------LRDVEPSKMPPPDLP 1012
Cdd:cd05631   216 -RVKEDQEEYSEKFSED-------AKSICRMLLTKNPKERlgCRGNGAAGVKQhpifkninFKRLEANMLEPPFCP 283
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
705-928 2.24e-18

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: 86.98  E-value: 2.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRL-DNEKEGFPItairEIKILRQLTHQSIIN------MKEIVTDKEDA 777
Cdd:cd06636    18 FELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVtEDEEEEIKL----EINMLKKYSHHRNIAtyygafIKKSPPGHDDQ 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 LdfkkdkgafYLVFEYMDH----DLMGLLESGLvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKL 853
Cdd:cd06636    94 L---------WLVMEFCGAgsvtDLVKNTKGNA--LKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKL 162
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  854 ADFGLARLYSSEESRPYTNkVITLWYRPPELLLGEER----YTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISR 928
Cdd:cd06636   163 VDFGVSAQLDRTVGRRNTF-IGTPYWMAPEVIACDENpdatYDYRSDIWSLGITAIEMAEGAPPLCDMHPMRALFLIPR 240
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
710-994 2.27e-18

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: 86.44  E-value: 2.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPI----TAIREIKILRQLT----HQSIINMkeivtdkedaLDFK 781
Cdd:cd14101     7 LLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKLpgvnPVPNEVALLQSVGggpgHRGVIRL----------LDWF 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDKGAFYLVFEYMDH--DLMGLL-ESGLVhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR-GQIKLADFG 857
Cdd:cd14101    77 EIPEGFLLVLERPQHcqDLFDYItERGAL--DESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRtGDIKLIDFG 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARLYSSEesrPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLElisricgspcpav 937
Cdd:cd14101   155 SGATLKDS---MYTDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPFERDTDILKAK------------- 218
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  938 wpdviklPYFNTMkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14101   219 -------PSFNKR----------------VSNDCRSLIRSCLAYNPSDRPSLEQILL 252
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
711-998 2.38e-18

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: 86.91  E-value: 2.38e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILrQLTHQS--IINMKEIVTDKEDALdfkkdkgafy 788
Cdd:cd14197    17 LGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVL-ELAQANpwVINLHEVYETASEMI---------- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEY------MDHDLMGLLESglvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR---GQIKLADFGLA 859
Cdd:cd14197    86 LVLEYaaggeiFNQCVADREEA----FKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEsplGDIKIVDFGLS 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 R-LYSSEESRPYTNkviTLWYRPPELLlgeeRYTP---AIDVWSCGCILGELFTKKPIFQANQELAQLELISRicgspcp 935
Cdd:cd14197   162 RiLKNSEELREIMG---TPEYVAPEIL----SYEPistATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQ------- 227
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  936 avwpdvIKLPYFNtmkpkkqyrrklrEEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14197   228 ------MNVSYSE-------------EEFEHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
710-903 2.42e-18

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: 86.55  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITaiREIKILRQLTHQSIINMKeivtdkeDALDFKKDkgaFYL 789
Cdd:cd14192    11 VLGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVK--NEINIMNQLNHVNLIQLY-------DAFESKTN---LTL 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNIL-LNNRG-QIKLADFGLARLYSSEE 866
Cdd:cd14192    79 IMEYVDGgELFDRITDESYQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILcVNSTGnQIKIIDFGLARRYKPRE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 145309300  867 SrpytnkvITLWYRPPELLLGE----ERYTPAIDVWSCGCI 903
Cdd:cd14192   159 K-------LKVNFGTPEFLAPEvvnyDFVSFPTDMWSVGVI 192
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
702-1014 2.44e-18

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: 87.43  E-value: 2.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgfpitairEIK-ILRQLthqsiinmkEIVTDKEDALDF 780
Cdd:cd06618    14 LNDLENLGEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSGNKE--------ENKrILMDL---------DVVLKSHDCPYI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 KKDKGAF------YLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKK-NFLHRDIKCSNILLNNRGQIKL 853
Cdd:cd06618    77 VKCYGYFitdsdvFICMELMSTCLDKLLKRIQGPIPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGNVKL 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  854 ADFGLA-RLYsseESRPYTNKVITLWYRPPELLLGEE--RYTPAIDVWSCGCILGELFTKKPIFQANQelAQLELISRIC 930
Cdd:cd06618   157 CDFGISgRLV---DSKAKTRSAGCAAYMAPERIDPPDnpKYDIRADVWSLGISLVELATGQFPYRNCK--TEFEVLTKIL 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  931 GSPCPavwpdviKLPYfntmkpkkqyrrklREEF--VFIpaaalDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKMpp 1008
Cdd:cd06618   232 NEEPP-------SLPP--------------NEGFspDFC-----SFVDLCLTKDHRYRPKYRELLQHPFIRRYETAEV-- 283

                  ....*.
gi 145309300 1009 pDLPLW 1014
Cdd:cd06618   284 -DVASW 288
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
704-904 2.98e-18

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: 86.36  E-value: 2.98e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVrldneKEGFPITA--IREIKILRQLTHQSIINMKEIV-TDKEDALdf 780
Cdd:cd14662     1 RYELVKDIGSGNFGVARLMRNKETKELVAVKYI-----ERGLKIDEnvQREIINHRSLRHPNIIRFKEVVlTPTHLAI-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdkgafylVFEYM-DHDLMG-LLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR--GQIKLADF 856
Cdd:cd14662    74 ---------VMEYAaGGELFErICNAG--RFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDF 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 145309300  857 GLARlYSSEESRPYTNkVITLWYRPPELLLGEERYTPAIDVWSCGCIL 904
Cdd:cd14662   143 GYSK-SSVLHSQPKST-VGTPAYIAPEVLSRKEYDGKVADVWSCGVTL 188
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
710-903 3.41e-18

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 86.13  E-value: 3.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgfPITAIREIKILRQLTHQSIINMKEIVTDKEDALdfkkdkgafyL 789
Cdd:cd14190    11 VLGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKD--KEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIV----------L 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG--QIKLADFGLARLYSSEE 866
Cdd:cd14190    79 FMEYVEGgELFERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTghQVKIIDFGLARRYNPRE 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 145309300  867 SrpytnkvITLWYRPPELLLGE----ERYTPAIDVWSCGCI 903
Cdd:cd14190   159 K-------LKVNFGTPEFLSPEvvnyDQVSFPTDMWSMGVI 192
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
685-907 3.85e-18

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: 86.62  E-value: 3.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  685 PRYGETKEKDIDWGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRL-DNEKEGFPITAIREIKILRQLTHQS 763
Cdd:cd08229     6 PQFQPQKALRPDMGYNTLANFRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIfDLMDAKARADCIKEIDLLKQLNHPN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  764 IINM-KEIVTDKEdaldfkkdkgaFYLVFEYMDhdlMGLLESGLVHFN-------ENHIKSFMRQLMEGLDYCHKKNFLH 835
Cdd:cd08229    86 VIKYyASFIEDNE-----------LNIVLELAD---AGDLSRMIKHFKkqkrlipEKTVWKYFVQLCSALEHMHSRRVMH 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  836 RDIKCSNILLNNRGQIKLADFGLARLYSSEESRPYTnKVITLWYRPPElLLGEERYTPAIDVWSCGCILGEL 907
Cdd:cd08229   152 RDIKPANVFITATGVVKLGDLGLGRFFSSKTTAAHS-LVGTPYYMSPE-RIHENGYNFKSDIWSLGCLLYEM 221
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
711-909 4.47e-18

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 86.35  E-value: 4.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNE-----KEGFPItairEIKILRQLTHQSIINMKEIvtdkEDALDFKKDKG 785
Cdd:cd13989     1 LGSGGFGYVTLWKHQDTGEYVAIKKCRQELSpsdknRERWCL----EVQIMKKLNHPNVVSARDV----PPELEKLSPND 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 AFYLVFEYMDH-DLMGLLE-----SGLvhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL---NNRGQIKLADF 856
Cdd:cd13989    73 LPLLAMEYCSGgDLRKVLNqpencCGL---KESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLqqgGGRVIYKLIDL 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 145309300  857 GLARLYSSEESrpYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd13989   150 GYAKELDQGSL--CTSFVGTLQYLAPE-LFESKKYTCTVDYWSFGTLAFECIT 199
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
711-928 4.49e-18

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: 85.68  E-value: 4.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEmVALKKVRLDN-EKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAFYL 789
Cdd:cd05114    12 LGSGLFGVVRLGKWRAQYK-VAIKAIREGAmSEEDF----IEEAKVMMKLTHPKLVQLYGVCTQQK----------PIYI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDHD-LMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESR 868
Cdd:cd05114    77 VTEFMENGcLLNYLRQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYT 156
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  869 PYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTK-KPIFQANQELAQLELISR 928
Cdd:cd05114   157 SSSGAKFPVKWSPPEVFN-YSKFSSKSDVWSFGVLMWEVFTEgKMPFESKSNYEVVEMVSR 216
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
710-929 4.50e-18

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: 86.23  E-value: 4.50e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDN-EKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAFY 788
Cdd:cd05630     7 VLGKGGFGEVCACQVRATGKMYACKKLEKKRiKKRKGEAMALNEKQILEKVNSRFVVSLAYAYETKD----------ALC 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDH-DL-MGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLArlYSSEE 866
Cdd:cd05630    77 LVLTLMNGgDLkFHIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLA--VHVPE 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  867 SRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRI 929
Cdd:cd05630   155 GQTIKGRVGTVGYMAPE-VVKNERYTFSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERL 216
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
711-998 4.61e-18

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: 85.76  E-value: 4.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLD-----NEKEGFPItairEIKILRQLTHQSIINMKeivtdkedalDFKKDKG 785
Cdd:cd14187    15 LGKGGFAKCYEITDADTKEVFAGKIVPKSlllkpHQKEKMSM----EIAIHRSLAHQHVVGFH----------GFFEDND 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 AFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL--YS 863
Cdd:cd14187    81 FVYVVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKveYD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEESRPYTNkviTLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQanqelaqlelisricgspcpavwpdvik 943
Cdd:cd14187   161 GERKKTLCG---TPNYIAPE-VLSKKGHSFEVDIWSIGCIMYTLLVGKPPFE---------------------------- 208
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  944 lpyfnTMKPKKQYRRKLREEFVF---IPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14187   209 -----TSCLKETYLRIKKNEYSIpkhINPVAASLIQKMLQTDPTARPTINELLNDEFF 261
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
711-964 4.85e-18

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: 85.71  E-value: 4.85e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTgemvalKKVRLDNEKEGF--PITAIREIKILRQLTHQSIINMKEIVTdkedaldfkkdKGAFY 788
Cdd:cd05067    15 LGAGQFGEVWMGYYNGH------TKVAIKSLKQGSmsPDAFLAEANLMKQLQHQRLVRLYAVVT-----------QEPIY 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDH-DLMGLLESGLVH-FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL----- 861
Cdd:cd05067    78 IITEYMENgSLVDFLKTPSGIkLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLiedne 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  862 YSSEESRPYTNKvitlWYRPPELLLGEerYTPAIDVWSCGCILGELFTKKPI---FQANQELAQ-LELISRI-CGSPCPA 936
Cdd:cd05067   158 YTAREGAKFPIK----WTAPEAINYGT--FTIKSDVWSFGILLTEIVTHGRIpypGMTNPEVIQnLERGYRMpRPDNCPE 231
                         250       260       270
                  ....*....|....*....|....*....|
gi 145309300  937 VWPDVIKLPYFNT--MKPKKQYRRKLREEF 964
Cdd:cd05067   232 ELYQLMRLCWKERpeDRPTFEYLRSVLEDF 261
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
703-994 4.86e-18

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 85.84  E-value: 4.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVA---LKKVRLDNEKEGFPITAI-REIKILRQLTHQSIINMKEIVTDKEDAL 778
Cdd:cd14194     5 DYYDTGEELGSGQFAVVKKCREKSTGLQYAakfIKKRRTKSSRRGVSREDIeREVSILKEIQHPNVITLHEVYENKTDVI 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 dfkkdkgafyLVFEYMD----HDLMGLLESglvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG----Q 850
Cdd:cd14194    85 ----------LILELVAggelFDFLAEKES----LTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpkpR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  851 IKLADFGLArlYSSEESRPYTNKVITLWYRPPELLlgeeRYTP---AIDVWSCGCILGELFTKKPIFQANQELAQLELIS 927
Cdd:cd14194   151 IKIIDFGLA--HKIDFGNEFKNIFGTPEFVAPEIV----NYEPlglEADMWSIGVITYILLSGASPFLGDTKQETLANVS 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  928 RIcgspcpavwpdviklpyfntmkpkkqyRRKLREEFvFIPAAAL--DLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14194   225 AV---------------------------NYEFEDEY-FSNTSALakDFIRRLLVKDPKKRMTIQDSLQ 265
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
710-915 5.78e-18

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: 85.45  E-value: 5.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALK-----KVRLDNEKEGFPitaiREIKILRQLTHQSIINMKEIVTDKEDaldfkkdk 784
Cdd:cd14188     8 VLGKGGFAKCYEMTDLTTNKVYAAKiiphsRVSKPHQREKID----KEIELHRILHHKHVVQFYHYFEDKEN-------- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gaFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL-ARLYS 863
Cdd:cd14188    76 --IYILLEYCSRRSMAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLaARLEP 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  864 SEESRpytnKVI--TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQ 915
Cdd:cd14188   154 LEHRR----RTIcgTPNYLSPE-VLNKQGHGCESDIWALGCVMYTMLLGRPPFE 202
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
710-928 6.06e-18

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: 85.87  E-value: 6.06e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKV---RLDNEKEGFpiTAIREIKILRQLTHQSIINMkeivtdkedALDFKKdKGA 786
Cdd:cd05605     7 VLGKGGFGEVCACQVRATGKMYACKKLekkRIKKRKGEA--MALNEKQILEKVNSRFVVSL---------AYAYET-KDA 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDH-DL------MGllESGlvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd05605    75 LCLVLTIMNGgDLkfhiynMG--NPG---FEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLA 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  860 rlYSSEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISR 928
Cdd:cd05605   150 --VEIPEGETIRGRVGTVGYMAPE-VVKNERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREEVDR 215
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
707-967 6.56e-18

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: 85.03  E-value: 6.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  707 IIGIIGEGTYGQVYKARDKdtGEMVALKKVRLDNEKEGFpitaIREIKILRQLTHQSIINMKEIVTDkedaldfkkDKGA 786
Cdd:cd05082    10 LLQTIGKGEFGDVMLGDYR--GNKVAVKCIKNDATAQAF----LAEASVMTQLRHSNLVQLLGVIVE---------EKGG 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDH-DLMGLLES-GLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSS 864
Cdd:cd05082    75 LYIVTEYMAKgSLVDYLRSrGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASS 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  865 EESrpyTNKVITLWYRPPELLlgEERYTPAIDVWSCGCILGEL--FTKKPIfqanQELAQLELISRI-------CGSPCP 935
Cdd:cd05082   155 TQD---TGKLPVKWTAPEALR--EKKFSTKSDVWSFGILLWEIysFGRVPY----PRIPLKDVVPRVekgykmdAPDGCP 225
                         250       260       270
                  ....*....|....*....|....*....|...
gi 145309300  936 AVWPDVIKLPYfnTMKPKKQYR-RKLREEFVFI 967
Cdd:cd05082   226 PAVYDVMKNCW--HLDAAMRPSfLQLREQLEHI 256
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
704-998 6.77e-18

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: 85.28  E-value: 6.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFpitAIREIKILRQLTHQSIINMKEIVTDKEDaldfkkd 783
Cdd:cd14087     2 KYDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIETKCRGREV---CESELNVLRRVRHTNIIQLIEVFETKER------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgafylVFEYMDHDLMGLLESGLV---HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG---QIKLADFG 857
Cdd:cd14087    72 ------VYMVMELATGGELFDRIIakgSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYYHPGpdsKIMITDFG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARLYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCPAV 937
Cdd:cd14087   146 LASTRKKGPNCLMKTTCGTPEYIAPEILL-RKPYTQSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYSGEP 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  938 WPDViklpyfntmkpkkqyrrklreefvfiPAAALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14087   225 WPSV--------------------------SNLAKDFIDRLLTVNPGERLSATQALKHPWI 259
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
705-1012 8.03e-18

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 85.82  E-value: 8.03e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARD---KDTGEMVALKKVRldnekegfPITAIREIKIL------RQ-LTHqsiINMKEIVTDK 774
Cdd:cd05613     2 FELLKVLGTGAYGKVFLVRKvsgHDAGKLYAMKVLK--------KATIVQKAKTAehtrteRQvLEH---IRQSPFLVTL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  775 EDAldFKKDKgAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLA 854
Cdd:cd05613    71 HYA--FQTDT-KLHLILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLT 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  855 DFGLARLYSSEESRPYTNKVITLWYRPPELLL-GEERYTPAIDVWSCGCILGELFTKKPIFQANQEL-AQLELISRICGS 932
Cdd:cd05613   148 DFGLSKEFLLDENERAYSFCGTIEYMAPEIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFTVDGEKnSQAEISRRILKS 227
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  933 pcpavwpdviKLPYFNTMKPkkqyrrklreefvfipaAALDLFDYMLALDPSKRC-----TAEQALQCEFLR-----DVE 1002
Cdd:cd05613   228 ----------EPPYPQEMSA-----------------LAKDIIQRLLMKDPKKRLgcgpnGADEIKKHPFFQkinwdDLA 280
                         330
                  ....*....|
gi 145309300 1003 PSKMPPPDLP 1012
Cdd:cd05613   281 AKKVPAPFKP 290
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
711-1011 8.43e-18

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 86.08  E-value: 8.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKV--RLDNEKEgfpitaiREIKILRQL-THQSIINMKEIVTDKEDAldfkkdkgaf 787
Cdd:cd14180    14 LGEGSFSVCRKCRHRQSGQEYAVKIIsrRMEANTQ-------REVAALRLCqSHPNIVALHEVLHDQYHT---------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDHDlmGLLE--SGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ---IKLADFGLARLY 862
Cdd:cd14180    77 YLVMELLRGG--ELLDriKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADESDgavLKVIDFGFARLR 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 sSEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRIcgspcpavwpdvi 942
Cdd:cd14180   155 -PQGSRPLQTPCFTLQYAAPE-LFSNQGYDESCDLWSLGVILYTMLSGQVPFQSKRGKMFHNHAADI------------- 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  943 klpyfntMKPKKQYRRKLR-EEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEPSKMPP---PDL 1011
Cdd:cd14180   220 -------MHKIKEGDFSLEgEAWKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQGGSALSSTPlmtPDV 285
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
711-912 8.89e-18

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: 85.12  E-value: 8.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDnEKEGFPITAIREIKILRQLTHQSIINMKEivtdkedalDFKKDKgAFYLV 790
Cdd:cd06641    12 IGKGSFGEVFKGIDNRTQKVVAIKIIDLE-EAEDEIEDIQQEITVLSQCDSPYVTKYYG---------SYLKDT-KLWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDH-DLMGLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA-RLYSSEESR 868
Cdd:cd06641    81 MEYLGGgSALDLLEPG--PLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAgQLTDTQIKR 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 145309300  869 pyTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKP 912
Cdd:cd06641   159 --N*FVGTPFWMAPE-VIKQSAYDSKADIWSLGITAIELARGEP 199
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
704-978 8.94e-18

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 88.60  E-value: 8.94e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYK-ARDKDTGEMVALKKVRLDNEKEG---------------FPITAIREIKILRQLTHQSIINM 767
Cdd:PHA03210  149 HFRVIDDLPAGAFGKIFIcALRASTEEAEARRGVNSTNQGKPkcerliakrvkagsrAAIQLENEILALGRLNHENILKI 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  768 KEIVTDKEDAldfkkdkgafYLVFEYMDHDLMGLLESGLVHFNEN----HIKSFMRQLMEGLDYCHKKNFLHRDIKCSNI 843
Cdd:PHA03210  229 EEILRSEANT----------YMITQKYDFDLYSFMYDEAFDWKDRpllkQTRAIMKQLLCAVEYIHDKKLIHRDIKLENI 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  844 LLNNRGQIKLADFGLARLYSSE-ESRPYtNKVITLWYRPPELLLGEErYTPAIDVWSCGCILgelftkkpifqanqelaq 922
Cdd:PHA03210  299 FLNCDGKIVLGDFGTAMPFEKErEAFDY-GWVGTVATNSPEILAGDG-YCEITDIWSCGLIL------------------ 358
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  923 LELISRicgSPCPAvwpdviklpYFNTMKPKKQYRRKLR------EEFvfiPAAALDLFDYM 978
Cdd:PHA03210  359 LDMLSH---DFCPI---------GDGGGKPGKQLLKIIDslsvcdEEF---PDPPCKLFDYI 405
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
711-938 9.91e-18

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: 84.87  E-value: 9.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKK-VRLDNE-KEGFpitaIREIKILRQLTHQSIINMKEIVTdkedaldfkKDKgAFY 788
Cdd:cd14154     1 LGKGFFGQAIKVTHRETGEVMVMKElIRFDEEaQRNF----LKEVKVMRSLDHPNVLKFIGVLY---------KDK-KLN 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDHD-LMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEES 867
Cdd:cd14154    67 LITEYIPGGtLKDVLKDMARPLPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLARLIVEERL 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  868 RPYTNK-------------------VITLWYRPPELLLGEErYTPAIDVWSCGCILGEL----------FTKKPIFQANQ 918
Cdd:cd14154   147 PSGNMSpsetlrhlkspdrkkrytvVGNPYWMAPEMLNGRS-YDEKVDIFSFGIVLCEIigrveadpdyLPRTKDFGLNV 225
                         250       260
                  ....*....|....*....|
gi 145309300  919 ElaqlELISRICgSPCPAVW 938
Cdd:cd14154   226 D----SFREKFC-AGCPPPF 240
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
704-906 1.03e-17

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: 85.17  E-value: 1.03e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMV-ALKKVRLDNEKEGFPITAIREIKILRQLT---HQSIINMkeivtdkedaLD 779
Cdd:cd14052     1 RFANVELIGSGEFSQVYKVSERVPTGKVyAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQL----------ID 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FKKDKGAFYLVFEYMDH-DLMGLLE--SGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd14052    71 SWEYHGHLYIQTELCENgSLDVFLSelGLLGRLDEFRVWKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDF 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSEESRPYTNKVItlwYRPPELLLGEERYTPAiDVWSCGCILGE 906
Cdd:cd14052   151 GMATVWPLIRGIEREGDRE---YIAPEILSEHMYDKPA-DIFSLGLILLE 196
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
703-907 1.07e-17

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: 85.29  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPiTAIREIKILRQLTHQSIINMKEIVTDKedaldfkk 782
Cdd:cd06622     1 DEIEVLDELGKGNYGSVYKVLHRPTGVTMAMKEIRLELDESKFN-QIIMELDILHKAVSPYIVDFYGAFFIE-------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkGAFYLVFEYMDHDLMGLLESGLVHFN---ENHIKSFMRQLMEGLDYCHKK-NFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd06622    72 --GAVYMCMEYMDAGSLDKLYAGGVATEgipEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGV 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  859 ARlySSEESRPYTNkVITLWYRPPELLLGEE-----RYTPAIDVWSCGCILGEL 907
Cdd:cd06622   150 SG--NLVASLAKTN-IGCQSYMAPERIKSGGpnqnpTYTVQSDVWSLGLSILEM 200
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
711-1003 1.08e-17

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


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 85.46  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKvrLDNEKEGFPITAIREIKILRQLTHQSIINMKE--IVTDKedaldfkkdkgaFY 788
Cdd:cd06657    28 IGEGSTGIVCIATVKSSGKLVAVKK--MDLRKQQRRELLFNEVVIMRDYQHENVVEMYNsyLVGDE------------LW 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDHdlmGLLESGLVH--FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEE 866
Cdd:cd06657    94 VVMEFLEG---GALTDIVTHtrMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQVSKEV 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  867 SRpYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISricgspcpavwpdviklpy 946
Cdd:cd06657   171 PR-RKSLVGTPYWMAPE-LISRLPYGPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIR------------------- 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  947 fNTMKPKKQYRRKlreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVEP 1003
Cdd:cd06657   230 -DNLPPKLKNLHK-------VSPSLKGFLDRLLVRDPAQRATAAELLKHPFLAKAGP 278
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
711-942 1.13e-17

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: 84.41  E-value: 1.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEmVALKKVRLDNEKEGFPITaiREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAFYLV 790
Cdd:cd05148    14 LGSGYFGEVWEGLWKNRVR-VAIKILKSDDLLKQQDFQ--KEVQALKRLRHKHLISLFAVCSVGE----------PVYII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDH-DLMGLLES--GLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL-----Y 862
Cdd:cd05148    81 TELMEKgSLLAFLRSpeGQV-LPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLikedvY 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEESR-PYTnkvitlWYRPPEllLGEERYTPAIDVWSCGCILGELFTKKPI---FQANQELaqLELISRICGSPCPAVW 938
Cdd:cd05148   160 LSSDKKiPYK------WTAPEA--ASHGTFSTKSDVWSFGILLYEMFTYGQVpypGMNNHEV--YDQITAGYRMPCPAKC 229

                  ....
gi 145309300  939 PDVI 942
Cdd:cd05148   230 PQEI 233
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
710-1060 1.26e-17

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: 85.83  E-value: 1.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVR----LDNEKEGFPITairEIKILRQLTHQSIINMKeIVTDKEDALDFkkdkg 785
Cdd:cd05595     2 LLGKGTFGKVILVREKATGRYYAMKILRkeviIAKDEVAHTVT---ESRVLQNTRHPFLTALK-YAFQTHDRLCF----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 afylVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSE 865
Cdd:cd05595    73 ----VMEYANGGELFFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEGITD 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  866 ESrpyTNKVI--TLWYRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGspcpavwpdviK 943
Cdd:cd05595   149 GA---TMKTFcgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEM---------------------MCG-----------R 192
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  944 LPYFNtMKPKKQYRRKLREEFVF---IPAAALDLFDYMLALDPSKRC-----TAEQALQCEFL-----RDVEPSKMPPPD 1010
Cdd:cd05595   193 LPFYN-QDHERLFELILMEEIRFprtLSPEAKSLLAGLLKKDPKQRLgggpsDAKEVMEHRFFlsinwQDVVQKKLLPPF 271
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|..
gi 145309300 1011 LPlwqdchELWSKKRRRQKQMGMTDDVSTIKAPRKDLSLGLDDS--RTNTPQ 1060
Cdd:cd05595   272 KP------QVTSEVDTRYFDDEFTAQSITITPPDRYDSLDLLESdqRTHFPQ 317
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
711-909 1.62e-17

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: 83.94  E-value: 1.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKdtGEMVALKKVRLD-NEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKedaldfkkdkGAFYL 789
Cdd:cd05039    14 IGKGEFGDVMLGDYR--GQKVAVKCLKDDsTAAQAF----LAEASVMTTLRHPNLVQLLGVVLEG----------NGLYI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLMGLLES-GLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARlysSEES 867
Cdd:cd05039    78 VTEYMAKgSLVDYLRSrGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAK---EASS 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 145309300  868 RPYTNKVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFT 909
Cdd:cd05039   155 NQDGGKLPIKWTAPEALREK--KFSTKSDVWSFGILLWEIYS 194
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
703-933 1.83e-17

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: 85.91  E-value: 1.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPITAIREIKILRQLTHQSIINMKEIvtdkeDALDFKK 782
Cdd:cd14227    15 NTYEVLEFLGRGTFGQVVKCWKRGTNEIVAIKILK---NHPSYARQGQIEVSILARLSTESADDYNFV-----RAYECFQ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFYLVFEYMDHDLMGLL-ESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ----IKLADFG 857
Cdd:cd14227    87 HKNHTCLVFEMLEQNLYDFLkQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPSRqpyrVKVIDFG 166
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  858 LARLYSSEESRPYTNkviTLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSP 933
Cdd:cd14227   167 SASHVSKAVCSTYLQ---SRYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQGLP 238
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
711-909 1.91e-17

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


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 84.64  E-value: 1.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGE--------------MVALKKVRLD---NEKEGFpitaIREIKILRQLTHQSIINMKEIVTd 773
Cdd:cd05097    13 LGEGQFGEVHLCEAEGLAEflgegapefdgqpvLVAVKMLRADvtkTARNDF----LKEIKIMSRLKNPNIIRLLGVCV- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  774 KEDALdfkkdkgafYLVFEYMDH-DLMGLL-----ESGLVHfnENHIKSFMR--------QLMEGLDYCHKKNFLHRDIK 839
Cdd:cd05097    88 SDDPL---------CMITEYMENgDLNQFLsqreiESTFTH--ANNIPSVSIanllymavQIASGMKYLASLNFVHRDLA 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  840 CSNILLNNRGQIKLADFGLAR-LYSSEESRPYTNKVITL-WYRPPELLLGeeRYTPAIDVWSCGCILGELFT 909
Cdd:cd05097   157 TRNCLVGNHYTIKIADFGMSRnLYSGDYYRIQGRAVLPIrWMAWESILLG--KFTTASDVWAFGVTLWEMFT 226
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
711-964 2.17e-17

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


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 83.44  E-value: 2.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRlDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAFYLV 790
Cdd:cd05084     4 IGRGNFGEVFSGRLRADNTPVAVKSCR-ETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQ----------PIYIV 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARlysSEESRP 869
Cdd:cd05084    73 MELVQGgDFLTFLRTEGPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSR---EEEDGV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  870 YT-----NKVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFTKKPIFQANQELAQL-ELISRICGSPCPAVWPDVIk 943
Cdd:cd05084   150 YAatggmKQIPVKWTAPEALNYG--RYSSESDVWSFGILLWETFSLGAVPYANLSNQQTrEAVEQGVRLPCPENCPDEV- 226
                         250       260
                  ....*....|....*....|.
gi 145309300  944 lpyFNTMKPKKQYRRKLREEF 964
Cdd:cd05084   227 ---YRLMEQCWEYDPRKRPSF 244
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
711-857 2.27e-17

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: 80.18  E-value: 2.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKkvRLDNEKEGFPITAIREIKILRQLT--HQSIINMkeivtdkedaLDFKKDKGAFY 788
Cdd:cd13968     1 MGEGASAKVFWAEGECTTIGVAVK--IGDDVNNEEGEDLESEMDILRRLKglELNIPKV----------LVTEDVDGPNI 68
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  789 LVFEYMDHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG 857
Cdd:cd13968    69 LLMELVKGGTLIAYTQE-EELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
711-928 2.48e-17

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: 83.95  E-value: 2.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDnEKEGFPITAIREIKILRQLTHQSIInmkeivtdKEDALDFKKDKgaFYLV 790
Cdd:cd06642    12 IGKGSFGEVYKGIDNRTKEVVAIKIIDLE-EAEDEIEDIQQEITVLSQCDSPYIT--------RYYGSYLKGTK--LWII 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDH-DLMGLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRP 869
Cdd:cd06642    81 MEYLGGgSALDLLKPG--PLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIKR 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  870 YTNKVITLWYRPPelLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISR 928
Cdd:cd06642   159 NTFVGTPFWMAPE--VIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIPK 215
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
703-993 2.53e-17

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: 83.54  E-value: 2.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVrlDNEK-EGFPITAIREIKILRQLTHQSIINM-KEIVTDKEdaldf 780
Cdd:cd14184     1 EKYKIGKVIGDGNFAVVKECVERSTGKEFALKII--DKAKcCGKEHLIENEVSILRRVKHPNIIMLiEEMDTPAE----- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdkgaFYLVFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL----NNRGQIKLAD 855
Cdd:cd14184    74 ------LYLVMELVKGgDLFDAITSS-TKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  856 FGLARLYSSeesrPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELaQLELISRICGSPCP 935
Cdd:cd14184   147 FGLATVVEG----PLYTVCGTPTYVAPE-IIAETGYGLKVDIWAAGVITYILLCGFPPFRSENNL-QEDLFDQILLGKLE 220
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  936 avWPDviklPYFNTmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQAL 993
Cdd:cd14184   221 --FPS----PYWDN-----------------ITDSAKELISHMLQVNVEARYTAEQIL 255
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
711-942 2.95e-17

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: 83.58  E-value: 2.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEmVALKKVRLDNEKegfPITAIREIKILRQLTHQSIINMKEIVTDKedaldfkkdkgAFYLV 790
Cdd:cd05071    17 LGQGCFGEVWMGTWNGTTR-VAIKTLKPGTMS---PEAFLQEAQVMKKLRHEKLVQLYAVVSEE-----------PIYIV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDhdlmgllESGLVHFNENHIKSFMR---------QLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL 861
Cdd:cd05071    82 TEYMS-------KGSLLDFLKGEMGKYLRlpqlvdmaaQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARL 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  862 YSSEEsrpYT----NKVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFTKK----PIFQANQELAQLELISRI-CGS 932
Cdd:cd05071   155 IEDNE---YTarqgAKFPIKWTAPEAALYG--RFTIKSDVWSFGILLTELTTKGrvpyPGMVNREVLDQVERGYRMpCPP 229
                         250
                  ....*....|
gi 145309300  933 PCPAVWPDVI 942
Cdd:cd05071   230 ECPESLHDLM 239
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
711-940 2.97e-17

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: 83.97  E-value: 2.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYkardkdTGEMVALKKVRLDNEKEG--FPITAIREIKILRQLTHQSIINMKEIVTDKedaldfkkdkgAFY 788
Cdd:cd05069    20 LGQGCFGEVW------MGTWNGTTKVAIKTLKPGtmMPEAFLQEAQIMKKLRHDKLVPLYAVVSEE-----------PIY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDH-DLMGLLESGL-VHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEE 866
Cdd:cd05069    83 IVTEFMGKgSLLDFLKEGDgKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  867 srpYT----NKVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFTKKPI---FQANQELaqLELISRICGSPCPAVWP 939
Cdd:cd05069   163 ---YTarqgAKFPIKWTAPEAALYG--RFTIKSDVWSFGILLTELVTKGRVpypGMVNREV--LEQVERGYRMPCPQGCP 235

                  .
gi 145309300  940 D 940
Cdd:cd05069   236 E 236
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
711-1000 3.40e-17

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


Pssm-ID: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 84.32  E-value: 3.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKV--RLDNEKEgfpitaiREIKILRQL-THQSIINMKEIVTDKEDAldfkkdkgaf 787
Cdd:cd14179    15 LGEGSFSICRKCLHKKTNQEYAVKIVskRMEANTQ-------REIAALKLCeGHPNIVKLHEVYHDQLHT---------- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEymdhdlmgLLESGLV--------HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL---NNRGQIKLADF 856
Cdd:cd14179    78 FLVME--------LLKGGELlerikkkqHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDF 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLySSEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQElaqleliSRICGSPcpa 936
Cdd:cd14179   150 GFARL-KPPDNQPLKTPCFTLHYAAPE-LLNYNGYDESCDLWSLGVILYTMLSGQVPFQCHDK-------SLTCTSA--- 217
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  937 vwpdviklpyFNTMKPKKQYRRKLR-EEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRD 1000
Cdd:cd14179   218 ----------EEIMKKIKQGDFSFEgEAWKNVSQEAKDLIQGLLTVDPNKRIKMSGLRYNEWLQD 272
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
710-964 3.52e-17

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: 82.75  E-value: 3.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEmVALKKVRLDNEKEgFPITAIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAFYL 789
Cdd:cd05085     3 LLGKGNFGEVYKGTLKDKTP-VAVKTCKEDLPQE-LKIKFLSEARILKQYDHPNIVKLIGVCTQRQ----------PIYI 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR-----LYS 863
Cdd:cd05085    71 VMELVPGgDFLSFLRKKKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRqeddgVYS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEESRPYTNKvitlWYRPPELLLGeeRYTPAIDVWSCGCILGELFT----KKPIFQANQELAQLELISRICgspCPAVWP 939
Cdd:cd05085   151 SSGLKQIPIK----WTAPEALNYG--RYSSESDVWSFGILLWETFSlgvcPYPGMTNQQAREQVEKGYRMS---APQRCP 221
                         250       260
                  ....*....|....*....|....*
gi 145309300  940 DVIklpyFNTMKPKKQYRRKLREEF 964
Cdd:cd05085   222 EDI----YKIMQRCWDYNPENRPKF 242
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
711-909 3.82e-17

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: 82.88  E-value: 3.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVY--KARDKDTgemVALKKVRLDN-EKEGFpitaIREIKILRQLTHQSIINMKEIVTDKedaldfkkdkGAF 787
Cdd:cd05059    12 LGSGQFGVVHlgKWRGKID---VAIKMIKEGSmSEDDF----IEEAKVMMKLSHPKLVQLYGVCTKQ----------RPI 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDHD-LMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEE 866
Cdd:cd05059    75 FIVTEYMANGcLLNYLRERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDE 154
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 145309300  867 srpYTNKVITLW---YRPPELLLgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05059   155 ---YTSSVGTKFpvkWSPPEVFM-YSKFSSKSDVWSFGVLMWEVFS 196
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
703-963 3.92e-17

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: 84.76  E-value: 3.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPITAIREIKILRQLThqsiinmkeivTDKEDALDFKK 782
Cdd:cd14228    15 NSYEVLEFLGRGTFGQVAKCWKRSTKEIVAIKILK---NHPSYARQGQIEVSILSRLS-----------SENADEYNFVR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFY------LVFEYMDHDLMGLL-ESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL----NNRGQI 851
Cdd:cd14228    81 SYECFQhknhtcLVFEMLEQNLYDFLkQNKFSPLPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLvdpvRQPYRV 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  852 KLADFGLARLYSSEESRPYTNkviTLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICG 931
Cdd:cd14228   161 KVIDFGSASHVSKAVCSTYLQ---SRYYRAPEIILGLP-FCEAIDMWSLGCVIAELFLGWPLYPGASEYDQIRYISQTQG 236
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 145309300  932 SPCPAVWPDVIKLPYFNTMKPKKQY---RRKLREE 963
Cdd:cd14228   237 LPAEYLLSAGTKTSRFFNRDPNLGYplwRLKTPEE 271
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
711-909 3.95e-17

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: 82.54  E-value: 3.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKdtGEMVALKKVRldNEKEgfpitaiREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAFYLV 790
Cdd:cd14059     1 LGSGAQGAVFLGKFR--GEEVAVKKVR--DEKE-------TDIKHLRKLNHPNIIKFKGVCTQAP----------CYCIL 59
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDH-DLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYsSEESRP 869
Cdd:cd14059    60 MEYCPYgQLYEVLRAGRE-ITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKEL-SEKSTK 137
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 145309300  870 YTNKVITLWYRPPelLLGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd14059   138 MSFAGTVAWMAPE--VIRNEPCSEKVDIWSFGVVLWELLT 175
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
703-939 4.58e-17

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: 83.19  E-value: 4.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKardkdtGEMVALKKVRLDNEKEGF--PITAIREIKILRQLTHQSIINMKEIVTDKedaldf 780
Cdd:cd05070     9 ESLQLIKRLGNGQFGEVWM------GTWNGNTKVAIKTLKPGTmsPESFLEEAQIMKKLKHDKLVQLYAVVSEE------ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdkgAFYLVFEYMDH-DLMGLLESGLVH-FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd05070    77 -----PIYIVTEYMSKgSLLDFLKDGEGRaLKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYSSEESRPYTN-KVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFTKKPI-FQANQELAQLELISRICGSPCPA 936
Cdd:cd05070   152 ARLIEDNEYTARQGaKFPIKWTAPEAALYG--RFTIKSDVWSFGILLTELVTKGRVpYPGMNNREVLEQVERGYRMPCPQ 229

                  ...
gi 145309300  937 VWP 939
Cdd:cd05070   230 DCP 232
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
711-904 4.90e-17

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: 83.09  E-value: 4.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALK---KVRLdNEKEGFP---------------------ITAI-REIKILRQLTHQSII 765
Cdd:cd14199    10 IGKGSYGVVKLAYNEDDNTYYAMKvlsKKKL-MRQAGFPrrppprgaraapegctqprgpIERVyQEIAILKKLDHPNVV 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  766 NMKEIVTD-KEDALdfkkdkgafYLVFEymdhdlmgLLESGLVH-------FNENHIKSFMRQLMEGLDYCHKKNFLHRD 837
Cdd:cd14199    89 KLVEVLDDpSEDHL---------YMVFE--------LVKQGPVMevptlkpLSEDQARFYFQDLIKGIEYLHYQKIIHRD 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  838 IKCSNILLNNRGQIKLADFGLARLYSSEESRpYTNKVITLWYRPPElLLGEERYT---PAIDVWSCGCIL 904
Cdd:cd14199   152 VKPSNLLVGEDGHIKIADFGVSNEFEGSDAL-LTNTVGTPAFMAPE-TLSETRKIfsgKALDVWAMGVTL 219
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
704-912 5.43e-17

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: 82.94  E-value: 5.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPItaIREIKILRQLT-HQSIINMKEIVTDKEDALDfkk 782
Cdd:cd14036     1 KLRIKRVIAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAI--IQEINFMKKLSgHPNIVQFCSAASIGKEESD--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFYLVfeymdhdLMGLLESGLV----------HFNENHIKSFMRQLMEGLDYCHKKN--FLHRDIKCSNILLNNRGQ 850
Cdd:cd14036    76 QGQAEYLL-------LTELCKGQLVdfvkkveapgPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQ 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  851 IKLADFGLArlySSEESRP-YT-------------NKVITLWYRPPELLLGEERY--TPAIDVWSCGCILGEL-FTKKP 912
Cdd:cd14036   149 IKLCDFGSA---TTEAHYPdYSwsaqkrslvedeiTRNTTPMYRTPEMIDLYSNYpiGEKQDIWALGCILYLLcFRKHP 224
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
710-940 5.85e-17

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: 83.00  E-value: 5.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgFPITAIREIKILRQLTHQSIINMKeivtdkedaldfkkdkGAFY- 788
Cdd:cd06619     8 ILGHGNGGTVYKAYHLLTRRILAVKVIPLDITVE-LQKQIMSELEILYKCDSPYIIGFY----------------GAFFv 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 -----LVFEYMDHDLMGLLESglvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYS 863
Cdd:cd06619    71 enrisICTEFMDGGSLDVYRK----IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLV 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEESRPYtnkVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKK---PIFQANQ-ELAQLELISRICGSPCPaVWP 939
Cdd:cd06619   147 NSIAKTY---VGTNAYMAPERISGEQ-YGIHSDVWSLGISFMELALGRfpyPQIQKNQgSLMPLQLLQCIVDEDPP-VLP 221

                  .
gi 145309300  940 D 940
Cdd:cd06619   222 V 222
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
696-923 6.83e-17

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 86.71  E-value: 6.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  696 DWGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKE 775
Cdd:PTZ00266    6 DDGESRLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRFLNKA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  776 DAldfkkdkgAFYLVFEYMDH-DLMGLLESGLVHF---NENHIKSFMRQLMEGLDYCHK-------KNFLHRDIKCSNIL 844
Cdd:PTZ00266   86 NQ--------KLYILMEFCDAgDLSRNIQKCYKMFgkiEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIF 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  845 -----------------LNNRGQIKLADFGLARLYSSEESRpyTNKVITLWYRPPELLLGEER-YTPAIDVWSCGCILGE 906
Cdd:PTZ00266  158 lstgirhigkitaqannLNGRPIAKIGDFGLSKNIGIESMA--HSCVGTPYYWSPELLLHETKsYDDKSDMWALGCIIYE 235
                         250
                  ....*....|....*..
gi 145309300  907 LFTKKPIFQANQELAQL 923
Cdd:PTZ00266  236 LCSGKTPFHKANNFSQL 252
pknD PRK13184
serine/threonine-protein kinase PknD;
704-909 6.95e-17

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 86.75  E-value: 6.95e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVR---LDNE--KEGFpitaIREIKILRQLTHQSIINMKEIVTDKEdal 778
Cdd:PRK13184    3 RYDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIRedlSENPllKKRF----LREAKIAADLIHPGIVPVYSICSDGD--- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 dfkkdkgAFYLVFEYMD-HDLMGLLES-------GLVHFNENHIKSFMR---QLMEGLDYCHKKNFLHRDIKCSNILLNN 847
Cdd:PRK13184   76 -------PVYYTMPYIEgYTLKSLLKSvwqkeslSKELAEKTSVGAFLSifhKICATIEYVHSKGVLHRDLKPDNILLGL 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  848 RGQIKLADFGLARLYSSEE------SRPYTN----------KVI-TLWYRPPELLLGEERyTPAIDVWSCGCILGELFT 909
Cdd:PRK13184  149 FGEVVILDWGAAIFKKLEEedlldiDVDERNicyssmtipgKIVgTPDYMAPERLLGVPA-SESTDIYALGVILYQMLT 226
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
711-935 7.05e-17

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: 82.78  E-value: 7.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKAR------DKDTgEMVALKKVR--LDNEKEGFPitaiREIKILRQLTHQSIINMKEIVTDKEDALdfkk 782
Cdd:cd05093    13 LGEGAFGKVFLAEcynlcpEQDK-ILVAVKTLKdaSDNARKDFH----REAELLTNLQHEHIVKFYGVCVEGDPLI---- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgafyLVFEYMDH-DLMGLLES------------GLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG 849
Cdd:cd05093    84 ------MVFEYMKHgDLNKFLRAhgpdavlmaegnRPAELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  850 QIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT--KKPIFQ-ANQELAQLEL 925
Cdd:cd05093   158 LVKIGDFGMSRdVYSTDYYRVGGHTMLPIRWMPPESIM-YRKFTTESDVWSLGVVLWEIFTygKQPWYQlSNNEVIECIT 236
                         250
                  ....*....|..
gi 145309300  926 ISRICGSP--CP 935
Cdd:cd05093   237 QGRVLQRPrtCP 248
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
788-997 8.31e-17

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: 82.02  E-value: 8.31e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDHDLMG-LLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN---RGQIKLADFGLARLYS 863
Cdd:cd14012    80 YLLTEYAPGGSLSeLLDSVG-SVPLDTARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLDRdagTGIVKLTDYSLGKTLL 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWScgciLGELFtkkpifqanqelaqlelISRICGSPCPAvwpdvik 943
Cdd:cd14012   159 DMCSRGSLDEFKQTYWLPPELAQGSKSPTRKTDVWD----LGLLF-----------------LQMLFGLDVLE------- 210
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  944 lpYFNTMKPKKqyrrklreEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEF 997
Cdd:cd14012   211 --KYTSPNPVL--------VSLDLSASLQDFLSKCLSLDPKKRPTALELLPHEF 254
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
704-999 8.49e-17

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 82.22  E-value: 8.49e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgfpITAIREIKILRQLTHQSIINMKEIVTDKEDaldfkkd 783
Cdd:cd14104     1 KYMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQ---VLVKKEISILNIARHRNILRLHESFESHEE------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgaFYLVFEYMD-HDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR--GQIKLADFGLAR 860
Cdd:cd14104    71 ---LVMIFEFISgVDIFERITTARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRrgSYIKIIEFGQSR 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 lysseESRPYTNkvITLWYRPPELLLGE----ERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELIsricgspCPA 936
Cdd:cd14104   148 -----QLKPGDK--FRLQYTSAEFYAPEvhqhESVSTATDMWSLGCLVYVLLSGINPFEAETNQQTIENI-------RNA 213
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  937 VWPdviklpyFNTmkpkkqyrrklrEEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLR 999
Cdd:cd14104   214 EYA-------FDD------------EAFKNISIEALDFVDRLLVKERKSRMTAQEALNHPWLK 257
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
711-909 9.18e-17

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: 81.79  E-value: 9.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITA--IREIKILRQLTHQSIINMKEIVtdkedaldfkKDKGAFY 788
Cdd:cd14070    10 LGEGSFAKVREGLHAVTGEKVAIKVIDKKKAKKDSYVTKnlRREGRIQQMIRHPNITQLLDIL----------ETENSYY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEY-MDHDLMGLLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEE- 866
Cdd:cd14070    80 LVMELcPGGNLMHRIYDKK-RLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGy 158
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 145309300  867 SRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd14070   159 SDPFSTQCGSPAYAAPE-LLARKKYGPKVDVWSIGVNMYAMLT 200
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
700-907 1.17e-16

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: 82.23  E-value: 1.17e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  700 RCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRL-DNEKEGFPItaIREIKILRQLTHQSIIN-MKEIVTDKEDA 777
Cdd:cd14048     3 RFLTDFEPIQCLGRGGFGVVFEAKNKVDDCNYAVKRIRLpNNELAREKV--LREVRALAKLDHPGIVRyFNAWLERPPEG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 LDFKKDKGAFYLVF---------EYMDHDLMglLESGLVHFNENHIKsfmrQLMEGLDYCHKKNFLHRDIKCSNILLNNR 848
Cdd:cd14048    81 WQEKMDEVYLYIQMqlcrkenlkDWMNRRCT--MESRELFVCLNIFK----QIASAVEYLHSKGLIHRDLKPSNVFFSLD 154
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  849 GQIKLADFGLAR-----------LYSSEESRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILGEL 907
Cdd:cd14048   155 DVVKVGDFGLVTamdqgepeqtvLTPMPAYAKHTGQVGTRLYMSPEQIHGNQ-YSEKVDIFALGLILFEL 223
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
711-993 1.18e-16

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 81.89  E-value: 1.18e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILrQLTHQS--IINMKEIV-TDKEDALDFKKDKGAf 787
Cdd:cd14198    16 LGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVL-ELAKSNprVVNLHEVYeTTSEIILILEYAAGG- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 yLVFEYMDHDLMGLLesglvhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL---NNRGQIKLADFGLAR-LYS 863
Cdd:cd14198    94 -EIFNLCVPDLAEMV-------SENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLssiYPLGDIKIVDFGMSRkIGH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEESRPYTNkviTLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIF--QANQElaqlelisricgspcpavwpdv 941
Cdd:cd14198   166 ACELREIMG---TPEYLAPE-ILNYDPITTATDMWNIGVIAYMLLTHESPFvgEDNQE---------------------- 219
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 145309300  942 iklPYFNTMKPKKQYRrklREEFVFIPAAALDLFDYMLALDPSKRCTAEQAL 993
Cdd:cd14198   220 ---TFLNISQVNVDYS---EETFSSVSQLATDFIQKLLVKNPEKRPTAEICL 265
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
710-994 1.29e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 82.00  E-value: 1.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPITAI-REIKILRQLT-HQSIINMkeivtdkedaLDFKKDKGAF 787
Cdd:cd14173     9 VLGEGAYARVQTCINLITNKEYAVKIIE---KRPGHSRSRVfREVEMLYQCQgHRNVLEL----------IEFFEEEDKF 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQI---KLADFGLAR--LY 862
Cdd:cd14173    76 YLVFEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDLGSgiKL 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEESRPYTNKVIT----LWYRPPELL--LGEER--YTPAIDVWSCGCILGELFTKKPIFQANqelaqlelisriCGSPC 934
Cdd:cd14173   156 NSDCSPISTPELLTpcgsAEYMAPEVVeaFNEEAsiYDKRCDLWSLGVILYIMLSGYPPFVGR------------CGSDC 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  935 PAVW----PDVIKLPYFNTMKPKKQYRRKlreEFVFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14173   224 GWDRgeacPACQNMLFESIQEGKYEFPEK---DWAHISCAAKDLISKLLVRDAKQRLSAAQVLQ 284
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
704-998 1.36e-16

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


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 83.16  E-value: 1.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPITAIREIKILRQLTHQSIIN-MKEIVTDKEDALDFKK 782
Cdd:cd14216    11 RYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVK---SAEHYTETALDEIKLLKSVRNSDPNDpNREMVVQLLDDFKISG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFY-LVFEYMDHDLMG-LLESGLVHFNENHIKSFMRQLMEGLDYCHKK-NFLHRDIKCSNILLN------------- 846
Cdd:cd14216    88 VNGTHIcMVFEVLGHHLLKwIIKSNYQGLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILLSvneqyirrlaaea 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  847 -----------------NRGQIKLADFGLArlysSEESRPYTNKVITLWYRPPELLLGEERYTPAiDVWSCGCILGELFT 909
Cdd:cd14216   168 tewqrnflvnplepknaEKLKVKIADLGNA----CWVHKHFTEDIQTRQYRSLEVLIGSGYNTPA-DIWSTACMAFELAT 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  910 KKPIFQ--ANQELAQ--------LELISRI------CGSPCPAVWPDVIKLPYFNTMKPKKQYrRKLREEFVFIPAAALD 973
Cdd:cd14216   243 GDYLFEphSGEDYSRdedhialiIELLGKVprklivAGKYSKEFFTKKGDLKHITKLKPWGLF-EVLVEKYEWSQEEAAG 321
                         330       340
                  ....*....|....*....|....*...
gi 145309300  974 LFDY---MLALDPSKRCTAEQALQCEFL 998
Cdd:cd14216   322 FTDFllpMLELIPEKRATAAECLRHPWL 349
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
711-942 1.44e-16

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: 81.24  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKA--RDKDTGEM-VA---LKKVRLDNEKEGFpitaIREIKILRQLTHQSIINMkeIVTDKEDAldfkkdk 784
Cdd:cd05060     3 LGHGNFGSVRKGvyLMKSGKEVeVAvktLKQEHEKAGKKEF----LREASVMAQLDHPCIVRL--IGVCKGEP------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gaFYLVFEYMDhdlMGLLESGLV---HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR- 860
Cdd:cd05060    70 --LMLVMELAP---LGPLLKYLKkrrEIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRa 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 ------LYSSEESRPYTNKvitlWYRPPELLLGeeRYTPAIDVWSCGCILGELFT--KKPI--FQANQELAQLELISRIc 930
Cdd:cd05060   145 lgagsdYYRATTAGRWPLK----WYAPECINYG--KFSSKSDVWSYGVTLWEAFSygAKPYgeMKGPEVIAMLESGERL- 217
                         250
                  ....*....|..
gi 145309300  931 gsPCPAVWPDVI 942
Cdd:cd05060   218 --PRPEECPQEI 227
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
703-909 1.54e-16

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: 82.08  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDT-----GEM-VALKKVRLD-NEKEgfPITAIREIKILRQL-THQSIINMKEIVTDK 774
Cdd:cd05053    12 DRLTLGKPLGEGAFGQVVKAEAVGLdnkpnEVVtVAVKMLKDDaTEKD--LSDLVSEMEMMKMIgKHKNIINLLGACTQD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  775 edaldfkkdkGAFYLVFEYMDH-DLMGLLES-----------GLVHFNEN----HIKSFMRQLMEGLDYCHKKNFLHRDI 838
Cdd:cd05053    90 ----------GPLYVVVEYASKgNLREFLRArrppgeeaspdDPRVPEEQltqkDLVSFAYQVARGMEYLASKKCIHRDL 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  839 KCSNILLNNRGQIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05053   160 AARNVLVTEDNVMKIADFGLARdIHHIDYYRKTTNGRLPVKWMAPEALF-DRVYTHQSDVWSFGVLLWEIFT 230
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
710-937 1.59e-16

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: 81.45  E-value: 1.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGE---MVALKKVR---LDNEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDALdfkkd 783
Cdd:cd05065    11 VIGAGEFGEVCRGRLKLPGKreiFVAIKTLKsgyTEKQRRDF----LSEASIMGQFDHPNIIHLEGVVTKSRPVM----- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgafyLVFEYMDHdlmGLLESGLV----HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd05065    82 -----IITEFMEN---GALDSFLRqndgQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLS 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RLYSSEESRP-YTN----KVITLWYRPPELLLgeERYTPAIDVWSCGCILGEL--FTKKPIFQ-ANQELAQ-LELISRIC 930
Cdd:cd05065   154 RFLEDDTSDPtYTSslggKIPIRWTAPEAIAY--RKFTSASDVWSYGIVMWEVmsYGERPYWDmSNQDVINaIEQDYRLP 231

                  ....*...
gi 145309300  931 GSP-CPAV 937
Cdd:cd05065   232 PPMdCPTA 239
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
710-994 1.78e-16

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: 81.16  E-value: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQ-VYKardkdtGEM----VALKKVRLDnekegFPITAIREIKILRQL-THQSIINMkeivtdkedaLDFKKD 783
Cdd:cd13982     8 VLGYGSEGTiVFR------GTFdgrpVAVKRLLPE-----FFDFADREVQLLRESdEHPNVIRY----------FCTEKD 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDHDLMGLLESGLVHFNENHI----KSFMRQLMEGLDYCHKKNFLHRDIKCSNILL-----NNRGQIKLA 854
Cdd:cd13982    67 RQFLYIALELCAASLQDLVESPRESKLFLRPglepVRLLRQIASGLAHLHSLNIVHRDLKPQNILIstpnaHGNVRAMIS 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  855 DFGLA-RLYSSEESRPYTNKVI-TLWYRPPELLLGE--ERYTPAIDVWSCGCIL------GE-LFTKKPIFQANqelaql 923
Cdd:cd13982   147 DFGLCkKLDVGRSSFSRRSGVAgTSGWIAPEMLSGStkRRQTRAVDIFSLGCVFyyvlsgGShPFGDKLEREAN------ 220
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  924 elisricgspcpavwpdvIKLPYFNTMKPkkqyrRKLREEFVfipaAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd13982   221 ------------------ILKGKYSLDKL-----LSLGEHGP----EAQDLIERMIDFDPEKRPSAEEVLN 264
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
709-944 1.85e-16

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: 80.78  E-value: 1.85e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  709 GIIGEGTYGQVYKA--RDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVtdkedaldfkkDKGA 786
Cdd:cd05116     1 GELGSGNFGTVKKGyyQMKKVVKTVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGIC-----------EAES 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDhdlMGLLESGLV---HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYS 863
Cdd:cd05116    70 WMLVMEMAE---LGPLNKFLQknrHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEES---RPYTNKVITLWYRPPelLLGEERYTPAIDVWSCGCILGELFT--KKPI--FQANQELAQLELISRI-CGSPCP 935
Cdd:cd05116   147 ADENyykAQTHGKWPVKWYAPE--CMNYYKFSSKSDVWSFGVLMWEAFSygQKPYkgMKGNEVTQMIEKGERMeCPAGCP 224

                  ....*....
gi 145309300  936 AVWPDVIKL 944
Cdd:cd05116   225 PEMYDLMKL 233
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
711-994 2.27e-16

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: 81.09  E-value: 2.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRlDNEKEGFPITAIREIKILRQLTHQSIINMKEIVtdkedaldfkKDKGAFYLV 790
Cdd:cd14169    11 LGEGAFSEVVLAQERGSQRLVALKCIP-KKALRGKEAMVENEIAVLRRINHENIVSLEDIY----------ESPTHLYLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHD--LMGLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN---RGQIKLADFGLARLyssE 865
Cdd:cd14169    80 MELVTGGelFDRIIERG--SYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSKI---E 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  866 ESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGSPcpavwpdviklP 945
Cdd:cd14169   155 AQGMLSTACGTPGYVAPE-LLEQKPYGKAVDVWAIGVISYIL---------------------LCGYP-----------P 201
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  946 YFNTMKPkKQYRRKLREEFVF-------IPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14169   202 FYDENDS-ELFNQILKAEYEFdspywddISESAKDFIRHLLERDPEKRFTCEQALQ 256
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
703-909 2.60e-16

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: 80.86  E-value: 2.60e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEmVALKKVRLDNEK-EGFpitaIREIKILRQLTHQSIINMKEIVTDKEdaldfk 781
Cdd:cd05072     7 ESIKLVKKLGAGQFGEVWMGYYNNSTK-VAVKTLKPGTMSvQAF----LEEANLMKTLQHDKLVRLYAVVTKEE------ 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgAFYLVFEYMDH----DLMGLLESGLVHFNEnhIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG 857
Cdd:cd05072    76 ----PIYIITEYMAKgsllDFLKSDEGGKVLLPK--LIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFG 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  858 LARL-----YSSEESRPYTNKvitlWYRPPELLLGEerYTPAIDVWSCGCILGELFT 909
Cdd:cd05072   150 LARViedneYTAREGAKFPIK----WTAPEAINFGS--FTIKSDVWSFGILLYEIVT 200
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
705-986 3.31e-16

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 81.79  E-value: 3.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVA---LKKVRLDNEKEGFPITAirEIKILRQLTHQSIINMkeivtdkedaLDFK 781
Cdd:PTZ00263   20 FEMGETLGTGSFGRVRIAKHKGTGEYYAikcLKKREILKMKQVQHVAQ--EKSILMELSHPFIVNM----------MCSF 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDKGAFYLVFEY-MDHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR 860
Cdd:PTZ00263   88 QDENRVYFLLEFvVGGELFTHLRKA-GRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 LYSseeSRPYTnKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGSPcpavwpd 940
Cdd:PTZ00263  167 KVP---DRTFT-LCGTPEYLAPE-VIQSKGHGKAVDWWTMGVLLYEF---------------------IAGYP------- 213
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 145309300  941 viklPYFNTmKPKKQYRRKLREEFVF---IPAAALDLFDYMLALDPSKR 986
Cdd:PTZ00263  214 ----PFFDD-TPFRIYEKILAGRLKFpnwFDGRARDLVKGLLQTDHTKR 257
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
711-904 3.64e-16

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 80.76  E-value: 3.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALK---KVRL--------------------DNEKEGFPITAI-REIKILRQLTHQSIIN 766
Cdd:cd14200     8 IGKGSYGVVKLAYNESDDKYYAMKvlsKKKLlkqygfprrppprgskaaqgEQAKPLAPLERVyQEIAILKKLDHVNIVK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  767 MKEIVTD-KEDALdfkkdkgafYLVFEymdhdlmgLLESGLVH-------FNENHIKSFMRQLMEGLDYCHKKNFLHRDI 838
Cdd:cd14200    88 LIEVLDDpAEDNL---------YMVFD--------LLRKGPVMevpsdkpFSEDQARLYFRDIVLGIEYLHYQKIVHRDI 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  839 KCSNILLNNRGQIKLADFGLARLYSSEESRpYTNKVITLWYRPPELLL--GEERYTPAIDVWSCGCIL 904
Cdd:cd14200   151 KPSNLLLGDDGHVKIADFGVSNQFEGNDAL-LSSTAGTPAFMAPETLSdsGQSFSGKALDVWAMGVTL 217
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
711-910 3.79e-16

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: 79.99  E-value: 3.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEmVALKKVRldnekEGFPITA--IREIKILRQLTHQSIINMKEIVTDKedaldfkkdkGAFY 788
Cdd:cd05112    12 IGSGQFGLVHLGYWLNKDK-VAIKTIR-----EGAMSEEdfIEEAEVMMKLSHPKLVQLYGVCLEQ----------APIC 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDHD-LMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEES 867
Cdd:cd05112    76 LVFEFMEHGcLSDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQY 155
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 145309300  868 RPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTK 910
Cdd:cd05112   156 TSSTGTKFPVKWSSPE-VFSFSRYSSKSDVWSFGVLMWEVFSE 197
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
703-909 3.87e-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: 80.65  E-value: 3.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKAR-------DKDTgeMVALKKVR----LDNEKEGFpitaiREIKILRQLTHQSIINMKEIV 771
Cdd:cd05050     5 NNIEYVRDIGQGAFGRVFQARapgllpyEPFT--MVAVKMLKeeasADMQADFQ-----REAALMAEFDHPNIVKLLGVC 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  772 TDKEdaldfkkdkgAFYLVFEYMDH-DLMGLL-------ESGLVH--------------FNENHIKSFMRQLMEGLDYCH 829
Cdd:cd05050    78 AVGK----------PMCLLFEYMAYgDLNEFLrhrspraQCSLSHstssarkcglnplpLSCTEQLCIAKQVAAGMAYLS 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  830 KKNFLHRDIKCSNILLNNRGQIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELF 908
Cdd:cd05050   148 ERKFVHRDLATRNCLVGENMVVKIADFGLSRnIYSADYYKASENDAIPIRWMPPESIF-YNRYTTESDVWAYGVVLWEIF 226

                  .
gi 145309300  909 T 909
Cdd:cd05050   227 S 227
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
711-909 4.19e-16

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 79.74  E-value: 4.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTgemVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKDKGA-FYL 789
Cdd:cd14062     1 IGSGSFGTVYKGRWHGD---VAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYMTKPQLAIVTQWCEGSsLYK 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDhdlmgllesglVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA----RLYSSE 865
Cdd:cd14062    78 HLHVLE-----------TKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLAtvktRWSGSQ 146
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 145309300  866 ESRPYTNKVitLWYRPPEL-LLGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd14062   147 QFEQPTGSI--LWMAPEVIrMQDENPYSFQSDVYAFGIVLYELLT 189
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
711-914 4.37e-16

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: 80.12  E-value: 4.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKdtGEMVALKKVRLDNEKEGFPITAIREIKILRqLTHQSIINMKEIVTdkedaldfKKDKGAFYLV 790
Cdd:cd13979    11 LGSGGFGSVYKATYK--GETVAVKIVRRRRKNRASRQSFWAELNAAR-LRHENIVRVLAAET--------GTDFASLGLI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 -FEYMD-HDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY--SSEE 866
Cdd:cd13979    80 iMEYCGnGTLQQLIYEGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLgeGNEV 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 145309300  867 SRPYTNKVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIF 914
Cdd:cd13979   160 GTPRSHIGGTYTYRAPELLKG-ERVTPKADIYSFGITLWQMLTRELPY 206
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
710-939 4.38e-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: 80.16  E-value: 4.38e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKA---RDKDTGEMVALKKVRLDNE---KEGFpitaIREIKILRQLTHQSIINMKEIVTDKedaldfkkd 783
Cdd:cd05056    13 CIGEGQFGDVYQGvymSPENEKIAVAVKTCKNCTSpsvREKF----LQEAYIMRQFDHPHIVKLIGVITEN--------- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgAFYLVFE-YMDHDLMGLLESglvhfNENHIKS-----FMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG 857
Cdd:cd05056    80 --PVWIVMElAPLGELRSYLQV-----NKYSLDLaslilYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARlYSSEESRpYTNKVITL---WYRPPELLLgeERYTPAIDVWSCGCILGELFT--KKPIF--QANQELAQLELISRIc 930
Cdd:cd05056   153 LSR-YMEDESY-YKASKGKLpikWMAPESINF--RRFTSASDVWMFGVCMWEILMlgVKPFQgvKNNDVIGRIENGERL- 227

                  ....*....
gi 145309300  931 gsPCPAVWP 939
Cdd:cd05056   228 --PMPPNCP 234
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
707-904 4.51e-16

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: 79.69  E-value: 4.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  707 IIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEGFpitAIREIKILRQLTHQSIINMKEIVtdkedaldfkKD 783
Cdd:cd14075     6 IRGELGSGNFSQVKLGIHQLTKEKVAIKildKTKLDQKTQRL---LSREISSMEKLHHPNIIRLYEVV----------ET 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd14075    73 LSKLHLVMEYASGgELYTKISTE-GKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHA 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 145309300  863 SSEE-------SRPYTnkvitlwyrPPELLLGEERYTPAIDVWSCGCIL 904
Cdd:cd14075   152 KRGEtlntfcgSPPYA---------APELFKDEHYIGIYVDIWALGVLL 191
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
710-919 5.27e-16

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: 80.72  E-value: 5.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVA---LKKVR-LDNEKEGFPITairEIKILRQ-LTHQSIINMKEIVTDKEDaldfkkdk 784
Cdd:cd05570     2 VLGKGSFGKVMLAERKKTDELYAikvLKKEViIEDDDVECTMT---EKRVLALaNRHPFLTGLHACFQTEDR-------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gaFYLVFEYMDH-DLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARlys 863
Cdd:cd05570    71 --LYFVMEYVNGgDLMFHIQRARR-FTEERARFYAAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCK--- 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 seESRPYTNKVITLW----YRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANQE 919
Cdd:cd05570   145 --EGIWGGNTTSTFCgtpdYIAPEILR-EQDYGFSVDWWALGVLLYEMLAGQSPFEGDDE 201
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
710-928 5.57e-16

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: 80.91  E-value: 5.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGE------MVALKK---VRldNEKEGFPITAIReiKILRQLTHQSIINMKeivtdkedaLDF 780
Cdd:cd05584     3 VLGKGGYGKVFQVRKTTGSDkgkifaMKVLKKasiVR--NQKDTAHTKAER--NILEAVKHPFIVDLH---------YAF 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 KKDkGAFYLVFEYMDH-DLMGLLE-SGLvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd05584    70 QTG-GKLYLILEYLSGgELFMHLErEGI--FMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGL 146
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  859 ARLYSSEESRPYTNkVITLWYRPPELLL--GEERytpAIDVWSCGCILGELFTKKPIFQANQELAQLELISR 928
Cdd:cd05584   147 CKESIHDGTVTHTF-CGTIEYMAPEILTrsGHGK---AVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILK 214
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
704-923 6.33e-16

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: 79.28  E-value: 6.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIgiIGEGTYGQVYKARDKDTGEMVA---LKKVRLDN-EKEGFPitaiREIKILRQLTHQSIINM----KEIVtdke 775
Cdd:cd14033     4 KFNIE--IGRGSFKTVYRGLDTETTVEVAwceLQTRKLSKgERQRFS----EEVEMLKGLQHPNIVRFydswKSTV---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  776 daldfkKDKGAFYLVFEYMDHdlmGLLESGLVHFNENHIKSFMR---QLMEGLDYCHKKN--FLHRDIKCSNILLNN-RG 849
Cdd:cd14033    74 ------RGHKCIILVTELMTS---GTLKTYLKRFREMKLKLLQRwsrQILKGLHFLHSRCppILHRDLKCDNIFITGpTG 144
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  850 QIKLADFGLARLYSSEesrpYTNKVI-TLWYRPPELLlgEERYTPAIDVWSCG-CILgELFTKKPIFQANQELAQL 923
Cdd:cd14033   145 SVKIGDLGLATLKRAS----FAKSVIgTPEFMAPEMY--EEKYDEAVDVYAFGmCIL-EMATSEYPYSECQNAAQI 213
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
703-922 7.29e-16

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 80.10  E-value: 7.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRL-----DNEKEGFPITAIREIKILRQLTHQSIINMKEIvtdkeda 777
Cdd:cd14040     6 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLnkswrDEKKENYHKHACREYRIHKELDHPRIVKLYDY------- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 ldFKKDKGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCH--KKNFLHRDIKCSNILLNNR---GQIK 852
Cdd:cd14040    79 --FSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGtacGEIK 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFGLARL-----YSSEESRPYTNKVITLWYRPPE-LLLGEE--RYTPAIDVWSCGCILGE-LFTKKPI--FQANQELA 921
Cdd:cd14040   157 ITDFGLSKImdddsYGVDGMDLTSQGAGTYWYLPPEcFVVGKEppKISNKVDVWSVGVIFFQcLYGRKPFghNQSQQDIL 236

                  .
gi 145309300  922 Q 922
Cdd:cd14040   237 Q 237
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
705-1000 7.62e-16

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: 79.76  E-value: 7.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGfpiTAIREIKILRQLTHQSIINM--KEIVTDKEDALDfkk 782
Cdd:cd06637     8 FELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEEE---EIKQEINMLKKYSHHRNIATyyGAFIKKNPPGMD--- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkGAFYLVFEYMDH----DLMGLLESGLVhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd06637    82 --DQLWLVMEFCGAgsvtDLIKNTKGNTL--KEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYSSEESRPYTNkVITLWYRPPELLLGEER----YTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRicgSPC 934
Cdd:cd06637   158 SAQLDRTVGRRNTF-IGTPYWMAPEVIACDENpdatYDFKSDLWSLGITAIEMAEGAPPLCDMHPMRALFLIPR---NPA 233
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  935 PAVwpdviklpyfntmkPKKQYRRKLREefvFIPAAaldlfdymLALDPSKRCTAEQALQCEFLRD 1000
Cdd:cd06637   234 PRL--------------KSKKWSKKFQS---FIESC--------LVKNHSQRPSTEQLMKHPFIRD 274
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
705-903 7.63e-16

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


Pssm-ID: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 79.16  E-value: 7.63e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGfpiTAIREIKILRQLTHQSIINMkeivtdkedaLDFKKDK 784
Cdd:cd14107     4 YEVKEEIGRGTFGFVKRVTHKGNGECCAAKFIPLRSSTRA---RAFQERDILARLSHRRLTCL----------LDQFETR 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVFEY------MDHdlmgLLESGLVhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL--NNRGQIKLADF 856
Cdd:cd14107    71 KTLILILELcsseelLDR----LFLKGVV--TEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDF 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 145309300  857 GLARLYSSeeSRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCI 903
Cdd:cd14107   145 GFAQEITP--SEHQFSKYGSPEFVAPE-IVHQEPVSAATDIWALGVI 188
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
690-994 7.96e-16

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: 79.81  E-value: 7.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  690 TKEKDIDWGKRcvdkfdiigiIGEGTYGQVYKARDKDTGEMVALKkVRLDNEKegfpitAIREIKILRQL-THQSIINMK 768
Cdd:cd14171     3 LEEYEVNWTQK----------LGTGISGPVRVCVKKSTGERFALK-ILLDRPK------ARTEVRLHMMCsGHPNIVQIY 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  769 EIVTDKedaLDFKKD---KGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL 845
Cdd:cd14171    66 DVYANS---VQFPGEsspRARLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  846 NNRGQ---IKLADFGLARLYSSEESRPYtnkvITLWYRPPELLLGEER----------------YTPAIDVWSCGCILGE 906
Cdd:cd14171   143 KDNSEdapIKLCDFGFAKVDQGDLMTPQ----FTPYYVAPQVLEAQRRhrkersgiptsptpytYDKSCDMWSLGVIIYI 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  907 LftkkpifqanqelaqlelisrICGSPcpavwpdviklPYFNTMKPK---KQYRRKL--------REEFVFIPAAALDLF 975
Cdd:cd14171   219 M---------------------LCGYP-----------PFYSEHPSRtitKDMKRKImtgsyefpEEEWSQISEMAKDIV 266
                         330
                  ....*....|....*....
gi 145309300  976 DYMLALDPSKRCTAEQALQ 994
Cdd:cd14171   267 RKLLCVDPEERMTIEEVLH 285
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
710-994 9.72e-16

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: 79.30  E-value: 9.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPITAI-REIKILRQLthQSIINMKEIVtdkedalDFKKDKGAFY 788
Cdd:cd14174     9 LLGEGAYAKVQGCVSLQNGKEYAVKIIE---KNAGHSRSRVfREVETLYQC--QGNKNILELI-------EFFEDDTRFY 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ---IKLADFGLA---RLY 862
Cdd:cd14174    77 LVFEKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKvspVKICDFDLGsgvKLN 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSeeSRPYTNKVITL-----WYRPPEL--LLGEER--YTPAIDVWSCGCILGELFTKKPIFQANqelaqlelisriCGSP 933
Cdd:cd14174   157 SA--CTPITTPELTTpcgsaEYMAPEVveVFTDEAtfYDKRCDLWSLGVILYIMLSGYPPFVGH------------CGTD 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  934 CPAVWPDVIKLPYFNTMKPKKQYRRKLRE-EFVFIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14174   223 CGWDRGEVCRVCQNKLFESIQEGKYEFPDkDWSHISSEAKDLISKLLVRDAKERLSAAQVLQ 284
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
710-928 1.04e-15

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: 78.47  E-value: 1.04e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKE-GFPITAIR---EIKILRQLTH--QSIINMkeivtdkedaLDFKKD 783
Cdd:cd14100     7 LLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEwGELPNGTRvpmEIVLLKKVGSgfRGVIRL----------LDWFER 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMD--HDLMGLL-ESGLVHfnENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLN-NRGQIKLADFGLA 859
Cdd:cd14100    77 PDSFVLVLERPEpvQDLFDFItERGALP--EELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSG 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  860 RLYsseESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISR 928
Cdd:cd14100   155 ALL---KDTVYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFR 220
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
711-942 1.25e-15

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: 79.28  E-value: 1.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKA--------RDKDTGEMVALKKVRLDNEKEgfpitAIREIKILRQLTHQSIINMKEIVTDKEDALdfkk 782
Cdd:cd05094    13 LGEGAFGKVFLAecynlsptKDKMLVAVKTLKDPTLAARKD-----FQREAELLTNLQHDHIVKFYGVCGDGDPLI---- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgafyLVFEYMDH------------DLMGLLESGLVHFNEN-------HIKSfmrQLMEGLDYCHKKNFLHRDIKCSNI 843
Cdd:cd05094    84 ------MVFEYMKHgdlnkflrahgpDAMILVDGQPRQAKGElglsqmlHIAT---QIASGMVYLASQHFVHRDLATRNC 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  844 LLNNRGQIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT--KKPIFQ-ANQE 919
Cdd:cd05094   155 LVGANLLVKIGDFGMSRdVYSTDYYRVGGHTMLPIRWMPPESIM-YRKFTTESDVWSFGVILWEIFTygKQPWFQlSNTE 233
                         250       260
                  ....*....|....*....|....*
gi 145309300  920 LAQLELISRICGSP--CPAVWPDVI 942
Cdd:cd05094   234 VIECITQGRVLERPrvCPKEVYDIM 258
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
699-1060 1.28e-15

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: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  699 KRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALK----KVRLDNEKEGFPITairEIKILRQLTHQSIINMKEIVTDK 774
Cdd:cd05593    11 RKTMNDFDYLKLLGKGTFGKVILVREKASGKYYAMKilkkEVIIAKDEVAHTLT---ESRVLKNTRHPFLTSLKYSFQTK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  775 eDALDFkkdkgafylVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLA 854
Cdd:cd05593    88 -DRLCF---------VMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKIT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  855 DFGLARLYSSEESrpyTNKVI--TLWYRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGs 932
Cdd:cd05593   158 DFGLCKEGITDAA---TMKTFcgTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEM---------------------MCG- 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  933 pcpavwpdviKLPYFNtMKPKKQYRRKLREEFVF---IPAAALDLFDYMLALDPSKRC-----TAEQALQCEFL-----R 999
Cdd:cd05593   212 ----------RLPFYN-QDHEKLFELILMEDIKFprtLSADAKSLLSGLLIKDPNKRLgggpdDAKEIMRHSFFtgvnwQ 280
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300 1000 DVEPSKMPPPDLPlwqdchELWSKKRRRQKQMGMTDDVSTIKAPRKDLSLGLD----DSRTNTPQ 1060
Cdd:cd05593   281 DVYDKKLVPPFKP------QVTSETDTRYFDEEFTAQTITITPPEKYDEDGMDcmdnERRPHFPQ 339
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
703-914 1.29e-15

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


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 80.82  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVrldNEKEgfpITAIREIKILRQLTHQSIINMKEIVTDKEDALdfkK 782
Cdd:cd05624    72 DDFEIIKVIGRGAFGEVAVVKMKNTERIYAMKIL---NKWE---MLKRAETACFREERNVLVNGDCQWITTLHYAF---Q 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFYLVFEY-MDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL 861
Cdd:cd05624   143 DENYLYLVMDYyVGGDLLTLLSKFEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSCLK 222
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  862 YSSEESRPYTNKVITLWYRPPELLLGEE----RYTPAIDVWSCG-CILGELFTKKPIF 914
Cdd:cd05624   223 MNDDGTVQSSVAVGTPDYISPEILQAMEdgmgKYGPECDWWSLGvCMYEMLYGETPFY 280
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
707-907 1.47e-15

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: 78.48  E-value: 1.47e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  707 IIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEgfPITAIREIKILRQLT-HQSIINMkeivtdkedaLDFK--KD 783
Cdd:cd14037     7 IEKYLAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHD--LNVCKREIEIMKRLSgHKNIVGY----------IDSSanRS 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDH-------DLMGL-LESGlvhFNENHIKSFMRQLMEGLDYCH--KKNFLHRDIKCSNILLNNRGQIKL 853
Cdd:cd14037    75 GNGVYEVLLLMEYckgggviDLMNQrLQTG---LTESEILKIFCDVCEAVAAMHylKPPLIHRDLKVENVLISDSGNYKL 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  854 ADFGLArlysSEESRPYTN------------KVITLWYRPPEL--LLGEERYTPAIDVWSCGCILGEL 907
Cdd:cd14037   152 CDFGSA----TTKILPPQTkqgvtyveedikKYTTLQYRAPEMidLYRGKPITEKSDIWALGCLLYKL 215
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
699-919 1.76e-15

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: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  699 KRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVR-----LDNEKEgfpITAIREIKILRQLTHQSIINMKEIVTD 773
Cdd:cd05619     1 KLTIEDFVLHKMLGKGSFGKVFLAELKGTNQFFAIKALKkdvvlMDDDVE---CTMVEKRVLSLAWEHPFLTHLFCTFQT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  774 KEDaldfkkdkgaFYLVFEYMDH-DLMGLLESglVH-FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQI 851
Cdd:cd05619    78 KEN----------LFFVMEYLNGgDLMFHIQS--CHkFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHI 145
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  852 KLADFGLARLYSSEESRPYTNkVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQE 919
Cdd:cd05619   146 KIADFGMCKENMLGDAKTSTF-CGTPDYIAPEILLG-QKYNTSVDWWSFGVLLYEMLIGQSPFHGQDE 211
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
705-1027 1.84e-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: 78.94  E-value: 1.84e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKeGFPITAIREIKILRQLTHQSIINMKEIVTDKEDaldfkkdk 784
Cdd:cd14168    12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALK-GKESSIENEIAVLRKIKHENIVALEDIYESPNH-------- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gaFYLVFEYMDHDLM--GLLESGLvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR---GQIKLADFGLA 859
Cdd:cd14168    83 --LYLVMQLVSGGELfdRIVEKGF--YTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYFSQdeeSKIMISDFGLS 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 RLYSSEESrpYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGSPcpavwp 939
Cdd:cd14168   159 KMEGKGDV--MSTACGTPGYVAPE-VLAQKPYSKAVDCWSIGVIAYIL---------------------LCGYP------ 208
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  940 dviklPYFNTmKPKKQYRRKLREEFVF-------IPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDvepskmpppDLP 1012
Cdd:cd14168   209 -----PFYDE-NDSKLFEQILKADYEFdspywddISDSAKDFIRNLMEKDPNKRYTCEQALRHPWIAG---------DTA 273
                         330
                  ....*....|....*
gi 145309300 1013 LWQDCHELWSKKRRR 1027
Cdd:cd14168   274 LCKNIHESVSAQIRK 288
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
711-919 1.89e-15

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


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 78.88  E-value: 1.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVY--------KARDKD--------TGEMVALKKVRLD---NEKEGFpitaIREIKILRQLTHQSIINMKEIV 771
Cdd:cd05095    13 LGEGQFGEVHlceaegmeKFMDKDfalevsenQPVLVAVKMLRADankNARNDF----LKEIKIMSRLKDPNIIRLLAVC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  772 TdKEDALdfkkdkgafYLVFEYMDH-DLMGLL-----ESGLVHFNENHIKSFMR------QLMEGLDYCHKKNFLHRDIK 839
Cdd:cd05095    89 I-TDDPL---------CMITEYMENgDLNQFLsrqqpEGQLALPSNALTVSYSDlrfmaaQIASGMKYLSSLNFVHRDLA 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  840 CSNILLNNRGQIKLADFGLAR-LYSSEESRPYTNKVITL-WYRPPELLLGeeRYTPAIDVWSCGCILGELFT---KKPIF 914
Cdd:cd05095   159 TRNCLVGKNYTIKIADFGMSRnLYSGDYYRIQGRAVLPIrWMSWESILLG--KFTTASDVWAFGVTLWETLTfcrEQPYS 236

                  ....*
gi 145309300  915 QANQE 919
Cdd:cd05095   237 QLSDE 241
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
710-928 2.09e-15

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


Pssm-ID: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 78.41  E-value: 2.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKV---RLdnEKEGFPITAIREIKILRQLTHQSIINMkeivtdkedALDFKKdKGA 786
Cdd:cd05607     9 VLGKGGFGEVCAVQVKNTGQMYACKKLdkkRL--KKKSGEKMALLEKEILEKVNSPFIVSL---------AYAFET-KTH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDH-DL-MGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLArlYSS 864
Cdd:cd05607    77 LCLVMSLMNGgDLkYHIYNVGERGIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLA--VEV 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  865 EESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISR 928
Cdd:cd05607   155 KEGKPITQRAGTNGYMAPEILK-EESYSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEELKR 217
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
709-923 2.22e-15

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: 78.56  E-value: 2.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  709 GIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKegfpitaiREIKILRQlTHQSII---NMKEIVtdKEDALDFKKdkG 785
Cdd:cd06616    12 GEIGRGAFGTVNKMLHKPSGTIMAVKRIRSTVDE--------KEQKRLLM-DLDVVMrssDCPYIV--KFYGALFRE--G 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 AFYLVFEYMDHDL----MGLLESGLVHFNENHIKSFMRQLMEGLDYCHKK-NFLHRDIKCSNILLNNRGQIKLADFGLA- 859
Cdd:cd06616    79 DCWICMELMDISLdkfyKYVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISg 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  860 RLyssEESRPYTNKVITLWYRPPELLLGE---ERYTPAIDVWSCGCILGELFTKK-PIFQANQELAQL 923
Cdd:cd06616   159 QL---VDSIAKTRDAGCRPYMAPERIDPSasrDGYDVRSDVWSLGITLYEVATGKfPYPKWNSVFDQL 223
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
750-909 2.42e-15

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: 77.61  E-value: 2.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  750 IREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAFYLVFEYMDHD-LMGLLESGLVHFNENHIKSFMRQLMEGLDYC 828
Cdd:cd05113    47 IEEAKVMMNLSHEKLVQLYGVCTKQR----------PIFIITEYMANGcLLNYLREMRKRFQTQQLLEMCKDVCEAMEYL 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  829 HKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEEsrpYTNKVITLW---YRPPELLLgEERYTPAIDVWSCGCILG 905
Cdd:cd05113   117 ESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDE---YTSSVGSKFpvrWSPPEVLM-YSKFSSKSDVWAFGVLMW 192

                  ....
gi 145309300  906 ELFT 909
Cdd:cd05113   193 EVYS 196
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
702-916 2.50e-15

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: 79.34  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEgfpiTAI--REIKILRQLTHQSIINMKEIvtdked 776
Cdd:cd05596    25 AEDFDVIKVIGRGAFGEVQLVRHKSTKKVYAMKllsKFEMIKRSD----SAFfwEERDIMAHANSEWIVQLHYA------ 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 aldFKKDKgAFYLVFEYM-DHDLMGLLESglVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLAD 855
Cdd:cd05596    95 ---FQDDK-YLYMVMDYMpGGDLVNLMSN--YDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLAD 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  856 FGLARLYSSEESRPYTNKVITLWYRPPELLLGEER---YTPAIDVWSCGCILGELFTKKPIFQA 916
Cdd:cd05596   169 FGTCMKMDKDGLVRSDTAVGTPDYISPEVLKSQGGdgvYGRECDWWSVGVFLYEMLVGDTPFYA 232
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
705-1009 2.50e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 79.65  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKvrldNEKEGfpitAIREIKILRQLTHQSIINMKEIVT-DKEDALDFKKD 783
Cdd:PHA03212   94 FSILETFTPGAEGFAFACIDNKTCEHVVIKA----GQRGG----TATEAHILRAINHPSIIQLKGTFTyNKFTCLILPRY 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEymDHDLMGLLEsglvhfnenhIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYS 863
Cdd:PHA03212  166 KTDLYCYLA--AKRNIAICD----------ILAIERSVLRAIQYLHENRIIHRDIKAENIFINHPGDVCLGDFGAACFPV 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT-KKPIFQAN------QELAQLELISRICGSPcPA 936
Cdd:PHA03212  234 DINANKYYGWAGTIATNAPE-LLARDPYGPAVDIWSAGIVLFEMATcHDSLFEKDgldgdcDSDRQIKLIIRRSGTH-PN 311
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  937 VWP----DVIKLPYFNTMK--PKKQYRRKLREEFVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDVePSKMPPP 1009
Cdd:PHA03212  312 EFPidaqANLDEIYIGLAKksSRKPGSRPLWTNLYELPIDLEYLICKMLAFDAHHRPSAEALLDFAAFQDI-PDPYPNP 389
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
702-1012 2.58e-15

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: 79.15  E-value: 2.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnekegfpitaiREIKILRQLTHQsiinmkeiVTDKEDALDFK 781
Cdd:cd05610     3 IEEFVIVKPISRGAFGKVYLGRKKNNSKLYAVKVVK-------------KADMINKNMVHQ--------VQAERDALALS 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDK------------GAFYLVFEYM-DHDLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR 848
Cdd:cd05610    62 KSPfivhlyyslqsaNNVYLVMEYLiGGDVKSLLHI-YGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNE 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  849 GQIKLADFGLARLYSSEE-------------------SR------------------PY-TNKVI--------------T 876
Cdd:cd05610   141 GHIKLTDFGLSKVTLNRElnmmdilttpsmakpkndySRtpgqvlslisslgfntptPYrTPKSVrrgaarvegerilgT 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  877 LWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFqaNQELAQlELISRICGSPCPavWPDViklpyfntmkpkkqy 956
Cdd:cd05610   221 PDYLAPELLLGKP-HGPAVDWWALGVCLFEFLTGIPPF--NDETPQ-QVFQNILNRDIP--WPEG--------------- 279
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  957 rrklREEFVFIPAAALDLfdyMLALDPSKRCTAEQALQCEFLRDVE--------PSKMPPPDLP 1012
Cdd:cd05610   280 ----EEELSVNAQNAIEI---LLTMDPTKRAGLKELKQHPLFHGVDwenlqnqtMPFIPQPDDE 336
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
703-903 3.25e-15

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: 3.25e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITaiREIKILRQLTHQSIINMKEIVTDKEDALDFKK 782
Cdd:cd14191     2 DFYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFFKAYSAKEKENIR--QEISIMNCLHHPKLVQCVDAFEEKANIVMVLE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFYLVFEYMDHDLmgllesglvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR--GQIKLADFGLAR 860
Cdd:cd14191    80 MVSGGELFERIIDEDF---------ELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTKIKLIDFGLAR 150
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 145309300  861 LYSSEESrpytnkvITLWYRPPELLLGE----ERYTPAIDVWSCGCI 903
Cdd:cd14191   151 RLENAGS-------LKVLFGTPEFVAPEvinyEPIGYATDMWSIGVI 190
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
711-907 4.28e-15

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: 77.29  E-value: 4.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKK-VRLDNEKEGfpiTAIREIKILRQLTHQSIINMKEIVTdkedaldfkKDKgAFYL 789
Cdd:cd14222     1 LGKGFFGQAIKVTHKATGKVMVMKElIRCDEETQK---TFLTEVKVMRSLDHPNVLKFIGVLY---------KDK-RLNL 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRP 869
Cdd:cd14222    68 LTEFIEGGTLKDFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKP 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  870 ----YTNKVITL---------------WYRPPELLLGeERYTPAIDVWSCGCILGEL 907
Cdd:cd14222   148 ppdkPTTKKRTLrkndrkkrytvvgnpYWMAPEMLNG-KSYDEKVDIFSFGIVLCEI 203
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
710-916 4.93e-15

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: 77.83  E-value: 4.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVY---KARDKDTGEMVALK-------KVRlDNEKEGFpitairEIKILRQLTHQSIINMKeivtdkedaLD 779
Cdd:cd05582     2 VLGQGSFGKVFlvrKITGPDAGTLYAMKvlkkatlKVR-DRVRTKM------ERDILADVNHPFIVKLH---------YA 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FKKDkGAFYLVFEYM-DHDLMGLLeSGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd05582    66 FQTE-GKLYLILDFLrGGDLFTRL-SKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGL 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  859 ARLYSSEESRPYTNkVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQA 916
Cdd:cd05582   144 SKESIDHEKKAYSF-CGTVEYMAPE-VVNRRGHTQSADWWSFGVLMFEMLTGSLPFQG 199
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
710-909 5.03e-15

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: 76.45  E-value: 5.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKArdKDTGEMVALKKVRLDNEKEGFpitaIREIKILRQLTHQSIINMKEIVTdkedaldfkkdKGAFYL 789
Cdd:cd05083    13 IIGEGEFGAVLQG--EYMGQKVAVKNIKCDVTAQAF----LEETAVMTKLQHKNLVRLLGVIL-----------HNGLYI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLMGLLES-GLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLysseES 867
Cdd:cd05083    76 VMELMSKgNLVNFLRSrGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKV----GS 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 145309300  868 RPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05083   152 MGVDNSRLPVKWTAPE-ALKNKKFSSKSDVWSYGVLLWEVFS 192
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
711-909 5.17e-15

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


Pssm-ID: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 77.31  E-value: 5.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRldneKEGFPITAIR---EIKILRQLTHQSIINMKEIvtdkEDALDFKKDKGAF 787
Cdd:cd14038     2 LGTGGFGNVLRWINQETGEQVAIKQCR----QELSPKNRERwclEIQIMKRLNHPNVVAARDV----PEGLQKLAPNDLP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDH-DL---MGLLES--GLvhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQI---KLADFGL 858
Cdd:cd14038    74 LLAMEYCQGgDLrkyLNQFENccGL---REGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRlihKIIDLGY 150
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 145309300  859 ARlySSEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd14038   151 AK--ELDQGSLCTSFVGTLQYLAPE-LLEQQKYTVTVDYWSFGTLAFECIT 198
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
705-906 5.85e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 79.17  E-value: 5.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKvrldnekeGFPITAIREIKILRQLTHQSIINMkeivtdkedaLDFKKDK 784
Cdd:PHA03211  171 FAIHRALTPGSEGCVFESSHPDYPQRVVVKA--------GWYASSVHEARLLRRLSHPAVLAL----------LDVRVVG 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSS 864
Cdd:PHA03211  233 GLTCLVLPKYRSDLYTYLGARLRPLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGAACFARG 312
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 145309300  865 EESRPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGE 906
Cdd:PHA03211  313 SWSTPFHYGIAgTVDTNAPEVLAGDP-YTPSVDIWSAGLVIFE 354
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
703-985 7.50e-15

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


Pssm-ID: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 77.40  E-value: 7.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDnEKEGFPITAIREIKILRQLTHQSIINMKeivtdkedaldfkk 782
Cdd:cd06650     5 DDFEKISELGAGNGGVVFKVSHKPSGLVMARKLIHLE-IKPAIRNQIIRELQVLHECNSPYIVGFY-------------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkGAFY------LVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKN-FLHRDIKCSNILLNNRGQIKLAD 855
Cdd:cd06650    70 --GAFYsdgeisICMEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLREKHkIMHRDVKPSNILVNSRGEIKLCD 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  856 FGLARLYSSEESRPYtnkVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKK-PIFQANQElaQLELISRICGSPC 934
Cdd:cd06650   148 FGVSGQLIDSMANSF---VGTRSYMSPERLQGTH-YSVQSDIWSMGLSLVEMAVGRyPIPPPDAK--ELELMFGCQVEGD 221
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 145309300  935 PAVWPDVIKLPyfntMKPKKQYRRKLREefvfiPAAALDLFDYMLALDPSK 985
Cdd:cd06650   222 AAETPPRPRTP----GRPLSSYGMDSRP-----PMAIFELLDYIVNEPPPK 263
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
710-909 8.09e-15

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: 76.44  E-value: 8.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEM---VALKKVRL---DNEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDALdfkkd 783
Cdd:cd05066    11 VIGAGEFGEVCSGRLKLPGKReipVAIKTLKAgytEKQRRDF----LSEASIMGQFDHPNIIHLEGVVTRSKPVM----- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgafyLVFEYMDHdlmGLLESGLV----HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd05066    82 -----IVTEYMEN---GSLDAFLRkhdgQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 145309300  860 RLYSSEESRPYTN---KVITLWYRPPELLLgeERYTPAIDVWSCGCILGELFT 909
Cdd:cd05066   154 RVLEDDPEAAYTTrggKIPIRWTAPEAIAY--RKFTSASDVWSYGIVMWEVMS 204
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
751-993 9.42e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 77.96  E-value: 9.42e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  751 REIKILRQLTHQSIINmkeivtdkedALDFKKDKGAFYLVFEYMDHDLMGLLEsGLVHFNENHIKSFMRQLMEGLDYCHK 830
Cdd:PHA03207  135 REIDILKTISHRAIIN----------LIHAYRWKSTVCMVMPKYKCDLFTYVD-RSGPLPLEQAITIQRRLLEALAYLHG 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  831 KNFLHRDIKCSNILLNNRGQIKLADFGLArlySSEESRPYTNK----VITLWYRPPElLLGEERYTPAIDVWSCGCILGE 906
Cdd:PHA03207  204 RGIIHRDVKTENIFLDEPENAVLGDFGAA---CKLDAHPDTPQcygwSGTLETNSPE-LLALDPYCAKTDIWSAGLVLFE 279
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  907 LFTKK-PIF--QANQELAQLELISRiCGSPCPAVWPdviKLPYFNTMKPKKQYRRKLREEFVfIP------AAALDLfDY 977
Cdd:PHA03207  280 MSVKNvTLFgkQVKSSSSQLRSIIR-CMQVHPLEFP---QNGSTNLCKHFKQYAIVLRPPYT-IPpvirkyGMHMDV-EY 353
                         250       260
                  ....*....|....*....|
gi 145309300  978 ----MLALDPSKRCTAEQAL 993
Cdd:PHA03207  354 liakMLTFDQEFRPSAQDIL 373
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
703-933 9.89e-15

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: 76.46  E-value: 9.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKV---RLDNEKeGFPiTAIREIKILRQLTHQSIINMKEIVTDKED--- 776
Cdd:cd05608     1 DWFLDFRVLGKGGFGEVSACQMRATGKLYACKKLnkkRLKKRK-GYE-GAMVEKRILAKVHSRFIVSLAYAFQTKTDlcl 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 ALDFKKDKGAFYLVFEyMDHDLMGllesglvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd05608    79 VMTIMNGGDLRYHIYN-VDEENPG--------FQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDL 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSS--EESRPYTNkviTLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQE-LAQLELISRICGSP 933
Cdd:cd05608   150 GLAVELKDgqTKTKGYAG---TPGFMAPELLLGEE-YDYSVDYFTLGVTLYEMIAARGPFRARGEkVENKELKQRILNDS 225
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
711-913 1.06e-14

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


Pssm-ID: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 76.40  E-value: 1.06e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTgeMVALKKVRLDNE------KEGFpitaIREIKILRQLTHQSIInmkeivtdkeDALDFKKDK 784
Cdd:cd14159     1 IGEGGFGCVYQAVMRNT--EYAVKRLKEDSEldwsvvKNSF----LTEVEKLSRFRHPNIV----------DLAGYSAQQ 64
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 GAFYLVFEYMDHdlmGLLESGLvHFNENHIKSFMRQLME-------GLDYCHK--KNFLHRDIKCSNILLNNRGQIKLAD 855
Cdd:cd14159    65 GNYCLIYVYLPN---GSLEDRL-HCQVSCPCLSWSQRLHvllgtarAIQYLHSdsPSLIHGDVKSSNILLDAALNPKLGD 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  856 FGLARlYSSEESRPYTNKVI--------TLWYRPPElLLGEERYTPAIDVWSCGCILGELFT-KKPI 913
Cdd:cd14159   141 FGLAR-FSRRPKQPGMSSTLartqtvrgTLAYLPEE-YVKTGTLSVEIDVYSFGVVLLELLTgRRAM 205
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
703-914 1.13e-14

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: 77.00  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKV-RLDNEKEGfpitairEIKILRQLTHQSIINMKEIVTDKEDALdfk 781
Cdd:cd05597     1 DDFEILKVIGRGAFGEVAVVKLKSTEKVYAMKILnKWEMLKRA-------ETACFREERDVLVNGDRRWITKLHYAF--- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDKGAFYLVFE-YMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGlAR 860
Cdd:cd05597    71 QDENYLYLVMDyYCGGDLLTLLSKFEDRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG-SC 149
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 LYSSEESRPYTN-KVITLWYRPPELLL----GEERYTPAIDVWSCG-CILGELFTKKPIF 914
Cdd:cd05597   150 LKLREDGTVQSSvAVGTPDYISPEILQamedGKGRYGPECDWWSLGvCMYEMLYGETPFY 209
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
705-928 1.29e-14

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: 75.38  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIR---EIKILRQL--THQSIINMkeivtdkedaLD 779
Cdd:cd14102     2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNGVMvplEIVLLKKVgsGFRGVIKL----------LD 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FKKDKGAFYLVFEYMD--HDLMGLL-ESGLVhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR-GQIKLAD 855
Cdd:cd14102    72 WYERPDGFLIVMERPEpvKDLFDFItEKGAL--DEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRtGELKLID 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  856 FGLARLYsseESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISR 928
Cdd:cd14102   150 FGSGALL---KDTVYTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGRLYFR 219
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
710-910 1.32e-14

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


Pssm-ID: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 75.65  E-value: 1.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKA---RDKDTGEMVALKKVRLDN----EKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDALDFKK 782
Cdd:cd05035     6 ILGEGEFGSVMEAqlkQDDGSQLKVAVKTMKVDIhtysEIEEF----LSEAACMKDFDHPNVMRLIGVCFTASDLNKPPS 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DkgafYLVFEYMDH-DLMGLL-----ESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd05035    82 P----MVILPFMKHgDLHSYLlysrlGGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADF 157
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  857 GLAR-LYSSEESRP-YTNKVITLWYRPPEllLGEERYTPAIDVWSCGCILGELFTK 910
Cdd:cd05035   158 GLSRkIYSGDYYRQgRISKMPVKWIALES--LADNVYTSKSDVWSFGVTMWEIATR 211
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
695-914 1.50e-14

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: 77.75  E-value: 1.50e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  695 IDWGKRCVDK----------FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVrldNEKEgfpITAIREIKILRQLTHQSI 764
Cdd:cd05623    54 LEWAKPFTSKvkqmrlhkedFEILKVIGRGAFGEVAVVKLKNADKVFAMKIL---NKWE---MLKRAETACFREERDVLV 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  765 INMKEIVTDKEDALdfkKDKGAFYLVFEY-MDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNI 843
Cdd:cd05623   128 NGDSQWITTLHYAF---QDDNNLYLVMDYyVGGDLLTLLSKFEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNI 204
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  844 LLNNRGQIKLADFGLARLYSSEESRPYTNKVITLWYRPPELLL----GEERYTPAIDVWSCG-CILGELFTKKPIF 914
Cdd:cd05623   205 LMDMNGHIRLADFGSCLKLMEDGTVQSSVAVGTPDYISPEILQamedGKGKYGPECDWWSLGvCMYEMLYGETPFY 280
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
714-945 1.61e-14

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


Pssm-ID: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 75.23  E-value: 1.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  714 GTYGQVYKARDKDTGEMVaLKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKedaldfkkdkGAFYLVFEY 793
Cdd:cd14027     4 GGFGKVSLCFHRTQGLVV-LKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEE----------GKYSLVMEY 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  794 MDH-DLMGLLESGLVHFNenhIKS-FMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL-----YSSEE 866
Cdd:cd14027    73 MEKgNLMHVLKKVSVPLS---VKGrIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFkmwskLTKEE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  867 SR-------PYTNKVITLWYRPPELLLG-EERYTPAIDVWSCGCILGELFT-KKPIFQANQElaqleliSRICGSPCPAV 937
Cdd:cd14027   150 HNeqrevdgTAKKNAGTLYYMAPEHLNDvNAKPTEKSDVYSFAIVLWAIFAnKEPYENAINE-------DQIIMCIKSGN 222

                  ....*...
gi 145309300  938 WPDVIKLP 945
Cdd:cd14027   223 RPDVDDIT 230
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
710-907 1.62e-14

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: 75.55  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALK---KVRLdNEKEGfPITAIREIKILRQLTHQS----IINMkeivtdkedALDFKK 782
Cdd:cd05606     1 IIGRGGFGEVYGCRKADTGKMYAMKcldKKRI-KMKQG-ETLALNERIMLSLVSTGGdcpfIVCM---------TYAFQT 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 -DKGAFYLvfeymdhDLM--GLLESGLVH---FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd05606    70 pDKLCFIL-------DLMngGDLHYHLSQhgvFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDL 142
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 145309300  857 GLARLYSSEesRPYTNkVITLWYRPPELLLGEERYTPAIDVWSCGCILGEL 907
Cdd:cd05606   143 GLACDFSKK--KPHAS-VGTHGYMAPEVLQKGVAYDSSADWFSLGCMLYKL 190
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
711-905 1.63e-14

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: 75.72  E-value: 1.63e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLD---NEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDALDfkkdkGAF 787
Cdd:cd14039     1 LGTGGFGNVCLYQNQETGEKIAIKSCRLElsvKNKDRW----CHEIQIMKKLNHPNVVKACDVPEEMNFLVN-----DVP 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDH-DLMGLLES-----GLvhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN-RGQI--KLADFGL 858
Cdd:cd14039    72 LLAMEYCSGgDLRKLLNKpenccGL---KESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEiNGKIvhKIIDLGY 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 145309300  859 ARlySSEESRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCG-----CILG 905
Cdd:cd14039   149 AK--DLDQGSLCTSFVGTLQYLAPELFENKS-YTVTVDYWSFGtmvfeCIAG 197
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
711-939 1.64e-14

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: 75.82  E-value: 1.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKAR----DKDTGEMVALKKVRLDNEKEGFPiTAIREIKILRQLTHQSIINMKEIVTDKEDALdfkkdkga 786
Cdd:cd05090    13 LGECAFGKIYKGHlylpGMDHAQLVAIKTLKDYNNPQQWN-EFQQEASLMTELHHPNIVCLLGVVTQEQPVC-------- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 fyLVFEYMD----HDLM----------------GLLESGLVHFNENHIKSfmrQLMEGLDYCHKKNFLHRDIKCSNILLN 846
Cdd:cd05090    84 --MLFEFMNqgdlHEFLimrsphsdvgcssdedGTVKSSLDHGDFLHIAI---QIAAGMEYLSSHFFVHKDLAARNILVG 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  847 NRGQIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTK--KPIFQ-ANQELaq 922
Cdd:cd05090   159 EQLHVKISDLGLSReIYSSDYYRVQNKSLLPIRWMPPEAIM-YGKFSSDSDIWSFGVVLWEIFSFglQPYYGfSNQEV-- 235
                         250
                  ....*....|....*..
gi 145309300  923 LELISRICGSPCPAVWP 939
Cdd:cd05090   236 IEMVRKRQLLPCSEDCP 252
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
710-1012 1.68e-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: 76.27  E-value: 1.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGE---MVALKK--VRLDNEKEgfpITAIrEIKILRQLTHQSIINMKEIVTDKEDALdfkkdk 784
Cdd:cd05592     2 VLGKGSFGKVMLAELKGTNQyfaIKALKKdvVLEDDDVE---CTMI-ERRVLALASQHPFLTHLFCTFQTESHL------ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gafYLVFEYMDH-DLMGLLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYS 863
Cdd:cd05592    72 ---FFVMEYLNGgDLMFHIQQSG-RFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENI 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEESRPYTNkVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQElaqLELISRICGSPcpavwpdvik 943
Cdd:cd05592   148 YGENKASTF-CGTPDYIAPEILKG-QKYNQSVDWWSFGVLLYEMLIGQSPFHGEDE---DELFWSICNDT---------- 212
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  944 lPYFntmkPKkqyrrklreefvFIPAAALDLFDYMLALDPSKR-----CTAEQALQCEFLRDV-----EPSKMPPPDLP 1012
Cdd:cd05592   213 -PHY----PR------------WLTKEAASCLSLLLERNPEKRlgvpeCPAGDIRDHPFFKTIdwdklERREIDPPFKP 274
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
710-1012 1.91e-14

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 76.24  E-value: 1.91e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVA---LKK-VRLDNEKEGFPITairEIKILRQLTHQSIINMKEIVTDKeDALDFkkdkg 785
Cdd:cd05571     2 VLGKGTFGKVILCREKATGELYAikiLKKeVIIAKDEVAHTLT---ENRVLQNTRHPFLTSLKYSFQTN-DRLCF----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 afylVFEYMDHdlmGLLESGLVH---FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARly 862
Cdd:cd05571    73 ----VMEYVNG---GELFFHLSRervFSEDRTRFYGAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCK-- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 sseESRPYTNKVITLW----YRPPELLLgEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGspcpavw 938
Cdd:cd05571   144 ---EEISYGATTKTFCgtpeYLAPEVLE-DNDYGRAVDWWGLGVVMYEM---------------------MCG------- 191
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  939 pdviKLPYFNTmKPKKQYRRKLREEFVF---IPAAALDLFDYMLALDPSKRC-----TAEQALQCEFLR-----DVEPSK 1005
Cdd:cd05571   192 ----RLPFYNR-DHEVLFELILMEEVRFpstLSPEAKSLLAGLLKKDPKKRLgggprDAKEIMEHPFFAsinwdDLYQKK 266

                  ....*..
gi 145309300 1006 MPPPDLP 1012
Cdd:cd05571   267 IPPPFKP 273
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
703-926 1.94e-14

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: 75.94  E-value: 1.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDnEKEGFPITAIREIKILRQLTHQSIINMKeivtdkedaldfkk 782
Cdd:cd06615     1 DDFEKLGELGAGNGGVVTKVLHRPSGLIMARKLIHLE-IKPAIRNQIIRELKVLHECNSPYIVGFY-------------- 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkGAFY------LVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKK-NFLHRDIKCSNILLNNRGQIKLAD 855
Cdd:cd06615    66 --GAFYsdgeisICMEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCD 143
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  856 FGLA-RLYSSeesrpYTNK-VITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKK-PIFQANQelAQLELI 926
Cdd:cd06615   144 FGVSgQLIDS-----MANSfVGTRSYMSPERLQG-THYTVQSDIWSLGLSLVEMAIGRyPIPPPDA--KELEAM 209
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
708-909 2.36e-14

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: 75.19  E-value: 2.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  708 IGIIGEGTYGQVYKARDKDTGE-------MV-ALKKVRLDNEKEGFPitaiREIKILRQLTHQSIINMKEIVTDKEdald 779
Cdd:cd05046    10 ITTLGRGEFGEVFLAKAKGIEEeggetlvLVkALQKTKDENLQSEFR----RELDMFRKLSHKNVVRLLGLCREAE---- 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkkdkgAFYLVFEYMD-HDLMGLLESGLVHFNEN--------HIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ 850
Cdd:cd05046    82 ------PHYMILEYTDlGDLKQFLRATKSKDEKLkppplstkQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQRE 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  851 IKLADFGLARLYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05046   156 VKVSLLSLSKDVYNSEYYKLRNALIPLRWLAPEAVQ-EDDFSTKSDVWSFGVLMWEVFT 213
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
710-986 2.99e-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: 74.74  E-value: 2.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVY---KARDKDTGEMVA---LKKVRLDNEKEGFPIT--------AIREIKILRQLtHQSiinmkeivtdke 775
Cdd:cd05583     1 VLGTGAYGKVFlvrKVGGHDAGKLYAmkvLKKATIVQKAKTAEHTmterqvleAVRQSPFLVTL-HYA------------ 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  776 daldFKKDkGAFYLVFEYMDHdlmGLLESGLV---HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIK 852
Cdd:cd05583    68 ----FQTD-AKLHLILDYVNG---GELFTHLYqreHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFGLARLY-SSEESRPYTnKVITLWYRPPELLLGEER-YTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRic 930
Cdd:cd05583   140 LTDFGLSKEFlPGENDRAYS-FCGTIEYMAPEVVRGGSDgHDKAVDWWSLGVLTYELLTGASPFTVDGERNSQSEISK-- 216
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  931 gspcpavwpdviKLPYFNTMKPKKqyrrklreefvfIPAAALDLFDYMLALDPSKR 986
Cdd:cd05583   217 ------------RILKSHPPIPKT------------FSAEAKDFILKLLEKDPKKR 248
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
705-1002 3.07e-14

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: 74.75  E-value: 3.07e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNekegfpitaireiKILRQLTHQsIINMKEIVTDKEDAL------ 778
Cdd:cd05609     2 FETIKLISNGAYGAVYLVRHRETRQRFAMKKINKQN-------------LILRNQIQQ-VFVERDILTFAENPFvvsmyc 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 DFKKDKgAFYLVFEYMDH-DLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG 857
Cdd:cd05609    68 SFETKR-HLCMVMEYVEGgDCATLLKN-IGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFG 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARL------------YSSEESRPYTNKVI--TLWYRPPELLLgEERYTPAIDVWSCGCILGE-LFTKKPIFQANQElaq 922
Cdd:cd05609   146 LSKIglmslttnlyegHIEKDTREFLDKQVcgTPEYIAPEVIL-RQGYGKPVDWWAMGIILYEfLVGCVPFFGDTPE--- 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  923 lELISRICGSpcPAVWPdviklpyfntmkpkkqyrrklrEEFVFIPAAALDLFDYMLALDPSKR---CTAEQALQCEFLR 999
Cdd:cd05609   222 -ELFGQVISD--EIEWP----------------------EGDDALPDDAQDLITRLLQQNPLERlgtGGAEEVKQHPFFQ 276

                  ...
gi 145309300 1000 DVE 1002
Cdd:cd05609   277 DLD 279
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
703-967 3.15e-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: 74.69  E-value: 3.15e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKA-----RDKDTGEMVALKKVRlDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDA 777
Cdd:cd05032     6 EKITLIRELGQGSFGMVYEGlakgvVKGEPETRVAIKTVN-ENASMRERIEFLNEASVMKEFNCHHVVRLLGVVSTGQPT 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 LdfkkdkgafyLVFEYMDH-DLMGLLESglvHFNENHIKSF----MRQLM--------EGLDYCHKKNFLHRDIKCSNIL 844
Cdd:cd05032    85 L----------VVMELMAKgDLKSYLRS---RRPEAENNPGlgppTLQKFiqmaaeiaDGMAYLAAKKFVHRDLAARNCM 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  845 LNNRGQIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPifQANQELAQL 923
Cdd:cd05032   152 VAEDLTVKIGDFGMTRdIYETDYYRKGGKGLLPVRWMAPESLK-DGVFTTKSDVWSFGVVLWEMATLAE--QPYQGLSNE 228
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 145309300  924 ELISRICGS-----P--CPAVWPDVIKLPYfntmkpkkQYRRKLREEFVFI 967
Cdd:cd05032   229 EVLKFVIDGghldlPenCPDKLLELMRMCW--------QYNPKMRPTFLEI 271
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
702-882 3.48e-14

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: 75.86  E-value: 3.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIR-EIKILRQLTHQSIINMKEIVTDKEDaldf 780
Cdd:cd05627     1 LDDFESLKVIGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVAHIRaERDILVEADGAWVVKMFYSFQDKRN---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  781 kkdkgaFYLVFEYM-DHDLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd05627    77 ------LYLIMEFLpGGDMMTLLMKKDT-LSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLC 149
                         170       180
                  ....*....|....*....|....
gi 145309300  860 R-LYSSEESRPYTNkvitLWYRPP 882
Cdd:cd05627   150 TgLKKAHRTEFYRN----LTHNPP 169
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
711-1018 4.11e-14

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: 74.68  E-value: 4.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVrlDNEKEgfpiTAIREIKILRQL-THQSIINMKeivtdkedalDFKKDKGAFYL 789
Cdd:cd14175     9 IGVGSYSVCKRCVHKATNMEYAVKVI--DKSKR----DPSEEIEILLRYgQHPNIITLK----------DVYDDGKHVYL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDHDlmGLLESGLVH--FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL----NNRGQIKLADFGLARLYS 863
Cdd:cd14175    73 VTELMRGG--ELLDKILRQkfFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYvdesGNPESLRICDFGFAKQLR 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEESRPYTnKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCpavwpdVIK 943
Cdd:cd14175   151 AENGLLMT-PCYTANFVAPE-VLKRQGYDEGCDIWSLGILLYTMLAGYTPFANGPSDTPEEILTRIGSGKF------TLS 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  944 LPYFNTmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCEFLrdVEPSKMPPPDLPlWQDCH 1018
Cdd:cd14175   223 GGNWNT-----------------VSDAAKDLVSKMLHVDPHQRLTAKQVLQHPWI--TQKDKLPQSQLN-HQDVQ 277
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
711-913 4.42e-14

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: 74.07  E-value: 4.42e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARdKDTGEMVALKKV---RLDNEKEGFPitaiREIKILRQLTHQSIINMKEIVTDKEDALdfkkdkgaf 787
Cdd:cd14664     1 IGRGGAGTVYKGV-MPNGTLVAVKRLkgeGTQGGDHGFQ----AEIQTLGMIRHRNIVRLRGYCSNPTTNL--------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 yLVFEYMDH-DLMGLLESGlvHFNENHIKSFMRQLM-----EGLDYCHKK---NFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd14664    67 -LVYEYMPNgSLGELLHSR--PESQPPLDWETRQRIalgsaRGLAYLHHDcspLIIHRDVKSNNILLDEEFEAHVADFGL 143
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  859 ARLYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT-KKPI 913
Cdd:cd14664   144 AKLMDDKDSHVMSSVAGSYGYIAPEYAY-TGKVSEKSDVYSYGVVLLELITgKRPF 198
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
711-909 4.68e-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: 73.91  E-value: 4.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKAR-DKDTgemvalkKVRLDNEKEG-FPITA-IREIKILRQLTHQSIINMKEIVTdkedaldfkkdKGAF 787
Cdd:cd05073    19 LGAGQFGEVWMATyNKHT-------KVAVKTMKPGsMSVEAfLAEANVMKTLQHDKLVKLHAVVT-----------KEPI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDH-DLMGLLESGlvHFNENHIKS---FMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL-- 861
Cdd:cd05073    81 YIITEFMAKgSLLDFLKSD--EGSKQPLPKlidFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVie 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 145309300  862 ---YSSEESRPYTNKvitlWYRPPELLLGEerYTPAIDVWSCGCILGELFT 909
Cdd:cd05073   159 dneYTAREGAKFPIK----WTAPEAINFGS--FTIKSDVWSFGILLMEIVT 203
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
703-914 4.97e-14

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: 75.66  E-value: 4.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPITAIREIKILRQLTHQSiiNMKEIVTdkedaLDFK- 781
Cdd:cd05629     1 EDFHTVKVIGKGAFGEVRLVQKKDTGKIYAMKTLL---KSEMFKKDQLAHVKAERDVLAES--DSPWVVS-----LYYSf 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 KDKGAFYLVFEYM-DHDLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA- 859
Cdd:cd05629    71 QDAQYLYLIMEFLpGGDLMTMLIKYDT-FSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSt 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  860 ------------RLYSSEESRPYTNKV-----------------ITLW----------------YRPPELLLGEErYTPA 894
Cdd:cd05629   150 gfhkqhdsayyqKLLQGKSNKNRIDNRnsvavdsinltmsskdqIATWkknrrlmaystvgtpdYIAPEIFLQQG-YGQE 228
                         250       260
                  ....*....|....*....|
gi 145309300  895 IDVWSCGCILGELFTKKPIF 914
Cdd:cd05629   229 CDWWSLGAIMFECLIGWPPF 248
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
711-909 4.99e-14

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


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 73.92  E-value: 4.99e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKAR-DKDTGEM--VALKKVRLDN-EKEGFPITAIREIKILRQLTHQSIINMKEIVTDK------EDA--- 777
Cdd:cd05040     3 LGDGSFGVVRRGEwTTPSGKViqVAVKCLKSDVlSQPNAMDDFLKEVNAMHSLDHPNLIRLYGVVLSSplmmvtELAplg 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 --LDFKKDKGAFYLVFEYMDhdlmgllesglvhfnenhiksFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLAD 855
Cdd:cd05040    83 slLDRLRKDQGHFLISTLCD---------------------YAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGD 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  856 FGLAR-------LYSSEESRpytnKVITLWYRPPELLLGeeRYTPAIDVWSCGCILGELFT 909
Cdd:cd05040   142 FGLMRalpqnedHYVMQEHR----KVPFAWCAPESLKTR--KFSHASDVWMFGVTLWEMFT 196
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
711-909 5.84e-14

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: 73.61  E-value: 5.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDN-EKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkgAFYL 789
Cdd:cd05052    14 LGGGQYGEVYEGVWKKYNLTVAVKTLKEDTmEVEEF----LKEAAVMKEIKHPNLVQLLGVCTREP----------PFYI 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDHdlmGLLESGLVHFNENHIKS----FM-RQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSS 864
Cdd:cd05052    80 ITEFMPY---GNLLDYLRECNREELNAvvllYMaTQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTG 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 145309300  865 EEsrpYT----NKVITLWYRPPEllLGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05052   157 DT---YTahagAKFPIKWTAPES--LAYNKFSIKSDVWAFGVLLWEIAT 200
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
710-910 6.61e-14

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: 73.66  E-value: 6.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKAR--DKDTGEM-VALKKV-RLDN--EKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEdaldfkkd 783
Cdd:cd05058     2 VIGKGHFGCVYHGTliDSDGQKIhCAVKSLnRITDieEVEQF----LKEGIIMKDFSHPNVLSLLGICLPSE-------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kGAFYLVFEYMDHdlmglleSGLVHF--NENH------IKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLAD 855
Cdd:cd05058    70 -GSPLVVLPYMKH-------GDLRNFirSETHnptvkdLIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVAD 141
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  856 FGLAR-LYSSEESRPYTNKVITLwyrPPELL----LGEERYTPAIDVWSCGCILGELFTK 910
Cdd:cd05058   142 FGLARdIYDKEYYSVHNHTGAKL---PVKWMalesLQTQKFTTKSDVWSFGVLLWELMTR 198
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
710-991 7.60e-14

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


Pssm-ID: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 73.49  E-value: 7.60e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKkVRLDNEKegfpitAIREIKIlrqltHQSIINMKEIVTDKEDALDFKKDKGAFYL 789
Cdd:cd14172    11 VLGLGVNGKVLECFHRRTGQKCALK-LLYDSPK------ARREVEH-----HWRASGGPHIVHILDVYENMHHGKRCLLI 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLMG-LLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR---GQIKLADFGLARlySS 864
Cdd:cd14172    79 IMECMEGgELFSrIQERGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKekdAVLKLTDFGFAK--ET 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  865 EESRPYTNKVITLWYRPPELLlGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRicgspcpavwpdVIKL 944
Cdd:cd14172   157 TVQNALQTPCYTPYYVAPEVL-GPEKYDKSCDMWSLGVIMYILLCGFPPFYSNTGQAISPGMKR------------RIRM 223
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 145309300  945 PYFNTMKPkkqyrrklreEFVFIPAAALDLFDYMLALDPSKRCTAEQ 991
Cdd:cd14172   224 GQYGFPNP----------EWAEVSEEAKQLIRHLLKTDPTERMTITQ 260
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
705-912 7.90e-14

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: 73.60  E-value: 7.90e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALdfk 781
Cdd:cd05057     9 LEKGKVLGSGAFGTVYKGVWIPEGEKVKIPvaiKVLREETGPKANEEILDEAYVMASVDHPHLVRLLGICLSSQVQL--- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgafylVFEYMDhdLMGLLEsgLVHFNENHIKS-----FMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADF 856
Cdd:cd05057    86 --------ITQLMP--LGCLLD--YVRNHRDNIGSqlllnWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDF 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSEES--RPYTNKVITLWYRPPELLLGEerYTPAIDVWSCGCILGELFT--KKP 912
Cdd:cd05057   154 GLAKLLDVDEKeyHAEGGKVPIKWMALESIQYRI--YTHKSDVWSYGVTVWELMTfgAKP 211
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
703-903 8.36e-14

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: 73.01  E-value: 8.36e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGfpiTAIREIKILRQLTHQSIINMKEIvtdkedaldFKK 782
Cdd:cd14108     2 DYYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPVRAKKKT---SARRELALLAELDHKSIVRFHDA---------FEK 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dKGAFYLVFEYMDHDLMgLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRG--QIKLADFGLAR 860
Cdd:cd14108    70 -RRVVIIVTELCHEELL-ERITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQ 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 145309300  861 LYSSEEsrPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCI 903
Cdd:cd14108   148 ELTPNE--PQYCKYGTPEFVAPE-IVNQSPVSKVTDIWPVGVI 187
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
710-921 8.93e-14

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 72.81  E-value: 8.93e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKdtGEMVALKKVRLDNEKEgFPITA---IREIKILRQLTHQSIINMKEIVTDKEDaldfkkdkga 786
Cdd:cd14061     1 VIGVGGFGKVYRGIWR--GEEVAVKAARQDPDED-ISVTLenvRQEARLFWMLRHPNIIALRGVCLQPPN---------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEY-----MDHDLMGLLESGLVHFNenhiksFMRQLMEGLDYCHKKN---FLHRDIKCSNILLNNRGQ-------- 850
Cdd:cd14061    68 LCLVMEYarggaLNRVLAGRKIPPHVLVD------WAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAIEnedlenkt 141
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  851 IKLADFGLARlyssEESRpyTNKVI---TLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELA 921
Cdd:cd14061   142 LKITDFGLAR----EWHK--TTRMSaagTYAWMAPE-VIKSSTFSKASDVWSYGVLLWELLTGEVPYKGIDGLA 208
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
705-1001 1.04e-13

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 74.53  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKvrldnekeGFPITAIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdk 784
Cdd:PHA03209   68 YTVIKTLTPGSEGRVFVATKPGQPDPVVLKI--------GQKGTTLIEAMLLQNVNHPSVIRMKDTLVSGA--------- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSS 864
Cdd:PHA03209  131 -ITCMVLPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQVCIGDLGAAQFPVV 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  865 EESrpYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT-KKPIFQA----------NQELAQLELISRI---- 929
Cdd:PHA03209  210 APA--FLGLAGTVETNAPE-VLARDKYNSKADIWSAGIVLFEMLAyPSTIFEDppstpeeyvkSCHSHLLKIISTLkvhp 286
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  930 ---CGSPCPAVWPDVIKlpYFNTM-KPKKQYRRKLReefVFIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRDV 1001
Cdd:PHA03209  287 eefPRDPGSRLVRGFIE--YASLErQPYTRYPCFQR---VNLPIDGEFLVHKMLTFDAAMRPSAEEILNYPMFAQL 357
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
704-904 1.05e-13

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: 74.13  E-value: 1.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLdNEKEGFPItAIREIKILR--QLTHQSIINMKEIVTDK------- 774
Cdd:cd13977     1 KYSLIREVGRGSYGVVYEAVVRRTGARVAVKKIRC-NAPENVEL-ALREFWALSsiQRQHPNVIQLEECVLQRdglaqrm 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  775 --------------------EDALDFKKdkgAFYL--VFEYMDH-DLMGLLESGLVHFNENhiKSFMRQLMEGLDYCHKK 831
Cdd:cd13977    79 shgssksdlylllvetslkgERCFDPRS---ACYLwfVMEFCDGgDMNEYLLSRRPDRQTN--TSFMLQLSSALAFLHRN 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  832 NFLHRDIKCSNILL-NNRGQ--IKLADFGLARLYSSEESRPYTNKVI----------TLWYRPPELLlgEERYTPAIDVW 898
Cdd:cd13977   154 QIVHRDLKPDNILIsHKRGEpiLKVADFGLSKVCSGSGLNPEEPANVnkhflssacgSDFYMAPEVW--EGHYTAKADIF 231

                  ....*.
gi 145309300  899 SCGCIL 904
Cdd:cd13977   232 ALGIII 237
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
710-910 1.25e-13

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: 73.24  E-value: 1.25e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKdtGEMVALKKVRLDNEKEGFpitaiREIKILR--QLTHQSIINMkeIVTDKEDALDFKKdkgaF 787
Cdd:cd13998     2 VIGKGRFGEVWKASLK--NEPVAVKIFSSRDKQSWF-----REKEIYRtpMLKHENILQF--IAADERDTALRTE----L 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDH------------------DLMGLLESGLVHFNENHIKSFMrqlmegldycHKKNFLHRDIKCSNILLNNRG 849
Cdd:cd13998    69 WLVTAFHPNgsl*dylslhtidwvslcRLALSVARGLAHLHSEIPGCTQ----------GKPAIAHRDLKSKNILVKNDG 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  850 QIKLADFGLA-RLYSSEESRPYTN--KVITLWYRPPELLLG------EERYTpAIDVWSCGCILGELFTK 910
Cdd:cd13998   139 TCCIADFGLAvRLSPSTGEEDNANngQVGTKRYMAPEVLEGainlrdFESFK-RVDIYAMGLVLWEMASR 207
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
710-923 1.44e-13

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: 73.46  E-value: 1.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEGFPITAIREIkILRQLTHQSIINMKEIVTDKEDaldfkkdkga 786
Cdd:cd05603     2 VIGKGSFGKVLLAKRKCDGKFYAVKvlqKKTILKKKEQNHIMAERNV-LLKNLKHPFLVGLHYSFQTSEK---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARlYSSEE 866
Cdd:cd05603    71 LYFVLDYVNGGELFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCK-EGMEP 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  867 SRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQAnQELAQL 923
Cdd:cd05603   150 EETTSTFCGTPEYLAPE-VLRKEPYDRTVDWWCLGAVLYEMLYGLPPFYS-RDVSQM 204
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
710-910 2.21e-13

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: 72.36  E-value: 2.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDtgEMVALKKVRLdNEKEGFpiTAIREIKILRQLTHQSIINM----KEIVTDKEDaldfkkdkg 785
Cdd:cd14053     2 IKARGRFGAVWKAQYLN--RLVAVKIFPL-QEKQSW--LTEREIYSLPGMKHENILQFigaeKHGESLEAE--------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 aFYLVFEYMDH-DLMGLLESGLVHFNE-NHIKSFMRQlmeGLDYCH----------KKNFLHRDIKCSNILLNNRGQIKL 853
Cdd:cd14053    68 -YWLITEFHERgSLCDYLKGNVISWNElCKIAESMAR---GLAYLHedipatngghKPSIAHRDFKSKNVLLKSDLTACI 143
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  854 ADFGLARLYSSEESRPYTN-KVITLWYRPPELLLGEERYTP----AIDVWSCGCILGELFTK 910
Cdd:cd14053   144 ADFGLALKFEPGKSCGDTHgQVGTRRYMAPEVLEGAINFTRdaflRIDMYAMGLVLWELLSR 205
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
732-909 2.24e-13

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: 72.43  E-value: 2.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  732 ALKKVRLDNEKEGFPITAIR---EIKILRQLTHQSIINMKeivtdkedALDFKKDkGAFYLVFEYMDHDLMGLLE----S 804
Cdd:cd14001    32 AVKKINSKCDKGQRSLYQERlkeEAKILKSLNHPNIVGFR--------AFTKSED-GSLCLAMEYGGKSLNDLIEeryeA 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  805 GLVHFNENHIKSFMRQLMEGLDYCH-KKNFLHRDIKCSNILLNNRGQ-IKLADFGLArLYSSEE----SRPYTNKVITLW 878
Cdd:cd14001   103 GLGPFPAATILKVALSIARALEYLHnEKKILHGDIKSGNVLIKGDFEsVKLCDFGVS-LPLTENlevdSDPKAQYVGTEP 181
                         170       180       190
                  ....*....|....*....|....*....|.
gi 145309300  879 YRPPELLLGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd14001   182 WKAKEALEEGGVITDKADIFAYGLVLWEMMT 212
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
708-942 2.31e-13

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: 72.04  E-value: 2.31e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  708 IGIIGEGTYGQVYKARDKDTgemVALKKVrldNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDaldfkkdkgaF 787
Cdd:cd13992     8 SSHTGEPKYVKKVGVYGGRT---VAIKHI---TFSRTEKRTILQELNQLKELVHDNLNKFIGICINPPN----------I 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDH-DLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNF-LHRDIKCSNILLNNRGQIKLADFGLARLYSSE 865
Cdd:cd13992    72 AVVTEYCTRgSLQDVLLNREIKMDWMFKSSFIKDIVKGMNYLHSSSIgYHGRLKSSNCLVDSRWVVKLTDFGLRNLLEEQ 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  866 ESRP---YTNKVITLWYrPPELL---LGEERYTPAIDVWSCGCILGELFTKKPIFqANQELAQLELISRICGSPCPAvwP 939
Cdd:cd13992   152 TNHQldeDAQHKKLLWT-APELLrgsLLEVRGTQKGDVYSFAIILYEILFRSDPF-ALEREVAIVEKVISGGNKPFR--P 227

                  ...
gi 145309300  940 DVI 942
Cdd:cd13992   228 ELA 230
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
703-911 2.33e-13

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: 72.07  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLD-NEKEgfpitairEIKILRQLThqsiINMKeiVTDKEDALDFK 781
Cdd:cd06617     1 DDLEVIEELGRGAYGVVDKMRHVPTGTIMAVKRIRATvNSQE--------QKRLLMDLD----ISMR--SVDCPYTVTFY 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkGAFY------LVFEYMDHDLMGL----LESGLvHFNENHIKSFMRQLMEGLDYCHKK-NFLHRDIKCSNILLNNRGQ 850
Cdd:cd06617    67 ---GALFregdvwICMEVMDTSLDKFykkvYDKGL-TIPEDILGKIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQ 142
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  851 IKLADFGLA-RLYSS------EESRPYTnkvitlwyrPPELLLGE---ERYTPAIDVWSCGCILGELFTKK 911
Cdd:cd06617   143 VKLCDFGISgYLVDSvaktidAGCKPYM---------APERINPElnqKGYDVKSDVWSLGITMIELATGR 204
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
711-936 2.40e-13

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: 71.90  E-value: 2.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYG----QVYKARDKDTGemVALKKVRLDNEKeGFPITAIREIKILRQLTHQSIINMKEIVtdkedaldfkkDKGA 786
Cdd:cd05115    12 LGSGNFGcvkkGVYKMRKKQID--VAIKVLKQGNEK-AVRDEMMREAQIMHQLDNPYIVRMIGVC-----------EAEA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDHD-LMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSE 865
Cdd:cd05115    78 LMLVMEMASGGpLNKFLSGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKALGAD 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  866 ESRpYTNKVITLW---YRPPELLLgEERYTPAIDVWSCGCILGELFT--KKPI--FQANQELAQLELISRI-CGSPCPA 936
Cdd:cd05115   158 DSY-YKARSAGKWplkWYAPECIN-FRKFSSRSDVWSYGVTMWEAFSygQKPYkkMKGPEVMSFIEQGKRMdCPAECPP 234
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
710-921 2.40e-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: 72.76  E-value: 2.40e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRlDNEKegfpitAIREIKIlrqltHQSIINMKEIVTDKEDALDFKKDKGAFYL 789
Cdd:cd14170     9 VLGLGINGKVLQIFNKRTQEKFALKMLQ-DCPK------ARREVEL-----HWRASQCPHIVRIVDVYENLYAGRKCLLI 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLMGLLES-GLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNR---GQIKLADFGLARLYSS 864
Cdd:cd14170    77 VMECLDGgELFSRIQDrGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTDFGFAKETTS 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  865 EESrpYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELA 921
Cdd:cd14170   157 HNS--LTTPCYTPYYVAPE-VLGPEKYDKSCDMWSLGVIMYILLCGYPPFYSNHGLA 210
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
711-909 2.66e-13

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: 72.37  E-value: 2.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKAR----------------DKDTGEMVALKKVRLD---NEKEGFpitaIREIKILRQLTHQSIINMKEIV 771
Cdd:cd05051    13 LGEGQFGEVHLCEanglsdltsddfigndNKDEPVLVAVKMLRPDaskNAREDF----LKEVKIMSQLKDPNIVRLLGVC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  772 TDKEDAldfkkdkgafYLVFEYMDH-DLMGLL------ESGLVHFNENHIKS----FM-RQLMEGLDYCHKKNFLHRDIK 839
Cdd:cd05051    89 TRDEPL----------CMIVEYMENgDLNQFLqkheaeTQGASATNSKTLSYgtllYMaTQIASGMKYLESLNFVHRDLA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  840 CSNILLNNRGQIKLADFGLAR-LYSSEESRPYTNKVITL-WYRPPELLLGeeRYTPAIDVWSCGCILGELFT 909
Cdd:cd05051   159 TRNCLVGPNYTIKIADFGMSRnLYSGDYYRIEGRAVLPIrWMAWESILLG--KFTTKSDVWAFGVTLWEILT 228
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
711-909 2.85e-13

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: 71.41  E-value: 2.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKdtGEMVALKKVRLD-----NEKEGFpitaIREIKILRQLTHQSIINMKEIVTDkedaldfkkDKG 785
Cdd:cd14064     1 IGSGSFGKVYKGRCR--NKIVAIKRYRANtycskSDVDMF----CREVSILCRLNHPCVIQFVGACLD---------DPS 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 AFYLVFEYMDHdlmGLLESgLVHFNENHI--KSFMR---QLMEGLDYCHK--KNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd14064    66 QFAIVTQYVSG---GSLFS-LLHEQKRVIdlQSKLIiavDVAKGMEYLHNltQPIIHRDLNSHNILLYEDGHAVVADFGE 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 145309300  859 ARLYSSEESRPYTNKVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd14064   142 SRFLQSLDEDNMTKQPGNLRWMAPEVFTQCTRYSIKADVFSYALCLWELLT 192
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
705-919 2.88e-13

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 72.72  E-value: 2.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDN--EKEGFPITAIrEIKILRQLTHQSIINMKEIVTDKEDALdfkk 782
Cdd:cd05616     2 FNFLMVLGKGSFGKVMLAERKGTDELYAVKILKKDVviQDDDVECTMV-EKRVLALSGKPPFLTQLHSCFQTMDRL---- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgafYLVFEYMDH-DLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR- 860
Cdd:cd05616    77 -----YFVMEYVNGgDLMYHIQQ-VGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKe 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 -LYSSEESRPYTNkviTLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQE 919
Cdd:cd05616   151 nIWDGVTTKTFCG---TPDYIAPE-IIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDE 206
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
710-967 3.57e-13

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: 71.61  E-value: 3.57e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKdtGEMVALKKVRLDNEKEgfpITAI-----REIKILRQLTHQSIINMKEIVTDKEDaldfkkdk 784
Cdd:cd14146     1 IIGVGGFGKVYRATWK--GQEVAVKAARQDPDED---IKATaesvrQEAKLFSMLRHPNIIKLEGVCLEEPN-------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gaFYLVFEYMDHdlmGLLESGLVHFNENHIKSFMR------------QLMEGLDYCHKKNF---LHRDIKCSNILLNN-- 847
Cdd:cd14146    68 --LCLVMEFARG---GTLNRALAAANAAPGPRRARripphilvnwavQIARGMLYLHEEAVvpiLHRDLKSSNILLLEki 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  848 ------RGQIKLADFGLARLYSSeesrpyTNKVITL----WYRPPelLLGEERYTPAIDVWSCGCILGELFTKKPIFQAN 917
Cdd:cd14146   143 ehddicNKTLKITDFGLAREWHR------TTKMSAAgtyaWMAPE--VIKSSLFSKGSDIWSYGVLLWELLTGEVPYRGI 214
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  918 QELA--------QLELisricgsPCPAVWPDviklPYFNTMKPKKQYRRKLREEFVFI 967
Cdd:cd14146   215 DGLAvaygvavnKLTL-------PIPSTCPE----PFAKLMKECWEQDPHIRPSFALI 261
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
710-926 3.68e-13

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 72.28  E-value: 3.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVR-----LDNEKEgfpiTAIREIKILRQLTHQSIINMKEIVTDKEDALdfkkdk 784
Cdd:cd05620     2 VLGKGSFGKVLLAELKGKGEYFAVKALKkdvvlIDDDVE----CTMVEKRVLALAWENPFLTHLYCTFQTKEHL------ 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gafYLVFEYMDH-DLM-GLLESGlvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLY 862
Cdd:cd05620    72 ---FFVMEFLNGgDLMfHIQDKG--RFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKEN 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  863 SSEESRPYTNkVITLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELI 926
Cdd:cd05620   147 VFGDNRASTF-CGTPDYIAPEILQG-LKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESI 208
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
710-909 3.81e-13

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: 71.23  E-value: 3.81e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKAR-DKDTGEMVA----LKKVRLDNEKEGFPitaiREIKILRQL-THQSIINMkeivtdkedaLDFKKD 783
Cdd:cd05047     2 VIGEGNFGQVLKARiKKDGLRMDAaikrMKEYASKDDHRDFA----GELEVLCKLgHHPNIINL----------LGACEH 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDH-DLMGLLESGLV---------------HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN 847
Cdd:cd05047    68 RGYLYLAIEYAPHgNLLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGE 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  848 RGQIKLADFGLARlysSEESrpYTNKVITlwyRPPELLLGEER-----YTPAIDVWSCGCILGELFT 909
Cdd:cd05047   148 NYVAKIADFGLSR---GQEV--YVKKTMG---RLPVRWMAIESlnysvYTTNSDVWSYGVLLWEIVS 206
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
709-904 3.97e-13

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 71.39  E-value: 3.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  709 GIIGEGTYGQVYKARDKDTGEMVALKKVRLdnekEGFpitAIREIKILRQLTHQSIINMKEIVTDkedaldfkkdkGAFY 788
Cdd:cd13991    12 LRIGRGSFGEVHRMEDKQTGFQCAVKKVRL----EVF---RAEELMACAGLTSPRVVPLYGAVRE-----------GPWV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVF-EYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ-IKLADFGLA-RLYSSE 865
Cdd:cd13991    74 NIFmDLKEGGSLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSdAFLCDFGHAeCLDPDG 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 145309300  866 ESRP-YTNKVI--TLWYRPPELLLGEERYTPAiDVWSCGCIL 904
Cdd:cd13991   154 LGKSlFTGDYIpgTETHMAPEVVLGKPCDAKV-DVWSSCCMM 194
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
714-907 4.28e-13

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: 71.94  E-value: 4.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  714 GTYGQVYKArdKDTGEMVALKKVRLDNE-KEGFpiTAI-REIKILRQLTHQSIINMKEIVTDKEDaldfkkdkgaFYLVF 791
Cdd:cd08216    13 GGVVHLAKH--KPTNTLVAVKKINLESDsKEDL--KFLqQEILTSRQLQHPNILPYVTSFVVDND----------LYVVT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  792 EYMDH----DLM-GLLESGlvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEE 866
Cdd:cd08216    79 PLMAYgscrDLLkTHFPEG---LPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAYSMVKHG 155
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 145309300  867 SRPYT------NKVITLWYRPPELL----LGeerYTPAIDVWSCGCILGEL 907
Cdd:cd08216   156 KRQRVvhdfpkSSEKNLPWLSPEVLqqnlLG---YNEKSDIYSVGITACEL 203
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
703-993 4.30e-13

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


Pssm-ID: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 71.00  E-value: 4.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDII-GIIGEGTYGQVYKARDKDTGEMVALKKVRLDNekegfpiTAIREIKILRQLTHQSIINMKEIVTDKEDALdfk 781
Cdd:cd14109     3 ELYEIGeEDEKRAAQGAPFHVTERSTGRNFLAQLRYGDP-------FLMREVDIHNSLDHPNIVQMHDAYDDEKLAV--- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgafyLVFEYMDHDLMGLLESGLV---HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNrGQIKLADFGL 858
Cdd:cd14109    73 -------TVIDNLASTIELVRDNLLPgkdYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQD-DKLKLADFGQ 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARlysseesRPYTNKVITLWYRPPELLLGE----ERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLElisricgspc 934
Cdd:cd14109   145 SR-------RLLRGKLTTLIYGSPEFVSPEivnsYPVTLATDMWSVGVLTYVLLGGISPFLGDNDRETLT---------- 207
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  935 pavwpdviklpyfNTMKPKKQYRrklREEFVFIPAAALDLFDYMLALDPSKRCTAEQAL 993
Cdd:cd14109   208 -------------NVRSGKWSFD---SSPLGNISDDARDFIKKLLVYIPESRLTVDEAL 250
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
705-919 4.93e-13

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: 72.34  E-value: 4.93e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDN--EKEGFPITAIrEIKILRQLTHQSIINMKEIVTDKEDALdfkk 782
Cdd:cd05615    12 FNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDVviQDDDVECTMV-EKRVLALQDKPPFLTQLHSCFQTVDRL---- 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkgafYLVFEYMDH-DLMGLLESgLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARL 861
Cdd:cd05615    87 -----YFVMEYVNGgDLMYHIQQ-VGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKE 160
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  862 YSSE--ESRPYTNkviTLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQE 919
Cdd:cd05615   161 HMVEgvTTRTFCG---TPDYIAPE-IIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDE 216
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
710-926 5.87e-13

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: 71.86  E-value: 5.87e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTdkedaldFKKDKGAFYl 789
Cdd:cd05590     2 VLGKGSFGKVMLARLKESGRLYAVKVLKKDVILQDDDVECTMTEKRILSLARNHPFLTQLYCC-------FQTPDRLFF- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 VFEYMDH-DLMGLLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARlyssEESR 868
Cdd:cd05590    74 VMEFVNGgDLMFHIQKSR-RFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCK----EGIF 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  869 pytNKVITLW------YRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELI 926
Cdd:cd05590   149 ---NGKTTSTfcgtpdYIAPE-ILQEMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAI 208
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
703-994 6.08e-13

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: 71.98  E-value: 6.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVrlDNEKEgfpiTAIREIKIL-RQLTHQSIINMKEIVTDKEdaldfk 781
Cdd:cd14176    19 DGYEVKEDIGVGSYSVCKRCIHKATNMEFAVKII--DKSKR----DPTEEIEILlRYGQHPNIITLKDVYDDGK------ 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgAFYLVFEYMDHDlmGLLESGLVH--FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL----NNRGQIKLAD 855
Cdd:cd14176    87 ----YVYVVTELMKGG--ELLDKILRQkfFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYvdesGNPESIRICD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  856 FGLARLYSSEESRPYTnKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSPCP 935
Cdd:cd14176   161 FGFAKQLRAENGLLMT-PCYTANFVAPE-VLERQGYDAACDIWSLGVLLYTMLTGYTPFANGPDDTPEEILARIGSGKFS 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  936 avwpdvIKLPYFNTmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14176   239 ------LSGGYWNS-----------------VSDTAKDLVSKMLHVDPHQRLTAALVLR 274
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
703-994 6.55e-13

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: 71.20  E-value: 6.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVrlDNEKEgfpiTAIREIKIL-RQLTHQSIINMKEIVtdkedaldfk 781
Cdd:cd14178     3 DGYEIKEDIGIGSYSVCKRCVHKATSTEYAVKII--DKSKR----DPSEEIEILlRYGQHPNIITLKDVY---------- 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kDKGAF-YLVFEYMdhdlMG--LLESGLVH--FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL----NNRGQIK 852
Cdd:cd14178    67 -DDGKFvYLVMELM----RGgeLLDRILRQkcFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYmdesGNPESIR 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFGLARLYSSEESRPYTnKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRIcGS 932
Cdd:cd14178   142 ICDFGFAKQLRAENGLLMT-PCYTANFVAPE-VLKRQGYDAACDIWSLGILLYTMLAGFTPFANGPDDTPEEILARI-GS 218
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  933 PCPAV----WPDviklpyfntmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQ 994
Cdd:cd14178   219 GKYALsggnWDS--------------------------ISDAAKDIVSKMLHVDPHQRLTAPQVLR 258
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
711-901 6.61e-13

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: 70.33  E-value: 6.61e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGfpiTAIREIKILRQLTHQSIINMK-EIVTDKEDALDFKKDKGAfyl 789
Cdd:cd14110    11 INRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDKQ---LVLREYQVLRRLSHPRIAQLHsAYLSPRHLVLIEELCSGP--- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  790 vfeymdHDLMGLLESGLvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRP 869
Cdd:cd14110    85 ------ELLYNLAERNS--YSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLM 156
                         170       180       190
                  ....*....|....*....|....*....|..
gi 145309300  870 YTNKVITLWYRPPELLLGEErYTPAIDVWSCG 901
Cdd:cd14110   157 TDKKGDYVETMAPELLEGQG-AGPQTDIWAIG 187
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
711-909 6.66e-13

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 71.53  E-value: 6.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKAR----DKDTGEMVALKKVRL--DNEKEGFPITAIREIKILRQL-THQSIINMKEIVTDKedaldfkkd 783
Cdd:cd05099    20 LGEGCFGQVVRAEaygiDKSRPDQTVTVAVKMlkDNATDKDLADLISEMELMKLIgKHKNIINLLGVCTQE--------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kGAFYLVFEY-----------------MDHDLMGL-LESGLVHFNEnhIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL 845
Cdd:cd05099    91 -GPLYVIVEYaakgnlreflrarrppgPDYTFDITkVPEEQLSFKD--LVSCAYQVARGMEYLESRRCIHRDLAARNVLV 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  846 NNRGQIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05099   168 TEDNVMKIADFGLARgVHDIDYYKKTSNGRLPVKWMAPEALF-DRVYTHQSDVWSFGILMWEIFT 231
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
710-909 6.97e-13

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: 70.98  E-value: 6.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKAR-----DKDTGEMVALK----KVRLDnEKEGFpitaIREIKILRQL-THQSIINMKEIVTDKedald 779
Cdd:cd05055    42 TLGAGAFGKVVEATayglsKSDAVMKVAVKmlkpTAHSS-EREAL----MSELKIMSHLgNHENIVNLLGACTIG----- 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkkdkGAFYLVFEYMDH-DLMGLLESGLVHFNE-NHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG 857
Cdd:cd05055   112 -----GPILVITEYCCYgDLLNFLRRKRESFLTlEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFG 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  858 LARLYSSEESrpYTNKVITL----WYRPPELLlgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05055   187 LARDIMNDSN--YVVKGNARlpvkWMAPESIF--NCVYTFESDVWSYGILLWEIFS 238
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
706-909 7.24e-13

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: 70.46  E-value: 7.24e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  706 DIIGIIGEGTYGQVYKARDKdtGEmVALKKVRLDNEKEGFPITAIREIKILRQLTHQSII-----NMKE----IVTDked 776
Cdd:cd14063     3 EIKEVIGKGRFGRVHRGRWH--GD-VAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVlfmgaCMDPphlaIVTS--- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  777 aldFKKDKGAFYLVFEYMDHdlmgllesglvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNrGQIKLADF 856
Cdd:cd14063    77 ---LCKGRTLYSLIHERKEK------------FDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDF 140
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  857 GLARL--YSSEESRPYTNKVITLW--YRPPELL---------LGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd14063   141 GLFSLsgLLQPGRREDTLVIPNGWlcYLAPEIIralspdldfEESLPFTKASDVYAFGTVWYELLA 206
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
705-953 8.05e-13

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


Pssm-ID: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 71.97  E-value: 8.05e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVR---LDNEKEGFPITAIREIkiLRQLTHQSIINMKEIVTDKEDaldfk 781
Cdd:cd05626     3 FVKIKTLGIGAFGEVCLACKVDTHALYAMKTLRkkdVLNRNQVAHVKAERDI--LAEADNEWVVKLYYSFQDKDN----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgaFYLVFEYM-DHDLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR 860
Cdd:cd05626    76 -----LYFVMDYIpGGDMMSLLIRMEV-FPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 LYSSEESRPYTNK----------------------------------------------VITLWYRPPELLLgEERYTPA 894
Cdd:cd05626   150 GFRWTHNSKYYQKgshirqdsmepsdlwddvsncrcgdrlktleqratkqhqrclahslVGTPNYIAPEVLL-RKGYTQL 228
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  895 IDVWSCGCILGELFTKKPIFQANQEL-AQLELISricgspcpavWPDVIKLPYFNTMKPK 953
Cdd:cd05626   229 CDWWSVGVILFEMLVGQPPFLAPTPTeTQLKVIN----------WENTLHIPPQVKLSPE 278
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
710-909 8.08e-13

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: 70.02  E-value: 8.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKdtGEMVALKKVRLDNEKEgFPITA---IREIKILRQLTHQSIINMKEIVTDKEDaldfkkdkga 786
Cdd:cd14148     1 IIGVGGFGKVYKGLWR--GEEVAVKAARQDPDED-IAVTAenvRQEARLFWMLQHPNIIALRGVCLNPPH---------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEY-----MDHDLMGLLESGLVHFNenhiksFMRQLMEGLDYCHKKNF---LHRDIKCSNILLNNRGQ-------- 850
Cdd:cd14148    68 LCLVMEYarggaLNRALAGKKVPPHVLVN------WAVQIARGMNYLHNEAIvpiIHRDLKSSNILILEPIEnddlsgkt 141
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  851 IKLADFGLARLYssEESRPYTNKVITLWYRPPELLLgeERYTPAIDVWSCGCILGELFT 909
Cdd:cd14148   142 LKITDFGLAREW--HKTTKMSAAGTYAWMAPEVIRL--SLFSKSSDVWSFGVLLWELLT 196
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
703-914 9.79e-13

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


Pssm-ID: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 71.61  E-value: 9.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIR-EIKILRQLTHQSIINMKEIVTDKEDaldfk 781
Cdd:cd05628     1 EDFESLKVIGRGAFGEVRLVQKKDTGHVYAMKILRKADMLEKEQVGHIRaERDILVEADSLWVVKMFYSFQDKLN----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgaFYLVFEYM-DHDLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR 860
Cdd:cd05628    76 -----LYLIMEFLpGGDMMTLLMKKDT-LTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  861 -LYSSEESRPYTN---------------------------------KVITLWYRPPELLLgEERYTPAIDVWSCGCILGE 906
Cdd:cd05628   150 gLKKAHRTEFYRNlnhslpsdftfqnmnskrkaetwkrnrrqlafsTVGTPDYIAPEVFM-QTGYNKLCDWWSLGVIMYE 228

                  ....*...
gi 145309300  907 LFTKKPIF 914
Cdd:cd05628   229 MLIGYPPF 236
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
704-923 9.79e-13

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: 70.13  E-value: 9.79e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIgiIGEGTYGQVYKARDKDTGEMVA---LKKVRLDN-EKEGFPitaiREIKILRQLTHQSIINMKEivtDKEDALd 779
Cdd:cd14031    13 KFDIE--LGRGAFKTVYKGLDTETWVEVAwceLQDRKLTKaEQQRFK----EEAEMLKGLQHPNIVRFYD---SWESVL- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkKDKGAFYLVFEYMDHdlmGLLESGLVHFN---ENHIKSFMRQLMEGLDYCHKKN--FLHRDIKCSNILLNN-RGQIKL 853
Cdd:cd14031    83 --KGKKCIVLVTELMTS---GTLKTYLKRFKvmkPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKI 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  854 ADFGLARLYSSEesrpYTNKVI-TLWYRPPELLlgEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQL 923
Cdd:cd14031   158 GDLGLATLMRTS----FAKSVIgTPEFMAPEMY--EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQI 222
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
710-914 1.01e-12

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: 70.81  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEGFPITAIREIkILRQLTHQSIINMKeivtdkedaLDFK-KDKg 785
Cdd:cd05575     2 VIGKGSFGKVLLARHKAEGKLYAVKvlqKKAILKRNEVKHIMAERNV-LLKNVKHPFLVGLH---------YSFQtKDK- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 aFYLVFEYMDHdlmGLLESGLV---HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR-- 860
Cdd:cd05575    71 -LYFVLDYVNG---GELFFHLQrerHFPEPRARFYAAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCKeg 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  861 LYSSEESRPYTNkviTLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIF 914
Cdd:cd05575   147 IEPSDTTSTFCG---TPEYLAPEVLRKQP-YDRTVDWWCLGAVLYEMLYGLPPF 196
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
712-962 1.04e-12

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals.The MLTK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 69.60  E-value: 1.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  712 GEGTYGQVYKARDKDTGEMVALKKVrLDNEKEGfpitaireiKILRQLTHQSIINMKEIVTDKEDaldfkkdkgaFYLVF 791
Cdd:cd14060     2 GGGSFGSVYRAIWVSQDKEVAVKKL-LKIEKEA---------EILSVLSHRNIIQFYGAILEAPN----------YGIVT 61
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  792 EYMD----HDLMGLLESGLVHFNenHIKSFMRQLMEGLDYCHKK---NFLHRDIKCSNILLNNRGQIKLADFGLARLYSS 864
Cdd:cd14060    62 EYASygslFDYLNSNESEEMDMD--QIMTWATDIAKGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFHSH 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  865 EESRPYTNkviTLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISR-----ICGSPCPAVWP 939
Cdd:cd14060   140 TTHMSLVG---TFPWMAPEVIQSLP-VSETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEknerpTIPSSCPRSFA 215
                         250       260
                  ....*....|....*....|...
gi 145309300  940 DVIKLPYFNTMKPKKQYRRKLRE 962
Cdd:cd14060   216 ELMRRCWEADVKERPSFKQIIGI 238
PTZ00284 PTZ00284
protein kinase; Provisional
693-938 1.09e-12

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 72.31  E-value: 1.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  693 KDIDWGKRcvdKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnekeGFPiTAIREIKILRQLthqsiinMKEI-V 771
Cdd:PTZ00284  122 EDIDVSTQ---RFKILSLLGEGTFGKVVEAWDRKRKEYCAVKIVR------NVP-KYTRDAKIEIQF-------MEKVrQ 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  772 TDKEDALD-------FKKDKGAFYLVfeyMDHDLMGLLESGLVH--FNENHIKSFMRQLMEGLDYCHKK-NFLHRDIKCS 841
Cdd:PTZ00284  185 ADPADRFPlmkiqryFQNETGHMCIV---MPKYGPCLLDWIMKHgpFSHRHLAQIIFQTGVALDYFHTElHLMHTDLKPE 261
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  842 NILL----------NNRG------QIKLADFGlarlYSSEESRPYTNKVITLWYRPPELLLGEErYTPAIDVWSCGCILG 905
Cdd:PTZ00284  262 NILMetsdtvvdpvTNRAlppdpcRVRICDLG----GCCDERHSRTAIVSTRHYRSPEVVLGLG-WMYSTDMWSMGCIIY 336
                         250       260       270
                  ....*....|....*....|....*....|...
gi 145309300  906 ELFTKKPIFQANQELAQLELISRICGSpCPAVW 938
Cdd:PTZ00284  337 ELYTGKLLYDTHDNLEHLHLMEKTLGR-LPSEW 368
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
710-1012 1.20e-12

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: 70.76  E-value: 1.20e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALK----KVRLdNEKEGFPITAIREIkILRQLTHQSIINMKEI--VTDKedaldfkkd 783
Cdd:cd05604     3 VIGKGSFGKVLLAKRKRDGKYYAVKvlqkKVIL-NRKEQKHIMAERNV-LLKNVKHPFLVGLHYSfqTTDK--------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgaFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYS 863
Cdd:cd05604    72 ---LYFVLDFVNGGELFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEGI 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SeESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQaNQELAQLelisricgspcpavWPDVIK 943
Cdd:cd05604   149 S-NSDTTTTFCGTPEYLAPEVIR-KQPYDNTVDWWCLGSVLYEMLYGLPPFY-CRDTAEM--------------YENILH 211
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  944 LPYfnTMKPKkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQ----CEFLR-----DVEPSKMPPPDLP 1012
Cdd:cd05604   212 KPL--VLRPG-------------ISLTAWSILEELLEKDRQLRLGAKEDFLeiknHPFFEsinwtDLVQKKIPPPFNP 274
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
702-918 1.21e-12

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: 70.86  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLdNEKEGfpitairEIKILRQLTHQSIINMKEIvtdkedal 778
Cdd:cd05633     4 MNDFSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldKKRI-KMKQG-------ETLALNERIMLSLVSTGDC-------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 dfkkdkgAFYLVFEYMDHD------LMGLLESGLVH--------FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNIL 844
Cdd:cd05633    68 -------PFIVCMTYAFHTpdklcfILDLMNGGDLHyhlsqhgvFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANIL 140
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  845 LNNRGQIKLADFGLARLYSseESRPYTNkVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQ 918
Cdd:cd05633   141 LDEHGHVRISDLGLACDFS--KKKPHAS-VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHK 211
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
680-928 1.22e-12

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 72.21  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  680 PKICGpRYGETKEKDIDWGKRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQL 759
Cdd:PTZ00283   10 GRVCR-TFPDTFAKDEATAKEQAKKYWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVCCLLNC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  760 THQSIINMKEivtdkedalDF-KKDKG------AFYLVFEYMDH-DLMGLLES---GLVHFNENHIKSFMRQLMEGLDYC 828
Cdd:PTZ00283   89 DFFSIVKCHE---------DFaKKDPRnpenvlMIALVLDYANAgDLRQEIKSrakTNRTFREHEAGLLFIQVLLAVHHV 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  829 HKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEES----RPYTNkviTLWYRPPELLLgEERYTPAIDVWSCGCIL 904
Cdd:PTZ00283  160 HSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAATVSddvgRTFCG---TPYYVAPEIWR-RKPYSKKADMFSLGVLL 235
                         250       260
                  ....*....|....*....|....*.
gi 145309300  905 GELFT-KKPIFQAN-QELAQLELISR 928
Cdd:PTZ00283  236 YELLTlKRPFDGENmEEVMHKTLAGR 261
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
820-1000 1.32e-12

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: 70.04  E-value: 1.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  820 QLMEGLDYCH-KKNFLHRDIKCSNILLNNRGQIKLADFGLArlYSSEESRPYTNKV------------ITLWYRPPELLL 886
Cdd:cd14011   122 QISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFC--ISSEQATDQFPYFreydpnlpplaqPNLNYLAPEYIL 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  887 gEERYTPAIDVWSCGCILGELFTK-KPIFQANQELAQLELISRicgspcpavwpdviklpyfntmkpkkQYRRKLREEFV 965
Cdd:cd14011   200 -SKTCDPASDMFSLGVLIYAIYNKgKPLFDCVNNLLSYKKNSN--------------------------QLRQLSLSLLE 252
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 145309300  966 FIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRD 1000
Cdd:cd14011   253 KVPEELRDHVKTLLNVTPEVRPDAEQLSKIPFFDD 287
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
711-909 1.46e-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: 70.04  E-value: 1.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKAR----DKDTGEM---VALKKVRLDNEKEGFPiTAIREIKILRQL-THQSIINMKEIVTDKedaldfkk 782
Cdd:cd05098    21 LGEGCFGQVVLAEaiglDKDKPNRvtkVAVKMLKSDATEKDLS-DLISEMEMMKMIgKHKNIINLLGACTQD-------- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkGAFYLVFEYMDH-DLMGLLES----GLVH-FNENHIK----------SFMRQLMEGLDYCHKKNFLHRDIKCSNILLN 846
Cdd:cd05098    92 --GPLYVIVEYASKgNLREYLQArrppGMEYcYNPSHNPeeqlsskdlvSCAYQVARGMEYLASKKCIHRDLAARNVLVT 169
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  847 NRGQIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05098   170 EDNVMKIADFGLARdIHHIDYYKKTTNGRLPVKWMAPEALF-DRIYTHQSDVWSFGVLLWEIFT 232
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
702-998 1.59e-12

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 69.50  E-value: 1.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  702 VDKFDIIgiigEGTYGQVYKARDKDTGEMVALKKVRLDNekegfpITAIrEIKIlRQLT--HQSIINMKEIVTDKEDALd 779
Cdd:PHA03390   19 VKKLKLI----DGKFGKVSVLKHKPTQKLFVQKIIKAKN------FNAI-EPMV-HQLMkdNPNFIKLYYSVTTLKGHV- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkkdkgafyLVFEYM-DHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLN-NRGQIKLADFG 857
Cdd:PHA03390   86 ---------LIMDYIkDGDLFDLLKKE-GKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKDRIYLCDYG 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 LARLYSSEESrpYTNkviTLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQElaqlelisricgspcpav 937
Cdd:PHA03390  156 LCKIIGTPSC--YDG---TLDYFSPEKIKG-HNYDVSFDWWAVGVLTYELLTGKHPFKEDED------------------ 211
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  938 wpDVIKLpyfNTMKpKKQYRRKLREEFVfiPAAALDLFDYMLALDPSKR-CTAEQALQCEFL 998
Cdd:PHA03390  212 --EELDL---ESLL-KRQQKKLPFIKNV--SKNANDFVQSMLKYNINYRlTNYNEIIKHPFL 265
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
704-923 2.56e-12

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: 68.95  E-value: 2.56e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIgiIGEGTYGQVYKARDKDTGEMVA---LKKVRLDN-EKEGFPitaiREIKILRQLTHQSIINMKEIVTDKedald 779
Cdd:cd14032     4 KFDIE--LGRGSFKTVYKGLDTETWVEVAwceLQDRKLTKvERQRFK----EEAEMLKGLQHPNIVRFYDFWESC----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fKKDKGAFYLVFEYMDHdlmGLLESGLVHFN---ENHIKSFMRQLMEGLDYCHKKN--FLHRDIKCSNILLNN-RGQIKL 853
Cdd:cd14032    73 -AKGKRCIVLVTELMTS---GTLKTYLKRFKvmkPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGpTGSVKI 148
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  854 ADFGLARLYSSEesrpYTNKVI-TLWYRPPELLlgEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQL 923
Cdd:cd14032   149 GDLGLATLKRAS----FAKSVIgTPEFMAPEMY--EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQI 213
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
686-917 2.69e-12

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


Pssm-ID: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 70.42  E-value: 2.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  686 RYGETKEKDIDWGKRCVDkFDIIGIIGEGTYGQVYKARDKDTGEMVALKKV-RLDNEKEGFPITAIREIKILRQLTHQSI 764
Cdd:cd05622    57 RYKDTINKIRDLRMKAED-YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLsKFEMIKRSDSAFFWEERDIMAFANSPWV 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  765 INMkeivtdkedALDFKKDKgAFYLVFEYM-DHDLMGLLESGLVhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNI 843
Cdd:cd05622   136 VQL---------FYAFQDDR-YLYMVMEYMpGGDLVNLMSNYDV--PEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNM 203
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  844 LLNNRGQIKLADFGLARLYSSEESRPYTNKVITLWYRPPELLL---GEERYTPAIDVWSCGCILGELFTKKPIFQAN 917
Cdd:cd05622   204 LLDKSGHLKLADFGTCMKMNKEGMVRCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYAD 280
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
703-1007 2.82e-12

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: 69.27  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVrlDNEKEgfpiTAIREIKIL-RQLTHQSIINMKEIVtdkedaldfk 781
Cdd:cd14177     4 DVYELKEDIGVGSYSVCKRCIHRATNMEFAVKII--DKSKR----DPSEEIEILmRYGQHPNIITLKDVY---------- 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kDKGAF-YLVFEYMDHDlmGLLESGLVH--FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL----NNRGQIKLA 854
Cdd:cd14177    68 -DDGRYvYLVTELMKGG--ELLDRILRQkfFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYmddsANADSIRIC 144
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  855 DFGLARLYSSEESRPYTnKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICG--- 931
Cdd:cd14177   145 DFGFAKQLRGENGLLLT-PCYTANFVAPEVLM-RQGYDAACDIWSLGVLLYTMLAGYTPFANGPNDTPEEILLRIGSgkf 222
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  932 SPCPAVWPDViklpyfntmkpkkqyrrklreefvfiPAAALDLFDYMLALDPSKRCTAEQALQCEFL--RDVEPSKMP 1007
Cdd:cd14177   223 SLSGGNWDTV--------------------------SDAAKDLLSHMLHVDPHQRYTAEQVLKHSWIacRDQLPHYQL 274
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
711-909 3.05e-12

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: 68.50  E-value: 3.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTgemVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTdkedaldfkkdKGAFYLV 790
Cdd:cd14150     8 IGTGSFGTVFRGKWHGD---VAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNILLFMGFMT-----------RPNFAII 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMD-HDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSS-EESR 868
Cdd:cd14150    74 TQWCEgSSLYRHLHVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRwSGSQ 153
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 145309300  869 PYTNKVITLWYRPPELLLGEER--YTPAIDVWSCGCILGELFT 909
Cdd:cd14150   154 QVEQPSGSILWMAPEVIRMQDTnpYSFQSDVYAYGVVLYELMS 196
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
703-998 3.82e-12

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 68.46  E-value: 3.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDI----IGIIGEGTYGQVYKARDKDTGEMVALKKVrldNEKEGFPITAIREIKILRQLTHQSIINMkeivtdkedaL 778
Cdd:cd14113     3 DNFDSfyseVAELGRGRFSVVKKCDQRGTKRAVATKFV---NKKLMKRDQVTHELGVLQSLQHPQLVGL----------L 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 DFKKDKGAFYLVFEYMDHdlmGLLESGLV---HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLN---NRGQIK 852
Cdd:cd14113    70 DTFETPTSYILVLEMADQ---GRLLDYVVrwgNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDqslSKPTIK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  853 LADFGLARLYSSEesrPYTNKVI-TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTK-KPIFQANQELAQLElISRIC 930
Cdd:cd14113   147 LADFGDAVQLNTT---YYIHQLLgSPEFAAPEIILGNP-VSLTSDLWSIGVLTYVLLSGvSPFLDESVEETCLN-ICRLD 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  931 GSpcpavWPDviklPYFNTMKPKkqyrrklreefvfipaaALDLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14113   222 FS-----FPD----DYFKGVSQK-----------------AKDFVCFLLQMDPAKRPSAALCLQEQWL 263
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
704-879 4.06e-12

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: 68.05  E-value: 4.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPItairEIKILRQLthQSiinmKEIVTDkedALDFKKD 783
Cdd:cd14017     1 RWKVVKKIGGGGFGEIYKVRDVVDGEEVAMKVESKSQPKQVLKM----EVAVLKKL--QG----KPHFCR---LIGCGRT 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDHDLMGLLES-GLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL----NNRGQIKLADFGL 858
Cdd:cd14017    68 ERYNYIVMTLLGPNLAELRRSqPRGKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgrgpSDERTVYILDFGL 147
                         170       180
                  ....*....|....*....|....*..
gi 145309300  859 ARLY---SSEESRPYTNKVI---TLWY 879
Cdd:cd14017   148 ARQYtnkDGEVERPPRNAAGfrgTVRY 174
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
705-918 4.89e-12

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 68.92  E-value: 4.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLdNEKEGfpitairEIKILRQLTHQSIINMKEIvtdkedaldfk 781
Cdd:cd14223     2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKcldKKRI-KMKQG-------ETLALNERIMLSLVSTGDC----------- 62
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgAFYLVFEYMDHD------LMGLLESGLVH--------FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN 847
Cdd:cd14223    63 ----PFIVCMSYAFHTpdklsfILDLMNGGDLHyhlsqhgvFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDE 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  848 RGQIKLADFGLARLYSseESRPYTNkVITLWYRPPELLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQ 918
Cdd:cd14223   139 FGHVRISDLGLACDFS--KKKPHAS-VGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHK 206
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
711-968 6.94e-12

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: 67.75  E-value: 6.94e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKArdKDTGEmVALKKVRL-DNEKEGFpiTAIR-EIKILRQLTHQSIINMKEIVTdkedaldfkkdKGAFY 788
Cdd:cd14149    20 IGSGSFGTVYKG--KWHGD-VAVKILKVvDPTPEQF--QAFRnEVAVLRKTRHVNILLFMGYMT-----------KDNLA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMD-HDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLA----RLYS 863
Cdd:cd14149    84 IVTQWCEgSSLYKHLHVQETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLAtvksRWSG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEESRPYTNKVitLWYRPPELLLGEER-YTPAIDVWSCGCILGELFTKK-PIFQANQELAQLELISRicgspcPAVWPDV 941
Cdd:cd14149   164 SQQVEQPTGSI--LWMAPEVIRMQDNNpFSFQSDVYSYGIVLYELMTGElPYSHINNRDQIIFMVGR------GYASPDL 235
                         250       260       270
                  ....*....|....*....|....*....|.
gi 145309300  942 IKLpYFNTMKPKKQYR----RKLREEFVFIP 968
Cdd:cd14149   236 SKL-YKNCPKAMKRLVadciKKVKEERPLFP 265
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
704-923 8.85e-12

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: 67.77  E-value: 8.85e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIgiIGEGTYGQVYKARDKDTGEMVA---LKKVRLD-NEKEGFPitaiREIKILRQLTHQSIINMKEivtDKEDALd 779
Cdd:cd14030    28 KFDIE--IGRGSFKTVYKGLDTETTVEVAwceLQDRKLSkSERQRFK----EEAGMLKGLQHPNIVRFYD---SWESTV- 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkKDKGAFYLVFEYMDHdlmGLLESGLVHFNENHIK---SFMRQLMEGLDYCHKKN--FLHRDIKCSNILLNN-RGQIKL 853
Cdd:cd14030    98 --KGKKCIVLVTELMTS---GTLKTYLKRFKVMKIKvlrSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGpTGSVKI 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 145309300  854 ADFGLARLYSSEesrpYTNKVI-TLWYRPPELLlgEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQL 923
Cdd:cd14030   173 GDLGLATLKRAS----FAKSVIgTPEFMAPEMY--EEKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQI 237
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
703-909 8.89e-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: 8.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKAR----DKDTGE---MVALKKVRlDNEKEGFPITAIREIKILRQL-THQSIINMKEIVTDK 774
Cdd:cd05101    24 DKLTLGKPLGEGCFGQVVMAEavgiDKDKPKeavTVAVKMLK-DDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQD 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  775 edaldfkkdkGAFYLVFEYM-------------------DHDLMGLLESGLVhFNEnhIKSFMRQLMEGLDYCHKKNFLH 835
Cdd:cd05101   103 ----------GPLYVIVEYAskgnlreylrarrppgmeySYDINRVPEEQMT-FKD--LVSCTYQLARGMEYLASQKCIH 169
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  836 RDIKCSNILLNNRGQIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05101   170 RDLAARNVLVTENNVMKIADFGLARdINNIDYYKKTTNGRLPVKWMAPEALF-DRVYTHQSDVWSFGVLMWEIFT 243
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
703-1012 1.04e-11

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: 67.65  E-value: 1.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVrldnEKEgfpiTAIREIKILRQLTHQSIINMKE---IVTdkedaL- 778
Cdd:cd05574     1 DHFKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVL----DKE----EMIKRNKVKRVLTEREILATLDhpfLPT-----Ly 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 -DFKKDKgAFYLVFEY-MDHDLMGLLESGLVH-FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLAD 855
Cdd:cd05574    68 aSFQTST-HLCFVMDYcPGGELFRLLQKQPGKrLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTD 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  856 FGLARLySSEESRPYTNKVITLWYRP-----------------------------PELLLGEErYTPAIDVWSCGCILGE 906
Cdd:cd05574   147 FDLSKQ-SSVTPPPVRKSLRKGSRRSsvksieketfvaepsarsnsfvgteeyiaPEVIKGDG-HGSAVDWWTLGILLYE 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  907 -LFTKKPIFQANQElaqlELISRICGSPcpavwpdviklPYFNTMKPkkqyrrklreefvfIPAAALDLFDYMLALDPSK 985
Cdd:cd05574   225 mLYGTTPFKGSNRD----ETFSNILKKE-----------LTFPESPP--------------VSSEAKDLIRKLLVKDPSK 275
                         330       340       350
                  ....*....|....*....|....*....|....
gi 145309300  986 RC----TAEQALQCEFLRDVEPSK---MPPPDLP 1012
Cdd:cd05574   276 RLgskrGASEIKRHPFFRGVNWALirnMTPPIIP 309
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
704-994 1.10e-11

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


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 68.12  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPITAIREIKILRQLTHQSIINMK-EIVTDKEDALDFKK 782
Cdd:cd14218    11 RYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVK---SAVHYTETAVDEIKLLKCVRDSDPSDPKrETIVQLIDDFKISG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFY-LVFEYMDHDLMG-LLESGLVHFNENHIKSFMRQLMEGLDYCHKK-NFLHRDIKCSNILL-------------- 845
Cdd:cd14218    88 VNGVHVcMVLEVLGHQLLKwIIKSNYQGLPLPCVKSILRQVLQGLDYLHTKcKIIHTDIKPENILMcvdegyvrrlaaea 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  846 --------------------------------NNRGQIKLADFGLArlysSEESRPYTNKVITLWYRPPELLLGEERYTP 893
Cdd:cd14218   168 tiwqqagapppsgssvsfgasdflvnplepqnADKIRVKIADLGNA----CWVHKHFTEDIQTRQYRALEVLIGAEYGTP 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  894 AiDVWSCGCILGELFTKKPIFQAN------QELAQLELISRICGSPCPA-VWPDVIKLPYFN---------TMKPKKQYr 957
Cdd:cd14218   244 A-DIWSTACMAFELATGDYLFEPHsgedytRDEDHIAHIVELLGDIPPHfALSGRYSREYFNrrgelrhikNLKHWGLY- 321
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 145309300  958 RKLREEFVFIPAAALDLFDY---MLALDPSKRCTAEQALQ 994
Cdd:cd14218   322 EVLVEKYEWPLEQAAQFTDFllpMMEFLPEKRATAAQCLQ 361
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
705-914 1.10e-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: 68.14  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVR--LDNEKEGFPITAIREIKILRQLTHQSIINMKEIvtdkedaldFKK 782
Cdd:cd05618    22 FDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKkeLVNDDEDIDWVQTEKHVFEQASNHPFLVGLHSC---------FQT 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFYlVFEYMDH-DLMGLLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARl 861
Cdd:cd05618    93 ESRLFF-VIEYVNGgDLMFHMQRQR-KLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCK- 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  862 yssEESRPYTNKVI---TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIF 914
Cdd:cd05618   170 ---EGLRPGDTTSTfcgTPNYIAPEILRGED-YGFSVDWWALGVLMFEMMAGRSPF 221
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
705-927 1.16e-11

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 68.53  E-value: 1.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLdnekegfpitaiREIKILRQLTHqsIINMKEIVTDKEDALDFK--- 781
Cdd:cd05625     3 FVKIKTLGIGAFGEVCLARKVDTKALYATKTLRK------------KDVLLRNQVAH--VKAERDILAEADNEWVVRlyy 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 --KDKGAFYLVFEYM-DHDLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd05625    69 sfQDKDNLYFVMDYIpGGDMMSLLIRMGV-FPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGL 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ---------ARLYSS-----EESRPYTNK--------------------------------VITLWYRPPELLLgEERYT 892
Cdd:cd05625   148 ctgfrwthdSKYYQSgdhlrQDSMDFSNEwgdpencrcgdrlkplerraarqhqrclahslVGTPNYIAPEVLL-RTGYT 226
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 145309300  893 PAIDVWSCGCILGELFTKKPIFQANQEL-AQLELIS 927
Cdd:cd05625   227 QLCDWWSVGVILFEMLVGQPPFLAQTPLeTQMKVIN 262
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
711-912 1.31e-11

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


Pssm-ID: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 66.39  E-value: 1.31e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFpitaIREIKILRQLTHQSIINMKEIVTdkedaldfkKDkGAFYLV 790
Cdd:cd14156     1 IGSGFFSKVYKVTHGATGKVMVVKIYKNDVDQHKI----VREISLLQKLSHPNIVRYLGICV---------KD-EKLHPI 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHD-LMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIK---LADFGLAR----LY 862
Cdd:cd14156    67 LEYVSGGcLEELLAREELPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLARevgeMP 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 145309300  863 SSEESRPYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKP 912
Cdd:cd14156   147 ANDPERKLS-LVGSAFWMAPEMLRGEP-YDRKVDVFSFGIVLCEILARIP 194
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
703-923 1.71e-11

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


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 66.64  E-value: 1.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKA----RDKDTGEM-VALK---KVRLDNEKEGFpitaIREIKILRQLTHQSIINMKEIVTDK 774
Cdd:cd05036     6 KNLTLIRALGQGAFGEVYEGtvsgMPGDPSPLqVAVKtlpELCSEQDEMDF----LMEALIMSKFNHPNIVRCIGVCFQR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  775 EdaldfkkdkgAFYLVFEYMDHdlmGLLESGLVHfNENHIKS----FMRQLME-------GLDYCHKKNFLHRDIKCSNI 843
Cdd:cd05036    82 L----------PRFILLELMAG---GDLKSFLRE-NRPRPEQpsslTMLDLLQlaqdvakGCRYLEENHFIHRDIAARNC 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  844 LLNNRGQ---IKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT--KKPI-FQA 916
Cdd:cd05036   148 LLTCKGPgrvAKIGDFGMARdIYRADYYRKGGKAMLPVKWMPPEAFL-DGIFTSKTDVWSFGVLLWEIFSlgYMPYpGKS 226

                  ....*..
gi 145309300  917 NQELAQL 923
Cdd:cd05036   227 NQEVMEF 233
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
711-909 1.83e-11

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: 66.29  E-value: 1.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKD-----TGEM-VALKKVR---LDNEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDAldfk 781
Cdd:cd05044     3 LGSGAFGEVFEGTAKDilgdgSGETkVAVKTLRkgaTDQEKAEF----LKEAHLMSNFKHPNILKLLGVCLDNDPQ---- 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgafYLVFEYMDH-DLMGLLESGLVHFNENHIKSFMRQL------MEGLDYCHKKNFLHRDIKCSNILLNNRGQ---- 850
Cdd:cd05044    75 ------YIILELMEGgDLLSYLRAARPTAFTPPLLTLKDLLsicvdvAKGCVYLEDMHFVHRDLAARNCLVSSKDYrerv 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  851 IKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05044   149 VKIGDFGLARdIYKNDYYRKEGEGLLPVRWMAPESLV-DGVFTTQSDVWAFGVLMWEILT 207
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
710-919 1.91e-11

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: 67.13  E-value: 1.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDnekegfpiTAIREIKILRQLTHQSIINMKE---IVTDKEDALDfKKDKga 786
Cdd:cd05591     2 VLGKGSFGKVMLAERKGTDEVYAIKVLKKD--------VILQDDDVDCTMTEKRILALAAkhpFLTALHSCFQ-TKDR-- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDH-DLMGLLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARlYSSE 865
Cdd:cd05591    71 LFFVMEYVNGgDLMFQIQRAR-KFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCK-EGIL 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  866 ESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQE 919
Cdd:cd05591   149 NGKTTTTFCGTPDYIAPE-ILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNE 201
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
705-914 2.18e-11

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: 67.35  E-value: 2.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIR-EIKILRQLTHQSIINMKEIVTDKEDALdfkkd 783
Cdd:cd05617    17 FDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVHDDEDIDWVQtEKHVFEQASSNPFLVGLHSCFQTTSRL----- 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 kgafYLVFEYMDH-DLMGLLESGLvHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARly 862
Cdd:cd05617    92 ----FLVIEYVNGgDLMFHMQRQR-KLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCK-- 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  863 ssEESRPYTNKVI---TLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIF 914
Cdd:cd05617   165 --EGLGPGDTTSTfcgTPNYIAPEILRGEE-YGFSVDWWALGVLMFEMMAGRSPF 216
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
703-967 2.21e-11

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: 2.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYK--ARDKDTGEM---VALKKVrldNEKEGFP--ITAIREIKILRQLTHQSIINMKEIVTDKE 775
Cdd:cd05061     6 EKITLLRELGQGSFGMVYEgnARDIIKGEAetrVAVKTV---NESASLRerIEFLNEASVMKGFTCHHVVRLLGVVSKGQ 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  776 DALdfkkdkgafyLVFEYMDH-DLMGLLESgLVHFNEN-------HIKSFMR---QLMEGLDYCHKKNFLHRDIKCSNIL 844
Cdd:cd05061    83 PTL----------VVMELMAHgDLKSYLRS-LRPEAENnpgrpppTLQEMIQmaaEIADGMAYLNAKKFVHRDLAARNCM 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  845 LNNRGQIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFT--KKPiFQ--ANQE 919
Cdd:cd05061   152 VAHDFTVKIGDFGMTRdIYETDYYRKGGKGLLPVRWMAPE-SLKDGVFTTSSDMWSFGVVLWEITSlaEQP-YQglSNEQ 229
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 145309300  920 LAQLELISRICGSP--CPAVWPDVIKLPYfntmkpkkQYRRKLREEFVFI 967
Cdd:cd05061   230 VLKFVMDGGYLDQPdnCPERVTDLMRMCW--------QFNPKMRPTFLEI 271
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
711-859 2.42e-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: 66.69  E-value: 2.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKA--RDKDTGEM---VALKKVRLDNEKEgfpitAIREIKILRQLTHqsiiNMKEIVTDKEDALDFKKDKG 785
Cdd:cd14013     3 LGEGGFGTVYKGslLQKDPGGEkrrVVLKKAKEYGEVE-----IWMNERVRRACPS----SCAEFVGAFLDTTSKKFTKP 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 AFYLVFEYM-DHDLMGLLESGLVHFN-------------------ENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL 845
Cdd:cd14013    74 SLWLVWKYEgDATLADLMQGKEFPYNlepiifgrvlipprgpkreNVIIKSIMRQILVALRKLHSTGIVHRDVKPQNIIV 153
                         170
                  ....*....|....*
gi 145309300  846 NNR-GQIKLADFGLA 859
Cdd:cd14013   154 SEGdGQFKIIDLGAA 168
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
699-1055 2.44e-11

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: 66.98  E-value: 2.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  699 KRCVDKFDIIGIIGEGTYGQVYKARDKDTGEMVALK----KVRLDNEKEGFPITairEIKILRQLTHQSIINMKeIVTDK 774
Cdd:cd05594    21 KVTMNDFEYLKLLGKGTFGKVILVKEKATGRYYAMKilkkEVIVAKDEVAHTLT---ENRVLQNSRHPFLTALK-YSFQT 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  775 EDALDFkkdkgafylVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCH-KKNFLHRDIKCSNILLNNRGQIKL 853
Cdd:cd05594    97 HDRLCF---------VMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKI 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  854 ADFGLARlYSSEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELftkkpifqanqelaqlelisrICGsp 933
Cdd:cd05594   168 TDFGLCK-EGIKDGATMKTFCGTPEYLAPE-VLEDNDYGRAVDWWGLGVVMYEM---------------------MCG-- 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  934 cpavwpdviKLPYFNtMKPKKQYRRKLREEFVF---IPAAALDLFDYMLALDPSKRC-----TAEQALQCEFL-----RD 1000
Cdd:cd05594   223 ---------RLPFYN-QDHEKLFELILMEEIRFprtLSPEAKSLLSGLLKKDPKQRLgggpdDAKEIMQHKFFagivwQD 292
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300 1001 VEPSKMPPPDLPlwqdchELWSKKRRRQKQMGMTDDVSTIKAPRKDLSL-GLDDSR 1055
Cdd:cd05594   293 VYEKKLVPPFKP------QVTSETDTRYFDEEFTAQMITITPPDQDDSMeTVDNER 342
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
703-917 2.96e-11

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: 66.95  E-value: 2.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEGFPITAIREIkilrqlthQSIINMKEIVtdkEDALD 779
Cdd:cd05621    52 EDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKllsKFEMIKRSDSAFFWEERDI--------MAFANSPWVV---QLFCA 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FKKDKgAFYLVFEYM-DHDLMGLLESGLVhfNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd05621   121 FQDDK-YLYMVMEYMpGGDLVNLMSNYDV--PEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGT 197
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  859 ARLYSSEESRPYTNKVITLWYRPPELLL---GEERYTPAIDVWSCGCILGELFTKKPIFQAN 917
Cdd:cd05621   198 CMKMDETGMVHCDTAVGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLFEMLVGDTPFYAD 259
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
711-907 3.34e-11

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


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 65.96  E-value: 3.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKdtGEMVALKKVRLDNEKEGFPITAIREIKILRqltHQSIINMkeIVTDKedaldfkKDKGAFYLV 790
Cdd:cd14144     3 VGKGRYGEVWKGKWR--GEKVAVKIFFTTEEASWFRETEIYQTVLMR---HENILGF--IAADI-------KGTGSWTQL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDHDLMGLLESGLvHFNENHIKSFMR---QLMEGLDYCH--------KKNFLHRDIKCSNILLNNRGQIKLADFGLA 859
Cdd:cd14144    69 YLITDYHENGSLYDFL-RGNTLDTQSMLKlaySAACGLAHLHteifgtqgKPAIAHRDIKSKNILVKKNGTCCIADLGLA 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  860 RLYSSEESR---PYTNKVITLWYRPPELL---LGEERYTPAI--DVWSCGCILGEL 907
Cdd:cd14144   148 VKFISETNEvdlPPNTRVGTKRYMAPEVLdesLNRNHFDAYKmaDMYSFGLVLWEI 203
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
703-907 3.52e-11

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: 66.23  E-value: 3.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDnEKEGFPITAIREIKILRQLTHQSIINMKeivtdkedaldfkk 782
Cdd:cd06649     5 DDFERISELGAGNGGVVTKVQHKPSGLIMARKLIHLE-IKPAIRNQIIRELQVLHECNSPYIVGFY-------------- 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkGAFY------LVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKN-FLHRDIKCSNILLNNRGQIKLAD 855
Cdd:cd06649    70 --GAFYsdgeisICMEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLREKHqIMHRDVKPSNILVNSRGEIKLCD 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 145309300  856 FGLARLYSSEESRPYtnkVITLWYRPPELLLGEErYTPAIDVWSCGCILGEL 907
Cdd:cd06649   148 FGVSGQLIDSMANSF---VGTRSYMSPERLQGTH-YSVQSDIWSMGLSLVEL 195
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
710-910 5.32e-11

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 65.34  E-value: 5.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKD---TGEMVALKKVRLDN----EKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDAldfKK 782
Cdd:cd14204    14 VLGEGEFGSVMEGELQQpdgTNHKVAVKTMKLDNfsqrEIEEF----LSEAACMKDFNHPNVIRLLGVCLEVGSQ---RI 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFYLVF-EYMD-HD--LMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd14204    87 PKPMVILPFmKYGDlHSflLRSRLGSGPQHVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGL 166
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  859 A-RLYSSEESRP-YTNKVITLWYRPPEllLGEERYTPAIDVWSCGCILGELFTK 910
Cdd:cd14204   167 SkKIYSGDYYRQgRIAKMPVKWIAVES--LADRVYTVKSDVWAFGVTMWEIATR 218
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
711-901 6.73e-11

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: 65.21  E-value: 6.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKvrLDNEKEGFPITA-IREIKILRQLTHQSIINM---KEIVTDKEDALDFKK-DKG 785
Cdd:cd13988     1 LGQGATANVFRGRHKKTGDLYAVKV--FNNLSFMRPLDVqMREFEVLKKLNHKNIVKLfaiEEELTTRHKVLVMELcPCG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 AFYLVFEYMDhDLMGLLESglvhfnENHIksFMRQLMEGLDYCHKKNFLHRDIKCSNIL--LNNRGQ--IKLADFGLARl 861
Cdd:cd13988    79 SLYTVLEEPS-NAYGLPES------EFLI--VLRDVVAGMNHLRENGIVHRDIKPGNIMrvIGEDGQsvYKLTDFGAAR- 148
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 145309300  862 ySSEESRPYTNKVITLWYRPPELLlgeER----------YTPAIDVWSCG 901
Cdd:cd13988   149 -ELEDDEQFVSLYGTEEYLHPDMY---ERavlrkdhqkkYGATVDLWSIG 194
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
705-914 7.22e-11

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: 65.42  E-value: 7.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALK---KVRLDNEKEGFPITAIREIkILRQLTHQSIINMKEI--VTDKedald 779
Cdd:cd05602     9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKvlqKKAILKKKEEKHIMSERNV-LLKNVKHPFLVGLHFSfqTTDK----- 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 fkkdkgaFYLVFEYMDH-DLMGLLESGLVhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd05602    83 -------LYFVLDYINGgELFYHLQRERC-FLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGL 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  859 ARlYSSEESRPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIF 914
Cdd:cd05602   155 CK-ENIEPNGTTSTFCGTPEYLAPE-VLHKQPYDRTVDWWCLGAVLYEMLYGLPPF 208
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
710-909 8.62e-11

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


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 64.64  E-value: 8.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKAR-DKDTGEMVA----LKKVRLDNEKEGFPitaiREIKILRQLTHQ-SIINMkeivtdkedaLDFKKD 783
Cdd:cd05089     9 VIGEGNFGQVIKAMiKKDGLKMNAaikmLKEFASENDHRDFA----GELEVLCKLGHHpNIINL----------LGACEN 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDH-DLMGLLESGLV-----HFNENH----------IKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNN 847
Cdd:cd05089    75 RGYLYIAIEYAPYgNLLDFLRKSRVletdpAFAKEHgtastltsqqLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGE 154
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  848 RGQIKLADFGLARlysSEESrpYTNKVITlwyRPPELLLGEER-----YTPAIDVWSCGCILGELFT 909
Cdd:cd05089   155 NLVSKIADFGLSR---GEEV--YVKKTMG---RLPVRWMAIESlnysvYTTKSDVWSFGVLLWEIVS 213
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
705-919 1.04e-10

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: 65.01  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  705 FDIIGIIGEGTYGQVYKARDKDTGEMVALKKVR------------LDNEKEGFP-ITAIReikilrqltHQSIINMKEIV 771
Cdd:cd05589     1 FRCIAVLGRGHFGKVLLAEYKPTGELFAIKALKkgdiiardevesLMCEKRIFEtVNSAR---------HPFLVNLFACF 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  772 TDKEDALdfkkdkgafyLVFEYM-DHDLMGLLESGLvhFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ 850
Cdd:cd05589    72 QTPEHVC----------FVMEYAaGGDLMMHIHEDV--FSEPRAVFYAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGY 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  851 IKLADFGLARlysseESRPYTNKVITLWYRP----PELLLgEERYTPAIDVWSCGCILGELFTKKPIFQANQE 919
Cdd:cd05589   140 VKIADFGLCK-----EGMGFGDRTSTFCGTPeflaPEVLT-DTSYTRAVDWWGLGVLIYEMLVGESPFPGDDE 206
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
703-1000 1.08e-10

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: 63.86  E-value: 1.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRlDNEKEGFPITAIREIKILRQLTHQSIINM-KEIVTDKEdaldfk 781
Cdd:cd14183     6 ERYKVGRTIGDGNFAVVKECVERSTGREYALKIIN-KSKCRGKEHMIQNEVSILRRVKHPNIVLLiEEMDMPTE------ 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  782 kdkgaFYLVFEYMDH-DLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL----NNRGQIKLADF 856
Cdd:cd14183    79 -----LYLVMELVKGgDLFDAITST-NKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDF 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  857 GLARLYSSeesrPYTNKVITLWYRPPElLLGEERYTPAIDVWSCGCILGELFTKKPIFQANQELAQLELISRICGSpcpA 936
Cdd:cd14183   153 GLATVVDG----PLYTVCGTPTYVAPE-IIAETGYGLKVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQILMGQ---V 224
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  937 VWPdvikLPYFNTmkpkkqyrrklreefvfIPAAALDLFDYMLALDPSKRCTAEQALQCEFLRD 1000
Cdd:cd14183   225 DFP----SPYWDN-----------------VSDSAKELITMMLQVDVDQRYSALQVLEHPWVND 267
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
711-912 1.24e-10

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: 64.66  E-value: 1.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKAR----DKDTGE---MVALKKVRLDNEKEGFPiTAIREIKILRQL-THQSIINMKEIVTDKedaldfkk 782
Cdd:cd05100    20 LGEGCFGQVVMAEaigiDKDKPNkpvTVAVKMLKDDATDKDLS-DLVSEMEMMKMIgKHKNIINLLGACTQD-------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 dkGAFYLVFEY-----------------MDH--DLMGLLESGLVHfneNHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNI 843
Cdd:cd05100    91 --GPLYVLVEYaskgnlreylrarrppgMDYsfDTCKLPEEQLTF---KDLVSCAYQVARGMEYLASQKCIHRDLAARNV 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  844 LLNNRGQIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELFTKKP 912
Cdd:cd05100   166 LVTEDNVMKIADFGLARdVHNIDYYKKTTNGRLPVKWMAPEALF-DRVYTHQSDVWSFGVLLWEIFTLGG 234
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
710-909 1.36e-10

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: 64.21  E-value: 1.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIR----EIKILRQLTHQSIINMKEIVTDKedaldfkkdkG 785
Cdd:cd05045     7 TLGEGEFGKVVKATAFRLKGRAGYTTVAVKMLKENASSSELRdllsEFNLLKQVNHPHVIKLYGACSQD----------G 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 AFYLVFEYMDH-DLMGLL------------------ESGLVHFNENHIK-----SFMRQLMEGLDYCHKKNFLHRDIKCS 841
Cdd:cd05045    77 PLLLIVEYAKYgSLRSFLresrkvgpsylgsdgnrnSSYLDNPDERALTmgdliSFAWQISRGMQYLAEMKLVHRDLAAR 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  842 NILLNNRGQIKLADFGLARLYSSEES--RPYTNKVITLWYRPPELLlgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05045   157 NVLVAEGRKMKISDFGLSRDVYEEDSyvKRSKGRIPVKWMAIESLF--DHIYTTQSDVWSFGVLLWEIVT 224
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
711-1004 1.37e-10

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


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 63.81  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTgemVALKKVrLDNEKEGFPITAI-REIKILRQ--LTHQSIINMKE-IVTDKedaldfkkdkgA 786
Cdd:cd13980     8 LGSTRFLKVARARHDEG---LVVVKV-FVKPDPALPLRSYkQRLEEIRDrlLELPNVLPFQKvIETDK-----------A 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDHDLMGLLeSGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFG--------- 857
Cdd:cd13980    73 AYLIRQYVKYNLYDRI-STRPFLNLIEKKWIAFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFAsfkptylpe 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  858 -------------------LA--RLYSSeesrpyTNKVITLWYRPPELllgeeryTPAIDVWSCGCILGELFTK-KPIFq 915
Cdd:cd13980   152 dnpadfsyffdtsrrrtcyIApeRFVDA------LTLDAESERRDGEL-------TPAMDIFSLGCVIAELFTEgRPLF- 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  916 anqELAQL-----------ELISRIcgspcpavwpdviklpyfntmkPKKQYRRKLREefvfipaaaldlfdyMLALDPS 984
Cdd:cd13980   218 ---DLSQLlayrkgefspeQVLEKI----------------------EDPNIRELILH---------------MIQRDPS 257
                         330       340
                  ....*....|....*....|
gi 145309300  985 KRCTAEQALQcEFLRDVEPS 1004
Cdd:cd13980   258 KRLSAEDYLK-KYRGKVFPE 276
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
711-910 1.46e-10

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


Pssm-ID: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 63.87  E-value: 1.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEM--VALKKVRL----DNEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEDALDFKkdk 784
Cdd:cd05075     8 LGEGEFGSVMEGQLNQDDSVlkVAVKTMKIaictRSEMEDF----LSEAVCMKEFDHPNVMRLIGVCLQNTESEGYP--- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gAFYLVFEYMDH-DLMG-LLESGL----VHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd05075    81 -SPVVILPFMKHgDLHSfLLYSRLgdcpVYLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGL 159
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 145309300  859 A-RLYSSEESRP-YTNKVITLWYRPPEllLGEERYTPAIDVWSCGCILGELFTK 910
Cdd:cd05075   160 SkKIYNGDYYRQgRISKMPVKWIAIES--LADRVYTTKSDVWSFGVTMWEIATR 211
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
710-909 1.47e-10

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: 63.79  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKdtGEMVALKKVRLDNEKEGFPITAIREIKILRqLTHqsiiNMKEIVTDKEDA--LDFKKDKGAF 787
Cdd:cd14000     1 LLGDGGFGSVYRASYK--GEPVAVKIFNKHTSSNFANVPADTMLRHLR-ATD----AMKNFRLLRQELtvLSHLHHPSIV 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMdHDLMGLLE----SGLVHFNENHIKSFMR-----------QLMEGLDYCHKKNFLHRDIKCSNILL-----NN 847
Cdd:cd14000    74 YLLGIGI-HPLMLVLElaplGSLDHLLQQDSRSFASlgrtlqqrialQVADGLRYLHSAMIIYRDLKSHNVLVwtlypNS 152
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 145309300  848 RGQIKLADFGLARLYSSEESRPYTNkviTLWYRPPELLLGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd14000   153 AIIIKIADYGISRQCCRMGAKGSEG---TPGFRAPEIARGNVIYNEKVDVFSFGMLLYEILS 211
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
710-907 1.72e-10

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


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 63.62  E-value: 1.72e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKdtGEMVALKKVRLDNEKEGFPITAIREIKILRqltHQSIINMkeIVTDKedaldfkKDKGAF-- 787
Cdd:cd14143     2 SIGKGRFGEVWRGRWR--GEDVAVKIFSSREERSWFREAEIYQTVMLR---HENILGF--IAADN-------KDNGTWtq 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 -YLVFEYMDH------------DLMGLLE------SGLVHFNenhiksfmrqlMEGLDYCHKKNFLHRDIKCSNILLNNR 848
Cdd:cd14143    68 lWLVSDYHEHgslfdylnrytvTVEGMIKlalsiaSGLAHLH-----------MEIVGTQGKPAIAHRDLKSKNILVKKN 136
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  849 GQIKLADFGLARLYSSEESR---PYTNKVITLWYRPPELL------LGEERYTPAiDVWSCGCILGEL 907
Cdd:cd14143   137 GTCCIADLGLAVRHDSATDTidiAPNHRVGTKRYMAPEVLddtinmKHFESFKRA-DIYALGLVFWEI 203
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
710-921 1.74e-10

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: 63.52  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKArdKDTGEMVALKKVRLD-NEKEGFPITAIR-EIKILRQLTHQSIINMKEIVTdKEDALdfkkdkgaf 787
Cdd:cd14145    13 IIGIGGFGKVYRA--IWIGDEVAVKAARHDpDEDISQTIENVRqEAKLFAMLKHPNIIALRGVCL-KEPNL--------- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  788 YLVFEYMDHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNF---LHRDIKCSNILLNNRGQ--------IKLADF 856
Cdd:cd14145    81 CLVMEFARGGPLNRVLSG-KRIPPDILVNWAVQIARGMNYLHCEAIvpvIHRDLKSSNILILEKVEngdlsnkiLKITDF 159
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  857 GLARLYSSEESRPYTNkviTLWYRPPELLLGeERYTPAIDVWSCGCILGELFTKKPIFQANQELA 921
Cdd:cd14145   160 GLAREWHRTTKMSAAG---TYAWMAPEVIRS-SMFSKGSDVWSYGVLLWELLTGEVPFRGIDGLA 220
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
711-907 1.76e-10

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: 63.26  E-value: 1.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFpitaIREIKILRQLTHQSIINMKEIVTdkedaldfkkDKGAFYLV 790
Cdd:cd14155     1 IGSGFFSEVYKVRHRTSGQVMALKMNTLSSNRANM----LREVQLMNRLSHPNILRFMGVCV----------HQGQLHAL 66
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMDH-DLMGLLESGLVHFNENHIKsFMRQLMEGLDYCHKKNFLHRDIKCSNILL---NNRGQIKLADFGLAR---LYS 863
Cdd:cd14155    67 TEYINGgNLEQLLDSNEPLSWTVRVK-LALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLAEkipDYS 145
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 145309300  864 SEESRPYTnkVITLWYRPPELLLGEErYTPAIDVWSCGCILGEL 907
Cdd:cd14155   146 DGKEKLAV--VGSPYWMAPEVLRGEP-YNEKADVFSYGIILCEI 186
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
710-909 1.98e-10

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: 63.12  E-value: 1.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKdtGEMVALKKVRLDNEkEGFPITA---IREIKILRQLTHQSIINMKEIVTDKEDaldfkkdkga 786
Cdd:cd14147    10 VIGIGGFGKVYRGSWR--GELVAVKAARQDPD-EDISVTAesvRQEARLFAMLAHPNIIALKAVCLEEPN---------- 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDHdlmGLLESGLV--HFNENHIKSFMRQLMEGLDYCHKKNF---LHRDIKCSNILLNNRGQ--------IKL 853
Cdd:cd14147    77 LCLVMEYAAG---GPLSRALAgrRVPPHVLVNWAVQIARGMHYLHCEALvpvIHRDLKSNNILLLQPIEnddmehktLKI 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 145309300  854 ADFGLARLYSSEESRPYTNkviTLWYRPPElLLGEERYTPAIDVWSCGCILGELFT 909
Cdd:cd14147   154 TDFGLAREWHKTTQMSAAG---TYAWMAPE-VIKASTFSKGSDVWSFGVLLWELLT 205
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
711-939 3.14e-10

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


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 62.51  E-value: 3.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDkedaldfkkdkgAFYLV 790
Cdd:cd14025     4 VGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGICSE------------PVGLV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEYMD----------HDLMGLLESGLVHfnenhiksfmrQLMEGLDYCH--KKNFLHRDIKCSNILLNNRGQIKLADFGL 858
Cdd:cd14025    72 MEYMEtgslekllasEPLPWELRFRIIH-----------ETAVGMNFLHcmKPPLLHLDLKPANILLDAHYHVKISDFGL 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  859 ARLYSSEESRPYTNKVI--TLWYRPPELLLGEER-YTPAIDVWSCGCILGELFTKKPIFQANQELaqLELISRICG---- 931
Cdd:cd14025   141 AKWNGLSHSHDLSRDGLrgTIAYLPPERFKEKNRcPDTKHDVYSFAIVIWGILTQKKPFAGENNI--LHIMVKVVKghrp 218
                         250
                  ....*....|
gi 145309300  932 --SPCPAVWP 939
Cdd:cd14025   219 slSPIPRQRP 228
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
710-919 3.76e-10

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


Pssm-ID: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 63.18  E-value: 3.76e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMVAlkkvrldnekegfpitaireIKILRqlthqsiinmKEIVTDKED-----------AL 778
Cdd:cd05587     3 VLGKGSFGKVMLAERKGTDELYA--------------------IKILK----------KDVIIQDDDvectmvekrvlAL 52
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 dfkKDKGAF--------------YLVFEYMDH-DLMGLLESglVH-FNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSN 842
Cdd:cd05587    53 ---SGKPPFltqlhscfqtmdrlYFVMEYVNGgDLMYHIQQ--VGkFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDN 127
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  843 ILLNNRGQIKLADFGLAR--LYSSEESRPYTNkviTLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQE 919
Cdd:cd05587   128 VMLDAEGHIKIADFGMCKegIFGGKTTRTFCG---TPDYIAPEIIAYQP-YGKSVDWWAYGVLLYEMLAGQPPFDGEDE 202
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
711-959 4.21e-10

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


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 62.34  E-value: 4.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTG-----EMVALKKVRldNEKEGFPITAIREIKILR-QLTHQSIINMKEIVTdKEDALDfkkdk 784
Cdd:cd05091    14 LGEDRFGKVYKGHLFGTApgeqtQAVAIKTLK--DKAEGPLREEFRHEAMLRsRLQHPNIVCLLGVVT-KEQPMS----- 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  785 gafyLVFEYMDH-DLMGLLESGLVHFN------ENHIKSFMR---------QLMEGLDYCHKKNFLHRDIKCSNILLNNR 848
Cdd:cd05091    86 ----MIFSYCSHgDLHEFLVMRSPHSDvgstddDKTVKSTLEpadflhivtQIAAGMEYLSSHHVVHKDLATRNVLVFDK 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  849 GQIKLADFGLAR-LYSSEESRPYTNKVITL-WYRPPELLLGeeRYTPAIDVWSCGCILGELFTK--KPIF-QANQELaqL 923
Cdd:cd05091   162 LNVKISDLGLFReVYAADYYKLMGNSLLPIrWMSPEAIMYG--KFSIDSDIWSYGVVLWEVFSYglQPYCgYSNQDV--I 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 145309300  924 ELISR----ICGSPCPAvWPDVIKLPYFNTMkPKKQYRRK 959
Cdd:cd05091   238 EMIRNrqvlPCPDDCPA-WVYTLMLECWNEF-PSRRPRFK 275
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
711-933 4.64e-10

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: 62.39  E-value: 4.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKArdKDTGEmVALKKVRLDNEKEGFPITAIREIKILRQLTHQSIINMKEIVTDKEDALDFKKDKGAfylv 790
Cdd:cd14151    16 IGSGSFGTVYKG--KWHGD-VAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNILLFMGYSTKPQLAIVTQWCEGS---- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 feymdhDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSS-EESRP 869
Cdd:cd14151    89 ------SLYHHLHIIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRwSGSHQ 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  870 YTNKVITLWYRPPELLLGEER--YTPAIDVWSCGCILGELFTKK-PIFQANQELAQLELISRICGSP 933
Cdd:cd14151   163 FEQLSGSILWMAPEVIRMQDKnpYSFQSDVYAFGIVLYELMTGQlPYSNINNRDQIIFMVGRGYLSP 229
STKc_CK1_alpha cd14128
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 alpha; STKs catalyze ...
704-891 4.93e-10

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


Pssm-ID: 271030 [Multi-domain]  Cd Length: 266  Bit Score: 62.14  E-value: 4.93e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVAlkkVRLDNEKEGFPiTAIREIKILRQLthQSIINMKEIVTdkedaldFKKD 783
Cdd:cd14128     1 KYRLVRKIGSGSFGDIYLGINITNGEEVA---VKLESQKARHP-QLLYESKLYKIL--QGGVGIPHIRW-------YGQE 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  784 KGAFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILL---NNRGQIKLADFGLAR 860
Cdd:cd14128    68 KDYNVLVMDLLGPSLEDLFNFCSRRFTMKTVLMLADQMIGRIEYVHNKNFIHRDIKPDNFLMgigRHCNKLFLIDFGLAK 147
                         170       180       190
                  ....*....|....*....|....*....|.
gi 145309300  861 LYSSEESRPYtnkvitLWYRPPELLLGEERY 891
Cdd:cd14128   148 KYRDSRTRQH------IPYREDKNLTGTARY 172
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
703-909 6.59e-10

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


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 62.12  E-value: 6.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRLDNEKEGFPITAIR----EIKILRQLTHQ-SIINMKEIVTDKEDA 777
Cdd:cd05054     7 DRLKLGKPLGRGAFGKVIQASAFGIDKSATCRTVAVKMLKEGATASEHKalmtELKILIHIGHHlNVVNLLGACTKPGGP 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  778 L-------------DFKKDKGAFYL---------------VFEYMDHDLmgLLEsglvhfnenHIKSFMRQLMEGLDYCH 829
Cdd:cd05054    87 LmvivefckfgnlsNYLRSKREEFVpyrdkgardveeeedDDELYKEPL--TLE---------DLICYSFQVARGMEFLA 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  830 KKNFLHRDIKCSNILLNNRGQIKLADFGLAR-LYSSEESRPYTNKVITLWYRPPELLLgEERYTPAIDVWSCGCILGELF 908
Cdd:cd05054   156 SRKCIHRDLAARNILLSENNVVKICDFGLARdIYKDPDYVRKGDARLPLKWMAPESIF-DKVYTTQSDVWSFGVLLWEIF 234

                  .
gi 145309300  909 T 909
Cdd:cd05054   235 S 235
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
711-907 7.14e-10

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: 62.07  E-value: 7.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKdtGEMVALKKVRLDNEKEGFPITAIREIKILRqltHQSIINMkeIVTDkedaLDFKKDKGAFYLV 790
Cdd:cd14142    13 IGKGRYGEVWRGQWQ--GESVAVKIFSSRDEKSWFRETEIYNTVLLR---HENILGF--IASD----MTSRNSCTQLWLI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  791 FEY--------------MDHDLMGLL----ESGLVHFnenHIKSFMRQlmegldycHKKNFLHRDIKCSNILLNNRGQIK 852
Cdd:cd14142    82 THYhengslydylqrttLDHQEMLRLalsaASGLVHL---HTEIFGTQ--------GKPAIAHRDLKSKNILVKSNGQCC 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 145309300  853 LADFGLARLYSSEESR--PYTN-KVITLWYRPPELLlgEERYTPA-------IDVWSCGCILGEL 907
Cdd:cd14142   151 IADLGLAVTHSQETNQldVGNNpRVGTKRYMAPEVL--DETINTDcfesykrVDIYAFGLVLWEV 213
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
704-909 7.19e-10

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: 61.96  E-value: 7.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALkkvrldnekegfPITaireIKILRQLT----HQSIINMKEIVTDKEDALD 779
Cdd:cd05108     8 EFKKIKVLGSGAFGTVYKGLWIPEGEKVKI------------PVA----IKELREATspkaNKEILDEAYVMASVDNPHV 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FKKD----KGAFYLVFEYMDHD-LMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLA 854
Cdd:cd05108    72 CRLLgiclTSTVQLITQLMPFGcLLDYVREHKDNIGSQYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKIT 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  855 DFGLARLYSSEESRPYTN--KVITLWYRPPELLlgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd05108   152 DFGLAKLLGAEEKEYHAEggKVPIKWMALESIL--HRIYTHQSDVWSYGVTVWELMT 206
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
710-910 9.37e-10

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


Pssm-ID: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 61.47  E-value: 9.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKAR---DKDTGEMVALKKVRLD----NEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKedaldfkK 782
Cdd:cd05074    16 MLGKGEFGSVREAQlksEDGSFQKVAVKMLKADifssSDIEEF----LREAACMKEFDHPNVIKLIGVSLRS-------R 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAF---YLVFEYMDHD------LMGLLESGLVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKL 853
Cdd:cd05074    85 AKGRLpipMVILPFMKHGdlhtflLMSRIGEEPFTLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCV 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 145309300  854 ADFGLAR-LYSSEESRP-YTNKVITLWYRPPEllLGEERYTPAIDVWSCGCILGELFTK 910
Cdd:cd05074   165 ADFGLSKkIYSGDYYRQgCASKLPVKWLALES--LADNVYTTHSDVWAFGVTMWEIMTR 221
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
710-909 9.37e-10

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: 61.55  E-value: 9.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  710 IIGEGTYGQVYKARDKDTGEMV--ALKKVRLDNEKEGFPITAiREIKILRQL-THQSIINMkeivtdkedaLDFKKDKGA 786
Cdd:cd05088    14 VIGEGNFGQVLKARIKKDGLRMdaAIKRMKEYASKDDHRDFA-GELEVLCKLgHHPNIINL----------LGACEHRGY 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  787 FYLVFEYMDH-DLMGLLESGLV---------------HFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ 850
Cdd:cd05088    83 LYLAIEYAPHgNLLDFLRKSRVletdpafaianstasTLSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYV 162
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  851 IKLADFGLARlysseESRPYTNKVITlwyRPPELLLGEER-----YTPAIDVWSCGCILGELFT 909
Cdd:cd05088   163 AKIADFGLSR-----GQEVYVKKTMG---RLPVRWMAIESlnysvYTTNSDVWSYGVLLWEIVS 218
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
789-998 1.26e-09

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


Pssm-ID: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 61.10  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDHDLMGLLesgLVHFNENH----IKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQ-IKLADFGLarlyS 863
Cdd:cd14020    86 LLLELLDVSVSELL---LRSSNQGCsmwmIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEDEcFKLIDFGL----S 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  864 SEESRPYTNKVITLWYRPPELLL----------GEERYTPAIDVWSCGCILGELFT----KKPIFQANQELAQLELISRI 929
Cdd:cd14020   159 FKEGNQDVKYIQTDGYRAPEAELqnclaqaglqSETECTSAVDLWSLGIVLLEMFSgmklKHTVRSQEWKDNSSAIIDHI 238
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 145309300  930 CGSP---CPAvwpdviklpyfntmkpkkqyrrklreefvfIPAAAL-DLFDYMLALDPSKRCTAEQALQCEFL 998
Cdd:cd14020   239 FASNavvNPA------------------------------IPAYHLrDLIKSMLHNDPGKRATAEAALCSPFF 281
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
723-909 1.39e-09

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


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 61.56  E-value: 1.39e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  723 RDKDTGEMVALKKVRLDN--EKEGFPITAIREIKilrqlthqsiiNMKEIVTDKEDALDFKKDKgafyLVFEymdhDLMg 800
Cdd:cd14207   124 KEKKEAEPTGGKKKRLESvtSSESFASSGFQEDK-----------SLSDVEEEEEDSGDFYKRP----LTME----DLI- 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  801 llesglvhfnenhikSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLAR-LYSSEESRPYTNKVITLWY 879
Cdd:cd14207   184 ---------------SYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARdIYKNPDYVRKGDARLPLKW 248
                         170       180       190
                  ....*....|....*....|....*....|
gi 145309300  880 RPPELLLgEERYTPAIDVWSCGCILGELFT 909
Cdd:cd14207   249 MAPESIF-DKIYSTKSDVWSYGVLLWEIFS 277
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
703-920 1.47e-09

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 61.53  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  703 DKFDIIGIIGEGTYGQVYKARDKDtgemvalkkvrldnekEGFPITAIREI---KILRQLTHQSIINMKEIVTDKEDALD 779
Cdd:PTZ00426   30 EDFNFIRTLGTGSFGRVILATYKN----------------EDFPPVAIKRFeksKIIKQKQVDHVFSERKILNYINHPFC 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  780 FK-----KDKGAFYLVFEY-MDHDLMGLLESGlVHFNENHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKL 853
Cdd:PTZ00426   94 VNlygsfKDESYLYLVLEFvIGGEFFTFLRRN-KRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKM 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  854 ADFGLARLYsseESRPYTnKVITLWYRPPELLLGEErYTPAIDVWSCGCILGELFTKKPIFQANQEL 920
Cdd:PTZ00426  173 TDFGFAKVV---DTRTYT-LCGTPEYIAPEILLNVG-HGKAADWWTLGIFIYEILVGCPPFYANEPL 234
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
711-908 1.72e-09

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


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 60.72  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEM----------------VALKKVRLD---NEKEGFpitaIREIKILRQLTHQSIINMKEIV 771
Cdd:cd05096    13 LGEGQFGEVHLCEVVNPQDLptlqfpfnvrkgrpllVAVKILRPDankNARNDF----LKEVKILSRLKDPNIIRLLGVC 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  772 TDkEDALdfkkdkgafYLVFEYMD----------HDLMGLLESGLVHFNENH---------IKSFMRQLMEGLDYCHKKN 832
Cdd:cd05096    89 VD-EDPL---------CMITEYMEngdlnqflssHHLDDKEENGNDAVPPAHclpaisyssLLHVALQIASGMKYLSSLN 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 145309300  833 FLHRDIKCSNILLNNRGQIKLADFGLAR-LYSSEESRPYTNKVITL-WYRPPELLLGeeRYTPAIDVWSCGCILGELF 908
Cdd:cd05096   159 FVHRDLATRNCLVGENLTIKIADFGMSRnLYAGDYYRIQGRAVLPIrWMAWECILMG--KFTTASDVWAFGVTLWEIL 234
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
711-915 2.23e-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: 60.32  E-value: 2.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  711 IGEGTYGQVYKARDKDTGEMVALKKVRL-----DNEKEGFpitaIREIKILRQLTHQSIINMKEIVTDKEdaldfkkdkg 785
Cdd:cd14026     5 LSRGAFGTVSRARHADWRVTVAIKCLKLdspvgDSERNCL----LKEAEILHKARFSYILPILGICNEPE---------- 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  786 AFYLVFEYMDHDLMGLLESGLVHFNENHIKSFMRQLME---GLDYCHKKN--FLHRDIKCSNILLNNRGQIKLADFGLA- 859
Cdd:cd14026    71 FLGIVTEYMTNGSLNELLHEKDIYPDVAWPLRLRILYEialGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSk 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 145309300  860 -RLYSSEESRPYTNKVI--TLWYRPPelllgeERYTPA--------IDVWSCGCILGELFTKKPIFQ 915
Cdd:cd14026   151 wRQLSISQSRSSKSAPEggTIIYMPP------EEYEPSqkrrasvkHDIYSYAIIMWEVLSRKIPFE 211
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
709-925 2.47e-09

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: 60.45  E-value: 2.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  709 GIIGEGTYGQVYKARDKDtgEMVALKkVRLDNEKEGFpiTAIREIKILRQLTHQSIInmKEIVTDKEDALDFKKDkgaFY 788
Cdd:cd14054     1 QLIGQGRYGTVWKGSLDE--RPVAVK-VFPARHRQNF--QNEKDIYELPLMEHSNIL--RFIGADERPTADGRME---YL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  789 LVFEYMDHdlmglleSGLVHFNENHIKSFM------RQLMEGLDYCH---------KKNFLHRDIKCSNILLNNRGQIKL 853
Cdd:cd14054    71 LVLEYAPK-------GSLCSYLRENTLDWMsscrmaLSLTRGLAYLHtdlrrgdqyKPAIAHRDLNSRNVLVKADGSCVI 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  854 ADFGLA-RLYSS----EESRPYTNKVI----TLWYRPPELLLGE------ERYTPAIDVWSCGCILGELFTKKPIFQANQ 918
Cdd:cd14054   144 CDFGLAmVLRGSslvrGRPGAAENASIsevgTLRYMAPEVLEGAvnlrdcESALKQVDVYALGLVLWEIAMRCSDLYPGE 223

                  ....*..
gi 145309300  919 ELAQLEL 925
Cdd:cd14054   224 SVPPYQM 230
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
709-907 2.76e-09

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: 60.08  E-value: 2.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  709 GIIGEGTYGQVYKAR-DKDTG---EMVALKKVRLD------NEKEGFPITAIREIKILRQLTHQsiinMKEIVTDKEdal 778
Cdd:cd14055     1 KLVGKGRFAEVWKAKlKQNASgqyETVAVKIFPYEeyaswkNEKDIFTDASLKHENILQFLTAE----ERGVGLDRQ--- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  779 dfkkdkgaFYLVFEYMDHdlmglleSGLVHFNENHIKSFM------RQLMEGLDYCH---------KKNFLHRDIKCSNI 843
Cdd:cd14055    74 --------YWLITAYHEN-------GSLQDYLTRHILSWEdlckmaGSLARGLAHLHsdrtpcgrpKIPIAHRDLKSSNI 138
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 145309300  844 LLNNRGQIKLADFGLA-RLYSSEESRPYTN--KVITLWYRPPELLlgEERYTPA-------IDVWSCGCILGEL 907
Cdd:cd14055   139 LVKNDGTCVLADFGLAlRLDPSLSVDELANsgQVGTARYMAPEAL--ESRVNLEdlesfkqIDVYSMALVLWEM 210
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
812-909 2.82e-09

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


Pssm-ID: 173653 [Multi-domain]  Cd Length: 400  Bit Score: 60.81  E-value: 2.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  812 NHIKSFMRQLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESrpYTNKVITL----WYRPPELLlg 887
Cdd:cd05105   237 LDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLARDIMHDSN--YVSKGSTFlpvkWMAPESIF-- 312
                          90       100
                  ....*....|....*....|..
gi 145309300  888 EERYTPAIDVWSCGCILGELFT 909
Cdd:cd05105   313 DNLYTTLSDVWSYGILLWEIFS 334
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
820-909 2.91e-09

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: 60.04  E-value: 2.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  820 QLMEGLDYCHKKNFLHRDIKCSNILLNNRGQIKLADFGLARLYSSEESRPYTN--KVITLWYRPPELLlgEERYTPAIDV 897
Cdd:cd05109   117 QIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETEYHADggKVPIKWMALESIL--HRRFTHQSDV 194
                          90
                  ....*....|..
gi 145309300  898 WSCGCILGELFT 909
Cdd:cd05109   195 WSYGVTVWELMT 206
STKc_SRPK2 cd14217
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 2; STKs ...
704-915 2.97e-09

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


Pssm-ID: 271119 [Multi-domain]  Cd Length: 366  Bit Score: 60.81  E-value: 2.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  704 KFDIIGIIGEGTYGQVYKARDKDTGEMVALKKVRldnEKEGFPITAIREIKILRQLTHQSIIN-MKEIVTDKEDALDFKK 782
Cdd:cd14217    13 RYHVIRKLGWGHFSTVWLCWDMQGKRFVAMKVVK---SAQHYTETALDEIKLLRCVRESDPEDpNKDMVVQLIDDFKISG 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  783 DKGAFY-LVFEYMDHDLMG-LLESGLVHFNENHIKSFMRQLMEGLDYCHKK-NFLHRDIKCSNILL-------------- 845
Cdd:cd14217    90 MNGIHVcMVFEVLGHHLLKwIIKSNYQGLPIRCVKSIIRQVLQGLDYLHSKcKIIHTDIKPENILMcvddayvrrmaaea 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 145309300  846 -------------------------------NNRGQIKLADFGLArlysSEESRPYTNKVITLWYRPPELLLGEERYTPA 894
Cdd:cd14217   170 tewqkagapppsgsavstapdllvnpldprnADKIRVKIADLGNA----CWVHKHFTEDIQTRQYRSIEVLIGAGYSTPA 245
                         250       260
                  ....*....|....*....|.
gi 145309300  895 iDVWSCGCILGELFTKKPIFQ 915
Cdd:cd14217   246 -DIWSTACMAFELATGDYLFE 265
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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