NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|564380513|ref|XP_006249836|]
View 

dual serine/threonine and tyrosine protein kinase isoform X1 [Rattus norvegicus]

Protein Classification

dual serine/threonine and tyrosine protein kinase( domain architecture ID 10195577)

dual serine/threonine and tyrosine protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
551-812 0e+00

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


:

Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 595.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSVAV 630
Cdd:cd13975    1 KPKLGRELGRGQYGVVYACDSWGGHFPCALKSVVPPDDKHWNDLALEFHYTRSLPKHERIVSLHGSVIDYSYGGGSSIAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIV 710
Cdd:cd13975   81 LLIMERLHRDLYTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAMMSGSIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 711 GTPIHMAPELFTGKYDNSVDVYAFGILFWYICSGSIKLPEAFERCASKDHLWNNVRRGTRPERLPVFDEECWQLMEACWD 790
Cdd:cd13975  161 GTPIHMAPELFSGKYDNSVDVYAFGILFWYLCAGHVKLPEAFEQCASKDHLWNNVRKGVRPERLPVFDEECWNLMEACWS 240
                        250       260
                 ....*....|....*....|..
gi 564380513 791 GDPSKRPLLGIVQPILRSIMDR 812
Cdd:cd13975  241 GDPSQRPLLGIVQPKLQGIMDR 262
 
Name Accession Description Interval E-value
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
551-812 0e+00

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 595.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSVAV 630
Cdd:cd13975    1 KPKLGRELGRGQYGVVYACDSWGGHFPCALKSVVPPDDKHWNDLALEFHYTRSLPKHERIVSLHGSVIDYSYGGGSSIAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIV 710
Cdd:cd13975   81 LLIMERLHRDLYTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAMMSGSIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 711 GTPIHMAPELFTGKYDNSVDVYAFGILFWYICSGSIKLPEAFERCASKDHLWNNVRRGTRPERLPVFDEECWQLMEACWD 790
Cdd:cd13975  161 GTPIHMAPELFSGKYDNSVDVYAFGILFWYLCAGHVKLPEAFEQCASKDHLWNNVRKGVRPERLPVFDEECWNLMEACWS 240
                        250       260
                 ....*....|....*....|..
gi 564380513 791 GDPSKRPLLGIVQPILRSIMDR 812
Cdd:cd13975  241 GDPSQRPLLGIVQPKLQGIMDR 262
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
553-797 1.28e-45

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 164.24  E-value: 1.28e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513   553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSV-VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaVL 631
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTGKLVAIKVIkKKKIKKDRERILREIKILKKL-KHPNIVRLYDVFEDEDK-------LY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513   632 LIMERL-HRDLYTGLKA--GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PEAMMS 706
Cdd:smart00220  74 LVMEYCeGGDLFDLLKKrgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARqlDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513   707 GSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsiKLPeaFERCASKDHLWNNVRRGTR--PERLPVFDEECWQ 783
Cdd:smart00220 154 TTFVGTPEYMAPEVLLGKgYGKAVDIWSLGVILYELLTG--KPP--FPGDDQLLELFKKIGKPKPpfPPPEWDISPEAKD 229
                          250
                   ....*....|....
gi 564380513   784 LMEACWDGDPSKRP 797
Cdd:smart00220 230 LIRKLLVKDPEKRL 243
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
553-797 1.20e-37

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: 141.48  E-value: 1.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513  553 KLGQELGRGQYGVVYLC----DNWGGHFPCALKSVVPP-DEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggss 627
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGtlkgEGENTKIKVAVKTLKEGaDEEEREDFLEEASIMKKL-DHPNIVKLLGVCTQGEP----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513  628 vaVLLIMERL-HRDLYTGL---KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpeA 703
Cdd:pfam07714  76 --LYIVTEYMpGGDLLDFLrkhKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSR--D 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513  704 MMSGSIVGT------PIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSG------SIKLPEAFERcaskdhlwnnVRRGT 769
Cdd:pfam07714 152 IYDDDYYRKrgggklPIKwMAPEsLKDGKFTSKSDVWSFGVLLWEIFTLgeqpypGMSNEEVLEF----------LEDGY 221
                         250       260
                  ....*....|....*....|....*...
gi 564380513  770 RPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:pfam07714 222 RLPQPENCPDELYDLMKQCWAYDPEDRP 249
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
554-749 1.34e-32

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 132.44  E-value: 1.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLC-DNWGGHfPCALKSVVPPDEKHWNDLAL---EFHYMRSLpKHERLVdlhgSVIDYNYGGGSSVa 629
Cdd:COG0515   11 ILRLLGRGGMGVVYLArDLRLGR-PVALKVLRPELAADPEARERfrrEARALARL-NHPNIV----RVYDVGEEDGRPY- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 vlLIMERLH-RDLYTGLKAG--LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK----PE 702
Cdd:COG0515   84 --LVMEYVEgESLADLLRRRgpLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARalggAT 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564380513 703 AMMSGSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGsiKLP 749
Cdd:COG0515  162 LTQTGTVVGTPGYMAPEQARGePVDPRSDVYSLGVTLYELLTG--RPP 207
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
632-738 1.05e-13

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 74.83  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLH-RDLYTGLKAG--LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpeAM---- 704
Cdd:NF033483  84 IVMEYVDgRTLKDYIREHgpLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIAR--ALsstt 161
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 564380513 705 --MSGSIVGTPIHMAPELFTGKY-DNSVDVYAFGILF 738
Cdd:NF033483 162 mtQTNSVLGTVHYLSPEQARGGTvDARSDIYSLGIVL 198
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
660-744 2.27e-13

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 72.16  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILF 738
Cdd:PTZ00263 126 ELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFTLCGTPEYLAPEVIQSKgHGKAVDWWTMGVLL 205

                 ....*.
gi 564380513 739 WYICSG 744
Cdd:PTZ00263 206 YEFIAG 211
 
Name Accession Description Interval E-value
PKc_Dusty cd13975
Catalytic domain of the Dual-specificity Protein Kinase, Dusty; Dual-specificity PKs catalyze ...
551-812 0e+00

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


Pssm-ID: 270877 [Multi-domain]  Cd Length: 262  Bit Score: 595.62  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSVAV 630
Cdd:cd13975    1 KPKLGRELGRGQYGVVYACDSWGGHFPCALKSVVPPDDKHWNDLALEFHYTRSLPKHERIVSLHGSVIDYSYGGGSSIAV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIV 710
Cdd:cd13975   81 LLIMERLHRDLYTGIKAGLSLEERLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKKNRAKITDLGFCKPEAMMSGSIV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 711 GTPIHMAPELFTGKYDNSVDVYAFGILFWYICSGSIKLPEAFERCASKDHLWNNVRRGTRPERLPVFDEECWQLMEACWD 790
Cdd:cd13975  161 GTPIHMAPELFSGKYDNSVDVYAFGILFWYLCAGHVKLPEAFEQCASKDHLWNNVRKGVRPERLPVFDEECWNLMEACWS 240
                        250       260
                 ....*....|....*....|..
gi 564380513 791 GDPSKRPLLGIVQPILRSIMDR 812
Cdd:cd13975  241 GDPSQRPLLGIVQPKLQGIMDR 262
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
558-797 4.62e-47

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: 167.71  E-value: 4.62e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLcDNWGGHfPCALKS--VVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaVLLIME 635
Cdd:cd13999    1 IGSGSFGEVYK-GKWRGT-DVAIKKlkVEDDNDELLKEFRREVSILSKL-RHPNIVQFIGACLSPPP-------LCIVTE 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RLHR-DLYTGLKAG---LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA---MMSGS 708
Cdd:cd13999   71 YMPGgSLYDLLHKKkipLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNsttEKMTG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 709 IVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsiKLPeaFERCASKDHLWNNVRRGTRPERLPVFDEECWQLMEA 787
Cdd:cd13999  151 VVGTPRWMAPEVLRGEpYTEKADVYSFGIVLWELLTG--EVP--FKELSPIQIAAAVVQKGLRPPIPPDCPPELSKLIKR 226
                        250
                 ....*....|
gi 564380513 788 CWDGDPSKRP 797
Cdd:cd13999  227 CWNEDPEKRP 236
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
553-797 1.28e-45

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 164.24  E-value: 1.28e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513   553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSV-VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaVL 631
Cdd:smart00220   2 EILEKLGEGSFGKVYLARDKKTGKLVAIKVIkKKKIKKDRERILREIKILKKL-KHPNIVRLYDVFEDEDK-------LY 73
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513   632 LIMERL-HRDLYTGLKA--GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PEAMMS 706
Cdd:smart00220  74 LVMEYCeGGDLFDLLKKrgRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARqlDPGEKL 153
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513   707 GSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsiKLPeaFERCASKDHLWNNVRRGTR--PERLPVFDEECWQ 783
Cdd:smart00220 154 TTFVGTPEYMAPEVLLGKgYGKAVDIWSLGVILYELLTG--KPP--FPGDDQLLELFKKIGKPKPpfPPPEWDISPEAKD 229
                          250
                   ....*....|....
gi 564380513   784 LMEACWDGDPSKRP 797
Cdd:smart00220 230 LIRKLLVKDPEKRL 243
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
558-797 2.58e-43

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: 156.28  E-value: 2.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKH-WNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaVLLIMER 636
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKKlLEELLREIEILKKL-NHPNIVKLYDVFETENF-------LYLVMEY 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 637 L-HRDLYTGLK---AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK----PEAMMSGS 708
Cdd:cd00180   73 CeGGSLKDLLKenkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKdldsDDSLLKTT 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 709 IVGTPIHMAPE--LFTGKYDNSVDVYAFGILFWYIcsgsiklpeafercaskdhlwnnvrrgtrperlpvfdEECWQLME 786
Cdd:cd00180  153 GGTTPPYYAPPelLGGRYYGPKVDIWSLGVILYEL-------------------------------------EELKDLIR 195
                        250
                 ....*....|.
gi 564380513 787 ACWDGDPSKRP 797
Cdd:cd00180  196 RMLQYDPKKRP 206
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
553-797 4.67e-41

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: 151.16  E-value: 4.67e-41
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513   553 KLGQELGRGQYGVVYLC----DNWGGHFPCALKSVVPP-DEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDynygGGSS 627
Cdd:smart00221   2 TLGKKLGEGAFGEVYKGtlkgKGDGKEVEVAVKTLKEDaSEQQIEEFLREARIMRKL-DHPNIVKLLGVCTE----EEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513   628 VAVLLIMErlHRDLYTGLK----AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA 703
Cdd:smart00221  77 MIVMEYMP--GGDLLDYLRknrpKELSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLY 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513   704 -----MMSGSIVgtPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSGSIKLPEAFercaSKDHLWNNVRRGTRPERLPV 776
Cdd:smart00221 155 dddyyKVKGGKL--PIRwMAPEsLKEGKFTSKSDVWSFGVLLWEIFTLGEEPYPGM----SNAEVLEYLKKGYRLPKPPN 228
                          250       260
                   ....*....|....*....|.
gi 564380513   777 FDEECWQLMEACWDGDPSKRP 797
Cdd:smart00221 229 CPPELYKLMLQCWAEDPEDRP 249
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
553-797 2.97e-40

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 148.83  E-value: 2.97e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513   553 KLGQELGRGQYGVVYLCD----NWGGHFPCALKSV-VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDynygGGSS 627
Cdd:smart00219   2 TLGKKLGEGAFGEVYKGKlkgkGGKKKVEVAVKTLkEDASEQQIEEFLREARIMRKL-DHPNVVKLLGVCTE----EEPL 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513   628 VAVLLIMErlHRDLYTGLKA---GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPE-- 702
Cdd:smart00219  77 YIVMEYME--GGDLLSYLRKnrpKLSLSDLLSFALQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLyd 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513   703 ----AMMSGSIvgtPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSGSIKLPEAFercaSKDHLWNNVRRGTRPERLPV 776
Cdd:smart00219 155 ddyyRKRGGKL---PIRwMAPEsLKEGKFTSKSDVWSFGVLLWEIFTLGEQPYPGM----SNEEVLEYLKNGYRLPQPPN 227
                          250       260
                   ....*....|....*....|.
gi 564380513   777 FDEECWQLMEACWDGDPSKRP 797
Cdd:smart00219 228 CPPELYDLMLQCWAEDPEDRP 248
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
553-797 1.20e-37

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: 141.48  E-value: 1.20e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513  553 KLGQELGRGQYGVVYLC----DNWGGHFPCALKSVVPP-DEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggss 627
Cdd:pfam07714   2 TLGEKLGEGAFGEVYKGtlkgEGENTKIKVAVKTLKEGaDEEEREDFLEEASIMKKL-DHPNIVKLLGVCTQGEP----- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513  628 vaVLLIMERL-HRDLYTGL---KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpeA 703
Cdd:pfam07714  76 --LYIVTEYMpGGDLLDFLrkhKRKLTLKDLLSMALQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGLSR--D 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513  704 MMSGSIVGT------PIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSG------SIKLPEAFERcaskdhlwnnVRRGT 769
Cdd:pfam07714 152 IYDDDYYRKrgggklPIKwMAPEsLKDGKFTSKSDVWSFGVLLWEIFTLgeqpypGMSNEEVLEF----------LEDGY 221
                         250       260
                  ....*....|....*....|....*...
gi 564380513  770 RPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:pfam07714 222 RLPQPENCPDELYDLMKQCWAYDPEDRP 249
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
557-797 6.48e-35

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: 133.82  E-value: 6.48e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLC---DNWGGHFPCALKSVVP-PDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaVLL 632
Cdd:cd00192    2 KLGEGAFGEVYKGklkGGDGKTVDVAVKTLKEdASESERKDFLKEARVMKKL-GHPNVVRLLGVCTEEEP-------LYL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IME-----------RLHRD-LYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK 700
Cdd:cd00192   74 VMEymeggdlldflRKSRPvFPSPEPSTLSLKDLLSFAIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLSR 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 701 PEAMMSGSIVGT----PIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPEafercASKDHLWNNVRRGTRPER 773
Cdd:cd00192  154 DIYDDDYYRKKTggklPIRwMAPEsLKDGIFTSKSDVWSFGVLLWEIFTlGATPYPG-----LSNEEVLEYLRKGYRLPK 228
                        250       260
                 ....*....|....*....|....
gi 564380513 774 LPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd00192  229 PENCPDELYELMLSCWQLDPEDRP 252
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
553-797 4.19e-34

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: 131.55  E-value: 4.19e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKsVVPP----DEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssv 628
Cdd:cd14014    3 RLVRLLGRGGMGEVYRARDTLLGRPVAIK-VLRPelaeDEEFRERFLREARALARL-SHPNIVRVYDVGEDDGR------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 aVLLIMERLH-RDLYTGLKAG--LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA-- 703
Cdd:cd14014   75 -PYIVMEYVEgGSLADLLRERgpLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGds 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 --MMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsiKLPEAFERCASKDHLWNNVRRGTRPERLPVFDEE 780
Cdd:cd14014  154 glTQTGSVLGTPAYMAPEQARGGpVDPRSDIYSLGVVLYELLTG--RPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPA 231
                        250
                 ....*....|....*..
gi 564380513 781 CWQLMEACWDGDPSKRP 797
Cdd:cd14014  232 LDAIILRALAKDPEERP 248
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
554-749 1.34e-32

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 132.44  E-value: 1.34e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLC-DNWGGHfPCALKSVVPPDEKHWNDLAL---EFHYMRSLpKHERLVdlhgSVIDYNYGGGSSVa 629
Cdd:COG0515   11 ILRLLGRGGMGVVYLArDLRLGR-PVALKVLRPELAADPEARERfrrEARALARL-NHPNIV----RVYDVGEEDGRPY- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 vlLIMERLH-RDLYTGLKAG--LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK----PE 702
Cdd:COG0515   84 --LVMEYVEgESLADLLRRRgpLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARalggAT 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564380513 703 AMMSGSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGsiKLP 749
Cdd:COG0515  162 LTQTGTVVGTPGYMAPEQARGePVDPRSDVYSLGVTLYELLTG--RPP 207
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
553-797 5.01e-32

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: 125.57  E-value: 5.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHfpCALKSVvppdEKHWNDLAL------EFHYMRSlpKHERLVDLHG--SVIDYNYGG 624
Cdd:cd13979    6 RLQEPLGSGGFGSVYKATYKGET--VAVKIV----RRRRKNRASrqsfwaELNAARL--RHENIVRVLAaeTGTDFASLG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 625 gssvavLLIMER-----LHRDLYTGLKAgLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG-- 697
Cdd:cd13979   78 ------LIIMEYcgngtLQQLIYEGSEP-LPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGcs 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 698 -----FCKPEAMMSGsIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsiKLPEAFERCASkdhLWNNVRRGTRP 771
Cdd:cd13979  151 vklgeGNEVGTPRSH-IGGTYTYRAPELLKGErVTPKADIYSFGITLWQMLTR--ELPYAGLRQHV---LYAVVAKDLRP 224
                        250       260       270
                 ....*....|....*....|....*....|
gi 564380513 772 ERLPVFDEE----CWQLMEACWDGDPSKRP 797
Cdd:cd13979  225 DLSGLEDSEfgqrLRSLISRCWSAQPAERP 254
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
558-797 1.46e-29

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: 118.32  E-value: 1.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLC--DNWGGHFpcALKSV--VPPDEKHWNDLALEFHYMRSLpKHERLVDL---------HGSVIDYNYGG 624
Cdd:cd13978    1 LGSGGFGTVSKArhVSWFGMV--AIKCLhsSPNCIEERKALLKEAEKMERA-RHSYVLPLlgvcverrsLGLVMEYMENG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 625 gsSVAVLLIMErlhrdlYTGLKAGLsletRLQIALDVVEGIRFLH--SQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-- 700
Cdd:cd13978   78 --SLKSLLERE------IQDVPWSL----RFRIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHVKISDFGLSKlg 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 701 ------PEAMMSGSIVGTPIHMAPELF---TGKYDNSVDVYAFGILFWYICSGSiklpEAFERCASKDHLWNNVRRGTRP 771
Cdd:cd13978  146 mksisaNRRRGTENLGGTPIYMAPEAFddfNKKPTSKSDVYSFAIVIWAVLTRK----EPFENAINPLLIMQIVSKGDRP 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564380513 772 ErLPVFDEECW--------QLMEACWDGDPSKRP 797
Cdd:cd13978  222 S-LDDIGRLKQienvqeliSLMIRCWDGNPDARP 254
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
553-797 3.19e-28

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: 114.15  E-value: 3.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLcdnwGGHFP----CALKsVVP---PDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYggg 625
Cdd:cd14003    3 ELGKTLGEGSFGKVKL----ARHKLtgekVAIK-IIDkskLKEEIEEKIKREIEIMKLL-NHPNIIKLYEVIETENK--- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 626 ssvaVLLIMERLHR-DLYTGLKAGLSL---ETRL---QIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF 698
Cdd:cd14003   74 ----IYLVMEYASGgELFDYIVNNGRLsedEARRffqQL----ISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 699 CK---PEAMMSgSIVGTPIHMAPELFTG-KYDNS-VDVYAFGILFWYICSGsiKLPeaFERcASKDHLWNNVRRGTrPER 773
Cdd:cd14003  146 SNefrGGSLLK-TFCGTPAYAAPEVLLGrKYDGPkADVWSLGVILYAMLTG--YLP--FDD-DNDSKLFRKILKGK-YPI 218
                        250       260
                 ....*....|....*....|....
gi 564380513 774 LPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd14003  219 PSHLSPDARDLIRRMLVVDPSKRI 242
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
558-798 3.76e-28

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: 114.52  E-value: 3.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLC-DNWGGHFpcALKSVV--PPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVI-DYNYGggssvavlLI 633
Cdd:cd14027    1 LDSGGFGKVSLCfHRTQGLV--VLKTVYtgPNCIEHNEALLEEGKMMNRL-RHSRVVKLLGVILeEGKYS--------LV 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERLHR-DLYTGLKA-GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---------KPE 702
Cdd:cd14027   70 MEYMEKgNLMHVLKKvSVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLAsfkmwskltKEE 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 703 AMM-------SGSIVGTPIHMAPELFTGKYDNSV---DVYAFGILFWYICSGSiklpEAFERCASKDHLWNNVRRGTRPE 772
Cdd:cd14027  150 HNEqrevdgtAKKNAGTLYYMAPEHLNDVNAKPTeksDVYSFAIVLWAIFANK----EPYENAINEDQIIMCIKSGNRPD 225
                        250       260       270
                 ....*....|....*....|....*....|
gi 564380513 773 rLPVFDEEC----WQLMEACWDGDPSKRPL 798
Cdd:cd14027  226 -VDDITEYCpreiIDLMKLCWEANPEARPT 254
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
553-797 4.73e-28

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: 113.98  E-value: 4.73e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDnWGGHFpCALKsVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNygggssvAVLL 632
Cdd:cd05039    9 KLGELIGKGEFGDVMLGD-YRGQK-VAVK-CLKDDSTAAQAFLAEASVMTTL-RHPNLVQLLGVVLEGN-------GLYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERLHRD-----LYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAmmSG 707
Cdd:cd05039   78 VTEYMAKGslvdyLRSRGRAVITRKDQLGFALDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEAS--SN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 SIVGT-PIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPeafeRCASKDhLWNNVRRGTR---PERLPvfdEE 780
Cdd:cd05039  156 QDGGKlPIKwTAPEaLREKKFSTKSDVWSFGILLWEIYSfGRVPYP----RIPLKD-VVPHVEKGYRmeaPEGCP---PE 227
                        250
                 ....*....|....*..
gi 564380513 781 CWQLMEACWDGDPSKRP 797
Cdd:cd05039  228 VYKVMKNCWELDPAKRP 244
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
553-797 4.64e-26

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: 107.99  E-value: 4.64e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLC--DNWGGHFpcALKSV--VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssv 628
Cdd:cd06606    3 KKGELLGKGSFGSVYLAlnLDTGELM--AVKEVelSGDSEEELEALEREIRILSSL-KHPNIVRYLGTERTENT------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 aVLLIMERLH----RDLytgLKAGLSL-ETRLQI-ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-- 700
Cdd:cd06606   74 -LNIFLEYVPggslASL---LKKFGKLpEPVVRKyTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKrl 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 701 ---PEAMMSGSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGsiKLPeaFERCASKDHLWNNVRRGTRPERLPV 776
Cdd:cd06606  150 aeiATGEGTKSLRGTPYWMAPEVIRGeGYGRAADIWSLGCTVIEMATG--KPP--WSELGNPVAALFKIGSSGEPPPIPE 225
                        250       260
                 ....*....|....*....|..
gi 564380513 777 -FDEECWQLMEACWDGDPSKRP 797
Cdd:cd06606  226 hLSEEAKDFLRKCLQRDPKKRP 247
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
553-797 6.38e-26

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: 107.56  E-value: 6.38e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSV--VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaV 630
Cdd:cd05117    3 ELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIdkKKLKSEDEEMLRREIEILKRL-DHPNIVKLYEVFEDDKN-------L 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLH-RDLYTGLKAGLSL---ETRlQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA---KITDLGFCK--- 700
Cdd:cd05117   75 YLVMELCTgGELFDRIVKKGSFserEAA-KIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDspiKIIDFGLAKife 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 701 PEAMMSGsIVGTPIHMAPELFTGK-YDNSVDVYAFGI-------------------LFWYICSGSIKLPEAFercaskdh 760
Cdd:cd05117  154 EGEKLKT-VCGTPYYVAPEVLKGKgYGKKCDIWSLGVilyillcgyppfygeteqeLFEKILKGKYSFDSPE-------- 224
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 564380513 761 lWNNVrrgtrperlpvfDEECWQLMEACWDGDPSKRP 797
Cdd:cd05117  225 -WKNV------------SEEAKDLIKRLLVVDPKKRL 248
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
556-797 1.20e-25

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: 106.78  E-value: 1.20e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSV----VPPDEKhwnDLAL-EFHYMRSLpKHERLVDLHGSVIDYNYgggssvaV 630
Cdd:cd08215    6 RVIGKGSFGSAYLVRRKSDGKLYVLKEIdlsnMSEKER---EEALnEVKLLSKL-KHPNIVKYYESFEENGK-------L 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERL-HRDLYTGLKAGLSLETRL----------QIALdvveGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC 699
Cdd:cd08215   75 CIVMEYAdGGDLAQKIKKQKKKGQPFpeeqildwfvQICL----ALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGIS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 700 K---PEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSgsikLPEAFErcASKDH-LWNNVRRGTRPERL 774
Cdd:cd08215  151 KvleSTTDLAKTVVGTPYYLSPELCENKpYNYKSDIWALGCVLYELCT----LKHPFE--ANNLPaLVYKIVKGQYPPIP 224
                        250       260
                 ....*....|....*....|...
gi 564380513 775 PVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd08215  225 SQYSSELRDLVNSMLQKDPEKRP 247
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
556-744 1.84e-25

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: 106.14  E-value: 1.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKsVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaVLLIME 635
Cdd:cd06614    6 EKIGEGASGEVYKATDRATGKEVAIK-KMRLRKQNKELIINEILIMKEC-KHPNIVDYYDSYLVGDE-------LWVVME 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RLHRDLYTGLKAGLSLE-TRLQIA---LDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSGS 708
Cdd:cd06614   77 YMDGGSLTDIITQNPVRmNESQIAyvcREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAaqlTKEKSKRNS 156
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 564380513 709 IVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSG 744
Cdd:cd06614  157 VVGTPYWMAPEVIKRKdYGPKVDIWSLGIMCIEMAEG 193
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
553-736 2.09e-25

Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. This family is composed of STKs, and some dual-specificity PKs that phosphorylate both threonine and tyrosine residues of target proteins. Most members are kinases involved in mitogen-activated protein kinase (MAPK) signaling cascades, acting as MAPK kinases (MAPKKs), MAPKK kinases (MAPKKKs), or MAPKKK kinases (MAP4Ks). The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPKK, which itself is phosphorylated and activated by a MAPKKK. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAPKKK to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Other STE family members include p21-activated kinases (PAKs) and class III myosins, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain, which can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, as well as autophosphorylate the C-terminal motor domain. They play an important role in maintaining the structural integrity of photoreceptor cell microvilli. The STE family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 106.13  E-value: 2.09e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaVLL 632
Cdd:cd05122    3 EILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEKKESILNEIAILKKC-KHPNIVKYYGSYLKKDE-------LWI 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERLH----RDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PEAMMS 706
Cdd:cd05122   75 VMEFCSggslKDLLKNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAqlSDGKTR 154
                        170       180       190
                 ....*....|....*....|....*....|.
gi 564380513 707 GSIVGTPIHMAPELFTGK-YDNSVDVYAFGI 736
Cdd:cd05122  155 NTFVGTPYWMAPEVIQGKpYGFKADIWSLGI 185
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
558-796 2.85e-25

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: 106.10  E-value: 2.85e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLC-DNWGGHFpCALKSV-------------VPPDEKHW-NDLALEFHYMRSLpKHERLVDLHGsVIDYNY 622
Cdd:cd14008    1 LGRGSFGKVKLAlDTETGQL-YAIKIFnksrlrkrregknDRGKIKNAlDDVRREIAIMKKL-DHPNIVRLYE-VIDDPE 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 623 GGgssvAVLLIME------RLHRDLYTGLKAgLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDL 696
Cdd:cd14008   78 SD----KLYLVLEyceggpVMELDSGDRVPP-LPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 697 G----FCKPEAMMSGSiVGTPIHMAPELFTG---KYD-NSVDVYAFGILFWYICSGsiKLPeaFErCASKDHLWNNVRRG 768
Cdd:cd14008  153 GvsemFEDGNDTLQKT-AGTPAFLAPELCDGdskTYSgKAADIWALGVTLYCLVFG--RLP--FN-GDNILELYEAIQNQ 226
                        250       260
                 ....*....|....*....|....*....
gi 564380513 769 TRPERLPV-FDEECWQLMEACWDGDPSKR 796
Cdd:cd14008  227 NDEFPIPPeLSPELKDLLRRMLEKDPEKR 255
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
558-810 3.79e-25

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: 105.21  E-value: 3.79e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCdNWGGhFPCALKSVVPPDEKhwNDLALEFHYMrSLPKHERLVDLHGSVIdynygggSSVAVLLIME-- 635
Cdd:cd14058    1 VGRGSFGVVCKA-RWRN-QIVAVKIIESESEK--KAFEVEVRQL-SRVDHPNIIKLYGACS-------NQKPVCLVMEya 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 ---RLHRDLY-TGLKAGLSLETRLQIALDVVEGIRFLHS---QGLVHRDIKLKNVLLDKQNRA-KITDLGF-CKPEAMMS 706
Cdd:cd14058   69 eggSLYNVLHgKEPKPIYTAAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGGTVlKICDFGTaCDISTHMT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 707 GSiVGTPIHMAPELFTG-KYDNSVDVYAFGILFWyicsgsiklpEAFERCASKDHL-------WNNVRRGTRPERLPVFD 778
Cdd:cd14058  149 NN-KGSAAWMAPEVFEGsKYSEKCDVFSWGIILW----------EVITRRKPFDHIggpafriMWAVHNGERPPLIKNCP 217
                        250       260       270
                 ....*....|....*....|....*....|..
gi 564380513 779 EECWQLMEACWDGDPSKRPLLGIVQPILRSIM 810
Cdd:cd14058  218 KPIESLMTRCWSKDPEKRPSMKEIVKIMSHLM 249
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
550-810 4.74e-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: 105.93  E-value: 4.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 550 RKPKLGQELGRGQYGVVYLC------DNWGGHfpCALKSVVPP-DEKHWNDLALEFHYMRSLpKHERLVDLHGsvIDYNY 622
Cdd:cd05038    4 RHLKFIKQLGEGHFGSVELCrydplgDNTGEQ--VAVKSLQPSgEEQHMSDFKREIEILRTL-DHEYIVKYKG--VCESP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 623 GGGSsvaVLLIMERLH----RDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF 698
Cdd:cd05038   79 GRRS---LRLIMEYLPsgslRDYLQRHRDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 699 CKPEAMMSGSIVGT-----PIH-MAPE-LFTGKYDNSVDVYAFGI----LFWYICSGSIKLPEAFERCASKD------HL 761
Cdd:cd05038  156 AKVLPEDKEYYYVKepgesPIFwYAPEcLRESRFSSASDVWSFGVtlyeLFTYGDPSQSPPALFLRMIGIAQgqmivtRL 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 564380513 762 WNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRPLLGIVQPILRSIM 810
Cdd:cd05038  236 LELLKSGERLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLILIIDRLR 284
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
558-741 3.15e-24

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: 103.16  E-value: 3.15e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCD--NWGGHFPCALKSVVPPDEKHWND-----LALEFHYMRSLpKHERLVDlhgsVIDYNYGGGSSVav 630
Cdd:cd13994    1 IGKGATSVVRIVTkkNPRSGVLYAVKEYRRRDDESKRKdyvkrLTSEYIISSKL-HHPNIVK----VLDLCQDLHGKW-- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERL-HRDLYTGLKAG--LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKP-- 701
Cdd:cd13994   74 CLVMEYCpGGDLFTLIEKAdsLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGtaevFGMPae 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564380513 702 -EAMMSGSIVGTPIHMAPELFTGK-YD-NSVDVYAFGILFWYI 741
Cdd:cd13994  154 kESPMSAGLCGSEPYMAPEVFTSGsYDgRAVDVWSCGIVLFAL 196
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
554-797 9.25e-24

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: 101.37  E-value: 9.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLcDNWGGHFPCALKSVvppDEKHWN--DLALEFHYMRSLpKHERLVDLHGSVIDYNygggssvAVL 631
Cdd:cd05059    8 FLKELGSGQFGVVHL-GKWRGKIDVAIKMI---KEGSMSedDFIEEAKVMMKL-SHPKLVQLYGVCTKQR-------PIF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERL-HRDLYTGLKAG---LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK----PEA 703
Cdd:cd05059   76 IVTEYMaNGCLLNYLRERrgkFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARyvldDEY 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 MMSGsivGT--PIHMA-PELFT-GKYDNSVDVYAFGILFWYICSGSiKLPeaFERcASKDHLWNNVRRGTRPERLPVFDE 779
Cdd:cd05059  156 TSSV---GTkfPVKWSpPEVFMySKFSSKSDVWSFGVLMWEVFSEG-KMP--YER-FSNSEVVEHISQGYRLYRPHLAPT 228
                        250
                 ....*....|....*...
gi 564380513 780 ECWQLMEACWDGDPSKRP 797
Cdd:cd05059  229 EVYTIMYSCWHEKPEERP 246
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
555-806 1.80e-23

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: 100.39  E-value: 1.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 555 GQELGRGQYGVVYLCDNWGGHFPCALKS---VVPPDEKhwNDLALEFHYMRSLpKHERLVDLHGSVIDYNygggssvAVL 631
Cdd:cd05084    1 GERIGRGNFGEVFSGRLRADNTPVAVKScreTLPPDLK--AKFLQEARILKQY-SHPNIVRLIGVCTQKQ-------PIY 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLHR-DLYTGLK---AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA---- 703
Cdd:cd05084   71 IVMELVQGgDFLTFLRtegPRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEdgvy 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 MMSGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWyicsgsiklpEAFERCASKDHLWNN------VRRGTR---PE 772
Cdd:cd05084  151 AATGGMKQIPVKwTAPEaLNYGRYSSESDVWSFGILLW----------ETFSLGAVPYANLSNqqtreaVEQGVRlpcPE 220
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564380513 773 RLPvfdEECWQLMEACWDGDPSKRPLLGIVQPIL 806
Cdd:cd05084  221 NCP---DEVYRLMEQCWEYDPRKRPSFSTVHQDL 251
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
558-796 5.56e-23

Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases. Members of this family include cAMP-dependent Protein Kinase (PKA), cGMP-dependent Protein Kinase (PKG), Protein Kinase C (PKC), Protein Kinase B (PKB), G protein-coupled Receptor Kinase (GRK), Serum- and Glucocorticoid-induced Kinase (SGK), and 70 kDa ribosomal Protein S6 Kinase (p70S6K or S6K), among others. AGC kinases share an activation mechanism based on the phosphorylation of up to three sites: the activation loop (A-loop), the hydrophobic motif (HM) and the turn motif. Phosphorylation at the A-loop is required of most AGC kinases, which results in a disorder-to-order transition of the A-loop. The ordered conformation results in the access of substrates and ATP to the active site. A subset of AGC kinases with C-terminal extensions containing the HM also requires phosphorylation at this site. Phosphorylation at the HM allows the C-terminal extension to form an ordered structure that packs into the hydrophobic pocket of the catalytic domain, which then reconfigures the kinase into an active bi-lobed state. In addition, growth factor-activated AGC kinases such as PKB, p70S6K, RSK, MSK, PKC, and SGK, require phosphorylation at the turn motif (also called tail or zipper site), located N-terminal to the HM at the C-terminal extension. The AGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and Phosphoinositide 3-Kinase.


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 98.74  E-value: 5.56e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLC---DNwGGHFpcALKSVVPPDEKHWNDLA---LEFHYMRSLpKHERLVDLHGS---------VIDYNY 622
Cdd:cd05123    1 LGKGSFGKVLLVrkkDT-GKLY--AMKVLRKKEIIKRKEVEhtlNERNILERV-NHPFIVKLHYAfqteeklylVLDYVP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 623 GGgssvavllimerlhrDLYTGLKAGLSL-ETRLQI-ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK 700
Cdd:cd05123   77 GG---------------ELFSHLSKEGRFpEERARFyAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 701 P---EAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsiKLPeaFeRCASKDHLWNNVRRGtrPERLPV 776
Cdd:cd05123  142 ElssDGDRTYTFCGTPEYLAPEVLLGKgYGKAVDWWSLGVLLYEMLTG--KPP--F-YAENRKEIYEKILKS--PLKFPE 214
                        250       260
                 ....*....|....*....|.
gi 564380513 777 -FDEECWQLMEACWDGDPSKR 796
Cdd:cd05123  215 yVSPEAKSLISGLLQKDPTKR 235
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
556-796 7.33e-22

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: 96.54  E-value: 7.33e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLC------DNWGGHfpCALKSVVPPD-EKHWNDLALEFHYMRSLpKHERLVDLHGSVIDynyGGGSSV 628
Cdd:cd05079   10 RDLGEGHFGKVELCrydpegDNTGEQ--VAVKSLKPESgGNHIADLKKEIEILRNL-YHENIVKYKGICTE---DGGNGI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 AvlLIMERLH----RDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP--- 701
Cdd:cd05079   84 K--LIMEFLPsgslKEYLPRNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAiet 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 --EAMMSGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYI---CSGSIKLPEAFERCASKDH-------LWNNVRR 767
Cdd:cd05079  162 dkEYYTVKDDLDSPVFwYAPEcLIQSKFYIASDVWSFGVTLYELltyCDSESSPMTLFLKMIGPTHgqmtvtrLVRVLEE 241
                        250       260
                 ....*....|....*....|....*....
gi 564380513 768 GTRPERLPVFDEECWQLMEACWDGDPSKR 796
Cdd:cd05079  242 GKRLPRPPNCPEEVYQLMRKCWEFQPSKR 270
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
554-797 7.47e-22

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: 95.96  E-value: 7.47e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLcDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVidynyGGGSSVAVLL- 632
Cdd:cd05148   10 LERKLGSGYFGEVWE-GLWKNRVRVAIKILKSDDLLKQQDFQKEVQALKRL-RHKHLISLFAVC-----SVGEPVYIITe 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMER--LHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PEAMMSGS 708
Cdd:cd05148   83 LMEKgsLLAFLRSPEGQVLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARliKEDVYLSS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 709 IVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLP-----EAFERCASKdhlwnnvRRGTRPERLPvfdEE 780
Cdd:cd05148  163 DKKIPYKwTAPEaASHGTFSTKSDVWSFGILLYEMFTyGQVPYPgmnnhEVYDQITAG-------YRMPCPAKCP---QE 232
                        250
                 ....*....|....*..
gi 564380513 781 CWQLMEACWDGDPSKRP 797
Cdd:cd05148  233 IYKIMLECWAAEPEDRP 249
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
554-797 1.66e-21

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: 94.94  E-value: 1.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWGGhfPCALKSVvPPDEKHWNDLAlEFHYMRSLpKHERLVDLHGsVIDYNygggssvAVLLI 633
Cdd:cd05083   10 LGEIIGEGEFGAVLQGEYMGQ--KVAVKNI-KCDVTAQAFLE-ETAVMTKL-QHKNLVRLLG-VILHN-------GLYIV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERLHRD-----LYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGS 708
Cdd:cd05083   77 MELMSKGnlvnfLRSRGRALVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSMGVDN 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 709 IVGTPIHMAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPEafercASKDHLWNNVRRGTR---PERLPvfdEECWQ 783
Cdd:cd05083  157 SRLPVKWTAPEaLKNKKFSSKSDVWSYGVLLWEVFSyGRAPYPK-----MSVKEVKEAVEKGYRmepPEGCP---PDVYS 228
                        250
                 ....*....|....
gi 564380513 784 LMEACWDGDPSKRP 797
Cdd:cd05083  229 IMTSCWEAEPGKRP 242
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
553-797 1.80e-21

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: 94.46  E-value: 1.80e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKsVVPpdEKHWNDLALEfHYMR------SLPKHERLVDLHGSVIDynygggs 626
Cdd:cd14007    3 EIGKPLGKGKFGNVYLAREKKSGFIVALK-VIS--KSQLQKSGLE-HQLRreieiqSHLRHPNILRLYGYFED------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 627 SVAVLLIMERLHR-DLYTGLKAGLSL-ETR-----LQIAldvvEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC 699
Cdd:cd14007   72 KKRIYLILEYAPNgELYKELKKQKRFdEKEaakyiYQLA----LALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWS 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 700 K--PEAMMSgSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsiKLPeaFErCASKDHLWNNVRRGtRPERLPV 776
Cdd:cd14007  148 VhaPSNRRK-TFCGTLDYLPPEMVEGKeYDYKVDIWSLGVLCYELLVG--KPP--FE-SKSHQETYKRIQNV-DIKFPSS 220
                        250       260
                 ....*....|....*....|.
gi 564380513 777 FDEECWQLMEACWDGDPSKRP 797
Cdd:cd14007  221 VSPEAKDLISKLLQKDPSKRL 241
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
550-799 2.10e-21

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


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 95.08  E-value: 2.10e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 550 RKPKLGQELGRGQYGVVYLC------DNWGGhfPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVidynYG 623
Cdd:cd14205    4 RHLKFLQQLGKGNFGSVEMCrydplqDNTGE--VVAVKKLQHSTEEHLRDFEREIEILKSL-QHDNIVKYKGVC----YS 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 624 GGSSvAVLLIMERLH----RDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC 699
Cdd:cd14205   77 AGRR-NLRLIMEYLPygslRDYLQKHKERIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 700 K--PEAMMSGSIV---GTPIH-MAPELFT-GKYDNSVDVYAFGI----LFWYIcSGSIKLPEAFERCASKD--------- 759
Cdd:cd14205  156 KvlPQDKEYYKVKepgESPIFwYAPESLTeSKFSVASDVWSFGVvlyeLFTYI-EKSKSPPAEFMRMIGNDkqgqmivfh 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 564380513 760 --HLWNNVRRGTRPERLPvfdEECWQLMEACWDGDPSKRPLL 799
Cdd:cd14205  235 liELLKNNGRLPRPDGCP---DEIYMIMTECWNNNVNQRPSF 273
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
630-797 2.60e-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: 94.05  E-value: 2.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHR-DLYTGL---KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA-- 703
Cdd:cd05041   68 IMIVMELVPGgSLLTFLrkkGARLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEdg 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 --MMSGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLP-----EAFERcaskdhlwnnVRRGTR--- 770
Cdd:cd05041  148 eyTVSDGLKQIPIKwTAPEaLNYGRYTSESDVWSFGILLWEIFSlGATPYPgmsnqQTREQ----------IESGYRmpa 217
                        170       180
                 ....*....|....*....|....*..
gi 564380513 771 PERLPvfdEECWQLMEACWDGDPSKRP 797
Cdd:cd05041  218 PELCP---EAVYRLMLQCWAYDPENRP 241
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
553-737 1.61e-20

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: 92.64  E-value: 1.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPD------EKHWNDlalEFHYMRSLpKHERLVDLHGSVIDYNYgggs 626
Cdd:cd05580    4 EFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKiiklkqVEHVLN---EKRILSEV-RHPFIVNLLGSFQDDRN---- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 627 svaVLLIMERLHR-DLYTGL-KAG-LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA 703
Cdd:cd05580   76 ---LYMVMEYVPGgELFSLLrRSGrFPNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVK 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 564380513 704 MMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGIL 737
Cdd:cd05580  153 DRTYTLCGTPEYLAPEIILSKgHGKAVDWWALGIL 187
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
553-797 3.29e-20

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: 91.16  E-value: 3.29e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLcDNWGGHFPCALKSVVPPDEKHwNDLALEFHYMRSLpKHERLVDLHGSVIDynygggsSVAVLL 632
Cdd:cd05112    7 TFVQEIGSGQFGLVHL-GYWLNKDKVAIKTIREGAMSE-EDFIEEAEVMMKL-SHPKLVQLYGVCLE-------QAPICL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERLHR----DLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG---FCKPEAMM 705
Cdd:cd05112   77 VFEFMEHgclsDYLRTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGmtrFVLDDQYT 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 706 SGSIVGTPIH-MAPELFT-GKYDNSVDVYAFGILFWYICSGSiKLPeaFERcASKDHLWNNVRRGTRPERLPVFDEECWQ 783
Cdd:cd05112  157 SSTGTKFPVKwSSPEVFSfSRYSSKSDVWSFGVLMWEVFSEG-KIP--YEN-RSNSEVVEDINAGFRLYKPRLASTHVYE 232
                        250
                 ....*....|....
gi 564380513 784 LMEACWDGDPSKRP 797
Cdd:cd05112  233 IMNHCWKERPEDRP 246
Pkinase pfam00069
Protein kinase domain;
554-797 4.64e-20

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 89.61  E-value: 4.64e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513  554 LGQELGRGQYGVVYLCDN--WGGHFpcALKSVVPPDEKHWNDLAL--EFHYMRSLpKHERLVDLHGSVIDYNYgggssva 629
Cdd:pfam00069   3 VLRKLGSGSFGTVYKAKHrdTGKIV--AIKKIKKEKIKKKKDKNIlrEIKILKKL-NHPNIVRLYDAFEDKDN------- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513  630 VLLIMERLHrdlytglkaGLSLETRLQialdvvegirflHSQGLVHRDIK--LKNVLLdkqnrakitdlGFCKPEAMMSg 707
Cdd:pfam00069  73 LYLVLEYVE---------GGSLFDLLS------------EKGAFSEREAKfiMKQILE-----------GLESGSSLTT- 119
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513  708 sIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsiKLPeaFERCASKDHLWNNVRRGTRPERLP-VFDEECWQLM 785
Cdd:pfam00069 120 -FVGTPWYMAPEVLGGNpYGPKVDVWSLGCILYELLTG--KPP--FPGINGNEIYELIIDQPYAFPELPsNLSEEAKDLL 194
                         250
                  ....*....|..
gi 564380513  786 EACWDGDPSKRP 797
Cdd:pfam00069 195 KKLLKKDPSKRL 206
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
550-797 6.43e-20

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: 90.04  E-value: 6.43e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 550 RKPKLGQELGRGQYGVVYLCDNWGGHfpCALKSVvpPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNyGGGSSVA 629
Cdd:cd05082    6 KELKLLQTIGKGEFGDVMLGDYRGNK--VAVKCI--KNDATAQAFLAEASVMTQL-RHSNLVQLLGVIVEEK-GGLYIVT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpEAMMSGSI 709
Cdd:cd05082   80 EYMAKGSLVDYLRSRGRSVLGGDCLLKFSLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTK-EASSTQDT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 710 VGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPeafeRCASKDhLWNNVRRGTR---PERLPvfdEECWQ 783
Cdd:cd05082  159 GKLPVKwTAPEaLREKKFSTKSDVWSFGILLWEIYSfGRVPYP----RIPLKD-VVPRVEKGYKmdaPDGCP---PAVYD 230
                        250
                 ....*....|....
gi 564380513 784 LMEACWDGDPSKRP 797
Cdd:cd05082  231 VMKNCWHLDAAMRP 244
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
606-797 7.60e-20

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: 90.41  E-value: 7.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 606 KHERLVDLHGsvidYNYGGGSSVAVLLIMErlHRDLYTGLKAG-----LSLETRLQIALDVVEGIRFLHSQG---LVHRD 677
Cdd:cd14066   48 RHPNLVRLLG----YCLESDEKLLVYEYMP--NGSLEDRLHCHkgsppLPWPQRLKIAKGIARGLEYLHEECpppIIHGD 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 678 IKLKNVLLDKQNRAKITDLGFCK-----PEAMMSGSIVGTPIHMAPE-LFTGKYDNSVDVYAFGILFWYICSGSIKLPEA 751
Cdd:cd14066  122 IKSSNILLDEDFEPKLTDFGLARlippsESVSKTSAVKGTIGYLAPEyIRTGRVSTKSDVYSFGVVLLELLTGKPAVDEN 201
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 752 FERCASKDHLwNNVRRGTRPERLPVFD--------------EECWQLMEACWDGDPSKRP 797
Cdd:cd14066  202 RENASRKDLV-EWVESKGKEELEDILDkrlvdddgveeeevEALLRLALLCTRSDPSLRP 260
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
557-742 8.47e-20

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: 90.09  E-value: 8.47e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIdyNYGGGSSVaVLLIMER 636
Cdd:cd13985    7 QLGEGGFSYVYLAHDVNTGRRYALKRMYFNDEEQLRVAIKEIEIMKRLCGHPNIVQYYDSAI--LSSEGRKE-VLLLMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 637 LHRDLY----TGLKAGLSLETRLQIALDVVEGIRFLHSQG--LVHRDIKLKNVLLDKQNRAKITDLGFCKPEA--MMSGS 708
Cdd:cd13985   84 CPGSLVdileKSPPSPLSEEEVLRIFYQICQAVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGSATTEHypLERAE 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564380513 709 IVG----------TPIHMAPE---LFTGK-YDNSVDVYAFGILFWYIC 742
Cdd:cd13985  164 EVNiieeeiqkntTPMYRAPEmidLYSKKpIGEKADIWALGCLLYKLC 211
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
658-801 1.12e-19

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


Pssm-ID: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 90.91  E-value: 1.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAM---MSGSIVGTPIHMAPELFTG-KYDNSVDVYA 733
Cdd:cd05592  102 GAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYgenKASTFCGTPDYIAPEILKGqKYNQSVDWWS 181
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564380513 734 FGILFWYICSGSiklpEAFERCaSKDHLWNNVRRgTRPERLPVFDEECWQLMEACWDGDPSKRplLGI 801
Cdd:cd05592  182 FGVLLYEMLIGQ----SPFHGE-DEDELFWSICN-DTPHYPRWLTKEAASCLSLLLERNPEKR--LGV 241
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
558-745 1.63e-19

Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mammals have two cGK isoforms from different genes, cGKI and cGKII. cGKI exists as two splice variants, cGKI-alpha and cGKI-beta. cGK consists of an N-terminal regulatory domain containing a dimerization and an autoinhibitory pseudosubstrate region, two cGMP-binding domains, and a C-terminal catalytic domain. Binding of cGMP to both binding sites releases the inhibition of the catalytic center by the pseudosubstrate region, allowing autophosphorylation and activation of the kinase. cGKI is a soluble protein expressed in all smooth muscles, platelets, cerebellum, and kidney. It is also expressed at lower concentrations in other tissues. cGKII is a membrane-bound protein that is most abundantly expressed in the intestine. It is also present in the brain nuclei, adrenal cortex, kidney, lung, and prostate. cGKI is involved in the regulation of smooth muscle tone, smooth cell proliferation, and platelet activation. cGKII plays a role in the regulation of secretion, such as renin secretion by the kidney and aldosterone secretion by the adrenal. It also regulates bone growth and the circadian rhythm. The cGK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 89.21  E-value: 1.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVvppDEKHWNDLALEFHYMR-----SLPKHERLVDLHGSVIDYNYgggssvaVLL 632
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCV---KKRHIVQTRQQEHIFSekeilEECNSPFIVKLYRTFKDKKY-------LYM 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMER-LHRDLYTGL-KAGL--SLETRLQIALdVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpeAMMSG- 707
Cdd:cd05572   71 LMEYcLGGELWTILrDRGLfdEYTARFYTAC-VVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAK--KLGSGr 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564380513 708 ---SIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGS 745
Cdd:cd05572  148 ktwTFCGTPEYVAPEIILNKgYDFSVDYWSLGILLYELLTGR 189
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
550-797 1.95e-19

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: 88.76  E-value: 1.95e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 550 RKPKLGQELGRGQYGVVYLCDNWGGHFPCALKsVVPPD----EKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYggg 625
Cdd:cd14099    1 KRYRRGKFLGKGGFAKCYEVTDMSTGKVYAGK-VVPKSsltkPKQREKLKSEIKIHRSL-KHPNIVKFHDCFEDEEN--- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 626 ssvaVLLIMERLHR-DLYTGLKAGLSL---ETRlQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF--- 698
Cdd:cd14099   76 ----VYILLELCSNgSLMELLKRRKALtepEVR-YFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLaar 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 699 CKPEAMMSGSIVGTPIHMAPELFTGK--YDNSVDVYAFGILFWYICSGsiKLPeaFErCASKDHLWNNVRRG--TRPERL 774
Cdd:cd14099  151 LEYDGERKKTLCGTPNYIAPEVLEKKkgHSFEVDIWSLGVILYTLLVG--KPP--FE-TSDVKETYKRIKKNeySFPSHL 225
                        250       260
                 ....*....|....*....|...
gi 564380513 775 PVFDeECWQLMEACWDGDPSKRP 797
Cdd:cd14099  226 SISD-EAKDLIRSMLQPDPTKRP 247
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
658-805 2.06e-19

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: 90.00  E-value: 2.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAM---MSGSIVGTPIHMAPELFTG-KYDNSVDVYA 733
Cdd:cd05620  102 AAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFgdnRASTFCGTPDYIAPEILQGlKYTFSVDWWS 181
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380513 734 FGILFWYICSGSIKLpeafeRCASKDHLWNNVRRGTrPERLPVFDEECWQLMEACWDGDPSKRplLGIVQPI 805
Cdd:cd05620  182 FGVLLYEMLIGQSPF-----HGDDEDELFESIRVDT-PHYPRWITKESKDILEKLFERDPTRR--LGVVGNI 245
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
553-755 3.07e-19

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: 88.16  E-value: 3.07e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSV-VPPDEKHW-NDLALEFhYMRSLPKHERLVDLHGSVIDYNYgggssvaV 630
Cdd:cd14069    4 DLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVdMKRAPGDCpENIKKEV-CIQKMLSHKNVVRFYGHRREGEF-------Q 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMErlhrdlytgLKAGLSLETRlqIALDV--------------VEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDL 696
Cdd:cd14069   76 YLFLE---------YASGGELFDK--IEPDVgmpedvaqfyfqqlMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDF 144
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564380513 697 GFC-----KPEAMMSGSIVGTPIHMAPELFTGK-YDNS-VDVYAFGILFWYICSGSIKLPEAFERC 755
Cdd:cd14069  145 GLAtvfryKGKERLLNKMCGTLPYVAPELLAKKkYRAEpVDVWSCGIVLFAMLAGELPWDQPSDSC 210
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
550-809 5.06e-19

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: 88.03  E-value: 5.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 550 RKPKLGQELGRGQYGVV----YLCDNWGGHFPCALKSVV----PPDEKHWNDlalEFHYMRSLpKHERLVDLHGSVIDyn 621
Cdd:cd05080    4 RYLKKIRDLGEGHFGKVslycYDPTNDGTGEMVAVKALKadcgPQHRSGWKQ---EIDILKTL-YHENIVKYKGCCSE-- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 622 yGGGSSVavLLIMERLH----RDLYTglKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG 697
Cdd:cd05080   78 -QGGKSL--QLIMEYVPlgslRDYLP--KHSIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 698 FCK--PEAMMSGSIV---GTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYI---CSGSIKLPEAFERCASKDHLWNNVRR 767
Cdd:cd05080  153 LAKavPEGHEYYRVRedgDSPVFwYAPEcLKEYKFYYASDVWSFGVTLYELlthCDSSQSPPTKFLEMIGIAQGQMTVVR 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 564380513 768 GT----RPERLPVFDE---ECWQLMEACWDGDPSKRPLLGIVQPILRSI 809
Cdd:cd05080  233 LIelleRGERLPCPDKcpqEVYHLMKNCWETEASFRPTFENLIPILKTV 281
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
640-797 5.54e-19

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: 89.29  E-value: 5.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 640 DLYtglKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-----PEAMMSGSiVGTPI 714
Cdd:cd14207  171 DFY---KRPLTMEDLISYSFQVARGMEFLSSRKCIHRDLAARNILLSENNVVKICDFGLARdiyknPDYVRKGD-ARLPL 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 715 H-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPEAfercASKDHLWNNVRRGTRpERLPVF-DEECWQLMEACWD 790
Cdd:cd14207  247 KwMAPEsIFDKIYSTKSDVWSYGVLLWEIFSlGASPYPGV----QIDEDFCSKLKEGIR-MRAPEFaTSEIYQIMLDCWQ 321

                 ....*..
gi 564380513 791 GDPSKRP 797
Cdd:cd14207  322 GDPNERP 328
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
558-797 5.82e-19

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: 87.45  E-value: 5.82e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPD----EKHwnDLALEFHYMRSLpKHERLVDLHGSVIDYN-------YGGGS 626
Cdd:cd08530    8 LGKGSYGSVYKVKRLSDNQVYALKEVNLGSlsqkERE--DSVNEIRLLASV-NHPNIIRYKEAFLDGNrlcivmeYAPFG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 627 SVAVLLIMERLHRDLYTGlkaglslETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-PEAMM 705
Cdd:cd08530   85 DLSKLISKRKKKRRLFPE-------DDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKvLKKNL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 706 SGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsiKLPeaFERCASKDhLWNNVRRGTRPERLPVFDEECWQL 784
Cdd:cd08530  158 AKTQIGTPLYAAPEVWKGRpYDYKSDIWSLGCLLYEMATF--RPP--FEARTMQE-LRYKVCRGKFPPIPPVYSQDLQQI 232
                        250
                 ....*....|...
gi 564380513 785 MEACWDGDPSKRP 797
Cdd:cd08530  233 IRSLLQVNPKKRP 245
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
555-809 5.88e-19

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: 87.94  E-value: 5.88e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 555 GQELGRGQYGVVYLCDNWGGHfpCALKSVVPPDEKHWNDLALEF----HYMRSLpKHERLVDLHGsvidYNYGGGSSVAV 630
Cdd:cd14158   20 GNKLGEGGFGVVFKGYINDKN--VAVKKLAAMVDISTEDLTKQFeqeiQVMAKC-QHENLVELLG----YSCDGPQLCLV 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIM------ERLHRDLYTglkAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA- 703
Cdd:cd14158   93 YTYMpngsllDRLACLNDT---PPLSWHMRCKIAQGTANGINYLHENNHIHRDIKSANILLDETFVPKISDFGLARASEk 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 ----MMSGSIVGTPIHMAPELFTGKYDNSVDVYAFGILFWYICSGsikLPEAFERcaSKDHLWNNVRRGTRPERLPVFD- 778
Cdd:cd14158  170 fsqtIMTERIVGTTAYMAPEALRGEITPKSDIFSFGVVLLEIITG---LPPVDEN--RDPQLLLDIKEEIEDEEKTIEDy 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564380513 779 -------------EECWQLMEACWDGDPSKRPLLGIVQPILRSI 809
Cdd:cd14158  245 vdkkmgdwdstsiEAMYSVASQCLNDKKNRRPDIAKVQQLLQEL 288
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
558-806 7.26e-19

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: 87.10  E-value: 7.26e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVppdekhwndlalefhyMRSLPKHERLVDL----------HGSVIDYNYGGGSS 627
Cdd:cd08220    8 VGRGAYGTVYLCRRKDDNKLVIIKQIP----------------VEQMTKEERQAALnevkvlsmlhHPNIIEYYESFLED 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 VAVLLIME-----RLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDK-QNRAKITDLGFCKP 701
Cdd:cd08220   72 KALMIVMEyapggTLFEYIQQRKGSLLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKkRTVVKIGDFGISKI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 EAMMSG--SIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSgsikLPEAFErCASKDHLWNNVRRGTRPERLPVFD 778
Cdd:cd08220  152 LSSKSKayTVVGTPCYISPELCEGKpYNQKSDIWALGCVLYELAS----LKRAFE-AANLPALVLKIMRGTFAPISDRYS 226
                        250       260       270
                 ....*....|....*....|....*....|
gi 564380513 779 EECWQLMEACWDGDPSKRPLLG--IVQPIL 806
Cdd:cd08220  227 EELRHLILSMLHLDPNKRPTLSeiMAQPII 256
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
558-759 8.57e-19

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: 86.99  E-value: 8.57e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKsVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDynygggSSVAVLLIMER- 636
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALK-FVPKPSTKLKDFLREYNISLELSVHPHIIKTYDVAFE------TEDYYVFAQEYa 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 637 LHRDLYTGLK--AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLL-DKQ-NRAKITDLGFCKPEAMMSGSIVGT 712
Cdd:cd13987   74 PYGDLFSIIPpqVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLfDKDcRRVKLCDFGLTRRVGSTVKRVSGT 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564380513 713 PIHMAPELFTGK------YDNSVDVYAFGILFWYICSGsiKLPeaFERCASKD 759
Cdd:cd13987  154 IPYTAPEVCEAKknegfvVDPSIDVWAFGVLLFCCLTG--NFP--WEKADSDD 202
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
558-797 9.18e-19

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: 86.52  E-value: 9.18e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLC-DNWGGHFpCALKSVVPPDEKHWNDLAlEFHYMRSL---PKHERLVDLHGSVIDynyggGSSVAVLLI 633
Cdd:cd05118    7 IGEGAFGTVWLArDKVTGEK-VAIKKIKNDFRHPKAALR-EIKLLKHLndvEGHPNIVKLLDVFEH-----RGGNHLCLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERLHRDLYTGLKA---GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA-KITDLGFCKP--EAMMSG 707
Cdd:cd05118   80 FELMGMNLYELIKDyprGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLELGQlKLADFGLARSftSPPYTP 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 SIVgTPIHMAPELFTGK--YDNSVDVYAFGILFWYICSGSIKLPEAFErcasKDHLWNNVRR-GTrperlpvfdEECWQL 784
Cdd:cd05118  160 YVA-TRWYRAPEVLLGAkpYGSSIDIWSLGCILAELLTGRPLFPGDSE----VDQLAKIVRLlGT---------PEALDL 225
                        250
                 ....*....|...
gi 564380513 785 MEACWDGDPSKRP 797
Cdd:cd05118  226 LSKMLKYDPAKRI 238
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
558-797 1.03e-18

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: 86.57  E-value: 1.03e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLcDNWGGHFPCALKSVVP----PDekhwnDLALEFHYMRSLpKHERLVDL------------------HG 615
Cdd:cd05034    3 LGAGQFGEVWM-GVWNGTTKVAVKTLKPgtmsPE-----AFLQEAQIMKKL-RHDKLVQLyavcsdeepiyivtelmsKG 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 616 SVIDYnygggssvavllimerlhrdLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITD 695
Cdd:cd05034   76 SLLDY--------------------LRTGEGRALRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVAD 135
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 696 LGFCKpeaMMSGSI----VGT--PIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPEAFERcaskdHLWNNVR 766
Cdd:cd05034  136 FGLAR---LIEDDEytarEGAkfPIKwTAPEaALYGRFTIKSDVWSFGILLYEIVTyGRVPYPGMTNR-----EVLEQVE 207
                        250       260       270
                 ....*....|....*....|....*....|.
gi 564380513 767 RGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05034  208 RGYRMPKPPGCPDELYDIMLQCWKKEPEERP 238
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
558-736 1.53e-18

Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST1, MST2, and related proteins including Drosophila Hippo and Dictyostelium discoideum Krs1 (kinase responsive to stress 1). MST1/2 and Hippo are involved in a conserved pathway that governs cell contact inhibition, organ size control, and tumor development. MST1 activates the mitogen-activated protein kinases (MAPKs) p38 and c-Jun N-terminal kinase (JNK) through MKK7 and MEKK1 by acting as a MAPK kinase kinase kinase. Activation of JNK by MST1 leads to caspase activation and apoptosis. MST1 has also been implicated in cell proliferation and differentiation. Krs1 may regulate cell growth arrest and apoptosis in response to cellular stress. The MST1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 86.17  E-value: 1.53e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKsVVPPDEKHwNDLALEFHYMRSLpKHERLVDLHGS---------VIDYnYGGGSsv 628
Cdd:cd06612   11 LGEGSYGSVYKAIHKETGQVVAIK-VVPVEEDL-QEIIKEISILKQC-DSPYIVKYYGSyfkntdlwiVMEY-CGAGS-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 aVLLIMERLHRDLytglkaglsleTRLQIAL---DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC-KPEAM 704
Cdd:cd06612   85 -VSDIMKITNKTL-----------TEEEIAAilyQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSgQLTDT 152
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 564380513 705 M--SGSIVGTPIHMAPELFTG-KYDNSVDVYAFGI 736
Cdd:cd06612  153 MakRNTVIGTPFWMAPEVIQEiGYNNKADIWSLGI 187
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
554-797 1.70e-18

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: 87.16  E-value: 1.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWG-GHFPCA-------LKSVVPPDEKHwnDLALEFHYMRSLPKHERLVDLHGSVidyNYGGg 625
Cdd:cd05055   39 FGKTLGAGAFGKVVEATAYGlSKSDAVmkvavkmLKPTAHSSERE--ALMSELKIMSHLGNHENIVNLLGAC---TIGG- 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 626 ssvAVLLIMER-LHRDLYTGLK----AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK 700
Cdd:cd05055  113 ---PILVITEYcCYGDLLNFLRrkreSFLTLEDLLSFSYQVAKGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLAR 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 701 PEAMMSGSIVG----TPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPEAfercASKDHLWNNVRRGTR--- 770
Cdd:cd05055  190 DIMNDSNYVVKgnarLPVKwMAPEsIFNCVYTFESDVWSYGILLWEIFSlGSNPYPGM----PVDSKFYKLIKEGYRmaq 265
                        250       260
                 ....*....|....*....|....*..
gi 564380513 771 PERLPvfdEECWQLMEACWDGDPSKRP 797
Cdd:cd05055  266 PEHAP---AEIYDIMKTCWDADPLKRP 289
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
553-797 2.11e-18

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: 85.74  E-value: 2.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLC-DN-------WgghfpCALK-SVVPPDEKhwNDLALEFHYMRSLpKHERLVDLHGSVIDynyg 623
Cdd:cd13983    4 KFNEVLGRGSFKTVYRAfDTeegievaW-----NEIKlRKLPKAER--QRFKQEIEILKSL-KHPNIIKFYDSWES---- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 624 gGSSVAVLLIMErlhrdLYTG--LKAGLSLETRLQI------ALDVVEGIRFLHSQG--LVHRDIKLKNVLLD-KQNRAK 692
Cdd:cd13983   72 -KSKKEVIFITE-----LMTSgtLKQYLKRFKRLKLkvikswCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 693 ITDLGFCKpeaMMSG----SIVGTPIHMAPELFTGKYDNSVDVYAFGILFWYICSGsiKLPeaFERCASKDHLWNNVRRG 768
Cdd:cd13983  146 IGDLGLAT---LLRQsfakSVIGTPEFMAPEMYEEHYDEKVDIYAFGMCLLEMATG--EYP--YSECTNAAQIYKKVTSG 218
                        250       260       270
                 ....*....|....*....|....*....|
gi 564380513 769 TRPERLP-VFDEECWQLMEACWdGDPSKRP 797
Cdd:cd13983  219 IKPESLSkVKDPELKDFIEKCL-KPPDERP 247
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
554-797 2.43e-18

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: 86.32  E-value: 2.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWG------GHFPCALKSV-VPPDEKHWNDLALEFHYMRSLPKHERLVDLHGS---------V 617
Cdd:cd05053   16 LGKPLGEGAFGQVVKAEAVGldnkpnEVVTVAVKMLkDDATEKDLSDLVSEMEMMKMIGKHKNIINLLGActqdgplyvV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 618 IDYNYGGGssvavLLIMERLHRDLYTGLKAGLSLETRLQI--------ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN 689
Cdd:cd05053   96 VEYASKGN-----LREFLRARRPPGEEASPDDPRVPEEQLtqkdlvsfAYQVARGMEYLASKKCIHRDLAARNVLVTEDN 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 690 RAKITDLGFCKP-------EAMMSGSIvgtPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS--GS----IKLPEAFEr 754
Cdd:cd05053  171 VMKIADFGLARDihhidyyRKTTNGRL---PVKwMAPEaLFDRVYTHQSDVWSFGVLLWEIFTlgGSpypgIPVEELFK- 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 564380513 755 caskdhlwnNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05053  247 ---------LLKEGHRMEKPQNCTQELYMLMRDCWHEVPSQRP 280
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
646-797 2.76e-18

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: 86.39  E-value: 2.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 646 KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-----PEAMMSGSiVGTPIH-MAPE 719
Cdd:cd05054  132 KEPLTLEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARdiykdPDYVRKGD-ARLPLKwMAPE 210
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 720 -LFTGKYDNSVDVYAFGILFWYICS--GS----IKLPEAFercaskdhlWNNVRRGTR---PERLPvfdEECWQLMEACW 789
Cdd:cd05054  211 sIFDKVYTTQSDVWSFGVLLWEIFSlgASpypgVQMDEEF---------CRRLKEGTRmraPEYTT---PEIYQIMLDCW 278

                 ....*...
gi 564380513 790 DGDPSKRP 797
Cdd:cd05054  279 HGEPKERP 286
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
553-797 3.18e-18

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: 85.48  E-value: 3.18e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSV-VPPDE----KHWNDLALEFHYMRSLpKHERLVDLHGSVIDYN------ 621
Cdd:cd06625    3 KQGKLLGQGAFGQVYLCYDADTGRELAVKQVeIDPINteasKEVKALECEIQLLKNL-QHERIVQYYGCLQDEKslsifm 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 622 -YGGGSSVavllimeRLHRDLYTGLKAGLSLETRLQIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG--- 697
Cdd:cd06625   82 eYMPGGSV-------KDEIKAYGALTENVTRKYTRQI----LEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFGask 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 698 ----FCKPEAMmsGSIVGTPIHMAPELFTGK-YDNSVDVYAFGilfwyiCSG----SIKLPEA-FERCASkdhLWNNVRR 767
Cdd:cd06625  151 rlqtICSSTGM--KSVTGTPYWMSPEVINGEgYGRKADIWSVG------CTVvemlTTKPPWAeFEPMAA---IFKIATQ 219
                        250       260       270
                 ....*....|....*....|....*....|
gi 564380513 768 GTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd06625  220 PTNPQLPPHVSEDARDFLSLIFVRNKKQRP 249
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
658-737 3.74e-18

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: 86.11  E-value: 3.74e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpEAMMSGS----IVGTPIHMAPELFTGK-YDNSVDVY 732
Cdd:cd05570  102 AAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMCK-EGIWGGNttstFCGTPDYIAPEILREQdYGFSVDWW 180

                 ....*
gi 564380513 733 AFGIL 737
Cdd:cd05570  181 ALGVL 185
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
647-808 3.77e-18

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: 85.36  E-value: 3.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 647 AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVL---LDKQN--RAKITDLGFCKPEAMMSGSIV-GTPIHMAPEL 720
Cdd:cd14000  107 ASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLvwtLYPNSaiIIKIADYGISRQCCRMGAKGSeGTPGFRAPEI 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 721 FTGK--YDNSVDVYAFGILFWYICSGS------IKLPEAFErcaskdhlwnnVRRGTRP---ERLPVFDEECWQLMEACW 789
Cdd:cd14000  187 ARGNviYNEKVDVFSFGMLLYEILSGGapmvghLKFPNEFD-----------IHGGLRPplkQYECAPWPEVEVLMKKCW 255
                        170
                 ....*....|....*....
gi 564380513 790 DGDPSKRPLLGIVQPILRS 808
Cdd:cd14000  256 KENPQQRPTAVTVVSILNS 274
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
658-744 6.30e-18

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: 85.75  E-value: 6.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpEAMM----SGSIVGTPIHMAPELFTG-KYDNSVDVY 732
Cdd:cd05619  112 AAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCK-ENMLgdakTSTFCGTPDYIAPEILLGqKYNTSVDWW 190
                         90
                 ....*....|..
gi 564380513 733 AFGILFWYICSG 744
Cdd:cd05619  191 SFGVLLYEMLIG 202
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
555-808 6.33e-18

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: 84.29  E-value: 6.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 555 GQELGRGQYGVVY---LCDNwgghFPCALKSVvppDEKHWNDLALEFHYMRSLPK---HERLVDLHGSVIDYNygggssv 628
Cdd:cd05085    1 GELLGKGNFGEVYkgtLKDK----TPVAVKTC---KEDLPQELKIKFLSEARILKqydHPNIVKLIGVCTQRQ------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 AVLLIMERLHR-DLYTGL---KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPE-- 702
Cdd:cd05085   67 PIYIVMELVPGgDFLSFLrkkKDELKTKQLVKFSLDAAAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEdd 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 703 -AMMSGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPEAFERCASKdhlwnNVRRGTR---PERLP 775
Cdd:cd05085  147 gVYSSSGLKQIPIKwTAPEaLNYGRYSSESDVWSFGILLWETFSlGVCPYPGMTNQQARE-----QVEKGYRmsaPQRCP 221
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564380513 776 vfdEECWQLMEACWDGDPSKRPLLGIVQPILRS 808
Cdd:cd05085  222 ---EDIYKIMQRCWDYNPENRPKFSELQKELAA 251
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
556-803 6.65e-18

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: 84.16  E-value: 6.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLcDNWGGHFPCALKsVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGS---------VIDYNYGGgs 626
Cdd:cd05113   10 KELGTGQFGVVKY-GKWRGQYDVAIK-MIKEGSMSEDEFIEEAKVMMNL-SHEKLVQLYGVctkqrpifiITEYMANG-- 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 627 svaVLLIMERLHRDlytglkaGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK----PE 702
Cdd:cd05113   85 ---CLLNYLREMRK-------RFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRyvldDE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 703 AMMSgsiVGT--PIHMAPE--LFTGKYDNSVDVYAFGILFWYICSGSiKLP-EAFERCASKDHlwnnVRRGTRPERLPVF 777
Cdd:cd05113  155 YTSS---VGSkfPVRWSPPevLMYSKFSSKSDVWAFGVLMWEVYSLG-KMPyERFTNSETVEH----VSQGLRLYRPHLA 226
                        250       260       270
                 ....*....|....*....|....*....|
gi 564380513 778 DEECWQLMEACWDGDPSKRP----LLGIVQ 803
Cdd:cd05113  227 SEKVYTIMYSCWHEKADERPtfkiLLSNIL 256
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
551-802 6.73e-18

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: 84.70  E-value: 6.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQELGRGQYGVVYL-----CDNWGGHFPCALKSVVPPDEKHWNdlaLEF----HYMRSLPKHErLVDLHGSVIDYN 621
Cdd:cd05032    7 KITLIRELGQGSFGMVYEglakgVVKGEPETRVAIKTVNENASMRER---IEFlneaSVMKEFNCHH-VVRLLGVVSTGQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 622 ygggssvAVLLIMERLHR-DLYTGLKAG------------LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQ 688
Cdd:cd05032   83 -------PTLVVMELMAKgDLKSYLRSRrpeaennpglgpPTLQKFIQMAAEIADGMAYLAAKKFVHRDLAARNCMVAED 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 689 NRAKITDLGFC---------KPE--AMMsgsivgtPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSikLP----- 749
Cdd:cd05032  156 LTVKIGDFGMTrdiyetdyyRKGgkGLL-------PVRwMAPEsLKDGVFTTKSDVWSFGVVLWEMATlAE--QPyqgls 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564380513 750 --EAFERCASKDHLwnnvrrgTRPERLPVFdeeCWQLMEACWDGDPSKRPL-LGIV 802
Cdd:cd05032  227 neEVLKFVIDGGHL-------DLPENCPDK---LLELMRMCWQYNPKMRPTfLEIV 272
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
553-735 8.16e-18

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


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 84.31  E-value: 8.16e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSV-VPPD----EKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYN------ 621
Cdd:cd06653    5 RLGKLLGRGAFGEVYLCYDADTGRELAVKQVpFDPDsqetSKEVNALECEIQLLKNL-RHDRIVQYYGCLRDPEekklsi 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 622 ---YGGGSSVAVLLimerlhrDLYTGLKAGLSLETRLQIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF 698
Cdd:cd06653   84 fveYMPGGSVKDQL-------KAYGALTENVTRRYTRQI----LQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGA 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564380513 699 CK--PEAMMSG----SIVGTPIHMAPELFTGK-YDNSVDVYAFG 735
Cdd:cd06653  153 SKriQTICMSGtgikSVTGTPYWMSPEVISGEgYGRKADVWSVA 196
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
640-797 8.41e-18

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


Pssm-ID: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 85.80  E-value: 8.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 640 DLYtglKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-----PEAMMSGSiVGTPI 714
Cdd:cd05103  170 DLY---KDFLTLEDLICYSFQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARdiykdPDYVRKGD-ARLPL 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 715 H-MAPE-LFTGKYDNSVDVYAFGILFWYICS------GSIKLPEAFERcaskdhlwnNVRRGTRpERLPVFDE-ECWQLM 785
Cdd:cd05103  246 KwMAPEtIFDRVYTIQSDVWSFGVLLWEIFSlgaspyPGVKIDEEFCR---------RLKEGTR-MRAPDYTTpEMYQTM 315
                        170
                 ....*....|..
gi 564380513 786 EACWDGDPSKRP 797
Cdd:cd05103  316 LDCWHGEPSQRP 327
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
554-797 1.69e-17

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 83.23  E-value: 1.69e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWGGHFPCALKSV--VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNygggssvAVL 631
Cdd:cd08529    4 ILNKLGKGSFGVVYKVVRKVDGRVYALKQIdiSRMSRKMREEAIDEARVLSKL-NSPYVIKYYDSFVDKG-------KLN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIME-----RLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---PEA 703
Cdd:cd08529   76 IVMEyaengDLHSLIKSQRGRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKilsDTT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 MMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsiKLPeaFErCASKDHLWNNVRRGTRPERLPVFDEECW 782
Cdd:cd08529  156 NFAQTIVGTPYYLSPELCEDKpYNEKSDVWALGCVLYELCTG--KHP--FE-AQNQGALILKIVRGKYPPISASYSQDLS 230
                        250
                 ....*....|....*
gi 564380513 783 QLMEACWDGDPSKRP 797
Cdd:cd08529  231 QLIDSCLTKDYRQRP 245
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
556-797 1.89e-17

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


Pssm-ID: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 83.31  E-value: 1.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALK--SVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDynygggssvAVLLI 633
Cdd:cd14025    2 EKVGSGGFGQVYKVRHKHWKTWLAIKcpPSLHVDDSERMELLEEAKKMEMA-KFRHILPVYGICSE---------PVGLV 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERLHRDLYTGLKAGLSL--ETRLQIALDVVEGIRFLHSQG--LVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSG-- 707
Cdd:cd14025   72 MEYMETGSLEKLLASEPLpwELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAKWNGLSHShd 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 ----SIVGTPIHMAPELFTGK---YDNSVDVYAFGILFWYICSGsiKLPEAFERCASkdHLWNNVRRGTRPERLPVFDE- 779
Cdd:cd14025  152 lsrdGLRGTIAYLPPERFKEKnrcPDTKHDVYSFAIVIWGILTQ--KKPFAGENNIL--HIMVKVVKGHRPSLSPIPRQr 227
                        250       260
                 ....*....|....*....|...
gi 564380513 780 --ECWQ---LMEACWDGDPSKRP 797
Cdd:cd14025  228 psECQQmicLMKRCWDQDPRKRP 250
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
553-797 2.47e-17

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: 82.84  E-value: 2.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYL---CDNwgGHFpCALKSV-VPPDEKHWNDLALEFHY---MRSLPKHERLVDLHGSVID----YN 621
Cdd:cd06632    3 QKGQLLGSGSFGSVYEgfnGDT--GDF-FAVKEVsLVDDDKKSRESVKQLEQeiaLLSKLRHPNIVQYYGTEREednlYI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 622 Y----GGGSsvavllIMERLHRdlYTGLKAGL-SLETRlQIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDL 696
Cdd:cd06632   80 FleyvPGGS------IHKLLQR--YGAFEEPViRLYTR-QI----LSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADF 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 697 GFCK--PEAMMSGSIVGTPIHMAPELFTGK---YDNSVDVYAFGILFWYICSGsiKLP-EAFERCASkdhLWNNVRRGTR 770
Cdd:cd06632  147 GMAKhvEAFSFAKSFKGSPYWMAPEVIMQKnsgYGLAVDIWSLGCTVLEMATG--KPPwSQYEGVAA---IFKIGNSGEL 221
                        250       260
                 ....*....|....*....|....*..
gi 564380513 771 PERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd06632  222 PPIPDHLSPDAKDFIRLCLQRDPEDRP 248
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
556-736 2.51e-17

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


Pssm-ID: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 82.50  E-value: 2.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALK----SVVPPDEKhWNDLALEFHYMRSLpKHERLVDLHGS---------VIDYNY 622
Cdd:cd06607    7 REIGHGSFGAVYYARNKRTSEVVAIKkmsySGKQSTEK-WQDIIKEVKFLRQL-RHPNTIEYKGCylrehtawlVMEYCL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 623 GGGSsvavllimerlhrDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGfckPE 702
Cdd:cd06607   85 GSAS-------------DIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG---SA 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 564380513 703 AMMS--GSIVGTPIHMAPELF----TGKYDNSVDVYAFGI 736
Cdd:cd06607  149 SLVCpaNSFVGTPYWMAPEVIlamdEGQYDGKVDVWSLGI 188
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
558-799 2.59e-17

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: 82.78  E-value: 2.59e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVP--PDEKHWNDLALEFHY-----MRSLPKHERLVDLHgSVIDynygggSSVAV 630
Cdd:cd13993    8 IGEGAYGVVYLAVDLRTGRKYAIKCLYKsgPNSKDGNDFQKLPQLreidlHRRVSRHPNIITLH-DVFE------TEVAI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLHR-DLYTGL--KAGLSLETRL--QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQ-NRAKITDLGFCKPEAM 704
Cdd:cd13993   81 YIVLEYCPNgDLFEAIteNRIYVGKTELikNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFGLATTEKI 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 705 MSGSIVGTPIHMAPELFTGKYDN-------SVDVYAFGILFWYICSGSIKLPEAFErcASKDHLWNNVRRGTRPERLPVF 777
Cdd:cd13993  161 SMDFGVGSEFYMAPECFDEVGRSlkgypcaAGDIWSLGIILLNLTFGRNPWKIASE--SDPIFYDYYLNSPNLFDVILPM 238
                        250       260
                 ....*....|....*....|..
gi 564380513 778 DEECWQLMEACWDGDPSKRPLL 799
Cdd:cd13993  239 SDDFYNLLRQIFTVNPNNRILL 260
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
658-744 2.74e-17

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: 83.60  E-value: 2.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpEAMMSG----SIVGTPIHMAPELFTGK-YDNSVDVY 732
Cdd:cd05587  103 AAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCK-EGIFGGkttrTFCGTPDYIAPEIIAYQpYGKSVDWW 181
                         90
                 ....*....|..
gi 564380513 733 AFGILFWYICSG 744
Cdd:cd05587  182 AYGVLLYEMLAG 193
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
558-806 3.84e-17

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


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 82.46  E-value: 3.84e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVY---LCDNWG---GHFPCALKSV---VPPDEKhwNDLALEFHYMRSLpKHERLVDLHGSVIDYNygggssv 628
Cdd:cd05044    3 LGSGAFGEVFegtAKDILGdgsGETKVAVKTLrkgATDQEK--AEFLKEAHLMSNF-KHPNILKLLGVCLDND------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 AVLLIMERLHR-DLYTGLKA---------GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA----KIT 694
Cdd:cd05044   73 PQYIILELMEGgDLLSYLRAarptaftppLLTLKDLLSICVDVAKGCVYLEDMHFVHRDLAARNCLVSSKDYRervvKIG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 695 DLGFCKP-----------EAMMsgsivgtPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPeaferCASKDH 760
Cdd:cd05044  153 DFGLARDiykndyyrkegEGLL-------PVRwMAPEsLVDGVFTTQSDVWAFGVLMWEILTlGQQPYP-----ARNNLE 220
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 564380513 761 LWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRPLLGIVQPIL 806
Cdd:cd05044  221 VLHFVRAGGRLDQPDNCPDDLYELMLRCWSTDPEERPSFARILEQL 266
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
555-797 4.17e-17

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: 81.97  E-value: 4.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 555 GQELGRGQYGVVYLCDNWGGHFPCALKSV--VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGS-------VIDYNYGGG 625
Cdd:cd06626    5 GNKIGEGTFGKVYTAVNLDTGELMAMKEIrfQDNDPKTIKEIADEMKVLEGL-DHPNLVRYYGVevhreevYIFMEYCQE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 626 SSVAVLLIMERLHRDLYTGlkaglsletrlQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK----P 701
Cdd:cd06626   84 GTLEELLRHGRILDEAVIR-----------VYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVklknN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 EAMMSG----SIVGTPIHMAPELFTGK----YDNSVDVYAFGILFWYICSGSIKLPEAfercaskDHLWN---NVRRGTR 770
Cdd:cd06626  153 TTTMAPgevnSLVGTPAYMAPEVITGNkgegHGRAADIWSLGCVVLEMATGKRPWSEL-------DNEWAimyHVGMGHK 225
                        250       260       270
                 ....*....|....*....|....*....|
gi 564380513 771 PErLP---VFDEECWQLMEACWDGDPSKRP 797
Cdd:cd06626  226 PP-IPdslQLSPEGKDFLSRCLESDPKKRP 254
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
556-797 4.44e-17

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: 81.66  E-value: 4.44e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLC-DNWGGHFPCALKSVVP-PDEKHWNDLALEFHYMRSLPKHERLVDLHGS-------VIDYNYGGGS 626
Cdd:cd13997    6 EQIGSGSFSEVFKVrSKVDGCLYAVKKSKKPfRGPKERARALREVEAHAALGQHPNIVRYYSSweegghlYIQMELCENG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 627 SVAVLLimERLHRDLYtglkagLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpeAMMS 706
Cdd:cd13997   86 SLQDAL--EELSPISK------LSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLAT--RLET 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 707 GSIV--GTPIHMAPELFTGK--YDNSVDVYAFGILFWYICSGsIKLPEafercasKDHLWNNVRRGTRPERL-PVFDEEC 781
Cdd:cd13997  156 SGDVeeGDSRYLAPELLNENytHLPKADIFSLGVTVYEAATG-EPLPR-------NGQQWQQLRQGKLPLPPgLVLSQEL 227
                        250
                 ....*....|....*.
gi 564380513 782 WQLMEACWDGDPSKRP 797
Cdd:cd13997  228 TRLLKVMLDPDPTRRP 243
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
649-797 5.02e-17

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: 81.77  E-value: 5.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 649 LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAK---ITDLGFC---------KPEAMMSGSIVGTPIHM 716
Cdd:cd14065   86 LPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVREANRGRnavVADFGLArempdektkKPDRKKRLTVVGSPYWM 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 717 APELFTGK-YDNSVDVYAFGILFWYICSGSIKLPEAFERcaSKDHLWNnvRRGTRPERLPVFDEECWQLMEACWDGDPSK 795
Cdd:cd14065  166 APEMLRGEsYDEKVDVFSFGIVLCEIIGRVPADPDYLPR--TMDFGLD--VRAFRTLYVPDCPPSFLPLAIRCCQLDPEK 241

                 ..
gi 564380513 796 RP 797
Cdd:cd14065  242 RP 243
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
559-745 6.09e-17

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: 81.53  E-value: 6.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 559 GRGQYGVVYLCDNWGGHFPCALKsVVPPDEKHWNDLAL---EFHYMRSLpKHERLVDLHGSVidynyggGSSVAVLLIME 635
Cdd:cd14002   10 GEGSFGKVYKGRRKYTGQVVALK-FIPKRGKSEKELRNlrqEIEILRKL-NHPNIIEMLDSF-------ETKKEFVVVTE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RLHRDLYTGLKAGLSL-ETRLQ-IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpeAMMSGSIV--- 710
Cdd:cd14002   81 YAQGELFQILEDDGTLpEEEVRsIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFAR--AMSCNTLVlts 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564380513 711 --GTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGS 745
Cdd:cd14002  159 ikGTPLYMAPELVQEQpYDHTADLWSLGCILYELFVGQ 196
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
558-797 7.21e-17

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: 81.57  E-value: 7.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDlalefHYMRSLPKHERLvdLHGSVIDYnYGGGSSVAVLLI-ME- 635
Cdd:cd13996   14 LGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSASE-----KVLREVKALAKL--NHPNIVRY-YTAWVEEPPLYIqMEl 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 --------RLH-RDLYTGLKAGLSLETRLQIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKQ-NRAKITDLG-------- 697
Cdd:cd13996   86 ceggtlrdWIDrRNSSSKNDRKLALELFKQI----LKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGlatsignq 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 698 ----------FCKPEAMMSGSIvGTPIHMAPELFTG-KYDNSVDVYAFGILF---WYICSGsiklpeAFERCaskdHLWN 763
Cdd:cd13996  162 krelnnlnnnNNGNTSNNSVGI-GTPLYASPEQLDGeNYNEKADIYSLGIILfemLHPFKT------AMERS----TILT 230
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564380513 764 NVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd13996  231 DLRNGILPESFKAKHPKEADLIQSLLSKNPEERP 264
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
653-739 7.66e-17

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: 81.15  E-value: 7.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 653 TRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC--KPEAMMSGSIVGTPIHMAPELFTGK-YDNSV 729
Cdd:cd05578  102 VKFYIC-EIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIAtkLTDGTLATSTSGTKPYMAPEVFMRAgYSFAV 180
                         90
                 ....*....|
gi 564380513 730 DVYAFGILFW 739
Cdd:cd05578  181 DWWSLGVTAY 190
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
653-813 8.89e-17

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: 80.95  E-value: 8.89e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 653 TRL---QIA---LDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPELFTG 723
Cdd:cd06648   98 TRMneeQIAtvcRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCaqvSKEVPRRKSLVGTPYWMAPEVISR 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 724 K-YDNSVDVYAFGILFWYICSGsiklpeafercaskdhlwnnvrrgtRPerlPVFDEECWQLMEACWDGDPSKRPLLGIV 802
Cdd:cd06648  178 LpYGTEVDIWSLGIMVIEMVDG-------------------------EP---PYFNEPPLQAMKRIRDNEPPKLKNLHKV 229
                        170
                 ....*....|.
gi 564380513 803 QPILRSIMDRL 813
Cdd:cd06648  230 SPRLRSFLDRM 240
PTKc_PDGFR_alpha cd05105
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor alpha; ...
648-810 9.91e-17

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: 83.15  E-value: 9.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 648 GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpEAMMSGSIVGT-----PIH-MAPE-L 720
Cdd:cd05105  233 GLTTLDLLSFTYQVARGMEFLASKNCVHRDLAARNVLLAQGKIVKICDFGLAR-DIMHDSNYVSKgstflPVKwMAPEsI 311
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 721 FTGKYDNSVDVYAFGILFWYICS-GSIKLPEAFercaSKDHLWNNVRRGTR---PERLPvfdEECWQLMEACWDGDPSKR 796
Cdd:cd05105  312 FDNLYTTLSDVWSYGILLWEIFSlGGTPYPGMI----VDSTFYNKIKSGYRmakPDHAT---QEVYDIMVKCWNSEPEKR 384
                        170
                 ....*....|....
gi 564380513 797 PLLGIVQPILRSIM 810
Cdd:cd05105  385 PSFLHLSDIVESLL 398
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
556-797 1.41e-16

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


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 80.46  E-value: 1.41e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDnW----GGHFPCA---LKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYGGGSSV 628
Cdd:cd05040    1 EKLGDGSFGVVRRGE-WttpsGKVIQVAvkcLKSDVLSQPNAMDDFLKEVNAMHSL-DHPNLIRLYGVVLSSPLMMVTEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 AVL-LIMERLHRDlytglKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGfckpeaMMSG 707
Cdd:cd05040   79 APLgSLLDRLRKD-----QGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFG------LMRA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 SIVG-----------TPIH-MAPE-LFTGKYDNSVDVYAFGILFWYI----------CSGSIKLpEAFERcaskdhlwnN 764
Cdd:cd05040  148 LPQNedhyvmqehrkVPFAwCAPEsLKTRKFSHASDVWMFGVTLWEMftygeepwlgLNGSQIL-EKIDK---------E 217
                        250       260       270
                 ....*....|....*....|....*....|...
gi 564380513 765 VRRGTRPERLPvfdEECWQLMEACWDGDPSKRP 797
Cdd:cd05040  218 GERLERPDDCP---QDIYNVMLQCWAHKPADRP 247
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
553-806 1.69e-16

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: 80.32  E-value: 1.69e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLcDNWGGHFPCALKSVVPPDEKHWNDLAlEFHYMRSLpKHERLVDLHGSVidynygggSSVAVLL 632
Cdd:cd05067   10 KLVERLGAGQFGEVWM-GYYNGHTKVAIKSLKQGSMSPDAFLA-EANLMKQL-QHQRLVRLYAVV--------TQEPIYI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERLHRD-----LYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAM 704
Cdd:cd05067   79 ITEYMENGslvdfLKTPSGIKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLArliEDNEY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 705 MSGSIVGTPIH-MAPELFT-GKYDNSVDVYAFGILFWYICS-GSIKLPEafercASKDHLWNNVRRGTR---PERLPvfd 778
Cdd:cd05067  159 TAREGAKFPIKwTAPEAINyGTFTIKSDVWSFGILLTEIVThGRIPYPG-----MTNPEVIQNLERGYRmprPDNCP--- 230
                        250       260
                 ....*....|....*....|....*...
gi 564380513 779 EECWQLMEACWDGDPSKRPLLGIVQPIL 806
Cdd:cd05067  231 EELYQLMRLCWKERPEDRPTFEYLRSVL 258
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
554-797 1.78e-16

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: 80.30  E-value: 1.78e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLC----DNWGGHFPCAL--KSVVPPDEKHwNDLALEFHYMRSLpKHERLVDLHgSVIDYNYgggss 627
Cdd:cd14080    4 LGKTIGEGSYSKVKLAeytkSGLKEKVACKIidKKKAPKDFLE-KFLPRELEILRKL-RHPNIIQVY-SIFERGS----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 vAVLLIMERL-HRDL--YTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF-----C 699
Cdd:cd14080   76 -KVFIFMEYAeHGDLleYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFarlcpD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 700 KPEAMMSGSIVGTPIHMAPELFTGK-YDNSV-DVYAFG-ILFWYICSgsiKLPeaFERCASKDHLWNNVRRGTR-PERLP 775
Cdd:cd14080  155 DDGDVLSKTFCGSAAYAAPEILQGIpYDPKKyDIWSLGvILYIMLCG---SMP--FDDSNIKKMLKDQQNRKVRfPSSVK 229
                        250       260
                 ....*....|....*....|..
gi 564380513 776 VFDEECWQLMEACWDGDPSKRP 797
Cdd:cd14080  230 KLSPECKDLIDQLLEPDPTKRA 251
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
660-737 1.88e-16

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: 79.97  E-value: 1.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFG 735
Cdd:cd06647  111 ECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCaqiTPEQSKRSTMVGTPYWMAPEVVTRKaYGPKVDIWSLG 190

                 ..
gi 564380513 736 IL 737
Cdd:cd06647  191 IM 192
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
556-736 2.00e-16

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: 81.24  E-value: 2.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVV----PPDEKhWNDLALEFHYMRSLpKHERLVDLHGSVIDYNygggssvAVL 631
Cdd:cd06633   27 HEIGHGSFGAVYFATNSHTNEVVAIKKMSysgkQTNEK-WQDIIKEVKFLQQL-KHPNTIEYKGCYLKDH-------TAW 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERL---HRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGfCKPEAMMSGS 708
Cdd:cd06633   98 LVMEYClgsASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG-SASIASPANS 176
                        170       180       190
                 ....*....|....*....|....*....|..
gi 564380513 709 IVGTPIHMAPELF----TGKYDNSVDVYAFGI 736
Cdd:cd06633  177 FVGTPYWMAPEVIlamdEGQYDGKVDIWSLGI 208
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
593-797 2.10e-16

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: 80.08  E-value: 2.10e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 593 DLALEFHYMRSLPKHERLVDLHGS---------VIDYNYGGGssvavLLIMERLHRDLYT--------GLKAGLSLETRL 655
Cdd:cd05047   41 DFAGELEVLCKLGHHPNIINLLGAcehrgylylAIEYAPHGN-----LLDFLRKSRVLETdpafaianSTASTLSSQQLL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGT-PIH-MAPE-LFTGKYDNSVDVY 732
Cdd:cd05047  116 HFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGRlPVRwMAIEsLNYSVYTTNSDVW 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564380513 733 AFGILFWYICS--GSiklPEAFERCAskdHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05047  196 SYGVLLWEIVSlgGT---PYCGMTCA---ELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERP 256
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
557-738 2.11e-16

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK4/6-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 80.40  E-value: 2.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLC-DNWGGHFpCALKSV-VPPDEkhwNDLAL----EFHYMRSLPKHE-----RLVDlhgsvIDYNYGGG 625
Cdd:cd07838    6 EIGEGAYGTVYKArDLQDGRF-VALKKVrVPLSE---EGIPLstirEIALLKQLESFEhpnvvRLLD-----VCHGPRTD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 626 SSVAVLLIMERLHRDLYTGL----KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK- 700
Cdd:cd07838   77 RELKLTLVFEHVDQDLATYLdkcpKPGLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARi 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 564380513 701 -PEAMMSGSIVGTPIHMAPE-LFTGKYDNSVDVYAFGILF 738
Cdd:cd07838  157 ySFEMALTSVVVTLWYRAPEvLLQSSYATPVDMWSVGCIF 196
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
553-735 2.13e-16

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 80.09  E-value: 2.13e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSV-----VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDynyggGSS 627
Cdd:cd06652    5 RLGKLLGQGAFGRVYLCYDADTGRELAVKQVqfdpeSPETSKEVNALECEIQLLKNL-LHERIVQYYGCLRD-----PQE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 VAVLLIMERLHR-DLYTGLKA--GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PE 702
Cdd:cd06652   79 RTLSIFMEYMPGgSIKDQLKSygALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKrlQT 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564380513 703 AMMSG----SIVGTPIHMAPELFTGK-YDNSVDVYAFG 735
Cdd:cd06652  159 ICLSGtgmkSVTGTPYWMSPEVISGEgYGRKADIWSVG 196
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
661-797 2.23e-16

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: 79.78  E-value: 2.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---PEAMMSGSIVGTPIHMAPELFTG-KYDNSVDVYAFGI 736
Cdd:cd08221  110 IVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKvldSESSMAESIVGTPYYMSPELVQGvKYNFKSDIWAVGC 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564380513 737 LFWYIcsgsIKLPEAFErCASKDHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd08221  190 VLYEL----LTLKRTFD-ATNPLRLAVKIVQGEYEDIDEQYSEEIIQLVHDCLHQDPEDRP 245
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
554-810 2.45e-16

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: 80.39  E-value: 2.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVV-----YLCDNWGGHFPCALKSVVP-PDEKHWNDLALEFHYMRSLpKHERLVDLHGSVidynyggGSS 627
Cdd:cd05045    4 LGKTLGEGEFGKVvkataFRLKGRAGYTTVAVKMLKEnASSSELRDLLSEFNLLKQV-NHPHVIKLYGAC-------SQD 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 VAVLLIME-----------RLHRDL---YTGLKAG-------------LSLETRLQIALDVVEGIRFLHSQGLVHRDIKL 680
Cdd:cd05045   76 GPLLLIVEyakygslrsflRESRKVgpsYLGSDGNrnssyldnpderaLTMGDLISFAWQISRGMQYLAEMKLVHRDLAA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 681 KNVLLDKQNRAKITDLGFCK----PEAMMSGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPEAfe 753
Cdd:cd05045  156 RNVLVAEGRKMKISDFGLSRdvyeEDSYVKRSKGRIPVKwMAIEsLFDHIYTTQSDVWSFGVLLWEIVTlGGNPYPGI-- 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564380513 754 rcaSKDHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRPLLGIVQPILRSIM 810
Cdd:cd05045  234 ---APERLFNLLKTGYRMERPENCSEEMYNLMLTCWKQEPDKRPTFADISKELEKMM 287
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
588-797 2.79e-16

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: 80.43  E-value: 2.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 588 EKHWNDLALEFHYMRSLPKHERLVDLHGS---------VIDYN-YGGgssvavLLIMERLHRDLYT--------GLKAGL 649
Cdd:cd05089   43 ENDHRDFAGELEVLCKLGHHPNIINLLGAcenrgylyiAIEYApYGN------LLDFLRKSRVLETdpafakehGTASTL 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 650 SLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGT-PIH-MAPE-LFTGKYD 726
Cdd:cd05089  117 TSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGLSRGEEVYVKKTMGRlPVRwMAIEsLNYSVYT 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564380513 727 NSVDVYAFGILFWYICSGSiKLPEAFERCAskdHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05089  197 TKSDVWSFGVLLWEIVSLG-GTPYCGMTCA---ELYEKLPQGYRMEKPRNCDDEVYELMRQCWRDRPYERP 263
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
558-742 3.04e-16

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: 79.63  E-value: 3.04e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIdyNYGGGSSVAVLLIMErL 637
Cdd:cd14037   11 LAEGGFAHVYLVKTSNGGNRAALKRVYVNDEHDLNVCKREIEIMKRLSGHKNIVGYIDSSA--NRSGNGVYEVLLLME-Y 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 638 HRD------LYTGLKAGLSLETRLQIALDVVEGIRFLHS--QGLVHRDIKLKNVLLDKQNRAKITDLG-----FCKPEAM 704
Cdd:cd14037   88 CKGggvidlMNQRLQTGLTESEILKIFCDVCEAVAAMHYlkPPLIHRDLKVENVLISDSGNYKLCDFGsattkILPPQTK 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564380513 705 MSGSIV-------GTPIHMAPE---LFTGK-YDNSVDVYAFGILFWYIC 742
Cdd:cd14037  168 QGVTYVeedikkyTTLQYRAPEmidLYRGKpITEKSDIWALGCLLYKLC 216
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
558-797 3.07e-16

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: 79.08  E-value: 3.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLcdnwgGHF---PCALKSVvpPDEKHwndlaLEFHYMRSLpKHERLVDLHGSVIdynygggSSVAVLLIM 634
Cdd:cd14059    1 LGSGAQGAVFL-----GKFrgeEVAVKKV--RDEKE-----TDIKHLRKL-NHPNIIKFKGVCT-------QAPCYCILM 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 ERL-HRDLYTGLKAGLSLETRLQI--ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP--EAMMSGSI 709
Cdd:cd14059   61 EYCpYGQLYEVLRAGREITPSLLVdwSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKElsEKSTKMSF 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 710 VGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGSIklpeAFERCASKDHLWNnvrRGTRPERLPVFD---EECWQLM 785
Cdd:cd14059  141 AGTVAWMAPEVIRNEpCSEKVDIWSFGVVLWELLTGEI----PYKDVDSSAIIWG---VGSNSLQLPVPStcpDGFKLLM 213
                        250
                 ....*....|..
gi 564380513 786 EACWDGDPSKRP 797
Cdd:cd14059  214 KQCWNSKPRNRP 225
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
658-744 3.44e-16

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


Pssm-ID: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 80.43  E-value: 3.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpEAMMSG----SIVGTPIHMAPELFTGK-YDNSVDVY 732
Cdd:cd05616  107 AAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCK-ENIWDGvttkTFCGTPDYIAPEIIAYQpYGKSVDWW 185
                         90
                 ....*....|..
gi 564380513 733 AFGILFWYICSG 744
Cdd:cd05616  186 AFGVLLYEMLAG 197
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
640-807 3.72e-16

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: 79.02  E-value: 3.72e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 640 DLYTGLKA--GLSLETR------LQIALdvveGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---PEAMMSGS 708
Cdd:cd08223   86 DLYTRLKEqkGVLLEERqvvewfVQIAM----ALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARvleSSSDMATT 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 709 IVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSgsikLPEAFErcaSKD--HLWNNVRRGTRPERLPVFDEECWQLM 785
Cdd:cd08223  162 LIGTPYYMSPELFSNKpYNHKSDVWALGCCVYEMAT----LKHAFN---AKDmnSLVYKILEGKLPPMPKQYSPELGELI 234
                        170       180
                 ....*....|....*....|..
gi 564380513 786 EACWDGDPSKRPllgIVQPILR 807
Cdd:cd08223  235 KAMLHQDPEKRP---SVKRILR 253
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
558-737 3.96e-16

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: 80.42  E-value: 3.96e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCD--NWGGHFPC-ALKS--VVPPDEKhwNDLALE---FHYMRSLpKHERLVDLHGS---------VIDY 620
Cdd:cd05589    7 LGRGHFGKVLLAEykPTGELFAIkALKKgdIIARDEV--ESLMCEkriFETVNSA-RHPFLVNLFACfqtpehvcfVMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 621 NYGGGssvavllIMERLHRDLYTglkaglslETRLQI-ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC 699
Cdd:cd05589   84 AAGGD-------LMMHIHEDVFS--------EPRAVFyAACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLC 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564380513 700 KpEAM----MSGSIVGTPIHMAPELFT-GKYDNSVDVYAFGIL 737
Cdd:cd05589  149 K-EGMgfgdRTSTFCGTPEFLAPEVLTdTSYTRAVDWWGLGVL 190
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
553-799 3.97e-16

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: 78.82  E-value: 3.97e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVY----LCDNwgghFPCALKSVVPPDEKHW------NDLALE--FHYMRSLPKHERLVDLHG-SVID 619
Cdd:cd14005    3 EVGDLLGKGGFGTVYsgvrIRDG----LPVAVKFVPKSRVTEWamingpVPVPLEiaLLLKASKPGVPGVIRLLDwYERP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 620 YNYgggssvavLLIMERLH--RDLYTGLKAGLSLETRL--QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN-RAKIT 694
Cdd:cd14005   79 DGF--------LLIMERPEpcQDLFDFITERGALSENLarIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLRTgEVKLI 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 695 DLGfckpeammSGSIV---------GTPIHMAPELF-TGKYD-NSVDVYAFGILFWYICSGSIKLPEAFERCASKDHLWn 763
Cdd:cd14005  151 DFG--------CGALLkdsvytdfdGTRVYSPPEWIrHGRYHgRPATVWSLGILLYDMLCGDIPFENDEQILRGNVLFR- 221
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 564380513 764 nvrrgtrperlPVFDEECWQLMEACWDGDPSKRPLL 799
Cdd:cd14005  222 -----------PRLSKECCDLISRCLQFDPSKRPSL 246
PTKc_VEGFR3 cd05102
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 3; ...
646-810 4.42e-16

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


Pssm-ID: 270680 [Multi-domain]  Cd Length: 336  Bit Score: 80.41  E-value: 4.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 646 KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-----PEAMMSGSIVGTPIHMAPE- 719
Cdd:cd05102  166 QSPLTMEDLICYSFQVARGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLARdiykdPDYVRKGSARLPLKWMAPEs 245
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 720 LFTGKYDNSVDVYAFGILFWYICS------GSIKLPEAFerCaskdhlwNNVRRGTRPERLPVFDEECWQLMEACWDGDP 793
Cdd:cd05102  246 IFDKVYTTQSDVWSFGVLLWEIFSlgaspyPGVQINEEF--C-------QRLKDGTRMRAPEYATPEIYRIMLSCWHGDP 316
                        170
                 ....*....|....*..
gi 564380513 794 SKRPLLGIVQPILRSIM 810
Cdd:cd05102  317 KERPTFSDLVEILGDLL 333
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
557-736 4.57e-16

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: 79.40  E-value: 4.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGS---------VIDYNYGGgss 627
Cdd:cd06611   12 ELGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMVEIDILSEC-KHPNIVGLYEAyfyenklwiLIEFCDGG--- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 vAVLLIMERLHRDLytglkaglsleTRLQIAL---DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KP 701
Cdd:cd06611   88 -ALDSIMLELERGL-----------TEPQIRYvcrQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSaknKS 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 564380513 702 EAMMSGSIVGTPIHMAPELF---TGK---YDNSVDVYAFGI 736
Cdd:cd06611  156 TLQKRDTFIGTPYWMAPEVVaceTFKdnpYDYKADIWSLGI 196
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
631-808 5.29e-16

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


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 78.46  E-value: 5.29e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLHRD----LYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLL-----DKQNRAKITDLGFCKP 701
Cdd:cd14068   61 MLVMELAPKGsldaLLQQDNASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQY 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 EAMMS-GSIVGTPIHMAPELFTGK--YDNSVDVYAFGILFWYICSG------SIKLPEAFERCASKDHLwnnvrrgtrPE 772
Cdd:cd14068  141 CCRMGiKTSEGTPGFRAPEVARGNviYNQQADVYSFGLLLYDILTCgeriveGLKFPNEFDELAIQGKL---------PD 211
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564380513 773 rlPVFDEEC--W----QLMEACWDGDPSKRPLLGIVQPILRS 808
Cdd:cd14068  212 --PVKEYGCapWpgveALIKDCLKENPQCRPTSAQVFDILNS 251
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
660-753 5.48e-16

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: 78.94  E-value: 5.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKPEAMMSGSiVGTPIHMAPELFTGKYDN----SVDV 731
Cdd:cd14118  123 DIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGvsneFEGDDALLSST-AGTPAFMAPEALSESRKKfsgkALDI 201
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 564380513 732 YAFGI-------------------LFWYICSGSIKLPEAFE 753
Cdd:cd14118  202 WAMGVtlycfvfgrcpfeddhilgLHEKIKTDPVVFPDDPV 242
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
558-796 5.57e-16

Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also called N-rich kinase 1), is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Kic1p is required by budding yeast for cell integrity and morphogenesis. Kic1p interacts with Cdc31p, the yeast homologue of centrin, and phosphorylates substrates in a Cdc31p-dependent manner. The Nak1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 79.06  E-value: 5.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLcdnwGGHFPC----ALKSV---VPPDEKH--WNDLALEFHYMRSLPKHerLVDLHGSvidynYGGGSSV 628
Cdd:cd06917    9 VGRGSYGAVYR----GYHVKTgrvvALKVLnldTDDDDVSdiQKEVALLSQLKLGQPKN--IIKYYGS-----YLKGPSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 AVllIMERLHR-DLYTGLKAGLSLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMS 706
Cdd:cd06917   78 WI--IMDYCEGgSIRTLMRAGPIAERYIAVIMrEVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 707 G---SIVGTPIHMAPELFT-GK-YDNSVDVYAFGILFWYICSGSIklPEAFERCASKDHLWNNvrrgTRPERLP--VFDE 779
Cdd:cd06917  156 SkrsTFVGTPYWMAPEVITeGKyYDTKADIWSLGITTYEMATGNP--PYSDVDALRAVMLIPK----SKPPRLEgnGYSP 229
                        250
                 ....*....|....*..
gi 564380513 780 ECWQLMEACWDGDPSKR 796
Cdd:cd06917  230 LLKEFVAACLDEEPKDR 246
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
558-797 6.20e-16

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: 78.67  E-value: 6.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVppdeKH---WNDLAL-----EFHYMRSLpKHERLVDLHGSVIDYNygggssvA 629
Cdd:cd14098    8 LGSGTFAEVKKAVEVETGKMRAIKQIV----KRkvaGNDKNLqlfqrEINILKSL-EHPGIVRLIDWYEDDQ-------H 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHR-DLYTGLKA--GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNR--AKITDLGFCK---P 701
Cdd:cd14098   76 IYLVMEYVEGgDLMDFIMAwgAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDPviVKISDFGLAKvihT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 EAMMSgSIVGTPIHMAPELFTGK-------YDNSVDVYAFGILFWYICSGSIKLPEafercASKDHLWNNVRRGTRPERl 774
Cdd:cd14098  156 GTFLV-TFCGTMAYLAPEILMSKeqnlqggYSNLVDMWSVGCLVYVMLTGALPFDG-----SSQLPVEKRIRKGRYTQP- 228
                        250       260
                 ....*....|....*....|....*..
gi 564380513 775 PVFD----EECWQLMEACWDGDPSKRP 797
Cdd:cd14098  229 PLVDfnisEEAIDFILRLLDVDPEKRM 255
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
556-736 6.59e-16

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: 78.83  E-value: 6.59e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSV-VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDynyggGSSVAVllIM 634
Cdd:cd06609    7 ERIGKGSFGEVYKGIDKRTNQVVAIKVIdLEEAEDEIEDIQQEIQFLSQC-DSPYITKYYGSFLK-----GSKLWI--IM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 ERLH----RDLytgLKAGLSLETRLQ-IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGfckpeamMSGSI 709
Cdd:cd06609   79 EYCGggsvLDL---LKPGPLDETYIAfILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFG-------VSGQL 148
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564380513 710 ----------VGTPIHMAPELFT-GKYDNSVDVYAFGI 736
Cdd:cd06609  149 tstmskrntfVGTPFWMAPEVIKqSGYDEKADIWSLGI 186
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
557-797 6.62e-16

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: 78.90  E-value: 6.62e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLCDNWGGHFPCALKSV-VPPDEKHWNDLAL-EFHYMRSLpKHERLVDLhgsvIDYNYGGGSsvaVLLIM 634
Cdd:cd07833    8 VVGEGAYGVVLKCRNKATGEIVAIKKFkESEDDEDVKKTALrEVKVLRQL-RHENIVNL----KEAFRRKGR---LYLVF 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 ERLHRDLYTGLKA---GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF-----CKPEAMMS 706
Cdd:cd07833   80 EYVERTLLELLEAspgGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFaraltARPASPLT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 707 gSIVGTPIHMAPELFTG--KYDNSVDVYAFGILF-------------------WYI--CSGsiKLPEAFERCASKDHLWN 763
Cdd:cd07833  160 -DYVATRWYRAPELLVGdtNYGKPVDVWAIGCIMaelldgeplfpgdsdidqlYLIqkCLG--PLPPSHQELFSSNPRFA 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 564380513 764 NVR------RGTRPERLPVFDEECW-QLMEACWDGDPSKRP 797
Cdd:cd07833  237 GVAfpepsqPESLERRYPGKVSSPAlDFLKACLRMDPKERL 277
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
558-744 8.17e-16

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: 79.02  E-value: 8.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLC-DNWGGHFpCALKSVVPPD------EKHWNDlalEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaV 630
Cdd:cd05612    9 IGTGTFGRVHLVrDRISEHY-YALKVMAIPEvirlkqEQHVHN---EKRVLKEV-SHPFIIRLFWTEHDQRF-------L 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERL-HRDLYTGLKAG--LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSG 707
Cdd:cd05612   77 YMLMEYVpGGELFSYLRNSgrFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRTW 156
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564380513 708 SIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSG 744
Cdd:cd05612  157 TLCGTPEYLAPEVIQSKgHNKAVDWWALGILIYEMLVG 194
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
554-719 9.53e-16

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: 78.04  E-value: 9.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNW-GGHFpCALKSV----VPPDEkhWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssv 628
Cdd:cd06627    4 LGDLIGRGAFGSVYKGLNLnTGEF-VAIKQIslekIPKSD--LKSVMGEIDLLKKL-NHPNIVKYIGSVKTKDS------ 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 aVLLIMErlhrdlytgLKAGLSLETRL---------QIAL---DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDL 696
Cdd:cd06627   74 -LYIILE---------YVENGSLASIIkkfgkfpesLVAVyiyQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADF 143
                        170       180
                 ....*....|....*....|....*.
gi 564380513 697 GFC---KPEAMMSGSIVGTPIHMAPE 719
Cdd:cd06627  144 GVAtklNEVEKDENSVVGTPYWMAPE 169
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
554-797 1.22e-15

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: 78.52  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWG--GHFPCALKSVV------PPDEKHWNDLALEFHYMRSLPKHERLVDLHGS--------- 616
Cdd:cd05098   17 LGKPLGEGCFGQVVLAEAIGldKDKPNRVTKVAvkmlksDATEKDLSDLISEMEMMKMIGKHKNIINLLGActqdgplyv 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 617 VIDYNYGGGssvavllIMERLHRDLYTGLK----------AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLD 686
Cdd:cd05098   97 IVEYASKGN-------LREYLQARRPPGMEycynpshnpeEQLSSKDLVSCAYQVARGMEYLASKKCIHRDLAARNVLVT 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 687 KQNRAKITDLGFCKP-------EAMMSGSIvgtPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPEafercA 756
Cdd:cd05098  170 EDNVMKIADFGLARDihhidyyKKTTNGRL---PVKwMAPEaLFDRIYTHQSDVWSFGVLLWEIFTlGGSPYPG-----V 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 564380513 757 SKDHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05098  242 PVEELFKLLKEGHRMDKPSNCTNELYMMMRDCWHAVPSQRP 282
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
580-808 1.25e-15

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: 78.13  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 580 LKSVVPPdeKHWNDLALEFHYMRSLpKHERLVDLHGSVID-------YNYGGGSSVAVLLIMERLHRDLYTG------LK 646
Cdd:cd05090   42 LKDYNNP--QQWNEFQQEASLMTEL-HHPNIVCLLGVVTQeqpvcmlFEFMNQGDLHEFLIMRSPHSDVGCSsdedgtVK 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 647 AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP------EAMMSGSIVgtPIH-MAPE 719
Cdd:cd05090  119 SSLDHGDFLHIAIQIAAGMEYLSSHFFVHKDLAARNILVGEQLHVKISDLGLSREiyssdyYRVQNKSLL--PIRwMPPE 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 720 LFT-GKYDNSVDVYAFGILFWYICSGSIKLPEAFERcaskdhlwNNVRRGTRPERLPVFDEEC----WQLMEACWDGDPS 794
Cdd:cd05090  197 AIMyGKFSSDSDIWSFGVVLWEIFSFGLQPYYGFSN--------QEVIEMVRKRQLLPCSEDCpprmYSLMTECWQEIPS 268
                        250
                 ....*....|....
gi 564380513 795 KRPLLGIVQPILRS 808
Cdd:cd05090  269 RRPRFKDIHARLRS 282
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
553-797 1.32e-15

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: 77.96  E-value: 1.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNwggHFP---CALKSVVPPdEKHWND-LAL-EFHYMRSLPKHERLVDLHGSVIDYNYgggss 627
Cdd:cd07830    2 KVIKQLGDGTFGSVYLARN---KETgelVAIKKMKKK-FYSWEEcMNLrEVKSLRKLNEHPNIVKLKEVFRENDE----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 vaVLLIMERLHRDLYTGLKAG----LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGfckpea 703
Cdd:cd07830   73 --LYFVFEYMEGNLYQLMKDRkgkpFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFG------ 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 mMSGSI---------VGTPIHMAPELF--TGKYDNSVDVYAFG-IL------------------FWYICS--GSIK---L 748
Cdd:cd07830  145 -LAREIrsrppytdyVSTRWYRAPEILlrSTSYSSPVDIWALGcIMaelytlrplfpgsseidqLYKICSvlGTPTkqdW 223
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 564380513 749 PEAFERCASKDHLWNNVrRGTRPERL-PVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd07830  224 PEGYKLASKLGFRFPQF-APTSLHQLiPNASPEAIDLIKDMLRWDPKKRP 272
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
551-701 1.51e-15

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 77.50  E-value: 1.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQELGRGQYGVVYLCDNWGGHFPCALKsVVPPDEKHwNDLALEFHYMRSLPKHE---RLVDlHGSVIDYNYgggss 627
Cdd:cd14016    1 RYKLVKKIGSGSFGEVYLGIDLKTGEEVAIK-IEKKDSKH-PQLEYEAKVYKLLQGGPgipRLYW-FGQEGDYNV----- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 vavlLIMERLHRDL-----YTGLKagLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAK---ITDLGFC 699
Cdd:cd14016   73 ----MVMDLLGPSLedlfnKCGRK--FSLKTVLMLADQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLA 146

                 ..
gi 564380513 700 KP 701
Cdd:cd14016  147 KK 148
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
649-813 1.54e-15

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: 77.13  E-value: 1.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 649 LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNR---AKITDLGFCK--PEAMMSGS---IVGTPIHMAPEL 720
Cdd:cd14155   85 LSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIKRDENgytAVVGDFGLAEkiPDYSDGKEklaVVGSPYWMAPEV 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 721 FTGK-YDNSVDVYAFGILFWYICSGSIKLPEAFERCASKDHLWNNVrRGTRPERLPVFdeecWQLMEACWDGDPSKRPLL 799
Cdd:cd14155  165 LRGEpYNEKADVFSYGIILCEIIARIQADPDYLPRTEDFGLDYDAF-QHMVGDCPPDF----LQLAFNCCNMDPKSRPSF 239
                        170
                 ....*....|....
gi 564380513 800 GIVQPILRSIMDRL 813
Cdd:cd14155  240 HDIVKTLEEILEKL 253
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
558-796 1.56e-15

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: 77.73  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDN--WGGHFpcALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSvidYNygggSSVAVLLIME 635
Cdd:cd14166   11 LGSGAFSEVYLVKQrsTGKLY--ALKCIKKSPLSRDSSLENEIAVLKRI-KHENIVTLEDI---YE----STTHYYLVMQ 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 R----------LHRDLYTGLKAGLSLEtrlqialDVVEGIRFLHSQGLVHRDIKLKNVLL---DKQNRAKITDLGFCKPE 702
Cdd:cd14166   81 LvsggelfdriLERGVYTEKDASRVIN-------QVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSKME 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 703 --AMMSgSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsikLPEAFERCASKdhLWNNVRRGTRPERLPVFD- 778
Cdd:cd14166  154 qnGIMS-TACGTPGYVAPEVLAQKpYSKAVDCWSIGVITYILLCG---YPPFYEETESR--LFEKIKEGYYEFESPFWDd 227
                        250       260
                 ....*....|....*....|
gi 564380513 779 --EECWQLMEACWDGDPSKR 796
Cdd:cd14166  228 isESAKDFIRHLLEKNPSKR 247
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
558-745 1.57e-15

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: 77.78  E-value: 1.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLC--DNWGGHFPCALKSVV--PPDEKHWNDL----ALEFHYMRSLPKHERLVDLHGSVidynyggGSSVA 629
Cdd:cd14093   11 LGRGVSSTVRRCieKETGQEFAVKIIDITgeKSSENEAEELreatRREIEILRQVSGHPNIIELHDVF-------ESPTF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHR-DLYTGLKAGLSL---ETRLqIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PEA 703
Cdd:cd14093   84 IFLVFELCRKgELFDYLTEVVTLsekKTRR-IMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATrlDEG 162
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 MMSGSIVGTPIHMAPEL--------FTGkYDNSVDVYAFGILFWYICSGS 745
Cdd:cd14093  163 EKLRELCGTPGYLAPEVlkcsmydnAPG-YGKEVDMWACGVIMYTLLAGC 211
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
556-797 1.70e-15

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: 77.21  E-value: 1.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLcDNWGGHFPCALKSVvPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNygggSSVAVLLIME 635
Cdd:cd05114   10 KELGSGLFGVVRL-GKWRAQYKVAIKAI-REGAMSEEDFIEEAKVMMKL-THPKLVQLYGVCTQQK----PIYIVTEFME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RLHRDLYTGLKAG-LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---PEAMMSGSIVG 711
Cdd:cd05114   83 NGCLLNYLRQRRGkLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRyvlDDQYTSSSGAK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 712 TPIHMA-PELFT-GKYDNSVDVYAFGILFWYICSGSiKLPeaFERcASKDHLWNNVRRGTRPERLPVFDEECWQLMEACW 789
Cdd:cd05114  163 FPVKWSpPEVFNySKFSSKSDVWSFGVLMWEVFTEG-KMP--FES-KSNYEVVEMVSRGHRLYRPKLASKSVYEVMYSCW 238

                 ....*...
gi 564380513 790 DGDPSKRP 797
Cdd:cd05114  239 HEKPEGRP 246
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
553-797 1.73e-15

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: 77.45  E-value: 1.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVY--LcdnWGGHFPCALKSVvPPDEKHWNDLALEFHYMRSLpKHERLVDL----------------- 613
Cdd:cd05068   11 KLLRKLGSGQFGEVWegL---WNNTTPVAVKTL-KPGTMDPEDFLREAQIMKKL-RHPKLIQLyavctleepiyiitelm 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 614 -HGSVIDYNYGGGSSvavllimerlhrdlytglkagLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAK 692
Cdd:cd05068   86 kHGSLLEYLQGKGRS---------------------LQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICK 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 693 ITDLGFCKpeAMMSGSI----VGT--PIH-MAPEL-----FTGKydnsVDVYAFGILFWYICS-GSIKLP-----EAFEr 754
Cdd:cd05068  145 VADFGLAR--VIKVEDEyearEGAkfPIKwTAPEAanynrFSIK----SDVWSFGILLTEIVTyGRIPYPgmtnaEVLQ- 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 564380513 755 caskdhlwnNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05068  218 ---------QVERGYRMPCPPNCPPQLYDIMLECWKADPMERP 251
PTKc_Kit cd05104
Catalytic domain of the Protein Tyrosine Kinase, Kit; PTKs catalyze the transfer of the ...
649-809 1.80e-15

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


Pssm-ID: 270682 [Multi-domain]  Cd Length: 375  Bit Score: 79.18  E-value: 1.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 649 LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVG----TPIH-MAPE-LFT 722
Cdd:cd05104  211 LDTEDLLSFSYQVAKGMEFLASKNCIHRDLAARNILLTHGRITKICDFGLARDIRNDSNYVVKgnarLPVKwMAPEsIFE 290
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 723 GKYDNSVDVYAFGILFWYICS-GSIKLPeafeRCASKDHLWNNVRRGTR---PERLPVfdeECWQLMEACWDGDPSKRPL 798
Cdd:cd05104  291 CVYTFESDVWSYGILLWEIFSlGSSPYP----GMPVDSKFYKMIKEGYRmdsPEFAPS---EMYDIMRSCWDADPLKRPT 363
                        170
                 ....*....|..
gi 564380513 799 LG-IVQPILRSI 809
Cdd:cd05104  364 FKqIVQLIEQQL 375
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
661-796 1.89e-15

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: 77.35  E-value: 1.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQG--LVHRDIKLKNVLLD-KQNRAKITDLGFCK-PEAMMSGSIVGTPIHMAPELFTGKYDNSVDVYAFGI 736
Cdd:cd14033  113 ILKGLHFLHSRCppILHRDLKCDNIFITgPTGSVKIGDLGLATlKRASFAKSVIGTPEFMAPEMYEEKYDEAVDVYAFGM 192
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564380513 737 LFWYICSGSIKLPEaferCASKDHLWNNVRRGTRPERL-PVFDEECWQLMEACWDGDPSKR 796
Cdd:cd14033  193 CILEMATSEYPYSE----CQNAAQIYRKVTSGIKPDSFyKVKVPELKEIIEGCIRTDKDER 249
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
557-797 1.95e-15

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: 77.25  E-value: 1.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLCDNWGGHFPCALKSV-VPPDEKHWNDLALEFHYMRSLPkHERLVDLHGSVIDynygGGSsvaVLLIME 635
Cdd:cd06623    8 VLGQGSSGVVYKVRHKPTGKIYALKKIhVDGDEEFRKQLLRELKTLRSCE-SPYVVKCYGAFYK----EGE---ISIVLE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 -----RLHRDLYtglKAGLSLETRL-QIALDVVEGIRFLHSQ-GLVHRDIKLKNVLLDKQNRAKITDLGFCKP-EAMMSG 707
Cdd:cd06623   80 ymdggSLADLLK---KVGKIPEPVLaYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKVlENTLDQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 --SIVGTPIHMAPELFTGKYDN-SVDVYAFGILFWYICSGsiKLPEAFERCASKDHLWNNVRRGTRPErLP--VFDEECW 782
Cdd:cd06623  157 cnTFVGTVTYMSPERIQGESYSyAADIWSLGLTLLECALG--KFPFLPPGQPSFFELMQAICDGPPPS-LPaeEFSPEFR 233
                        250
                 ....*....|....*
gi 564380513 783 QLMEACWDGDPSKRP 797
Cdd:cd06623  234 DFISACLQKDPKKRP 248
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
554-810 2.31e-15

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: 78.08  E-value: 2.31e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWG--GHFPCALKSVV------PPDEKHWNDLALEFHYMRSLPKHERLVDLHGSV-------I 618
Cdd:cd05099   16 LGKPLGEGCFGQVVRAEAYGidKSRPDQTVTVAvkmlkdNATDKDLADLISEMELMKLIGKHKNIINLLGVCtqegplyV 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 619 DYNYGGGSSVAVLLIMER-----LHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKI 693
Cdd:cd05099   96 IVEYAAKGNLREFLRARRppgpdYTFDITKVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNVMKI 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 694 TDLGFCKP-------EAMMSGSIvgtPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPeaferCASKDHLWN 763
Cdd:cd05099  176 ADFGLARGvhdidyyKKTSNGRL---PVKwMAPEaLFDRVYTHQSDVWSFGILMWEIFTlGGSPYP-----GIPVEELFK 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 564380513 764 NVRRGTRPERLPVFDEECWQLMEACWDGDPSKRPLLGIVQPILRSIM 810
Cdd:cd05099  248 LLREGHRMDKPSNCTHELYMLMRECWHAVPTQRPTFKQLVEALDKVL 294
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
553-736 2.44e-15

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: 76.96  E-value: 2.44e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKsVVPPDEKhwNDLAL---EFHYMRSLpKHERLVDLHGSV-------IDYNY 622
Cdd:cd06613    3 ELIQRIGSGTYGDVYKARNIATGELAAVK-VIKLEPG--DDFEIiqqEISMLKEC-RHPNIVAYFGSYlrrdklwIVMEY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 623 GGGSSVAvllimerlhrDLYTGLKAgLSletRLQIAL---DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFc 699
Cdd:cd06613   79 CGGGSLQ----------DIYQVTGP-LS---ELQIAYvcrETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGV- 143
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564380513 700 kpEAMMSGSI------VGTPIHMAPELF----TGKYDNSVDVYAFGI 736
Cdd:cd06613  144 --SAQLTATIakrksfIGTPYWMAPEVAaverKGGYDGKCDIWALGI 188
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
553-806 2.52e-15

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 77.00  E-value: 2.52e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVylcdnWGGHFPCALKSVVP---PDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIdynygggSSVA 629
Cdd:cd05072   10 KLVKKLGAGQFGEV-----WMGYYNNSTKVAVKtlkPGTMSVQAFLEEANLMKTL-QHDKLVRLYAVVT-------KEEP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHR-DLYTGLKAG----LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---P 701
Cdd:cd05072   77 IYIITEYMAKgSLLDFLKSDeggkVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARvieD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 EAMMSGSIVGTPIH-MAPELFT-GKYDNSVDVYAFGILFWYICS-GSIKLPEAfercaSKDHLWNNVRRGTRPERLPVFD 778
Cdd:cd05072  157 NEYTAREGAKFPIKwTAPEAINfGSFTIKSDVWSFGILLYEIVTyGKIPYPGM-----SNSDVMSALQRGYRMPRMENCP 231
                        250       260
                 ....*....|....*....|....*...
gi 564380513 779 EECWQLMEACWDGDPSKRPLLGIVQPIL 806
Cdd:cd05072  232 DELYDIMKTCWKEKAEERPTFDYLQSVL 259
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
553-806 2.54e-15

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: 77.00  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLcDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvavLL 632
Cdd:cd14063    3 EIKEVIGKGRFGRVHR-GRWHGDVAIKLLNIDYLNEEQLEAFKEEVAAYKNT-RHDNLVLFMGACMDPPH--------LA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERL--HRDLYTGL---KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKqNRAKITDLGFCKPEAMMSG 707
Cdd:cd14063   73 IVTSLckGRTLYSLIherKEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLEN-GRVVITDFGLFSLSGLLQP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 S-------IV-GTPIHMAPELFTG-----------KYDNSVDVYAFGILFWYICSGsiKLPeaFERCASKDHLWnNVRRG 768
Cdd:cd14063  152 GrredtlvIPnGWLCYLAPEIIRAlspdldfeeslPFTKASDVYAFGTVWYELLAG--RWP--FKEQPAESIIW-QVGCG 226
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 564380513 769 TRPERLPV-FDEECWQLMEACWDGDPSKRPLLGIVQPIL 806
Cdd:cd14063  227 KKQSLSQLdIGREVKDILMQCWAYDPEKRPTFSDLLRML 265
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
660-797 3.92e-15

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: 76.54  E-value: 3.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQN-----RAKITDLGFCKPEAMMSGS------IVGTPIHMAPELFTGKYDN- 727
Cdd:cd13982  107 QIASGLAHLHSLNIVHRDLKPQNILISTPNahgnvRAMISDFGLCKKLDVGRSSfsrrsgVAGTSGWIAPEMLSGSTKRr 186
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380513 728 ---SVDVYAFGILFWYICSGSiKLP--EAFERCAskdhlwnNVRRGT----RPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd13982  187 qtrAVDIFSLGCVFYYVLSGG-SHPfgDKLEREA-------NILKGKysldKLLSLGEHGPEAQDLIERMIDFDPEKRP 257
PTKc_PDGFR_beta cd05107
Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; ...
635-797 3.92e-15

Catalytic domain of the Protein Tyrosine Kinase, Platelet Derived Growth Factor Receptor beta; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. PDGFR beta is a receptor PTK (RTK) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding to its ligands, the PDGFs, leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR beta forms homodimers or heterodimers with PDGFR alpha, depending on the nature of the PDGF ligand. PDGF-BB and PDGF-DD induce PDGFR beta homodimerization. PDGFR signaling plays many roles in normal embryonic development and adult physiology. PDGFR beta signaling leads to a variety of cellular effects including the stimulation of cell growth and chemotaxis, as well as the inhibition of apoptosis and GAP junctional communication. It is critical in normal angiogenesis as it is involved in the recruitment of pericytes and smooth muscle cells essential for vessel stability. Aberrant PDGFR beta expression is associated with some human cancers. The continuously-active fusion proteins of PDGFR beta with COL1A1 and TEL are associated with dermatofibrosarcoma protuberans (DFSP) and a subset of chronic myelomonocytic leukemia (CMML), respectively. The PDGFR beta subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133238 [Multi-domain]  Cd Length: 401  Bit Score: 78.13  E-value: 3.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 ERLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpEAMMSGSIVGT-- 712
Cdd:cd05107  222 ERTRRDTLINESPALSYMDLVGFSYQVANGMEFLASKNCVHRDLAARNVLICEGKLVKICDFGLAR-DIMRDSNYISKgs 300
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 713 ---PIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPEaferCASKDHLWNNVRRGTRPERLPVFDEECWQLME 786
Cdd:cd05107  301 tflPLKwMAPEsIFNNLYTTLSDVWSFGILLWEIFTlGGTPYPE----LPMNEQFYNAIKRGYRMAKPAHASDEIYEIMQ 376
                        170
                 ....*....|.
gi 564380513 787 ACWDGDPSKRP 797
Cdd:cd05107  377 KCWEEKFEIRP 387
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
556-738 4.95e-15

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: 76.37  E-value: 4.95e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLC-DNWGGHfPCALKSVVPPDEKhwnD----LAL-EFHYMRSLpKHERLVDLHgSVIdynYGGGSsva 629
Cdd:cd07829    5 EKLGEGTYGVVYKAkDKKTGE-IVALKKIRLDNEE---EgipsTALrEISLLKEL-KHPNIVKLL-DVI---HTENK--- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHRDLYTGLKA---GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKPE 702
Cdd:cd07829   73 LYLVFEYCDQDLKKYLDKrpgPLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFGlaraFGIPL 152
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564380513 703 AMMSGSIVgTPIHMAPELFTG--KYDNSVDVYAFGILF 738
Cdd:cd07829  153 RTYTHEVV-TLWYRAPEILLGskHYSTAVDIWSVGCIF 189
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
556-808 5.16e-15

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: 76.21  E-value: 5.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYlcdnwGGHF----------PCALKSVVPPDEkhwNDLALEFHY---MRSLPKHERLVDLHGSVID--- 619
Cdd:cd05091   12 EELGEDRFGKVY-----KGHLfgtapgeqtqAVAIKTLKDKAE---GPLREEFRHeamLRSRLQHPNIVCLLGVVTKeqp 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 620 ----YNYGGGSSVAVLLIMERLHRDLYTG-----LKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLL-DKQN 689
Cdd:cd05091   84 msmiFSYCSHGDLHEFLVMRSPHSDVGSTdddktVKSTLEPADFLHIVTQIAAGMEYLSSHHVVHKDLATRNVLVfDKLN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 690 rAKITDLGFCKP------EAMMSGSIVgtPIH-MAPELFT-GKYDNSVDVYAFGILFWYICSGSIKlpeafERCASKDHl 761
Cdd:cd05091  164 -VKISDLGLFREvyaadyYKLMGNSLL--PIRwMSPEAIMyGKFSIDSDIWSYGVVLWEVFSYGLQ-----PYCGYSNQ- 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564380513 762 wnNVRRGTRPERLPVFDEEC----WQLMEACWDGDPSKRPLLGIVQPILRS 808
Cdd:cd05091  235 --DVIEMIRNRQVLPCPDDCpawvYTLMLECWNEFPSRRPRFKDIHSRLRT 283
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
553-806 5.61e-15

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: 75.83  E-value: 5.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCdNWGGHFPCALKSVvPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVidynygggSSVAVLL 632
Cdd:cd05073   14 KLEKKLGAGQFGEVWMA-TYNKHTKVAVKTM-KPGSMSVEAFLAEANVMKTL-QHDKLVKLHAVV--------TKEPIYI 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERLHR-DLYTGLKAG----LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---PEAM 704
Cdd:cd05073   83 ITEFMAKgSLLDFLKSDegskQPLPKLIDFSAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARvieDNEY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 705 MSGSIVGTPIH-MAPELFT-GKYDNSVDVYAFGILFWYICS-GSIKLPEafercASKDHLWNNVRRGTRPERLPVFDEEC 781
Cdd:cd05073  163 TAREGAKFPIKwTAPEAINfGSFTIKSDVWSFGILLMEIVTyGRIPYPG-----MSNPEVIRALERGYRMPRPENCPEEL 237
                        250       260
                 ....*....|....*....|....*
gi 564380513 782 WQLMEACWDGDPSKRPLLGIVQPIL 806
Cdd:cd05073  238 YNIMMRCWKNRPEERPTFEYIQSVL 262
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
655-811 5.80e-15

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: 75.46  E-value: 5.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 655 LQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpeAMMSGSIVGT-------PIH-MAPELFT-GKY 725
Cdd:cd05060   98 KELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSR--ALGAGSDYYRattagrwPLKwYAPECINyGKF 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 726 DNSVDVYAFGILFWYICS------GSIKLPEAFErcaskdhLWNNVRRGTRPERLPvfdEECWQLMEACWDGDPSKRPLL 799
Cdd:cd05060  176 SSKSDVWSYGVTLWEAFSygakpyGEMKGPEVIA-------MLESGERLPRPEECP---QEIYSIMLSCWKYRPEDRPTF 245
                        170
                 ....*....|..
gi 564380513 800 GIVQPILRSIMD 811
Cdd:cd05060  246 SELESTFRRDPE 257
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
559-797 6.02e-15

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


Pssm-ID: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 75.38  E-value: 6.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 559 GRGQYGVVYLCdNWgghfpcalksvVPPDE----KHWNDLALEFHYMrSLPKHERLVDLHGSVIDY-NYGGGSSVAVLli 633
Cdd:cd14060    2 GGGSFGSVYRA-IW-----------VSQDKevavKKLLKIEKEAEIL-SVLSHRNIIQFYGAILEApNYGIVTEYASY-- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 mERLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQG---LVHRDIKLKNVLLDKQNRAKITDLG---FCKPEAMMsg 707
Cdd:cd14060   67 -GSLFDYLNSNESEEMDMDQIMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGasrFHSHTTHM-- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 SIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGSI--KLPEAFERCaskdhlWNNVRRGTRPErLPvfdEEC--- 781
Cdd:cd14060  144 SLVGTFPWMAPEVIQSlPVSETCDTYSYGVVLWEMLTREVpfKGLEGLQVA------WLVVEKNERPT-IP---SSCprs 213
                        250
                 ....*....|....*..
gi 564380513 782 -WQLMEACWDGDPSKRP 797
Cdd:cd14060  214 fAELMRRCWEADVKERP 230
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
653-760 7.04e-15

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


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 76.63  E-value: 7.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 653 TRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPE----AMMSgSIVGTPIHMAPE-LFTGKYDN 727
Cdd:cd05571   97 TRFYGA-EIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGLCKEEisygATTK-TFCGTPEYLAPEvLEDNDYGR 174
                         90       100       110
                 ....*....|....*....|....*....|...
gi 564380513 728 SVDVYAFGILFWYICSGsiKLPeaFercASKDH 760
Cdd:cd05571  175 AVDWWGLGVVMYEMMCG--RLP--F---YNRDH 200
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
558-775 7.48e-15

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 76.55  E-value: 7.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYL----CDnwgGHFPCA--LKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGS---------VIDYNY 622
Cdd:cd05603    3 IGKGSFGKVLLakrkCD---GKFYAVkvLQKKTILKKKEQNHIMAERNVLLKNLKHPFLVGLHYSfqtseklyfVLDYVN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 623 GGgssvAVLLIMERLHRdlytglkaglSLETRLQI-ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK- 700
Cdd:cd05603   80 GG----ELFFHLQRERC----------FLEPRARFyAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFGLCKe 145
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380513 701 ---PEAMMSgSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsikLPEAFERCASKdhLWNNVRRgtRPERLP 775
Cdd:cd05603  146 gmePEETTS-TFCGTPEYLAPEVLRKEpYDRTVDWWCLGAVLYEMLYG---LPPFYSRDVSQ--MYDNILH--KPLHLP 216
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
661-796 9.41e-15

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


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 75.53  E-value: 9.41e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQG--LVHRDIKLKNVLLD-KQNRAKITDLGFCK-PEAMMSGSIVGTPIHMAPELFTGKYDNSVDVYAFGI 736
Cdd:cd14031  122 ILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATlMRTSFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGM 201
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564380513 737 LFWYICSGSIKLPEaferCASKDHLWNNVRRGTRPERL-PVFDEECWQLMEACWDGDPSKR 796
Cdd:cd14031  202 CMLEMATSEYPYSE----CQNAAQIYRKVTSGIKPASFnKVTDPEVKEIIEGCIRQNKSER 258
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
658-752 9.43e-15

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: 75.52  E-value: 9.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGI 736
Cdd:cd14209  107 AAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSKgYNKAVDWWALGV 186
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564380513 737 LFW-----------------Y--ICSGSIKLPEAF 752
Cdd:cd14209  187 LIYemaagyppffadqpiqiYekIVSGKVRFPSHF 221
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
556-797 9.73e-15

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 75.48  E-value: 9.73e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDN-WGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDynygggssVAVLLI- 633
Cdd:cd14046   12 QVLGKGAFGQVVKVRNkLDGRYYAIKKIKLRSESKNNSRILREVMLLSRL-NHQHVVRYYQAWIE--------RANLYIq 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERLHRD-LYTGLKAGLSLET----RL--QIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG--------- 697
Cdd:cd14046   83 MEYCEKStLRDLIDSGLFQDTdrlwRLfrQI----LEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGlatsnklnv 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 698 ------------FCKPEAMMSGSIVGTPIHMAPEL---FTGKYDNSVDVYAFGILFWYICsgsIKLPEAFERcaskDHLW 762
Cdd:cd14046  159 elatqdinkstsAALGSSGDLTGNVGTALYVAPEVqsgTKSTYNEKVDMYSLGIIFFEMC---YPFSTGMER----VQIL 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 564380513 763 NNVrRGTRPERLPVFDE----ECWQLMEACWDGDPSKRP 797
Cdd:cd14046  232 TAL-RSVSIEFPPDFDDnkhsKQAKLIRWLLNHDPAKRP 269
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
661-799 1.04e-14

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: 74.86  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP--EAMMSGSIVGTPIHMAPELFTGK-YDN-SVDVYAFGI 736
Cdd:cd14072  108 IVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEftPGNKLDTFCGSPPYAAPELFQGKkYDGpEVDVWSLGV 187
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564380513 737 LFWYICSGSikLPeaFERCASKDhLWNNVRRGTRpeRLPVF-DEECWQLMEACWDGDPSKRPLL 799
Cdd:cd14072  188 ILYTLVSGS--LP--FDGQNLKE-LRERVLRGKY--RIPFYmSTDCENLLKKFLVLNPSKRGTL 244
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
675-797 1.06e-14

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 74.88  E-value: 1.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 675 HRDIKLKNVLLDKQNRAKITDLGFCKP---EAMMSGSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGSikLPe 750
Cdd:cd08217  133 HRDLKPANIFLDSDNNVKLGDFGLARVlshDSSFAKTYVGTPYYMSPELLNEqSYDEKSDIWSLGCLIYELCALH--PP- 209
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 564380513 751 aFErCASKDHLWNNVRRGTRPeRLP-VFDEECWQLMEACWDGDPSKRP 797
Cdd:cd08217  210 -FQ-AANQLELAKKIKEGKFP-RIPsRYSSELNEVIKSMLNVDPDKRP 254
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
558-808 1.33e-14

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: 74.95  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSV---VPPDEKHWNDLALE--------FHYMRSLPKHERLVDLHGSVIDYNYGGGs 626
Cdd:cd14026    5 LSRGAFGTVSRARHADWRVTVAIKCLkldSPVGDSERNCLLKEaeilhkarFSYILPILGICNEPEFLGIVTEYMTNGS- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 627 svavllIMERLHR-DLYTGLKAGLSLETRLQIALdvveGIRFLH--SQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA 703
Cdd:cd14026   84 ------LNELLHEkDIYPDVAWPLRLRILYEIAL----GVNYLHnmSPPLLHHDLKTQNILLDGEFHVKIADFGLSKWRQ 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 M--------MSGSIVGTPIHMAPELF----TGKYDNSVDVYAFGILFWYICSGsiKLPeaFERCASKDHLWNNVRRGTRP 771
Cdd:cd14026  154 LsisqsrssKSAPEGGTIIYMPPEEYepsqKRRASVKHDIYSYAIIMWEVLSR--KIP--FEEVTNPLQIMYSVSQGHRP 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 564380513 772 ----ERLPV---FDEECWQLMEACWDGDPSKRP----LLGIVQPILRS 808
Cdd:cd14026  230 dtgeDSLPVdipHRATLINLIESGWAQNPDERPsflkCLIELEPVLRT 277
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
553-738 1.35e-14

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: 75.10  E-value: 1.35e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQeLGRGQYGVVYLCDNWGGHFPCALKSVVPP-DEKHWNDLAL-EFHYMRSLpKHERLVDLHgsvidynygggssvAV 630
Cdd:cd07847    5 KLSK-IGEGSYGVVFKCRNRETGQIVAIKKFVESeDDPVIKKIALrEIRMLKQL-KHPNLVNLI--------------EV 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLH-------RDLYTGLKA---GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK 700
Cdd:cd07847   69 FRRKRKLHlvfeycdHTVLNELEKnprGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFAR 148
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564380513 701 ----PEAMMSgSIVGTPIHMAPELFTG--KYDNSVDVYAFGILF 738
Cdd:cd07847  149 iltgPGDDYT-DYVATRWYRAPELLVGdtQYGPPVDVWAIGCVF 191
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
558-738 1.57e-14

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: 74.92  E-value: 1.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYL-CDNWGGHfPCALKSVVPPDEKHWND----LAL-EFHYMRSLpKHERLVDLHgSVidynYGGGSSVAvl 631
Cdd:cd07841    8 LGEGTYAVVYKaRDKETGR-IVAIKKIKLGERKEAKDginfTALrEIKLLQEL-KHPNIIGLL-DV----FGHKSNIN-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLHRDLYTGLKAG---LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK----PEAM 704
Cdd:cd07841   79 LVFEFMETDLEKVIKDKsivLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFGLARsfgsPNRK 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 564380513 705 MSGSIVgTPIHMAPELFTG--KYDNSVDVYAFGILF 738
Cdd:cd07841  159 MTHQVV-TRWYRAPELLFGarHYGVGVDMWSVGCIF 193
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
641-806 1.67e-14

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: 74.10  E-value: 1.67e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 641 LYTGLKAGLSLETRLQIALDVVEGIRFLH--SQGLVHRDIKLKNVLLDKQNRAKITDLG---FCKP--EAMMSGSiVGTP 713
Cdd:cd14064   82 LLHEQKRVIDLQSKLIIAVDVAKGMEYLHnlTQPIIHRDLNSHNILLYEDGHAVVADFGesrFLQSldEDNMTKQ-PGNL 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 714 IHMAPELFT--GKYDNSVDVYAFGILFWYICSGSIKLPEAFERCASKDHLWnnvrRGTRPERLPVFDEECWQLMEACWDG 791
Cdd:cd14064  161 RWMAPEVFTqcTRYSIKADVFSYALCLWELLTGEIPFAHLKPAAAAADMAY----HHIRPPIGYSIPKPISSLLMRGWNA 236
                        170
                 ....*....|....*
gi 564380513 792 DPSKRPLLGIVQPIL 806
Cdd:cd14064  237 EPESRPSFVEIVALL 251
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
658-744 1.84e-14

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 75.42  E-value: 1.84e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpEAMMSG----SIVGTPIHMAPELFTGK-YDNSVDVY 732
Cdd:cd05615  117 AAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCK-EHMVEGvttrTFCGTPDYIAPEIIAYQpYGRSVDWW 195
                         90
                 ....*....|..
gi 564380513 733 AFGILFWYICSG 744
Cdd:cd05615  196 AYGVLLYEMLAG 207
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
550-742 1.90e-14

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: 74.78  E-value: 1.90e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 550 RKPKLGQELGRGQYGVVYlCDNWGGHfPCALKSVVPPDEKHWndlALEFH-YMRSLPKHERLVDLHGS-VIDYNygggSS 627
Cdd:cd14142    5 RQITLVECIGKGRYGEVW-RGQWQGE-SVAVKIFSSRDEKSW---FRETEiYNTVLLRHENILGFIASdMTSRN----SC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 VAVLLIMERL-HRDLYTGL-KAGLSLETRLQIALDVVEGIRFLHS-----QG---LVHRDIKLKNVLLDKQNRAKITDLG 697
Cdd:cd14142   76 TQLWLITHYHeNGSLYDYLqRTTLDHQEMLRLALSAASGLVHLHTeifgtQGkpaIAHRDLKSKNILVKSNGQCCIADLG 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564380513 698 FCKPEAMMSGSI-------VGTPIHMAPELFTGKYDNS-------VDVYAFGILFWYIC 742
Cdd:cd14142  156 LAVTHSQETNQLdvgnnprVGTKRYMAPEVLDETINTDcfesykrVDIYAFGLVLWEVA 214
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
556-806 1.93e-14

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: 73.80  E-value: 1.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLcDNWGGHFPCALKSVVPPDEKHWNDLAlEFHYMRSLpKHERLVDLHGSVidynygggSSVAVLLIME 635
Cdd:cd14203    1 VKLGQGCFGEVWM-GTWNGTTKVAIKTLKPGTMSPEAFLE-EAQIMKKL-RHDKLVQLYAVV--------SEEPIYIVTE 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RL-HRDLYTGLKAG----LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSG 707
Cdd:cd14203   70 FMsKGSLLDFLKDGegkyLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLArliEDNEYTAR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 SIVGTPIH-MAPE--LFtGKYDNSVDVYAFGILFW-YICSGSIKLPEAFERcaskdHLWNNVRRGTRPERLPVFDEECWQ 783
Cdd:cd14203  150 QGAKFPIKwTAPEaaLY-GRFTIKSDVWSFGILLTeLVTKGRVPYPGMNNR-----EVLEQVERGYRMPCPPGCPESLHE 223
                        250       260
                 ....*....|....*....|...
gi 564380513 784 LMEACWDGDPSKRPLLGIVQPIL 806
Cdd:cd14203  224 LMCQCWRKDPEERPTFEYLQSFL 246
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
558-744 1.95e-14

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: 74.28  E-value: 1.95e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGH-FPCALKSVVPPD-EKHWNDLALEFHYMRSLpKHERLVDLHgsviDYNYGGGSsvaVLLIME 635
Cdd:cd14202   10 IGHGAFAVVFKGRHKEKHdLEVAVKCINKKNlAKSQTLLGKEIKILKEL-KHENIVALY----DFQEIANS---VYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RLHR-DLYTGLKAGLSL-ETRLQIALDVVEG-IRFLHSQGLVHRDIKLKNVLLD-----KQN----RAKITDLGFCK--P 701
Cdd:cd14202   82 YCNGgDLADYLHTMRTLsEDTIRLFLQQIAGaMKMLHSKGIIHRDLKPQNILLSysggrKSNpnniRIKIADFGFARylQ 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564380513 702 EAMMSGSIVGTPIHMAPE-LFTGKYDNSVDVYAFGILFWYICSG 744
Cdd:cd14202  162 NNMMAATLCGSPMYMAPEvIMSQHYDAKADLWSIGTIIYQCLTG 205
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
660-749 2.05e-14

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: 75.04  E-value: 2.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP----EAMMSgSIVGTPIHMAPELFT-GKYDNSVDVYAF 734
Cdd:cd05595  103 EIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKEgitdGATMK-TFCGTPEYLAPEVLEdNDYGRAVDWWGL 181
                         90
                 ....*....|....*
gi 564380513 735 GILFWYICSGsiKLP 749
Cdd:cd05595  182 GVVMYEMMCG--RLP 194
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
658-744 2.13e-14

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


Pssm-ID: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 75.22  E-value: 2.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpEAMMSG----SIVGTPIHMAPELFTG-KYDNSVDVY 732
Cdd:cd05591  102 AAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCK-EGILNGktttTFCGTPDYIAPEILQElEYGPSVDWW 180
                         90
                 ....*....|..
gi 564380513 733 AFGILFWYICSG 744
Cdd:cd05591  181 ALGVLMYEMMAG 192
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
606-813 2.16e-14

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: 74.67  E-value: 2.16e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 606 KHERLVDLHGSvidynYGGGSSVAVllIMERLHRDLYTGL--KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNV 683
Cdd:cd06657   75 QHENVVEMYNS-----YLVGDELWV--VMEFLEGGALTDIvtHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSI 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 684 LLDKQNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGSIklpeafercaskd 759
Cdd:cd06657  148 LLTHDGRVKLSDFGFCaqvSKEVPRRKSLVGTPYWMAPELISRlPYGPEVDIWSLGIMVIEMVDGEP------------- 214
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564380513 760 hlwnnvrrgtrperlPVFDEECWQLMEACWDGDPSKRPLLGIVQPILRSIMDRL 813
Cdd:cd06657  215 ---------------PYFNEPPLKAMKMIRDNLPPKLKNLHKVSPSLKGFLDRL 253
PTKc_CSF-1R cd05106
Catalytic domain of the Protein Tyrosine Kinase, Colony-Stimulating Factor-1 Receptor; PTKs ...
649-797 2.19e-14

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


Pssm-ID: 133237 [Multi-domain]  Cd Length: 374  Bit Score: 75.65  E-value: 2.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 649 LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVG----TPIH-MAPE-LFT 722
Cdd:cd05106  209 LDLDDLLRFSSQVAQGMDFLASKNCIHRDVAARNVLLTDGRVAKICDFGLARDIMNDSNYVVKgnarLPVKwMAPEsIFD 288
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564380513 723 GKYDNSVDVYAFGILFWYICS-GSIKLPEAfercASKDHLWNNVRRGTRPERlPVF-DEECWQLMEACWDGDPSKRP 797
Cdd:cd05106  289 CVYTVQSDVWSYGILLWEIFSlGKSPYPGI----LVNSKFYKMVKRGYQMSR-PDFaPPEIYSIMKMCWNLEPTERP 360
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
555-735 2.25e-14

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: 74.35  E-value: 2.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 555 GQELGRGQYGVVYLCDNWGGHFPCALKSV-----VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYnygggSSVA 629
Cdd:cd06651   12 GKLLGQGAFGRVYLCYDVDTGRELAAKQVqfdpeSPETSKEVSALECEIQLLKNL-QHERIVQYYGCLRDR-----AEKT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERL-HRDLYTGLKA--GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PEAM 704
Cdd:cd06651   86 LTIFMEYMpGGSVKDQLKAygALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKrlQTIC 165
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 564380513 705 MSG----SIVGTPIHMAPELFTGK-YDNSVDVYAFG 735
Cdd:cd06651  166 MSGtgirSVTGTPYWMSPEVISGEgYGRKADVWSLG 201
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
554-736 2.41e-14

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: 74.26  E-value: 2.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWGGHFPCALKsVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSvAVLLI 633
Cdd:cd06608   10 LVEVIGEGTYGKVYKARHKKTGQLAAIK-IMDIIEDEEEEIKLEINILRKFSNHPNIATFYGAFIKKDPPGGDD-QLWLV 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERLH----RDLYTGLKAGLSLETRLQIAL---DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEA 703
Cdd:cd06608   88 MEYCGggsvTDLVKGLRKKGKRLKEEWIAYilrETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSaqlDSTL 167
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564380513 704 MMSGSIVGTPIHMAPELFTGK------YDNSVDVYAFGI 736
Cdd:cd06608  168 GRRNTFIGTPYWMAPEVIACDqqpdasYDARCDVWSLGI 206
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
553-785 2.66e-14

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: 73.87  E-value: 2.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYL--CDNWGGHfpCALKSVV---PPDEKHWNDLALEFHYMRSLpKHERLVDLHgSVIDynygggSS 627
Cdd:cd14162    3 IVGKTLGHGSYAVVKKaySTKHKCK--VAIKIVSkkkAPEDYLQKFLPREIEVIKGL-KHPNLICFY-EAIE------TT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 VAVLLIMERLHR-DLYTGLKA-GLSLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---- 700
Cdd:cd14162   73 SRVYIIMELAENgDLLDYIRKnGALPEPQARRWFrQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFARgvmk 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 701 ---PEAMMSGSIVGTPIHMAPELFTGK-YDNSV-DVYAFGILFWYICSGsiKLPeaFErcaSKDH--LWNNVRRGTRPER 773
Cdd:cd14162  153 tkdGKPKLSETYCGSYAYASPEILRGIpYDPFLsDIWSMGVVLYTMVYG--RLP--FD---DSNLkvLLKQVQRRVVFPK 225
                        250
                 ....*....|..
gi 564380513 774 LPVFDEECWQLM 785
Cdd:cd14162  226 NPTVSEECKDLI 237
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
557-797 2.96e-14

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: 73.53  E-value: 2.96e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLCDN-WGGHFpCALKSV-VPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNygggssvAVLLIM 634
Cdd:cd06605    8 ELGEGNGGVVSKVRHrPSGQI-MAVKVIrLEIDEALQKQILRELDVLHKC-NSPYIVGFYGAFYSEG-------DISICM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 ErlhrdlytgLKAGLSLETRLQ------------IALDVVEGIRFLHSQ-GLVHRDIKLKNVLLDKQNRAKITDLGFC-K 700
Cdd:cd06605   79 E---------YMDGGSLDKILKevgriperilgkIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSgQ 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 701 PEAMMSGSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGsiKLPEAFERCASKD---HLWNNVRRGTrPERLP- 775
Cdd:cd06605  150 LVDSLAKTFVGTRSYMAPERISGgKYTVKSDIWSLGLSLVELATG--RFPYPPPNAKPSMmifELLSYIVDEP-PPLLPs 226
                        250       260
                 ....*....|....*....|...
gi 564380513 776 -VFDEECWQLMEACWDGDPSKRP 797
Cdd:cd06605  227 gKFSPDFQDFVSQCLQKDPTERP 249
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
557-797 3.02e-14

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


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 74.23  E-value: 3.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLcDNWGGHFpCALKSVVPPDEKHWNDlalEFH-YMRSLPKHERLVdlhGSVIDYNYGGGSSVAVLLIME 635
Cdd:cd14056    2 TIGKGRYGEVWL-GKYRGEK-VAVKIFSSRDEDSWFR---ETEiYQTVMLRHENIL---GFIAADIKSTGSWTQLWLITE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 -RLHRDLYTGLKAG-LSLETRLQIALDVVEGIRFLHSQ--------GLVHRDIKLKNVLLDKQNRAKITDLG--FCKPEA 703
Cdd:cd14056   74 yHEHGSLYDYLQRNtLDTEEALRLAYSAASGLAHLHTEivgtqgkpAIAHRDLKSKNILVKRDGTCCIADLGlaVRYDSD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 MMSGSI-----VGTPIHMAPELFTGKYDNS-------VDVYAFGILFWYIC----SGSI----KLPeaFERCASKDHLWN 763
Cdd:cd14056  154 TNTIDIppnprVGTKRYMAPEVLDDSINPKsfesfkmADIYSFGLVLWEIArrceIGGIaeeyQLP--YFGMVPSDPSFE 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564380513 764 NVR-----RGTRPE------RLPVFDEECwQLMEACWDGDPSKRP 797
Cdd:cd14056  232 EMRkvvcvEKLRPPipnrwkSDPVLRSMV-KLMQECWSENPHARL 275
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
652-744 3.40e-14

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: 74.56  E-value: 3.40e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 652 ETRLQI-ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP---EAMMSGSIVGTPIHMAPELFTGK-YD 726
Cdd:cd05590   95 EARARFyAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEgifNGKTTSTFCGTPDYIAPEILQEMlYG 174
                         90
                 ....*....|....*...
gi 564380513 727 NSVDVYAFGILFWYICSG 744
Cdd:cd05590  175 PSVDWWAMGVLLYEMLCG 192
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
558-797 3.70e-14

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: 73.60  E-value: 3.70e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaVLLIMER- 636
Cdd:cd06624   16 LGKGTFGVVYAARDLSTQVRIAIKEIPERDSREVQPLHEEIALHSRL-SHKNIVQYLGSVSEDGF-------FKIFMEQv 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 637 -------LHRDLYTGLK---AGLSLETRlQIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA-KITDLGFCKPEA-- 703
Cdd:cd06624   88 pggslsaLLRSKWGPLKdneNTIGYYTK-QI----LEGLKYLHDNKIVHRDIKGDNVLVNTYSGVvKISDFGTSKRLAgi 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 -MMSGSIVGTPIHMAPELF-TGK--YDNSVDVYAFGILFWYICSGS---IKL--PEA--FERCASKDHlwnnvrrgtrPE 772
Cdd:cd06624  163 nPCTETFTGTLQYMAPEVIdKGQrgYGPPADIWSLGCTIIEMATGKppfIELgePQAamFKVGMFKIH----------PE 232
                        250       260
                 ....*....|....*....|....*
gi 564380513 773 RLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd06624  233 IPESLSEEAKSFILRCFEPDPDKRA 257
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
554-799 3.73e-14

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: 73.56  E-value: 3.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLcDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSlPKHERLVDLHGS------VIDYNYGGGSS 627
Cdd:cd14151   12 VGQRIGSGSFGTVYK-GKWHGDVAVKMLNVTAPTPQQLQAFKNEVGVLRK-TRHVNILLFMGYstkpqlAIVTQWCEGSS 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 vavllIMERLHrdlytGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSG 707
Cdd:cd14151   90 -----LYHHLH-----IIETKFEMIKLIDIARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVKSRWSG 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 S-----IVGTPIHMAPELF----TGKYDNSVDVYAFGILFWYICSGSikLPeaFERCASKDHLWNNVRRGTRPERLPVFD 778
Cdd:cd14151  160 ShqfeqLSGSILWMAPEVIrmqdKNPYSFQSDVYAFGIVLYELMTGQ--LP--YSNINNRDQIIFMVGRGYLSPDLSKVR 235
                        250       260
                 ....*....|....*....|....*
gi 564380513 779 EEC----WQLMEACWDGDPSKRPLL 799
Cdd:cd14151  236 SNCpkamKRLMAECLKKKRDERPLF 260
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
660-805 3.92e-14

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: 73.99  E-value: 3.92e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFG 735
Cdd:cd06655  123 ECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCaqiTPEQSKRSTMVGTPYWMAPEVVTRKaYGPKVDIWSLG 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 736 ILFWYICSGsiKLPEAFERCASKDHL--WNNVRRGTRPERL-PVFDEecwqLMEACWDGDPSKR---------PLLGIVQ 803
Cdd:cd06655  203 IMAIEMVEG--EPPYLNENPLRALYLiaTNGTPELQNPEKLsPIFRD----FLNRCLEMDVEKRgsakellqhPFLKLAK 276

                 ..
gi 564380513 804 PI 805
Cdd:cd06655  277 PL 278
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
553-736 4.03e-14

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: 73.16  E-value: 4.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVY--LCdnwgghFP----CALKSV----VPPDekhWNDLALEFHYMrSLPKHERLVDLHGS------ 616
Cdd:cd06610    4 ELIEVIGSGATAVVYaaYC------LPkkekVAIKRIdlekCQTS---MDELRKEIQAM-SQCNHPNVVSYYTSfvvgde 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 617 ---VIDYnYGGGSsvaVLLIMErlhrdlyTGLKAGLSLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAK 692
Cdd:cd06610   74 lwlVMPL-LSGGS---LLDIMK-------SSYPRGGLDEAIIATVLkEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVK 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564380513 693 ITDLG----FCKPEAMMSGS---IVGTPIHMAPELFTGK--YDNSVDVYAFGI 736
Cdd:cd06610  143 IADFGvsasLATGGDRTRKVrktFVGTPCWMAPEVMEQVrgYDFKADIWSFGI 195
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
554-797 4.24e-14

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: 74.29  E-value: 4.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWG-----GHFPCALKSVVPPDE---KHWNDLALEFHYMRSLPKHERLVDLHGS--------- 616
Cdd:cd05100   16 LGKPLGEGCFGQVVMAEAIGidkdkPNKPVTVAVKMLKDDatdKDLSDLVSEMEMMKMIGKHKNIINLLGActqdgplyv 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 617 VIDYNYGGGssvavllIMERLHRDLYTGL----------KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLD 686
Cdd:cd05100   96 LVEYASKGN-------LREYLRARRPPGMdysfdtcklpEEQLTFKDLVSCAYQVARGMEYLASQKCIHRDLAARNVLVT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 687 KQNRAKITDLGFCKP-------EAMMSGSIvgtPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPEafercA 756
Cdd:cd05100  169 EDNVMKIADFGLARDvhnidyyKKTTNGRL---PVKwMAPEaLFDRVYTHQSDVWSFGVLLWEIFTlGGSPYPG-----I 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 564380513 757 SKDHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05100  241 PVEELFKLLKEGHRMDKPANCTHELYMIMRECWHAVPSQRP 281
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
555-797 4.59e-14

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: 73.18  E-value: 4.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 555 GQELGRGQYGVVYLCDNWGGHFPCALKSV-VPP--DEKHWNDLALEFHYMRSlpKHERLVDL-HGSVIDY---------- 620
Cdd:cd06629    6 GELIGKGTYGRVYLAMNATTGEMLAVKQVeLPKtsSDRADSRQKTVVDALKS--EIDTLKDLdHPNIVQYlgfeetedyf 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 621 ----NYGGGSSVAVLLimeRLHRDLYTGLKAGLSLEtrlqialdVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDL 696
Cdd:cd06629   84 siflEYVPGGSIGSCL---RKYGKFEEDLVRFFTRQ--------ILDGLAYLHSKGILHRDLKADNILVDLEGICKISDF 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 697 GFCKPEAMMSG-----SIVGTPIHMAPELFTGK---YDNSVDVYAFGILFWYICSGsiklpeafERCASKDHLWNNVRR- 767
Cdd:cd06629  153 GISKKSDDIYGnngatSMQGSVFWMAPEVIHSQgqgYSAKVDIWSLGCVVLEMLAG--------RRPWSDDEAIAAMFKl 224
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564380513 768 GTRPERLPVFDE-----ECWQLMEACWDGDPSKRP 797
Cdd:cd06629  225 GNKRSAPPVPEDvnlspEALDFLNACFAIDPRDRP 259
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
551-797 4.68e-14

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: 73.90  E-value: 4.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQELGRGQYGVVYLCDNWGGHFPCALKSVV--------PPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDyny 622
Cdd:cd05101   25 KLTLGKPLGEGCFGQVVMAEAVGIDKDKPKEAVTvavkmlkdDATEKDLSDLVSEMEMMKMIGKHKNIINLLGACTQ--- 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 623 gGGSSVAVLLIMERLHRDLYTGLKAGLSLETRLQIA----------------LDVVEGIRFLHSQGLVHRDIKLKNVLLD 686
Cdd:cd05101  102 -DGPLYVIVEYASKGNLREYLRARRPPGMEYSYDINrvpeeqmtfkdlvsctYQLARGMEYLASQKCIHRDLAARNVLVT 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 687 KQNRAKITDLGFCKP-------EAMMSGSIvgtPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPEafercA 756
Cdd:cd05101  181 ENNVMKIADFGLARDinnidyyKKTTNGRL---PVKwMAPEaLFDRVYTHQSDVWSFGVLMWEIFTlGGSPYPG-----I 252
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 564380513 757 SKDHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05101  253 PVEELFKLLKEGHRMDKPANCTNELYMMMRDCWHAVPSQRP 293
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
550-797 5.06e-14

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: 73.39  E-value: 5.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 550 RKPKLGQELGRGQYGVVYLC------DNWGGHfpCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGsvidYNYG 623
Cdd:cd05081    4 RHLKYISQLGKGNFGSVELCrydplgDNTGAL--VAVKQLQHSGPDQQRDFQREIQILKAL-HSDFIVKYRG----VSYG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 624 GGSSvAVLLIMERLH----RDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC 699
Cdd:cd05081   77 PGRR-SLRLVMEYLPsgclRDFLQRHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 700 KPEAMMSGSIV-----GTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYI---CSGSIKLPEAFERCASKD-------HLW 762
Cdd:cd05081  156 KLLPLDKDYYVvrepgQSPIFwYAPEsLSDNIFSRQSDVWSFGVVLYELftyCDKSCSPSAEFLRMMGCErdvpalcRLL 235
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564380513 763 NNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05081  236 ELLEEGQRLPAPPACPAEVHELMKLCWAPSPQDRP 270
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
558-742 5.50e-14

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: 72.79  E-value: 5.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLcdnwGGH-----FPCALKSVVPPD-EKHWNDLALEFHYMRSLpKHERLVDLhgsvIDYNYGGGSsvaVL 631
Cdd:cd14120    1 IGHGAFAVVFK----GRHrkkpdLPVAIKCITKKNlSKSQNLLGKEIKILKEL-SHENVVAL----LDCQETSSS---VY 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLHR-DL--YTGLKAGLSLET-RL---QIAldvvEGIRFLHSQGLVHRDIKLKNVLLDKQN---------RAKITD 695
Cdd:cd14120   69 LVMEYCNGgDLadYLQAKGTLSEDTiRVflqQIA----AAMKALHSKGIVHRDLKPQNILLSHNSgrkpspndiRLKIAD 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564380513 696 LGFCK--PEAMMSGSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFwYIC 742
Cdd:cd14120  145 FGFARflQDGMMAATLCGSPMYMAPEVIMSlQYDAKADLWSIGTIV-YQC 193
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
664-744 5.86e-14

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


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 73.99  E-value: 5.86e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 664 GIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpEAMMSG----SIVGTPIHMAPELFTGK-YDNSVDVYAFGILF 738
Cdd:cd05588  108 ALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCK-EGLRPGdttsTFCGTPNYIAPEILRGEdYGFSVDWWALGVLM 186

                 ....*.
gi 564380513 739 WYICSG 744
Cdd:cd05588  187 FEMLAG 192
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
661-808 6.85e-14

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: 72.30  E-value: 6.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP----EAMMSGSIVGT-PIH-MAPELFT-GKYDNSVDVYA 733
Cdd:cd05116  104 VSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKAlradENYYKAQTHGKwPVKwYAPECMNyYKFSSKSDVWS 183
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564380513 734 FGILFWYICSGSIKlPEAFERCASKDHLWNNVRRGTRPERLPVfdeECWQLMEACWDGDPSKRPLLGIVQPILRS 808
Cdd:cd05116  184 FGVLMWEAFSYGQK-PYKGMKGNEVTQMIEKGERMECPAGCPP---EMYDLMKLCWTYDVDERPGFAAVELRLRN 254
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
556-796 7.23e-14

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: 72.51  E-value: 7.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDN--WGGHFpcALKSVVPPD---EKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYgggssvaV 630
Cdd:cd05611    2 KPISKGAFGSVYLAKKrsTGDYF--AIKVLKKSDmiaKNQVTNVKAERAIMMIQGESPYVAKLYYSFQSKDY-------L 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLHR-DLYTGLK--AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP--EAMM 705
Cdd:cd05611   73 YLVMEYLNGgDCASLIKtlGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNglEKRH 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 706 SGSIVGTPIHMAPELFTGKYDNS-VDVYAFGILFWYICSGSiklpEAFErCASKDHLWNNV--RRGTRPERLPVF-DEEC 781
Cdd:cd05611  153 NKKFVGTPDYLAPETILGVGDDKmSDWWSLGCVIFEFLFGY----PPFH-AETPDAVFDNIlsRRINWPEEVKEFcSPEA 227
                        250
                 ....*....|....*
gi 564380513 782 WQLMEACWDGDPSKR 796
Cdd:cd05611  228 VDLINRLLCMDPAKR 242
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
554-806 7.31e-14

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: 72.79  E-value: 7.31e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLcDNWGGHFPCALKSVVPPDEKHWNDLAlEFHYMRSLpKHERLVDLHGSVidynygggSSVAVLLI 633
Cdd:cd05070   13 LIKRLGNGQFGEVWM-GTWNGNTKVAIKTLKPGTMSPESFLE-EAQIMKKL-KHDKLVQLYAVV--------SEEPIYIV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERLHR-DLYTGLKAG----LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---PEAMM 705
Cdd:cd05070   82 TEYMSKgSLLDFLKDGegraLKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARlieDNEYT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 706 SGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFW-YICSGSIKLPEAFERcaskdHLWNNVRRGTR---PERLPVFDE 779
Cdd:cd05070  162 ARQGAKFPIKwTAPEaALYGRFTIKSDVWSFGILLTeLVTKGRVPYPGMNNR-----EVLEQVERGYRmpcPQDCPISLH 236
                        250       260
                 ....*....|....*....|....*..
gi 564380513 780 EcwqLMEACWDGDPSKRPLLGIVQPIL 806
Cdd:cd05070  237 E---LMIHCWKKDPEERPTFEYLQGFL 260
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
655-797 7.54e-14

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: 72.52  E-value: 7.54e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 655 LQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCkpeAMMSGSIV-----GTPIHMAPELFTGK-YDNS 728
Cdd:cd14047  120 LEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLV---TSLKNDGKrtkskGTLSYMSPEQISSQdYGKE 196
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380513 729 VDVYAFGILFWYICSgsiKLPEAFErcasKDHLWNNVRRGTRPerlPVFDEECW---QLMEACWDGDPSKRP 797
Cdd:cd14047  197 VDIYALGLILFELLH---VCDSAFE----KSKFWTDLRNGILP---DIFDKRYKiekTIIKKMLSKKPEDRP 258
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
558-752 8.46e-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: 72.53  E-value: 8.46e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVY--LCDNwggHFPCALKSVV---PPDEKHWNDLALEfhyMRSLPKHERLVDLHGSVID-------YNYGGG 625
Cdd:cd14664    1 IGRGGAGTVYkgVMPN---GTLVAVKRLKgegTQGGDHGFQAEIQ---TLGMIRHRNIVRLRGYCSNpttnllvYEYMPN 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 626 SSVAVLLiMERLHRdlytglKAGLSLETRLQIALDVVEGIRFLH---SQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-- 700
Cdd:cd14664   75 GSLGELL-HSRPES------QPPLDWETRQRIALGSARGLAYLHhdcSPLIIHRDVKSNNILLDEEFEAHVADFGLAKlm 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564380513 701 --PEAMMSGSIVGTPIHMAPE-LFTGKYDNSVDVYAFGILFWYICSGSIKLPEAF 752
Cdd:cd14664  148 ddKDSHVMSSVAGSYGYIAPEyAYTGKVSEKSDVYSYGVVLLELITGKRPFDEAF 202
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
558-797 9.25e-14

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: 72.46  E-value: 9.25e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVV--PPDEKHwNDLALEFHYMRSLpKHERLVDLHGSVID---------YNYGGGS 626
Cdd:cd06621    9 LGEGAGGSVTKCRLRNTKTIFALKTITtdPNPDVQ-KQILRELEINKSC-ASPYIVKYYGAFLDeqdssigiaMEYCEGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 627 SvavlliMERLHRDLytgLKAGLSLETR--LQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGfCKPEAM 704
Cdd:cd06621   87 S------LDSIYKKV---KKKGGRIGEKvlGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFG-VSGELV 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 705 --MSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGSIKLPEAFERCASKDHLWNNVRRGTRPErLPvfDEE- 780
Cdd:cd06621  157 nsLAGTFTGTSYYMAPERIQGGpYSITSDVWSLGLTLLEVAQNRFPFPPEGEPPLGPIELLSYIVNMPNPE-LK--DEPe 233
                        250       260
                 ....*....|....*....|....*
gi 564380513 781 ---CW-----QLMEACWDGDPSKRP 797
Cdd:cd06621  234 ngiKWsesfkDFIEKCLEKDGTRRP 258
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
660-737 1.00e-13

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


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 72.83  E-value: 1.00e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFG 735
Cdd:cd06654  124 ECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCaqiTPEQSKRSTMVGTPYWMAPEVVTRKaYGPKVDIWSLG 203

                 ..
gi 564380513 736 IL 737
Cdd:cd06654  204 IM 205
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
632-738 1.05e-13

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 74.83  E-value: 1.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLH-RDLYTGLKAG--LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpeAM---- 704
Cdd:NF033483  84 IVMEYVDgRTLKDYIREHgpLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIAR--ALsstt 161
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 564380513 705 --MSGSIVGTPIHMAPELFTGKY-DNSVDVYAFGILF 738
Cdd:NF033483 162 mtQTNSVLGTVHYLSPEQARGGTvDARSDIYSLGIVL 198
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
543-809 1.12e-13

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: 72.26  E-value: 1.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 543 LQDVLL-HRKPKLGQELGRGQYGVV---YLCDNWGGHFPCALKsVVPPDEKHWNDLA---LEFHYMRSLpKHERLVDLHG 615
Cdd:cd05074    1 LKDVLIqEQQFTLGRMLGKGEFGSVreaQLKSEDGSFQKVAVK-MLKADIFSSSDIEeflREAACMKEF-DHPNVIKLIG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 616 SVIDYNYGGGSSVAVLLIMERLHRDLYTGLKAG--------LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDK 687
Cdd:cd05074   79 VSLRSRAKGRLPIPMVILPFMKHGDLHTFLLMSrigeepftLPLQTLVRFMIDIASGMEYLSSKNFIHRDLAARNCMLNE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 688 QNRAKITDLGFCKP----EAMMSGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSGSiKLPEAferCASKDHL 761
Cdd:cd05074  159 NMTVCVADFGLSKKiysgDYYRQGCASKLPVKwLALEsLADNVYTTHSDVWAFGVTMWEIMTRG-QTPYA---GVENSEI 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 564380513 762 WNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRPLLGIVQPILRSI 809
Cdd:cd05074  235 YNYLIKGNRLKQPPDCLEDVYELMCQCWSPEPKCRPSFQHLRDQLELI 282
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
630-750 1.19e-13

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: 71.67  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHRDLytgLKAGLSLE--------TRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN---RAKITDLGF 698
Cdd:cd14082   77 VFVVMEKLHGDM---LEMILSSEkgrlperiTKFLVT-QILVALRYLHSKNIVHCDLKPENVLLASAEpfpQVKLCDFGF 152
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564380513 699 CK--PEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGSIKLPE 750
Cdd:cd14082  153 ARiiGEKSFRRSVVGTPAYLAPEVLRNKgYNRSLDMWSVGVIIYVSLSGTFPFNE 207
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
658-809 1.24e-13

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


Pssm-ID: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 71.66  E-value: 1.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQG---LVHRDIKLKNVLLDK--------QNRAKITDLGFC----KPEAMmsgSIVGTPIHMAPELF- 721
Cdd:cd14061   98 AIQIARGMNYLHNEApvpIIHRDLKSSNILILEaienedleNKTLKITDFGLArewhKTTRM---SAAGTYAWMAPEVIk 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 722 TGKYDNSVDVYAFGILFWYICSGSIKLPEAfercaskDHLWNNVRRGTRPERLPVFDE--ECW-QLMEACWDGDPSKRPL 798
Cdd:cd14061  175 SSTFSKASDVWSYGVLLWELLTGEVPYKGI-------DGLAVAYGVAVNKLTLPIPSTcpEPFaQLMKDCWQPDPHDRPS 247
                        170
                 ....*....|.
gi 564380513 799 LGIVQPILRSI 809
Cdd:cd14061  248 FADILKQLENI 258
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
632-738 1.35e-13

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: 72.65  E-value: 1.35e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLHR-DLYTGL--KAGLSLE-TRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP--EAMM 705
Cdd:cd05599   78 LIMEFLPGgDMMTLLmkKDTLTEEeTRFYIA-ETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGlkKSHL 156
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564380513 706 SGSIVGTPIHMAPELFTGK-YDNSVDVYAFG-ILF 738
Cdd:cd05599  157 AYSTVGTPDYIAPEVFLQKgYGKECDWWSLGvIMY 191
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
557-738 1.36e-13

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: 72.30  E-value: 1.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLC-DNWGGHFpCALKSV-VPPDEkhwNDLAL----EFHYMRSL-----PKHERLVDLHGSVidynyGGG 625
Cdd:cd07863    7 EIGVGAYGTVYKArDPHSGHF-VALKSVrVQTNE---DGLPLstvrEVALLKRLeafdhPNIVRLMDVCATS-----RTD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 626 SSVAVLLIMERLHRDLYTGLKA----GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP 701
Cdd:cd07863   78 RETKVTLVFEHVDQDLRTYLDKvpppGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARI 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 564380513 702 EA--MMSGSIVGTPIHMAPE-LFTGKYDNSVDVYAFGILF 738
Cdd:cd07863  158 YScqMALTPVVVTLWYRAPEvLLQSTYATPVDMWSVGCIF 197
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
553-738 1.41e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK10 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 72.40  E-value: 1.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQeLGRGQYGVVYLC-DNWGGHFpCALKSVVPPDEKhwNDLAL----EFHYMRSLpKHERLVDLHGSVIdynygGGSS 627
Cdd:cd07845   11 KLNR-IGEGTYGIVYRArDTTSGEI-VALKKVRMDNER--DGIPIsslrEITLLLNL-RHPNIVELKEVVV-----GKHL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 VAVLLIMERLHRDLYTGLKAGLSLETRLQ---IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCK 700
Cdd:cd07845   81 DSIFLVMEYCEQDLASLLDNMPTPFSESQvkcLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFGlartYGL 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 564380513 701 PEAMMSGSIVgTPIHMAPELFTG--KYDNSVDVYAFGILF 738
Cdd:cd07845  161 PAKPMTPKVV-TLWYRAPELLLGctTYTTAIDMWAVGCIL 199
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
558-742 1.66e-13

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: 72.10  E-value: 1.66e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSV---VPPDEKHWNDLALEFHYMRSLpKHERLVDLHgSVIDYNYGGGSSVAVLLIM 634
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKKCrqeLSPSDKNRERWCLEVQIMKKL-NHPNVVSAR-DVPPELEKLSPNDLPLLAM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 E-----RLHRDL-----YTGLKaglSLETRlQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA---KITDLGFCKP 701
Cdd:cd13989   79 EycsggDLRKVLnqpenCCGLK---ESEVR-TLLSDISSAISYLHENRIIHRDLKPENIVLQQGGGRviyKLIDLGYAKE 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564380513 702 --EAMMSGSIVGTPIHMAPELF-TGKYDNSVDVYAFGIL-FWYIC 742
Cdd:cd13989  155 ldQGSLCTSFVGTLQYLAPELFeSKKYTCTVDYWSFGTLaFECIT 199
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
555-797 1.95e-13

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: 71.41  E-value: 1.95e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 555 GQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWND---------LALEFHYMRSLpKHERLVDLHGSVIDYN---- 621
Cdd:cd06628    5 GALIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKdrkksmldaLQREIALLREL-QHENIVQYLGSSSDANhlni 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 622 ---YGGGSSVAVLLimerlhrDLYTGLKAGLSLETRLQIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF 698
Cdd:cd06628   84 fleYVPGGSVATLL-------NNYGAFEESLVRNFVRQI----LKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 699 CKP-EA-MMSG-------SIVGTPIHMAPELF-TGKYDNSVDVYAFGILFWYICSGSIKLPEaFERCASKDHLWNNVrrg 768
Cdd:cd06628  153 SKKlEAnSLSTknngarpSLQGSVFWMAPEVVkQTSYTRKADIWSLGCLVVEMLTGTHPFPD-CTQMQAIFKIGENA--- 228
                        250       260
                 ....*....|....*....|....*....
gi 564380513 769 tRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd06628  229 -SPTIPSNISSEARDFLEKTFEIDHNKRP 256
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
606-796 1.96e-13

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: 72.35  E-value: 1.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 606 KHERLVDLHGS---------VIDYNYGGGssvavllIMERLHRDLYTglkaglsLETRLQI-ALDVVEGIRFLHSQGLVH 675
Cdd:cd05575   54 KHPFLVGLHYSfqtkdklyfVLDYVNGGE-------LFFHLQRERHF-------PEPRARFyAAEIASALGYLHSLNIIY 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 676 RDIKLKNVLLDKQNRAKITDLGFCKpEAMMSG----SIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsikLPE 750
Cdd:cd05575  120 RDLKPENILLDSQGHVVLTDFGLCK-EGIEPSdttsTFCGTPEYLAPEVLRKQpYDRTVDWWCLGAVLYEMLYG---LPP 195
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564380513 751 AFercaSKDH--LWNNVRRgtRPERLPV-FDEECWQLMEACWDGDPSKR 796
Cdd:cd05575  196 FY----SRDTaeMYDNILH--KPLRLRTnVSPSARDLLEGLLQKDRTKR 238
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
660-744 2.27e-13

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 72.16  E-value: 2.27e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILF 738
Cdd:PTZ00263 126 ELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFTLCGTPEYLAPEVIQSKgHGKAVDWWTMGVLL 205

                 ....*.
gi 564380513 739 WYICSG 744
Cdd:PTZ00263 206 YEFIAG 211
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
660-737 2.31e-13

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 71.68  E-value: 2.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFG 735
Cdd:cd06656  123 ECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCaqiTPEQSKRSTMVGTPYWMAPEVVTRKaYGPKVDIWSLG 202

                 ..
gi 564380513 736 IL 737
Cdd:cd06656  203 IM 204
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
661-744 2.43e-13

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: 70.83  E-value: 2.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF---CKPEAMMSgSIVGTPIHMAPELFtgKYDN----SVDVYA 733
Cdd:cd14075  110 IVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFsthAKRGETLN-TFCGSPPYAAPELF--KDEHyigiYVDIWA 186
                         90
                 ....*....|.
gi 564380513 734 FGILFWYICSG 744
Cdd:cd14075  187 LGVLLYFMVTG 197
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
558-738 2.58e-13

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: 71.21  E-value: 2.58e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHW--NDLALEFHYMRSLPKHERLVDLHGSvidYNYGGGssvaVLLIME 635
Cdd:cd07832    8 IGEGAHGIVFKAKDRETGETVALKKVALRKLEGGipNQALREIKALQACQGHPYVVKLRDV---FPHGTG----FVLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RLHRDLYTGLKAGLSLETRLQI---ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKPEAMMSGS 708
Cdd:cd07832   81 YMLSSLSEVLRDEERPLTEAQVkryMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGlarlFSEEDPRLYSH 160
                        170       180       190
                 ....*....|....*....|....*....|..
gi 564380513 709 IVGTPIHMAPELFTG--KYDNSVDVYAFGILF 738
Cdd:cd07832  161 QVATRWYRAPELLYGsrKYDEGVDLWAVGCIF 192
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
553-796 2.62e-13

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: 70.75  E-value: 2.62e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLA-LEFHYMRSLpKHERLVDLHGsviDYNygggSSVAVL 631
Cdd:cd14185    3 EIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKEDMIeSEILIIKSL-SHPNIVKLFE---VYE----TEKEIY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLHR-DLYTGLKAGLSL---ETRLQIaLDVVEGIRFLHSQGLVHRDIKLKNVLL----DKQNRAKITDLGFCKPEA 703
Cdd:cd14185   75 LILEYVRGgDLFDAIIESVKFtehDAALMI-IDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 MMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsikLPEAFERCASKDHLWNNVRRGTRPERLPVFD---E 779
Cdd:cd14185  154 GPIFTVCGTPTYVAPEILSEKgYGLEVDMWAAGVILYILLCG---FPPFRSPERDQEELFQIIQLGHYEFLPPYWDnisE 230
                        250
                 ....*....|....*..
gi 564380513 780 ECWQLMEACWDGDPSKR 796
Cdd:cd14185  231 AAKDLISRLLVVDPEKR 247
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
553-806 3.39e-13

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: 70.87  E-value: 3.39e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLcDNWGGHFPCALKSVvPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVidynygggSSVAVLL 632
Cdd:cd05069   15 RLDVKLGQGCFGEVWM-GTWNGTTKVAIKTL-KPGTMMPEAFLQEAQIMKKL-RHDKLVPLYAVV--------SEEPIYI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERLHR-DLYTGLKAG----LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---PEAM 704
Cdd:cd05069   84 VTEFMGKgSLLDFLKEGdgkyLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARlieDNEY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 705 MSGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFW-YICSGSIKLPEAFERcaskdHLWNNVRRGTR---PERLPvfd 778
Cdd:cd05069  164 TARQGAKFPIKwTAPEaALYGRFTIKSDVWSFGILLTeLVTKGRVPYPGMVNR-----EVLEQVERGYRmpcPQGCP--- 235
                        250       260
                 ....*....|....*....|....*...
gi 564380513 779 EECWQLMEACWDGDPSKRPLLGIVQPIL 806
Cdd:cd05069  236 ESLHELMKLCWKKDPDERPTFEYIQSFL 263
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
560-797 3.51e-13

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: 70.71  E-value: 3.51e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 560 RGQYGVVYLC--DNWGGHFpcALKsVVPPDEKHWNDlalefhyMRSLPKHER--LVDLHG-SVIDYNYGGGSSVAVLLIM 634
Cdd:cd05579    3 RGAYGRVYLAkkKSTGDLY--AIK-VIKKRDMIRKN-------QVDSVLAERniLSQAQNpFVVKLYYSFQGKKNLYLVM 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 ERLHR-DLYTGLKAGLSLE---TRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-----PEAMM 705
Cdd:cd05579   73 EYLPGgDLYSLLENVGALDedvARIYIA-EIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKvglvrRQIKL 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 706 SG-------------SIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsikLP--------EAFERCASKDHLWn 763
Cdd:cd05579  152 SIqkksngapekedrRIVGTPDYLAPEILLGQgHGKTVDWWSLGVILYEFLVG---IPpfhaetpeEIFQNILNGKIEW- 227
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564380513 764 nvrrgtrPErLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05579  228 -------PE-DPEVSDEAKDLISKLLTPDPEKRL 253
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
655-797 4.13e-13

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: 70.49  E-value: 4.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 655 LQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQ---NRAKITDLGFCKP-----------EAMMsgsivgtPIH-MAPE 719
Cdd:cd05036  119 LQLAQDVAKGCRYLEENHFIHRDIAARNCLLTCKgpgRVAKIGDFGMARDiyradyyrkggKAML-------PVKwMPPE 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 720 LF-TGKYDNSVDVYAFGILFWYICS-GSIKLPeaferCASKDHLWNNVRRGTR---PERLPVfdeECWQLMEACWDGDPS 794
Cdd:cd05036  192 AFlDGIFTSKTDVWSFGVLLWEIFSlGYMPYP-----GKSNQEVMEFVTSGGRmdpPKNCPG---PVYRIMTQCWQHIPE 263

                 ...
gi 564380513 795 KRP 797
Cdd:cd05036  264 DRP 266
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
553-797 4.87e-13

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: 70.52  E-value: 4.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVY----LCDNWGGHFPCALKSVV-PPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIdynyggGSS 627
Cdd:cd05057   10 EKGKVLGSGAFGTVYkgvwIPEGEKVKIPVAIKVLReETGPKANEEILDEAYVMASV-DHPHLVRLLGICL------SSQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 VAVLLIMERL---------HRDlytGLKAGLSLETRLQIAldvvEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF 698
Cdd:cd05057   83 VQLITQLMPLgclldyvrnHRD---NIGSQLLLNWCVQIA----KGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 699 CK------PEAMMSGSIVgtPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSGSIKLPEAFERCASKDHLwnnvRRGTR 770
Cdd:cd05057  156 AKlldvdeKEYHAEGGKV--PIKwMALEsIQYRIYTHKSDVWSYGVTVWELMTFGAKPYEGIPAVEIPDLL----EKGER 229
                        250       260
                 ....*....|....*....|....*..
gi 564380513 771 PERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05057  230 LPQPPICTIDVYMVLVKCWMIDAESRP 256
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
556-736 4.96e-13

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: 70.41  E-value: 4.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKsVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYN-YGGGSsvaVLLIM 634
Cdd:cd06639   28 ETIGKGTYGKVYKVTNKKDGSLAAVK-ILDPISDVDEEIEAEYNILRSLPNHPNVVKFYGMFYKADqYVGGQ---LWLVL 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 ERLHRDLYTGLKAG-LSLETRLQ------IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAM 704
Cdd:cd06639  104 ELCNGGSVTELVKGlLKCGQRLDeamisyILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSaqlTSARL 183
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564380513 705 MSGSIVGTPIHMAPEL------FTGKYDNSVDVYAFGI 736
Cdd:cd06639  184 RRNTSVGTPFWMAPEViaceqqYDYSYDARCDVWSLGI 221
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
558-807 5.31e-13

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: 69.73  E-value: 5.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDnWggHFPCALK--SVVPPDEKHWNDLALEFHYMRSlPKHERLVDLHGSV------IDYNYGGGSSva 629
Cdd:cd14062    1 IGSGSFGTVYKGR-W--HGDVAVKklNVTDPTPSQLQAFKNEVAVLRK-TRHVNILLFMGYMtkpqlaIVTQWCEGSS-- 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 vllimerLHRDLYTgLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF---------CK 700
Cdd:cd14062   75 -------LYKHLHV-LETKFEMLQLIDIARQTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFGLatvktrwsgSQ 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 701 PEAMMSGSIvgtpIHMAPELFTGK----YDNSVDVYAFGILFWYICSGSikLPeaFERCASKDHLWNNVRRG-TRPERLP 775
Cdd:cd14062  147 QFEQPTGSI----LWMAPEVIRMQdenpYSFQSDVYAFGIVLYELLTGQ--LP--YSHINNRDQILFMVGRGyLRPDLSK 218
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564380513 776 VFDE---ECWQLMEACWDGDPSKRPLLGIVQPILR 807
Cdd:cd14062  219 VRSDtpkALRRLMEDCIKFQRDERPLFPQILASLE 253
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
556-736 5.40e-13

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: 70.85  E-value: 5.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVV---PPDEKHWNDLALEFHYMRSLpKHERLVDLHGS---------VIDYNYG 623
Cdd:cd06635   31 REIGHGSFGAVYFARDVRTSEVVAIKKMSysgKQSNEKWQDIIKEVKFLQRI-KHPNSIEYKGCylrehtawlVMEYCLG 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 624 GGSsvavllimerlhrDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGfCKPEA 703
Cdd:cd06635  110 SAS-------------DLLEVHKKPLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFG-SASIA 175
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 564380513 704 MMSGSIVGTPIHMAPELF----TGKYDNSVDVYAFGI 736
Cdd:cd06635  176 SPANSFVGTPYWMAPEVIlamdEGQYDGKVDVWSLGI 212
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
632-813 5.92e-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: 69.63  E-value: 5.92e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIME-----RLHRDLytglkAGLSLETRLQI--ALDVVEGIRFLHSQGLV---HRDIKLKNVLL-------DKQNRA-KI 693
Cdd:cd14148   70 LVMEyarggALNRAL-----AGKKVPPHVLVnwAVQIARGMNYLHNEAIVpiiHRDLKSSNILIlepiendDLSGKTlKI 144
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 694 TDLGFCKP-EAMMSGSIVGTPIHMAPELFT-GKYDNSVDVYAFGILFWYICSGSIKLPEaFERCASKDHLWNNVRRGTRP 771
Cdd:cd14148  145 TDFGLAREwHKTTKMSAAGTYAWMAPEVIRlSLFSKSSDVWSFGVLLWELLTGEVPYRE-IDALAVAYGVAMNKLTLPIP 223
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564380513 772 ERLPvfdEECWQLMEACWDGDPSKRPLLGivqpilrSIMDRL 813
Cdd:cd14148  224 STCP---EPFARLLEECWDPDPHGRPDFG-------SILKRL 255
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
607-822 6.48e-13

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: 70.07  E-value: 6.48e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 607 HERLVDLHGSvidynYGGGSSVAVllIMERLHRDLYTGL--KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVL 684
Cdd:cd06658   78 HENVVDMYNS-----YLVGDELWV--VMEFLEGGALTDIvtHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSIL 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 685 LDKQNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGSIklpeafercaskdh 760
Cdd:cd06658  151 LTSDGRIKLSDFGFCaqvSKEVPKRKSLVGTPYWMAPEVISRlPYGTEVDIWSLGIMVIEMIDGEP-------------- 216
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564380513 761 lwnnvrrgtrperlPVFDEECWQLMEACWDGDPSKRPLLGIVQPILRSIMD-RLCKCDSERPS 822
Cdd:cd06658  217 --------------PYFNEPPLQAMRRIRDNLPPRVKDSHKVSSVLRGFLDlMLVREPSQRAT 265
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
558-796 6.67e-13

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: 69.56  E-value: 6.67e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLcdnwGGH----FPCALKSVvppDEKHWND-----LALEFHYMRSLpKHERLVDLHGSVIDYNYgggssv 628
Cdd:cd14009    1 IGRGSFATVWK----GRHkqtgEVVAIKEI---SRKKLNKklqenLESEIAILKSI-KHPNIVRLYDVQKTEDF------ 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 aVLLIMER---------LHRdlYTGLKAGLSLETRLQIAldvvEGIRFLHSQGLVHRDIKLKNVLLDKQNRA---KITDL 696
Cdd:cd14009   67 -IYLVLEYcaggdlsqyIRK--RGRLPEAVARHFMQQLA----SGLKFLRSKNIIHRDLKPQNLLLSTSGDDpvlKIADF 139
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 697 GFCK--PEAMMSGSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGsiKLPeaFeRCASKDHLWNNVRRGTRPER 773
Cdd:cd14009  140 GFARslQPASMAETLCGSPLYMAPEILQFqKYDAKADLWSVGAILFEMLVG--KPP--F-RGSNHVQLLRNIERSDAVIP 214
                        250       260
                 ....*....|....*....|....*.
gi 564380513 774 LPV---FDEECWQLMEACWDGDPSKR 796
Cdd:cd14009  215 FPIaaqLSPDCKDLLRRLLRRDPAER 240
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
649-813 7.46e-13

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: 69.84  E-value: 7.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 649 LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC-------KPEAMMSGS------------- 708
Cdd:cd14154   88 LPWAQRVRFAKDIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLArliveerLPSGNMSPSetlrhlkspdrkk 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 709 ---IVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGSIKLPEAFERcaSKDHLWNnvRRGTRPERLPVFDEECWQL 784
Cdd:cd14154  168 rytVVGNPYWMAPEMLNGRsYDEKVDIFSFGIVLCEIIGRVEADPDYLPR--TKDFGLN--VDSFREKFCAGCPPPFFKL 243
                        170       180
                 ....*....|....*....|....*....
gi 564380513 785 MEACWDGDPSKRPLLGIVQPILRSIMDRL 813
Cdd:cd14154  244 AFLCCDLDPEKRPPFETLEEWLEALYLHL 272
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
558-745 7.59e-13

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


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 70.03  E-value: 7.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCAL-------KSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHgsvidynYGGGSSVAV 630
Cdd:cd05613    8 LGTGAYGKVFLVRKVSGHDAGKLyamkvlkKATIVQKAKTAEHTRTERQVLEHIRQSPFLVTLH-------YAFQTDTKL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLHR-DLYTGLKAGLSL-ETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKPEA 703
Cdd:cd05613   81 HLILDYINGgELFTHLSQRERFtENEVQIYIgEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGlskeFLLDEN 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564380513 704 MMSGSIVGTPIHMAPELFTG---KYDNSVDVYAFGILFWYICSGS 745
Cdd:cd05613  161 ERAYSFCGTIEYMAPEIVRGgdsGHDKAVDWWSLGVLMYELLTGA 205
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
554-796 7.78e-13

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


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 69.80  E-value: 7.78e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYL--CDNWGGHFPCALKSVVPPDEKHWNDLALEFHY---MRSLPKHERLVDLHGSVIDynygGGSSV 628
Cdd:cd05049    9 LKRELGEGAFGKVFLgeCYNLEPEQDKMLVAVKTLKDASSPDARKDFEReaeLLTNLQHENIVKFYGVCTE----GDPLL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 AVLLIMErlHRDLYTGLKAG----------------LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAK 692
Cdd:cd05049   85 MVFEYME--HGDLNKFLRSHgpdaaflasedsapgeLTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 693 ITDLGfckpeamMSGSIVGT-----------PIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSGSiKLPeAFERcaSKD 759
Cdd:cd05049  163 IGDFG-------MSRDIYSTdyyrvgghtmlPIRwMPPEsILYRKFTTESDVWSFGVVLWEIFTYG-KQP-WFQL--SNT 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 564380513 760 HLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKR 796
Cdd:cd05049  232 EVIECITQGRLLQRPRTCPSEVYAVMLGCWKREPQQR 268
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
556-797 7.97e-13

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: 69.37  E-value: 7.97e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCdNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDL------------------HGSV 617
Cdd:cd05052   12 HKLGGGQYGEVYEG-VWKKYNLTVAVKTLKEDTMEVEEFLKEAAVMKEI-KHPNLVQLlgvctreppfyiitefmpYGNL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 618 IDYnygggssvavlliMERLHRDLYTGLkaglsleTRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG 697
Cdd:cd05052   90 LDY-------------LRECNREELNAV-------VLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 698 FCKpeaMMSGSIVGT------PIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS------GSIKLPEAFercaskdHLWN 763
Cdd:cd05052  150 LSR---LMTGDTYTAhagakfPIKwTAPEsLAYNKFSIKSDVWAFGVLLWEIATygmspyPGIDLSQVY-------ELLE 219
                        250       260       270
                 ....*....|....*....|....*....|....
gi 564380513 764 NVRRGTRPERLPvfdEECWQLMEACWDGDPSKRP 797
Cdd:cd05052  220 KGYRMERPEGCP---PKVYELMRACWQWNPSDRP 250
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
661-744 8.24e-13

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: 69.33  E-value: 8.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC-KPEAMMSGSI---VGTPIHMAPELFTGK--YDNSVDVYAF 734
Cdd:cd14078  110 IVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCaKPKGGMDHHLetcCGSPAYAAPELIQGKpyIGSEADVWSM 189
                         90
                 ....*....|
gi 564380513 735 GILFWYICSG 744
Cdd:cd14078  190 GVLLYALLCG 199
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
606-745 8.24e-13

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


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 70.13  E-value: 8.24e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 606 KHERLVDLHgsvidynYGGGSSVAVLLIMERLHR-DLYTGL-KAGLSLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKN 682
Cdd:cd05584   58 KHPFIVDLH-------YAFQTGGKLYLILEYLSGgELFMHLeREGIFMEDTACFYLaEITLALGHLHSLGIIYRDLKPEN 130
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564380513 683 VLLDKQNRAKITDLGFCKP---EAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGS 745
Cdd:cd05584  131 ILLDAQGHVKLTDFGLCKEsihDGTVTHTFCGTIEYMAPEILTRSgHGKAVDWWSLGALMYDMLTGA 197
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
554-744 8.57e-13

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 69.44  E-value: 8.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLcdnwGGHFPCALKSVVP------------PDEKHWNDLALEFHYMRSLpKHERLVDLH------- 614
Cdd:cd14076    5 LGRTLGEGEFGKVKL----GWPLPKANHRSGVqvaiklirrdtqQENCQTSKIMREINILKGL-THPNIVRLLdvlktkk 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 615 --GSVIDYnYGGGSSVAVLLIMERLHRDLYTGLKAGLsletrlqialdvVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAK 692
Cdd:cd14076   80 yiGIVLEF-VSGGELFDYILARRRLKDSVACRLFAQL------------ISGVAYLHKKGVVHRDLKLENLLLDKNRNLV 146
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564380513 693 ITDLGFC------KPEaMMSGSiVGTPIHMAPELFTGK--YDNS-VDVYAFGILFWYICSG 744
Cdd:cd14076  147 ITDFGFAntfdhfNGD-LMSTS-CGSPCYAAPELVVSDsmYAGRkADIWSCGVILYAMLAG 205
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
558-745 8.60e-13

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: 69.61  E-value: 8.60e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLC--DNWGGHFPCALKSVVPPD------EKHWNDLALEFHYMRSLPKHERLVDLhgsvIDyNYGggSSVA 629
Cdd:cd14181   18 IGRGVSSVVRRCvhRHTGQEFAVKIIEVTAERlspeqlEEVRSSTLKEIHILRQVSGHPSIITL----ID-SYE--SSTF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHR-DLYTGLKAGLSL---ETRlQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPE 702
Cdd:cd14181   91 IFLVFDLMRRgELFDYLTEKVTLsekETR-SIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSchlEPG 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 564380513 703 AMMSgSIVGTPIHMAPELFTGKYDNS-------VDVYAFGILFWYICSGS 745
Cdd:cd14181  170 EKLR-ELCGTPGYLAPEILKCSMDEThpgygkeVDLWACGVILFTLLAGS 218
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
648-744 8.63e-13

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 69.95  E-value: 8.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 648 GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA---KITDLGFCK--PEAMMSGSIVGTPIHMAPELFT 722
Cdd:cd14039   95 GLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLQEINGKivhKIIDLGYAKdlDQGSLCTSFVGTLQYLAPELFE 174
                         90       100
                 ....*....|....*....|...
gi 564380513 723 GK-YDNSVDVYAFGILFWYICSG 744
Cdd:cd14039  175 NKsYTVTVDYWSFGTMVFECIAG 197
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
558-744 8.86e-13

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: 70.44  E-value: 8.86e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSV---VPPDEKHWNDLALEFHYMRSLPKHERLVDLHGS---------VIDYNYGGG 625
Cdd:cd05617   23 IGRGSYAKVLLVRLKKNDQIYAMKVVkkeLVHDDEDIDWVQTEKHVFEQASSNPFLVGLHSCfqttsrlflVIEYVNGGD 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 626 ssvaVLLIMERLHRdlytglkagLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpEAMM 705
Cdd:cd05617  103 ----LMFHMQRQRK---------LPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCK-EGLG 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564380513 706 SG----SIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSG 744
Cdd:cd05617  169 PGdttsTFCGTPNYIAPEILRGEeYGFSVDWWALGVLMFEMMAG 212
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
649-800 9.08e-13

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: 69.08  E-value: 9.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 649 LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNR---AKITDLGFCK---------PEAMMsgSIVGTPIHM 716
Cdd:cd14156   86 LSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRgreAVVTDFGLARevgempandPERKL--SLVGSAFWM 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 717 APELFTGK-YDNSVDVYAFGILFWYICSGSIKLPEAFERcaSKDHlwnNVRRGTRPERLPVFDEECWQLMEACWDGDPSK 795
Cdd:cd14156  164 APEMLRGEpYDRKVDVFSFGIVLCEILARIPADPEVLPR--TGDF---GLDVQAFKEMVPGCPEPFLDLAASCCRMDAFK 238

                 ....*
gi 564380513 796 RPLLG 800
Cdd:cd14156  239 RPSFA 243
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
652-813 9.22e-13

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: 69.63  E-value: 9.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 652 ETRL---QIA---LDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCkpeAMMSG------SIVGTPIHMAPE 719
Cdd:cd06659  111 QTRLneeQIAtvcEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFC---AQISKdvpkrkSLVGTPYWMAPE 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 720 LFT-GKYDNSVDVYAFGILFWYICSGsiklpeafercaskdhlwnnvrrgtRPerlPVFDEECWQLMEACWDGDPSKRPL 798
Cdd:cd06659  188 VISrCPYGTEVDIWSLGIMVIEMVDG-------------------------EP---PYFSDSPVQAMKRLRDSPPPKLKN 239
                        170
                 ....*....|....*
gi 564380513 799 LGIVQPILRSIMDRL 813
Cdd:cd06659  240 SHKASPVLRDFLERM 254
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
661-738 1.02e-12

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: 69.17  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG------------------FCKPEAMMS--GSIVGTPIHMAPEL 720
Cdd:cd05581  110 IVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGtakvlgpdsspestkgdaDSQIAYNQAraASFVGTAEYVSPEL 189
                         90       100
                 ....*....|....*....|
gi 564380513 721 FTGKY-DNSVDVYAFG-ILF 738
Cdd:cd05581  190 LNEKPaGKSSDLWALGcIIY 209
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
553-799 1.06e-12

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: 68.83  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLA-----LEFHYMRSLPKHERLVDlhgSVIDYNYgggSS 627
Cdd:cd14102    3 QVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTEWGTLNgvmvpLEIVLLKKVGSGFRGVI---KLLDWYE---RP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 VAVLLIMER--LHRDLYTGL--KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN-RAKITDLGfckpe 702
Cdd:cd14102   77 DGFLIVMERpePVKDLFDFIteKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRTgELKLIDFG----- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 703 ammSGSIV---------GTPIHMAPEL--FTGKYDNSVDVYAFGILFWYICSGSIKLPEAFERCASKDHLwnnvRRGTRP 771
Cdd:cd14102  152 ---SGALLkdtvytdfdGTRVYSPPEWirYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGRLYF----RRRVSP 224
                        250       260
                 ....*....|....*....|....*...
gi 564380513 772 erlpvfdeECWQLMEACWDGDPSKRPLL 799
Cdd:cd14102  225 --------ECQQLIKWCLSLRPSDRPTL 244
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
553-746 1.06e-12

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: 69.04  E-value: 1.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVvppDEKHWNDLALEfhymRSLPKH-ERLVDL-HGSVID-YNYGGGSSVA 629
Cdd:cd14165    4 ILGINLGEGSYAKVKSAYSERLKCNVAIKII---DKKKAPDDFVE----KFLPRElEILARLnHKSIIKtYEIFETSDGK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHR-DLYTGLKAGLSLETRL------QIALdvveGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP- 701
Cdd:cd14165   77 VYIVMELGVQgDLLEFIKLRGALPEDVarkmfhQLSS----AIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSKRc 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564380513 702 ------EAMMSGSIVGTPIHMAPELFTGK-YDNSV-DVYAFGILFWYICSGSI 746
Cdd:cd14165  153 lrdengRIVLSKTFCGSAAYAAPEVLQGIpYDPRIyDIWSLGVILYIMVCGSM 205
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
556-746 1.11e-12

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: 68.95  E-value: 1.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVVP---PDEKHWNDLALEFHYMRSLpKHERLVDLHgSVIDynygggSSVAVLL 632
Cdd:cd14073    7 ETLGKGTYGKVKLAIERATGREVAIKSIKKdkiEDEQDMVRIRREIEIMSSL-NHPHIIRIY-EVFE------NKDKIVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERLHR-DLYTGL--KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKPEAMm 705
Cdd:cd14073   79 VMEYASGgELYDYIseRRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGlsnlYSKDKLL- 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564380513 706 sGSIVGTPIHMAPELFTGK--YDNSVDVYAFGILFWYICSGSI 746
Cdd:cd14073  158 -QTFCGSPLYASPEIVNGTpyQGPEVDCWSLGVLLYTLVYGTM 199
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
557-736 1.15e-12

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: 69.29  E-value: 1.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGS---------VIDYNYGGgss 627
Cdd:cd06644   19 ELGDGAFGKVYKAKNKETGALAAAKVIETKSEEELEDYMVEIEILATC-NHPYIVKLLGAfywdgklwiMIEFCPGG--- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 vAVLLIMERLHRdlytGLKaglslETRLQ-IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA--- 703
Cdd:cd06644   95 -AVDAIMLELDR----GLT-----EPQIQvICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVSAKNVktl 164
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564380513 704 MMSGSIVGTPIHMAPELF---TGK---YDNSVDVYAFGI 736
Cdd:cd06644  165 QRRDSFIGTPYWMAPEVVmceTMKdtpYDYKADIWSLGI 203
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
558-809 1.30e-12

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 68.91  E-value: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCdNWGGHFPCALKSVVPPDEkhwnDLALEFHYMR------SLPKHERLVDLHGS---------VIDYNY 622
Cdd:cd14146    2 IGVGGFGKVYRA-TWKGQEVAVKAARQDPDE----DIKATAESVRqeaklfSMLRHPNIIKLEGVcleepnlclVMEFAR 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 623 GGGssvavllimerLHRDLYTGLKAGLSLETR-------LQIALDVVEGIRFLHSQGLV---HRDIKLKNVLL------- 685
Cdd:cd14146   77 GGT-----------LNRALAAANAAPGPRRARripphilVNWAVQIARGMLYLHEEAVVpilHRDLKSSNILLlekiehd 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 686 DKQNRA-KITDLGFCKP-EAMMSGSIVGTPIHMAPELF-TGKYDNSVDVYAFGILFWYICSGSIK------LPEAFERCA 756
Cdd:cd14146  146 DICNKTlKITDFGLAREwHRTTKMSAAGTYAWMAPEVIkSSLFSKGSDIWSYGVLLWELLTGEVPyrgidgLAVAYGVAV 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564380513 757 SKDHLwnnvrrgTRPERLPvfdEECWQLMEACWDGDPSKRPLLGIVQPILRSI 809
Cdd:cd14146  226 NKLTL-------PIPSTCP---EPFAKLMKECWEQDPHIRPSFALILEQLTAI 268
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
657-744 1.32e-12

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: 68.96  E-value: 1.32e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 657 IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN---RAKITDLGFCK--PEAMMSGSIVGTPIHMAPELF----TGKYDN 727
Cdd:cd14084  116 YFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEeecLIKITDFGLSKilGETSLMKTLCGTPTYLAPEVLrsfgTEGYTR 195
                         90
                 ....*....|....*..
gi 564380513 728 SVDVYAFGILFWYICSG 744
Cdd:cd14084  196 AVDCWSLGVILFICLSG 212
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
554-797 1.50e-12

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


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 68.60  E-value: 1.50e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVY---LCDNWGGHFPCALKSVVPPDEKHWNDLALEFHY-MRSLpKHERLVDLHGSVIDynygggssVA 629
Cdd:cd05056   10 LGRCIGEGQFGDVYqgvYMSPENEKIAVAVKTCKNCTSPSVREKFLQEAYiMRQF-DHPHIVKLIGVITE--------NP 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLH----RDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---PE 702
Cdd:cd05056   81 VWIVMELAPlgelRSYLQVNKYSLDLASLILYAYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRymeDE 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 703 AMMSGSIVGTPIH-MAPELFT-GKYDNSVDVYAFGILFWYICSGSIKlpeAFERCASKDHLwNNVRRGtrpERLPVfDEE 780
Cdd:cd05056  161 SYYKASKGKLPIKwMAPESINfRRFTSASDVWMFGVCMWEILMLGVK---PFQGVKNNDVI-GRIENG---ERLPM-PPN 232
                        250       260
                 ....*....|....*....|.
gi 564380513 781 C----WQLMEACWDGDPSKRP 797
Cdd:cd05056  233 CpptlYSLMTKCWAYDPSKRP 253
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
640-796 1.53e-12

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: 68.47  E-value: 1.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 640 DLYTGLKA--GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSG---------- 707
Cdd:cd14010   80 DLETLLRQdgNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGLARREGEILKelfgqfsdeg 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 ---------SIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSG-----SIKLPEAFERCASKDHLWNNVRRGTRPE 772
Cdd:cd14010  160 nvnkvskkqAKRGTPYYMAPELFQGGvHSFASDLWALGCVLYEMFTGkppfvAESFTELVEKILNEDPPPPPPKVSSKPS 239
                        170       180
                 ....*....|....*....|....
gi 564380513 773 rlpvfdEECWQLMEACWDGDPSKR 796
Cdd:cd14010  240 ------PDFKSLLKGLLEKDPAKR 257
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
661-788 1.62e-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: 68.57  E-value: 1.62e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQG--LVHRDIKLKNVLLD-KQNRAKITDLGFCK-PEAMMSGSIVGTPIHMAPELFTGKYDNSVDVYAFGI 736
Cdd:cd14032  113 ILKGLLFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATlKRASFAKSVIGTPEFMAPEMYEEHYDESVDVYAFGM 192
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564380513 737 LFWYICSGSIKLPEaferCASKDHLWNNVRRGTRPERL-PVFDEECWQLMEAC 788
Cdd:cd14032  193 CMLEMATSEYPYSE----CQNAAQIYRKVTCGIKPASFeKVTDPEIKEIIGEC 241
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
641-807 1.65e-12

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: 69.09  E-value: 1.65e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 641 LYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG---------FCKpeAMMSGSIvg 711
Cdd:cd05050  119 KCGLNPLPLSCTEQLCIAKQVAAGMAYLSERKFVHRDLATRNCLVGENMVVKIADFGlsrniysadYYK--ASENDAI-- 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 712 tPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSGSIKLPEAFercaSKDHLWNNVRRGTR---PERLPVfdeECWQLME 786
Cdd:cd05050  195 -PIRwMPPEsIFYNRYTTESDVWAYGVVLWEIFSYGMQPYYGM----AHEEVIYYVRDGNVlscPDNCPL---ELYNLMR 266
                        170       180
                 ....*....|....*....|.
gi 564380513 787 ACWDGDPSKRPLLGIVQPILR 807
Cdd:cd05050  267 LCWSKLPSDRPSFASINRILQ 287
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
661-788 1.71e-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: 68.92  E-value: 1.71e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQG--LVHRDIKLKNVLLD-KQNRAKITDLGFCK-PEAMMSGSIVGTPIHMAPELFTGKYDNSVDVYAFGI 736
Cdd:cd14030  137 ILKGLQFLHTRTppIIHRDLKCDNIFITgPTGSVKIGDLGLATlKRASFAKSVIGTPEFMAPEMYEEKYDESVDVYAFGM 216
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564380513 737 LFWYICSGSIKLPEaferCASKDHLWNNVRRGTRPERL-PVFDEECWQLMEAC 788
Cdd:cd14030  217 CMLEMATSEYPYSE----CQNAAQIYRRVTSGVKPASFdKVAIPEVKEIIEGC 265
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
558-796 1.73e-12

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: 69.66  E-value: 1.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPP------DEKHwndLALEFHYMRSLPKHERLVDLHGS---------VIDYNY 622
Cdd:cd05602   15 IGKGSFGKVLLARHKSDEKFYAVKVLQKKailkkkEEKH---IMSERNVLLKNVKHPFLVGLHFSfqttdklyfVLDYIN 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 623 GGGssvavllIMERLHRDLytglkagLSLETRLQI-ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP 701
Cdd:cd05602   92 GGE-------LFYHLQRER-------CFLEPRARFyAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKE 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 EAMMSG---SIVGTPIHMAPE-LFTGKYDNSVDVYAFGILFWYICSGsikLPEAFERCASKdhLWNNVRrgTRPERL-PV 776
Cdd:cd05602  158 NIEPNGttsTFCGTPEYLAPEvLHKQPYDRTVDWWCLGAVLYEMLYG---LPPFYSRNTAE--MYDNIL--NKPLQLkPN 230
                        250       260
                 ....*....|....*....|
gi 564380513 777 FDEECWQLMEACWDGDPSKR 796
Cdd:cd05602  231 ITNSARHLLEGLLQKDRTKR 250
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
551-796 1.82e-12

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: 68.20  E-value: 1.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQELGRGQYGVVYLCDNWGGHFPCALKSVvppDEKHWNDLALEFHYMR-----SLPKHERLVDLHgSVIdynyggG 625
Cdd:cd14663    1 RYELGRTLGEGTFAKVKFARNTKTGESVAIKII---DKEQVAREGMVEQIKReiaimKLLRHPNIVELH-EVM------A 70
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 626 SSVAVLLIMERLHR-DLYTGLKAGLSL--ETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-P 701
Cdd:cd14663   71 TKTKIFFVMELVTGgELFSKIAKNGRLkeDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSAlS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 EAMMSGSIV----GTPIHMAPELFTGK-YDNS-VDVYAFGILFWYICSGSikLPEAFERCASkdhLWNNVRRGtRPERLP 775
Cdd:cd14663  151 EQFRQDGLLhttcGTPNYVAPEVLARRgYDGAkADIWSCGVILFVLLAGY--LPFDDENLMA---LYRKIMKG-EFEYPR 224
                        250       260
                 ....*....|....*....|.
gi 564380513 776 VFDEECWQLMEACWDGDPSKR 796
Cdd:cd14663  225 WFSPGAKSLIKRILDPNPSTR 245
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
537-744 1.95e-12

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: 69.68  E-value: 1.95e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 537 SLESRSLQDVLLHRKpklgqeLGRGQYGVVYLCDNWGGHFPCALKSV---VPPDEKHWNDLALEFHYMRSLPKHERLVDL 613
Cdd:cd05618   13 ASSSLGLQDFDLLRV------IGRGSYAKVLLVRLKKTERIYAMKVVkkeLVNDDEDIDWVQTEKHVFEQASNHPFLVGL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 614 HGS---------VIDYNYGGGssvaVLLIMERLHRdlytglkagLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVL 684
Cdd:cd05618   87 HSCfqtesrlffVIEYVNGGD----LMFHMQRQRK---------LPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVL 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564380513 685 LDKQNRAKITDLGFCKpEAMMSG----SIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSG 744
Cdd:cd05618  154 LDSEGHIKLTDYGMCK-EGLRPGdttsTFCGTPNYIAPEILRGEdYGFSVDWWALGVLMFEMMAG 217
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
639-813 2.22e-12

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: 68.06  E-value: 2.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 639 RDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC-----------------KP 701
Cdd:cd14221   78 RGIIKSMDSHYPWSQRVSFAKDIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLArlmvdektqpeglrslkKP 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 EAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGSIKLPEAFERCASkdhLWNNVR----RGTRPERLPV 776
Cdd:cd14221  158 DRKKRYTVVGNPYWMAPEMINGRsYDEKVDVFSFGIVLCEIIGRVNADPDYLPRTMD---FGLNVRgfldRYCPPNCPPS 234
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 564380513 777 FdeecWQLMEACWDGDPSKRPLLGIVQPILRSIMDRL 813
Cdd:cd14221  235 F----FPIAVLCCDLDPEKRPSFSKLEHWLETLRMHL 267
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
629-739 2.25e-12

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: 68.11  E-value: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 AVLLIMERLHR-DLYTGLKAGLSL-ETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA---------KITDL 696
Cdd:cd14201   79 SVFLVMEYCNGgDLADYLQAKGTLsEDTIRVFLqQIAAAMRILHSKGIIHRDLKPQNILLSYASRKkssvsgiriKIADF 158
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564380513 697 GFCK--PEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFW 739
Cdd:cd14201  159 GFARylQSNMMAATLCGSPMYMAPEVIMSQhYDAKADLWSIGTVIY 204
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
547-746 2.31e-12

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: 68.06  E-value: 2.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 547 LLHRKPKLgQELGRGQYGVVYLCDNWGGHFpCALKSVVP---PDEKHWNDLALEFHYMRSLpKHERLVDLHgSVIDynyg 623
Cdd:cd14161    1 LKHRYEFL-ETLGKGTYGRVKKARDSSGRL-VAIKSIRKdriKDEQDLLHIRREIEIMSSL-NHPHIISVY-EVFE---- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 624 ggSSVAVLLIMERLHR-DLYTGL--KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC- 699
Cdd:cd14161   73 --NSSKIVIVMEYASRgDLYDYIseRQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSn 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564380513 700 --KPEAMMSgSIVGTPIHMAPELFTGK-YDN-SVDVYAFGILFWYICSGSI 746
Cdd:cd14161  151 lyNQDKFLQ-TYCGSPLYASPEIVNGRpYIGpEVDSWSLGVLLYILVHGTM 200
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
556-736 2.38e-12

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: 68.90  E-value: 2.38e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVV---PPDEKHWNDLALEFHYMRSLpKHERLVDLHGS---------VIDYNYG 623
Cdd:cd06634   21 REIGHGSFGAVYFARDVRNNEVVAIKKMSysgKQSNEKWQDIIKEVKFLQKL-RHPNTIEYRGCylrehtawlVMEYCLG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 624 GGSsvavllimerlhrDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA 703
Cdd:cd06634  100 SAS-------------DLLEVHKKPLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMA 166
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 564380513 704 mMSGSIVGTPIHMAPELF----TGKYDNSVDVYAFGI 736
Cdd:cd06634  167 -PANSFVGTPYWMAPEVIlamdEGQYDGKVDVWSLGI 202
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
559-796 2.40e-12

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: 68.23  E-value: 2.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 559 GRGQYGVVYLCdNWGGHfPCALKSVVPPDEKHW-NDLALefhYMRSLPKHERLVdlhGSVIDYNYGGGSSVAVLLIME-R 636
Cdd:cd13998    4 GKGRFGEVWKA-SLKNE-PVAVKIFSSRDKQSWfREKEI---YRTPMLKHENIL---QFIAADERDTALRTELWLVTAfH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 637 LHRDLYTGLKAG-LSLETRLQIALDVVEGIRFLHSQ---------GLVHRDIKLKNVLLDKQNRAKITDLGFCkpeAMMS 706
Cdd:cd13998   76 PNGSL*DYLSLHtIDWVSLCRLALSVARGLAHLHSEipgctqgkpAIAHRDLKSKNILVKNDGTCCIADFGLA---VRLS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 707 GSI----------VGTPIHMAPELFTGKYDNS-------VDVYAFGILFWYICS------GSI---KLP---EAFERCAS 757
Cdd:cd13998  153 PSTgeednanngqVGTKRYMAPEVLEGAINLRdfesfkrVDIYAMGLVLWEMASrctdlfGIVeeyKPPfysEVPNHPSF 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564380513 758 KDHLWNNVRRGTRPERLPVF--DEECWQL---MEACWDGDPSKR 796
Cdd:cd13998  233 EDMQEVVVRDKQRPNIPNRWlsHPGLQSLaetIEECWDHDAEAR 276
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
556-797 2.55e-12

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: 67.80  E-value: 2.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVVPP--------DEKHWNDLALEFHYMRSLPK--HERLVdlhgSVIDY----- 620
Cdd:cd14004    6 KEMGEGAYGQVNLAIYKSKGKEVVIKFIFKErilvdtwvRDRKLGTVPLEIHILDTLNKrsHPNIV----KLLDFfedde 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 621 NYgggssvavLLIMER--LHRDLYT--GLKAGL-SLETRLqIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITD 695
Cdd:cd14004   82 FY--------YLVMEKhgSGMDLFDfiERKPNMdEKEAKY-IFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLID 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 696 LGfcKPEAMMSG---SIVGTPIHMAPELFTG-KYDN-SVDVYAFGILFWYIcsgsiklpeafercASKDHLWNNVRRGTR 770
Cdd:cd14004  153 FG--SAAYIKSGpfdTFVGTIDYAAPEVLRGnPYGGkEQDIWALGVLLYTL--------------VFKENPFYNIEEILE 216
                        250       260
                 ....*....|....*....|....*....
gi 564380513 771 PE-RLP-VFDEECWQLMEACWDGDPSKRP 797
Cdd:cd14004  217 ADlRIPyAVSEDLIDLISRMLNRDVGDRP 245
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
559-735 2.64e-12

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: 68.30  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 559 GRGQYGVVYL--CDNWGGhfPCALKSVvPPDEKHWNdlaLEFHYMRSLpKHERLVDLhgsvIDY---NYGGGSSVAVLLI 633
Cdd:cd14137   13 GSGSFGVVYQakLLETGE--VVAIKKV-LQDKRYKN---RELQIMRRL-KHPNIVKL----KYFfysSGEKKDEVYLNLV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 ME----RLHRDLYTGLKAGLSLETRL------QIAldvvEGIRFLHSQGLVHRDIKLKNVLLDKQN-RAKITDLGFCKP- 701
Cdd:cd14137   82 MEympeTLYRVIRHYSKNKQTIPIIYvklysyQLF----RGLAYLHSLGICHRDIKPQNLLVDPETgVLKLCDFGSAKRl 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564380513 702 ---EAmmSGSIVGTPIHMAPELFTG--KYDNSVDVYAFG 735
Cdd:cd14137  158 vpgEP--NVSYICSRYYRAPELIFGatDYTTAIDIWSAG 194
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
558-720 2.64e-12

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: 67.68  E-value: 2.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKsVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaVLLIMERL 637
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAK-FIPKRDKKKEAVLREISILNQL-QHPRIIQLHEAYESPTE-------LVLILELC 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 638 H-RDLYTGLKAGLSL---ETRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLD--KQNRAKITDLGFCKP--EAMMSGSI 709
Cdd:cd14006   72 SgGELLDRLAERGSLseeEVRTYMR-QLLEGLQYLHNHHILHLDLKPENILLAdrPSPQIKIIDFGLARKlnPGEELKEI 150
                        170
                 ....*....|.
gi 564380513 710 VGTPIHMAPEL 720
Cdd:cd14006  151 FGTPEFVAPEI 161
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
556-796 2.66e-12

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: 68.09  E-value: 2.66e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKsvvppdekhwndlalefhYMRSLPKHERLVDLHGSVidynYGGGSSVAVLLIME 635
Cdd:cd14172   10 QVLGLGVNGKVLECFHRRTGQKCALK------------------LLYDSPKARREVEHHWRA----SGGPHIVHILDVYE 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RLHRD-----LYTGLKAGLSLETRLQ--------------IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA---KI 693
Cdd:cd14172   68 NMHHGkrcllIIMECMEGGELFSRIQergdqaftereaseIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDavlKL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 694 TDLGFCKPEAMMSG--SIVGTPIHMAPE-LFTGKYDNSVDVYAFGILFWYICSGsikLPEAFERC--ASKDHLWNNVRRG 768
Cdd:cd14172  148 TDFGFAKETTVQNAlqTPCYTPYYVAPEvLGPEKYDKSCDMWSLGVIMYILLCG---FPPFYSNTgqAISPGMKRRIRMG 224
                        250       260       270
                 ....*....|....*....|....*....|..
gi 564380513 769 T----RPERLPVfDEECWQLMEACWDGDPSKR 796
Cdd:cd14172  225 QygfpNPEWAEV-SEEAKQLIRHLLKTDPTER 255
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
661-796 2.98e-12

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: 67.98  E-value: 2.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPELFTG-KYDNSVDVYAFGI 736
Cdd:cd05608  114 IISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAvelKDGQTKTKGYAGTPGFMAPELLLGeEYDYSVDYFTLGV 193
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564380513 737 LFWYICSGsiKLP-----EAFERCASKDHLWNNVRrgTRPERlpvFDEECWQLMEACWDGDPSKR 796
Cdd:cd05608  194 TLYEMIAA--RGPfrargEKVENKELKQRILNDSV--TYSEK---FSPASKSICEALLAKDPEKR 251
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
553-799 3.33e-12

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: 67.67  E-value: 3.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVVppdEKHWNDLALEFHYMRSLP-----KHERLVDLHGSVIDynygggsS 627
Cdd:cd14116    8 EIGRPLGKGKFGNVYLAREKQSKFILALKVLF---KAQLEKAGVEHQLRREVEiqshlRHPNILRLYGYFHD-------A 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 VAVLLIMERLHR-DLYTGL-KAGLSLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC--KPE 702
Cdd:cd14116   78 TRVYLILEYAPLgTVYRELqKLSKFDEQRTATYItELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSvhAPS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 703 AMMSgSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsiKLPeaFERCASKDhlwnNVRRGTRPE-RLPVF-DE 779
Cdd:cd14116  158 SRRT-TLCGTLDYLPPEMIEGRmHDEKVDLWSLGVLCYEFLVG--KPP--FEANTYQE----TYKRISRVEfTFPDFvTE 228
                        250       260
                 ....*....|....*....|
gi 564380513 780 ECWQLMEACWDGDPSKRPLL 799
Cdd:cd14116  229 GARDLISRLLKHNPSQRPML 248
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
558-745 3.35e-12

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: 68.41  E-value: 3.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCAL-------KSVVPPDEKHWNDLALEfhymRSLPKHER----LVDLHGS---------V 617
Cdd:cd05614    8 LGTGAYGKVFLVRKVSGHDANKLyamkvlrKAALVQKAKTVEHTRTE----RNVLEHVRqspfLVTLHYAfqtdaklhlI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 618 IDYNYGGGssvavlLIMERLHRDLYTglkaglSLETRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG 697
Cdd:cd05614   84 LDYVSGGE------LFTHLYQRDHFS------EDEVRFYSG-EIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFG 150
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564380513 698 ----FCKPEAMMSGSIVGTPIHMAPELFTGK--YDNSVDVYAFGILFWYICSGS 745
Cdd:cd05614  151 lskeFLTEEKERTYSFCGTIEYMAPEIIRGKsgHGKAVDWWSLGILMFELLTGA 204
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
661-802 3.63e-12

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: 67.19  E-value: 3.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNR-AKITDLGFCK-----PEamMSGSIVGTPIHMAPELFTG-KYD-NSVDVY 732
Cdd:cd14164  109 MVGAVNYLHDMNIVHRDLKCENILLSADDRkIKIADFGFARfvedyPE--LSTTFCGSRAYTPPEVILGtPYDpKKYDVW 186
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564380513 733 AFGILFWYICSGSikLPeaFERCaskdhLWNNVRRGTRPERLP---VFDEECWQLMEACWDGDPSKRPLLGIV 802
Cdd:cd14164  187 SLGVVLYVMVTGT--MP--FDET-----NVRRLRLQQRGVLYPsgvALEEPCRALIRTLLQFNPSTRPSIQQV 250
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
630-796 3.77e-12

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: 67.55  E-value: 3.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIME--RLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAM 704
Cdd:cd05577   71 VLTLMNggDLKYHIYNVGTRGFSEARAIFYAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAvefKGGKK 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 705 MSGSiVGTPIHMAPELFTGK--YDNSVDVYAFGILFWYICSGSIKLPEAFERCASKDhlwnnVRRGTR--PERLP-VFDE 779
Cdd:cd05577  151 IKGR-VGTHGYMAPEVLQKEvaYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEE-----LKRRTLemAVEYPdSFSP 224
                        170
                 ....*....|....*..
gi 564380513 780 ECWQLMEACWDGDPSKR 796
Cdd:cd05577  225 EARSLCEGLLQKDPERR 241
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
553-797 4.40e-12

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: 67.30  E-value: 4.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVV---PPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNygggSSVA 629
Cdd:cd08224    3 EIEKKIGKGQFSVVYRARCLLDGRLVALKKVQifeMMDAKARQDCLKEIDLLQQL-NHPNIIKYLASFIENN----ELNI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMER--LHRDLYTGLKAGLSLETR------LQIALdvveGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG---F 698
Cdd:cd08224   78 VLELADAgdLSRLIKHFKKQKRLIPERtiwkyfVQLCS----ALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGlgrF 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 699 CKPEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSgsikLPEAFerCASKDHLWNNVRRGTRPERLPV- 776
Cdd:cd08224  154 FSSKTTAAHSLVGTPYYMSPERIREQgYDFKSDIWSLGCLLYEMAA----LQSPF--YGEKMNLYSLCKKIEKCEYPPLp 227
                        250       260
                 ....*....|....*....|....
gi 564380513 777 ---FDEECWQLMEACWDGDPSKRP 797
Cdd:cd08224  228 adlYSQELRDLVAACIQPDPEKRP 251
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
539-797 4.45e-12

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: 67.59  E-value: 4.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 539 ESRSLQDVllhrKPKlgQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDekhwNDLALE--FHYMRSLPKHErlvdlHGS 616
Cdd:cd14048    1 TSRFLTDF----EPI--QCLGRGGFGVVFEAKNKVDDCNYAVKRIRLPN----NELAREkvLREVRALAKLD-----HPG 65
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 617 VIDYNYGGGSS----------VAVLLIMERLHR--DLYTGLKAGLSLETR-----LQIALDVVEGIRFLHSQGLVHRDIK 679
Cdd:cd14048   66 IVRYFNAWLERppegwqekmdEVYLYIQMQLCRkeNLKDWMNRRCTMESRelfvcLNIFKQIASAVEYLHSKGLIHRDLK 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 680 LKNVLLDKQNRAKITDLGFC------KPE----------AMMSGSiVGTPIHMAPELFTGK-YDNSVDVYAFGILFWyic 742
Cdd:cd14048  146 PSNVFFSLDDVVKVGDFGLVtamdqgEPEqtvltpmpayAKHTGQ-VGTRLYMSPEQIHGNqYSEKVDIFALGLILF--- 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564380513 743 sgsiKLPEAFERCASKDHLWNNVRRGTRPerlPVFDE---ECWQLMEACWDGDPSKRP 797
Cdd:cd14048  222 ----ELIYSFSTQMERIRTLTDVRKLKFP---ALFTNkypEERDMVQQMLSPSPSERP 272
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
603-796 4.51e-12

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


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 67.74  E-value: 4.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 603 SLP--KHERLV-----DLHGSVIDYNYgggssvavLLIMERLHR-DLYTGLKAG-LSLETRLQIALDVVEGIRFLHSQ-- 671
Cdd:cd14053   42 SLPgmKHENILqfigaEKHGESLEAEY--------WLITEFHERgSLCDYLKGNvISWNELCKIAESMARGLAYLHEDip 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 672 --------GLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSGSI--VGTPIHMAPELFTGKYDNS------VDVY 732
Cdd:cd14053  114 atngghkpSIAHRDFKSKNVLLKSDLTACIADFGLAlkfEPGKSCGDTHgqVGTRRYMAPEVLEGAINFTrdaflrIDMY 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 733 AFGILFWYICS---------GSIKLP---EAFERCASKDHLWNNVRRGTRPERLPVFDE-----ECWQLMEACWDGDPSK 795
Cdd:cd14053  194 AMGLVLWELLSrcsvhdgpvDEYQLPfeeEVGQHPTLEDMQECVVHKKLRPQIRDEWRKhpglaQLCETIEECWDHDAEA 273

                 .
gi 564380513 796 R 796
Cdd:cd14053  274 R 274
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
558-797 5.22e-12

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: 67.45  E-value: 5.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNW-GGHFPCALKSVVPPDEKHWNDLAL-EFHYMRSLpKHERLVDLhgsvidynygggssVAVL---- 631
Cdd:cd07846    9 VGEGSYGMVMKCRHKeTGQIVAIKKFLESEDDKMVKKIAMrEIKMLKQL-RHENLVNL--------------IEVFrrkk 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 ---LIMERLHRDLYTGLKA---GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAmM 705
Cdd:cd07846   74 rwyLVFEFVDHTVLDDLEKypnGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLA-A 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 706 SGSI----VGTPIHMAPELFTG--KYDNSVDVYAFGILFWYICSGSIKLPEAFE--------RCA-----------SKDH 760
Cdd:cd07846  153 PGEVytdyVATRWYRAPELLVGdtKYGKAVDVWAVGCLVTEMLTGEPLFPGDSDidqlyhiiKCLgnliprhqelfQKNP 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 564380513 761 LWNNVRRGTRPE------RLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd07846  233 LFAGVRLPEVKEveplerRYPKLSGVVIDLAKKCLHIDPDKRP 275
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
556-797 5.75e-12

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: 67.32  E-value: 5.75e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNdLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSVAVLLIME 635
Cdd:cd13986    6 RLLGEGGFSFVYLVEDLSTGRLYALKKILCHSKEDVK-EAMREIENYRLFNHPNILRLLDSQIVKEAGGKKEVYLLLPYY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 R---LHRDLYTGLKAG--LSLETRLQIALDVVEGIRFLHSQGLV---HRDIKLKNVLLDKQNRAKITDLGFCKP------ 701
Cdd:cd13986   85 KrgsLQDEIERRLVKGtfFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEPILMDLGSMNParieie 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 ---EAMMSGSIV---GTPIHMAPELFTGK----YDNSVDVYAFGILFWYICSGsiKLPeaFERCASK-DHLWNNVRRG-T 769
Cdd:cd13986  165 grrEALALQDWAaehCTMPYRAPELFDVKshctIDEKTDIWSLGCTLYALMYG--ESP--FERIFQKgDSLALAVLSGnY 240
                        250       260
                 ....*....|....*....|....*...
gi 564380513 770 RPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd13986  241 SFPDNSRYSEELHQLVKSMLVVNPAERP 268
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
652-745 5.94e-12

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: 66.86  E-value: 5.94e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 652 ETRlQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF-CK-PEAMMSGSIVGTPIHMAPELFTGK----- 724
Cdd:cd14182  111 ETR-KIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFsCQlDPGEKLREVCGTPGYLAPEIIECSmddnh 189
                         90       100
                 ....*....|....*....|...
gi 564380513 725 --YDNSVDVYAFGILFWYICSGS 745
Cdd:cd14182  190 pgYGKEVDMWSTGVIMYTLLAGS 212
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
606-796 5.99e-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: 67.68  E-value: 5.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 606 KHERLVDLHGS---------VIDYNYGGGssvavllIMERLHRDLYTGlkaglslETRLQI-ALDVVEGIRFLHSQGLVH 675
Cdd:cd05604   55 KHPFLVGLHYSfqttdklyfVLDFVNGGE-------LFFHLQRERSFP-------EPRARFyAAEIASALGYLHSINIVY 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 676 RDIKLKNVLLDKQNRAKITDLGFCK---PEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsikLPEA 751
Cdd:cd05604  121 RDLKPENILLDSQGHIVLTDFGLCKegiSNSDTTTTFCGTPEYLAPEVIRKQpYDNTVDWWCLGSVLYEMLYG---LPPF 197
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564380513 752 FERCASKdhLWNNVRRGTRPERlPVFDEECWQLMEACWDGDPSKR 796
Cdd:cd05604  198 YCRDTAE--MYENILHKPLVLR-PGISLTAWSILEELLEKDRQLR 239
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
558-744 6.06e-12

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


Pssm-ID: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 67.03  E-value: 6.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCAL-------KSVVPPDEKhwndlALEfHYM--RSLPKHER----LVDLHGS-------- 616
Cdd:cd05583    2 LGTGAYGKVFLVRKVGGHDAGKLyamkvlkKATIVQKAK-----TAE-HTMteRQVLEAVRqspfLVTLHYAfqtdaklh 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 617 -VIDYNYGGgssvavllimeRLHRDLYTGLKAGLSlETRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITD 695
Cdd:cd05583   76 lILDYVNGG-----------ELFTHLYQREHFTES-EVRIYIG-EIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTD 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564380513 696 LGFCK----PEAMMSGSIVGTPIHMAPELFTGK---YDNSVDVYAFGILFWYICSG 744
Cdd:cd05583  143 FGLSKeflpGENDRAYSFCGTIEYMAPEVVRGGsdgHDKAVDWWSLGVLTYELLTG 198
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
556-761 6.34e-12

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: 67.60  E-value: 6.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVVPPdekhWNDLALEFHYMRSLP-----KHERLVDLHGSVIDynygggSSVAV 630
Cdd:cd07856   16 QPVGMGAFGLVCSARDQLTGQNVAVKKIMKP----FSTPVLAKRTYRELKllkhlRHENIISLSDIFIS------PLEDI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLHRDLYTGLKAGlSLETR-LQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-PEAMMSG 707
Cdd:cd07856   86 YFVTELLGTDLHRLLTSR-PLEKQfIQYFLyQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARiQDPQMTG 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564380513 708 sIVGTPIHMAPELFTG--KYDNSVDVYAFGILFWYICSGSIKLPeafercaSKDHL 761
Cdd:cd07856  165 -YVSTRYYRAPEIMLTwqKYDVEVDIWSAGCIFAEMLEGKPLFP-------GKDHV 212
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
554-796 6.61e-12

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


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 66.91  E-value: 6.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYL--CDNW---GGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDynygGGSSV 628
Cdd:cd05092    9 LKWELGEGAFGKVFLaeCHNLlpeQDKMLVAVKALKEATESARQDFQREAELLTVL-QHQHIVRFYGVCTE----GEPLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 AVLLIMErlHRDLYTGLKA-----------------GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA 691
Cdd:cd05092   84 MVFEYMR--HGDLNRFLRShgpdakildggegqapgQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 692 KITDLGfckpeamMSGSIVGT-----------PIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSGSiKLP-------EA 751
Cdd:cd05092  162 KIGDFG-------MSRDIYSTdyyrvggrtmlPIRwMPPEsILYRKFTTESDIWSFGVVLWEIFTYG-KQPwyqlsntEA 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564380513 752 FErCASKDhlwnnvRRGTRPERLPvfdEECWQLMEACWDGDPSKR 796
Cdd:cd05092  234 IE-CITQG------RELERPRTCP---PEVYAIMQGCWQREPQQR 268
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
550-797 8.01e-12

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: 66.59  E-value: 8.01e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 550 RKPKLGQELGRGQYGVVYLcDNWGGHFPCALKSVVPPDEkhwnDLALEFHYMR------SLPKHERLVDLHGSVIDynyg 623
Cdd:cd14147    3 QELRLEEVIGIGGFGKVYR-GSWRGELVAVKAARQDPDE----DISVTAESVRqearlfAMLAHPNIIALKAVCLE---- 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 624 ggsSVAVLLIMERLHRDLYTGLKAGLSLETRLQI--ALDVVEGIRFLHSQGLV---HRDIKLKNVLL-------DKQNRA 691
Cdd:cd14147   74 ---EPNLCLVMEYAAGGPLSRALAGRRVPPHVLVnwAVQIARGMHYLHCEALVpviHRDLKSNNILLlqpiendDMEHKT 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 692 -KITDLGFCKP-EAMMSGSIVGTPIHMAPELF-TGKYDNSVDVYAFGILFWYICSGSIK------LPEAFERCASKDHLw 762
Cdd:cd14147  151 lKITDFGLAREwHKTTQMSAAGTYAWMAPEVIkASTFSKGSDVWSFGVLLWELLTGEVPyrgidcLAVAYGVAVNKLTL- 229
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564380513 763 nnvrrgTRPERLPvfdEECWQLMEACWDGDPSKRP 797
Cdd:cd14147  230 ------PIPSTCP---EPFAQLMADCWAQDPHRRP 255
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
557-738 8.28e-12

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: 66.98  E-value: 8.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLCDNW--GGHFpCALKSVVPPDEKHWNDLAL--EFHYMRSLPKHE-----RLVDLHG-SVIDynygggS 626
Cdd:cd07862    8 EIGEGAYGKVFKARDLknGGRF-VALKRVRVQTGEEGMPLSTirEVAVLRHLETFEhpnvvRLFDVCTvSRTD------R 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 627 SVAVLLIMERLHRDLYTGLKA----GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPE 702
Cdd:cd07862   81 ETKLTLVFEHVDQDLTTYLDKvpepGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSGQIKLADFGLARIY 160
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564380513 703 A--MMSGSIVGTPIHMAPE-LFTGKYDNSVDVYAFGILF 738
Cdd:cd07862  161 SfqMALTSVVVTLWYRAPEvLLQSSYATPVDLWSVGCIF 199
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
649-797 8.72e-12

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: 66.94  E-value: 8.72e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 649 LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGT-PIH-MAPE-LFTGKY 725
Cdd:cd05088  121 LSSQQLLHFAADVARGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRGQEVYVKKTMGRlPVRwMAIEsLNYSVY 200
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380513 726 DNSVDVYAFGILFWYICSGSiKLPEAFERCAskdHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05088  201 TTNSDVWSYGVLLWEIVSLG-GTPYCGMTCA---ELYEKLPQGYRLEKPLNCDDEVYDLMRQCWREKPYERP 268
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
556-797 9.07e-12

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: 66.29  E-value: 9.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALK-----SV--VPPDEKhwNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssv 628
Cdd:cd08222    6 RKLGSGNFGTVYLVSDLKATADEELKvlkeiSVgeLQPDET--VDANREAKLLSKL-DHPAIVKFHDSFVEKES------ 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 aVLLIMERLH-RDLYTGL----KAGLSLETRLQIA--LDVVEGIRFLHSQGLVHRDIKLKNVLLdKQNRAKITDLGFCKp 701
Cdd:cd08222   77 -FCIVTEYCEgGDLDDKIseykKSGTTIDENQILDwfIQLLLAVQYMHERRILHRDLKAKNIFL-KNNVIKVGDFGISR- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 eaMMSGS------IVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSgsikLPEAFERcASKDHLWNNVRRGTRPERL 774
Cdd:cd08222  154 --ILMGTsdlattFTGTPYYMSPEVLKHEgYNSKSDIWSLGCILYEMCC----LKHAFDG-QNLLSVMYKIVEGETPSLP 226
                        250       260
                 ....*....|....*....|...
gi 564380513 775 PVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd08222  227 DKYSKELNAIYSRMLNKDPALRP 249
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
661-796 9.68e-12

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: 65.88  E-value: 9.68e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSgSIVGTPIHMAPELFTGK-YDN-SVDVYAFG 735
Cdd:cd14071  108 ILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSnffKPGELLK-TWCGSPPYAAPEVFEGKeYEGpQLDIWSLG 186
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380513 736 ILFWYICSGSikLPeaFErCASKDHLWNNVRRGTRpeRLPVF-DEECWQLMEACWDGDPSKR 796
Cdd:cd14071  187 VVLYVLVCGA--LP--FD-GSTLQTLRDRVLSGRF--RIPFFmSTDCEHLIRRMLVLDPSKR 241
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
551-813 9.91e-12

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: 66.57  E-value: 9.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQELGRGQYGVVY--LCDNWGGHFPCALKS--VVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVID--YNYGG 624
Cdd:cd05075    1 KLALGKTLGEGEFGSVMegQLNQDDSVLKVAVKTmkIAICTRSEMEDFLSEAVCMKEF-DHPNVMRLIGVCLQntESEGY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 625 GSSVAVLLIMErlHRDLYTGL---KAG-----LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDL 696
Cdd:cd05075   80 PSPVVILPFMK--HGDLHSFLlysRLGdcpvyLPTQMLVKFMTDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 697 GFCKP----EAMMSGSIVGTPIH-MAPELFTGK-YDNSVDVYAFGILFWYICS-GSIKLPeAFERCASKDHLwnnvRRGT 769
Cdd:cd05075  158 GLSKKiyngDYYRQGRISKMPVKwIAIESLADRvYTTKSDVWSFGVTMWEIATrGQTPYP-GVENSEIYDYL----RQGN 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564380513 770 RPERLPVFDEECWQLMEACWDGDPSKRPLLGIVQPILRSIMDRL 813
Cdd:cd05075  233 RLKQPPDCLDGLYELMSSCWLLNPKDRPSFETLRCELEKILKDL 276
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
660-739 1.09e-11

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: 66.51  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKPEAMMSgSIVGTPIHMAPEL-------FTGKydnS 728
Cdd:cd14200  132 DIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGvsnqFEGNDALLS-STAGTPAFMAPETlsdsgqsFSGK---A 207
                         90
                 ....*....|.
gi 564380513 729 VDVYAFGILFW 739
Cdd:cd14200  208 LDVWAMGVTLY 218
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
660-749 1.15e-11

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: 67.03  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---PEAMMSGSIVGTPIHMAPELFT-GKYDNSVDVYAFG 735
Cdd:cd05593  123 EIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKegiTDAATMKTFCGTPEYLAPEVLEdNDYGRAVDWWGLG 202
                         90
                 ....*....|....
gi 564380513 736 ILFWYICSGsiKLP 749
Cdd:cd05593  203 VVMYEMMCG--RLP 214
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
556-796 1.41e-11

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: 66.23  E-value: 1.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVY---LCDNwgghfPCALKsVVPPdekHWNDLALEFHYMRSLP--KHERLVDLHGSviDYNYGGGSSVAV 630
Cdd:cd14054    1 QLIGQGRYGTVWkgsLDER-----PVAVK-VFPA---RHRQNFQNEKDIYELPlmEHSNILRFIGA--DERPTADGRMEY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERL-HRDLYTGLKAG-LSLETRLQIALDVVEGIRFLHSQ---------GLVHRDIKLKNVLLDKQNRAKITDLGF- 698
Cdd:cd14054   70 LLVLEYApKGSLCSYLRENtLDWMSSCRMALSLTRGLAYLHTDlrrgdqykpAIAHRDLNSRNVLVKADGSCVICDFGLa 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 699 -----CKPEAMMSG-----SI--VGTPIHMAPELFTGKYD--------NSVDVYAFGILFWYI---CS--------GSIK 747
Cdd:cd14054  150 mvlrgSSLVRGRPGaaenaSIseVGTLRYMAPEVLEGAVNlrdcesalKQVDVYALGLVLWEIamrCSdlypgesvPPYQ 229
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564380513 748 LPeaFERCA----SKDHLWNNVRRGTRPERLPvfdeECW-----------QLMEACWDGDPSKR 796
Cdd:cd14054  230 MP--YEAELgnhpTFEDMQLLVSREKARPKFP----DAWkenslavrslkETIEDCWDQDAEAR 287
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
662-797 1.49e-11

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: 65.36  E-value: 1.49e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 662 VEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK------PEAMMSGSiVGTPIHMAPELFTGKYDNS---VDVY 732
Cdd:cd14119  107 IDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEaldlfaEDDTCTTS-QGSPAFQPPEIANGQDSFSgfkVDIW 185
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 733 AFGILFWYICSGsiKLPeaFErcasKDH---LWNNVRRG--TRPERLpvfDEECWQLMEACWDGDPSKRP 797
Cdd:cd14119  186 SAGVTLYNMTTG--KYP--FE----GDNiykLFENIGKGeyTIPDDV---DPDLQDLLRGMLEKDPEKRF 244
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
558-797 1.54e-11

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: 65.57  E-value: 1.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVY---LCDNWGGHFPCALKSVVP-PDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNyggGSSVAVLLI 633
Cdd:cd05058    3 IGKGHFGCVYhgtLIDSDGQKIHCAVKSLNRiTDIEEVEQFLKEGIIMKDF-SHPNVLSLLGICLPSE---GSPLVVLPY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MErlHRDLYTGLKAglslETR-------LQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP----- 701
Cdd:cd05058   79 MK--HGDLRNFIRS----ETHnptvkdlIGFGLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLARDiydke 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 -EAMMSGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPE--AFERCaskdHLWNNVRRGTRPERLP 775
Cdd:cd05058  153 yYSVHNHTGAKLPVKwMALEsLQTQKFTTKSDVWSFGVLLWELMTrGAPPYPDvdSFDIT----VYLLQGRRLLQPEYCP 228
                        250       260
                 ....*....|....*....|..
gi 564380513 776 vfdEECWQLMEACWDGDPSKRP 797
Cdd:cd05058  229 ---DPLYEVMLSCWHPKPEMRP 247
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
656-744 1.58e-11

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: 65.43  E-value: 1.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALDVVEGIRFLHSQGLVHRDIKLKNVL---LDKQNRAKITDLGFCKPEAmmSGSIV----GTPIHMAPELFTGK-YDN 727
Cdd:cd14167  105 KLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKIEG--SGSVMstacGTPGYVAPEVLAQKpYSK 182
                         90
                 ....*....|....*..
gi 564380513 728 SVDVYAFGILFWYICSG 744
Cdd:cd14167  183 AVDCWSIGVIAYILLCG 199
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
654-809 1.61e-11

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: 65.49  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 654 RLQIALDVVEGIRFLHSQGL-VHRDIKLKNVLLDKQNRAKITDLGFCKP-EAMMSGSIVGTPIH-----MAPELFTGKYD 726
Cdd:cd13992   99 KSSFIKDIVKGMNYLHSSSIgYHGRLKSSNCLVDSRWVVKLTDFGLRNLlEEQTNHQLDEDAQHkkllwTAPELLRGSLL 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 727 N-----SVDVYAFGILFWYICSGSIKLPEAFERCASKDhlwnnVRRGTRPERLPV-------FDEECWQLMEACWDGDPS 794
Cdd:cd13992  179 EvrgtqKGDVYSFAIILYEILFRSDPFALEREVAIVEK-----VISGGNKPFRPElavlldeFPPRLVLLVKQCWAENPE 253
                        170
                 ....*....|....*
gi 564380513 795 KRPLLGIVQPILRSI 809
Cdd:cd13992  254 KRPSFKQIKKTLTEN 268
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
661-796 1.67e-11

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: 65.39  E-value: 1.67e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQN--RAKITDLGFCKPEAMMS--GSIVGTPIHMAPELFTGK-YDNSV-DVYAF 734
Cdd:cd14665  105 LISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYSKSSVLHSqpKSTVGTPAYIAPEVLLKKeYDGKIaDVWSC 184
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564380513 735 GILFWYICSGSIklpeAFERCASKDHLWNNVRR-----GTRPERLPVfDEECWQLMEACWDGDPSKR 796
Cdd:cd14665  185 GVTLYVMLVGAY----PFEDPEEPRNFRKTIQRilsvqYSIPDYVHI-SPECRHLISRIFVADPATR 246
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
558-738 1.72e-11

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: 66.54  E-value: 1.72e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLC-DNWGGHFpCALKSVvppdeKHWNDLALEF--HYMRslpkhER----------LVDLHGS-------- 616
Cdd:cd05573    9 IGRGAFGEVWLVrDKDTGQV-YAMKIL-----RKSDMLKREQiaHVRA-----ERdiladadspwIVRLHYAfqdedhly 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 617 -VIDYnYGGGSSVAVLLIMERLHRDlytglkaglslETRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITD 695
Cdd:cd05573   78 lVMEY-MPGGDLMNLLIKYDVFPEE-----------TARFYIA-ELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLAD 144
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564380513 696 LGFCK-------------------------------PEAM-MSGSIVGTPIHMAPELFTG-KYDNSVDVYAFG-ILF 738
Cdd:cd05573  145 FGLCTkmnksgdresylndsvntlfqdnvlarrrphKQRRvRAYSAVGTPDYIAPEVLRGtGYGPECDWWSLGvILY 221
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
660-739 1.76e-11

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: 65.76  E-value: 1.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKPEAMMSgSIVGTPIHMAPE-------LFTGKydnS 728
Cdd:cd14199  134 DLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGvsneFEGSDALLT-NTVGTPAFMAPEtlsetrkIFSGK---A 209
                         90
                 ....*....|.
gi 564380513 729 VDVYAFGILFW 739
Cdd:cd14199  210 LDVWAMGVTLY 220
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
556-797 1.94e-11

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: 65.36  E-value: 1.94e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSV----VPPDEKHWNDLALefhYMRSLPKHERLVDLHGS---------VIDYNY 622
Cdd:cd08225    6 KKIGEGSFGKIYLAKAKSDSEHCVIKEIdltkMPVKEKEASKKEV---ILLAKMKHPNIVTFFASfqengrlfiVMEYCD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 623 GGGssvavllIMERLHRDLYTGLKAGLSLETRLQIALdvveGIRFLHSQGLVHRDIKLKNVLLDKQNR-AKITDLGFCKP 701
Cdd:cd08225   83 GGD-------LMKRINRQRGVLFSEDQILSWFVQISL----GLKHIHDRKILHRDIKSQNIFLSKNGMvAKLGDFGIARQ 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 --EAM-MSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSgsikLPEAFERcASKDHLWNNVRRGTRPERLPVF 777
Cdd:cd08225  152 lnDSMeLAYTCVGTPYYLSPEICQNRpYNNKTDIWSLGCVLYELCT----LKHPFEG-NNLHQLVLKICQGYFAPISPNF 226
                        250       260
                 ....*....|....*....|
gi 564380513 778 DEECWQLMEACWDGDPSKRP 797
Cdd:cd08225  227 SRDLRSLISQLFKVSPRDRP 246
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
645-797 2.01e-11

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: 65.46  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 645 LKAGLSLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPEL 720
Cdd:cd06640   93 LRAGPFDEFQIATMLkEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAgqlTDTQIKRNTFVGTPFWMAPEV 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 721 F-TGKYDNSVDVYAFGILfwyicsgSIKLPEAfERCASKDH---LWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKR 796
Cdd:cd06640  173 IqQSAYDSKADIWSLGIT-------AIELAKG-EPPNSDMHpmrVLFLIPKNNPPTLVGDFSKPFKEFIDACLNKDPSFR 244

                 .
gi 564380513 797 P 797
Cdd:cd06640  245 P 245
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
554-809 2.04e-11

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: 65.80  E-value: 2.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWG-----GHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDynygGGSSV 628
Cdd:cd05094    9 LKRELGEGAFGKVFLAECYNlsptkDKMLVAVKTLKDPTLAARKDFQREAELLTNL-QHDHIVKFYGVCGD----GDPLI 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 AVLLIMErlHRDLYTGLKAG------------------LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNR 690
Cdd:cd05094   84 MVFEYMK--HGDLNKFLRAHgpdamilvdgqprqakgeLGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 691 AKITDLGFCK----PEAMMSGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSGSiKLPeAFErcASKDHLWNN 764
Cdd:cd05094  162 VKIGDFGMSRdvysTDYYRVGGHTMLPIRwMPPEsIMYRKFTTESDVWSFGVILWEIFTYG-KQP-WFQ--LSNTEVIEC 237
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564380513 765 VRRGTRPERLPVFDEECWQLMEACWDGDPSKRPLLGIVQPILRSI 809
Cdd:cd05094  238 ITQGRVLERPRVCPKEVYDIMLGCWQREPQQRLNIKEIYKILHAL 282
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
553-808 2.34e-11

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: 65.38  E-value: 2.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWG------------GHFP--CALKSVVPPDEKHW-NDLALEFHYMRSLpKHERLVDLHGSV 617
Cdd:cd05097    8 RLKEKLGEGQFGEVHLCEAEGlaeflgegapefDGQPvlVAVKMLRADVTKTArNDFLKEIKIMSRL-KNPNIIRLLGVC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 618 IdynygggSSVAVLLIMERL----------HRDLYTGLKAG-----LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKN 682
Cdd:cd05097   87 V-------SDDPLCMITEYMengdlnqflsQREIESTFTHAnnipsVSIANLLYMAVQIASGMKYLASLNFVHRDLATRN 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 683 VLLDKQNRAKITDLGFCKpeAMMSGS---IVGT---PIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSGSIKLPEAF-- 752
Cdd:cd05097  160 CLVGNHYTIKIADFGMSR--NLYSGDyyrIQGRavlPIRwMAWEsILLGKFTTASDVWAFGVTLWEMFTLCKEQPYSLls 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564380513 753 --ERCASKDHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRPLLGIVQPILRS 808
Cdd:cd05097  238 deQVIENTGEFFRNQGRQIYLSQTPLCPSPVFKLMMRCWSRDIKDRPTFNKIHHFLRE 295
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
631-797 2.41e-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: 65.38  E-value: 2.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERL-HRDLYTGLKA------------GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG 697
Cdd:cd05061   85 LVVMELMaHGDLKSYLRSlrpeaennpgrpPPTLQEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFG 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 698 FCK----PEAMMSGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSgsikLPEAFERCASKDHLWNNVRRG--- 768
Cdd:cd05061  165 MTRdiyeTDYYRKGGKGLLPVRwMAPEsLKDGVFTTSSDMWSFGVVLWEITS----LAEQPYQGLSNEQVLKFVMDGgyl 240
                        170       180
                 ....*....|....*....|....*....
gi 564380513 769 TRPERLPvfdEECWQLMEACWDGDPSKRP 797
Cdd:cd05061  241 DQPDNCP---ERVTDLMRMCWQFNPKMRP 266
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
664-797 2.50e-11

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: 64.83  E-value: 2.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 664 GIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---PEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFW 739
Cdd:cd08218  113 ALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARvlnSTVELARTCIGTPYYLSPEICENKpYNNKSDIWALGCVLY 192
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564380513 740 YICSgsikLPEAFERCASKDhLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd08218  193 EMCT----LKHAFEAGNMKN-LVLKIIRGSYPPVPSRYSYDLRSLVSQLFKRNPRDRP 245
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
547-736 2.78e-11

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: 65.05  E-value: 2.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 547 LLHRKPK----LGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFhYMRSLPKHERLVDLHGSV----- 617
Cdd:cd06646    2 ILRRNPQhdyeLIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSLIQQEI-FMVKECKHCNIVAYFGSYlsrek 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 618 --IDYNYGGGSSVavllimerlhRDLY--TGLKAglsletRLQIAL---DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNR 690
Cdd:cd06646   81 lwICMEYCGGGSL----------QDIYhvTGPLS------ELQIAYvcrETLQGLAYLHSKGKMHRDIKGANILLTDNGD 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564380513 691 AKITDLGF-CKPEAMMS--GSIVGTPIHMAPELF----TGKYDNSVDVYAFGI 736
Cdd:cd06646  145 VKLADFGVaAKITATIAkrKSFIGTPYWMAPEVAavekNGGYNQLCDIWAVGI 197
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
558-813 2.91e-11

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: 65.00  E-value: 2.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVY---LCDNWGGHFPCALKSVVPP-DEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNygggSSVAVLLI 633
Cdd:cd05063   13 IGAGEFGEVFrgiLKMPGRKEVAVAIKTLKPGyTEKQRQDFLSEASIMGQF-SHHNIIRLEGVVTKFK----PAMIITEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERLHRDLYTGLKAGLSLETRLQIALD-VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-----PEAMMSG 707
Cdd:cd05063   88 MENGALDKYLRDHDGEFSSYQLVGMLRgIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRvleddPEGTYTT 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 SIVGTPIH-MAPELFT-GKYDNSVDVYAFGILFWYICSGSiklpeafERC---ASKDHLWNNVRRGTR---PERLPvfdE 779
Cdd:cd05063  168 SGGKIPIRwTAPEAIAyRKFTSASDVWSFGIVMWEVMSFG-------ERPywdMSNHEVMKAINDGFRlpaPMDCP---S 237
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564380513 780 ECWQLMEACWDGDPSKRPLLG-IVqpilrSIMDRL 813
Cdd:cd05063  238 AVYQLMLQCWQQDRARRPRFVdIV-----NLLDKL 267
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
553-810 3.21e-11

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: 64.86  E-value: 3.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVY---LCDNWGGHFPCALKS--VVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYGGG-- 625
Cdd:cd05035    2 KLGKILGEGEFGSVMeaqLKQDDGSQLKVAVKTmkVDIHTYSEIEEFLSEAACMKDF-DHPNVMRLIGVCFTASDLNKpp 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 626 SSVAVLLIMErlHRDLYT--------GLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG 697
Cdd:cd05035   81 SPMVILPFMK--HGDLHSyllysrlgGLPEKLPLQTLLKFMVDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 698 FCKP----EAMMSGSIVGTPIH------MAPELFTGKydnsVDVYAFGILFWYICS-GSIKLPEafercASKDHLWNNVR 766
Cdd:cd05035  159 LSRKiysgDYYRQGRISKMPVKwialesLADNVYTSK----SDVWSFGVTMWEIATrGQTPYPG-----VENHEIYDYLR 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564380513 767 RGTRPERLPVFDEECWQLMEACWDGDPSKRPLLGIVQPILRSIM 810
Cdd:cd05035  230 NGNRLKQPEDCLDEVYFLMYFCWTVDPKDRPTFTKLREVLENIL 273
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
661-746 3.27e-11

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: 64.48  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLL-DKQNRAK--ITDLGFC-----KPEAMMSgSIVGTPIHMAPELFTGK-YDNSVDV 731
Cdd:cd14087  106 VLDGVKYLHGLGITHRDLKPENLLYyHPGPDSKimITDFGLAstrkkGPNCLMK-TTCGTPEYIAPEILLRKpYTQSVDM 184
                         90
                 ....*....|....*
gi 564380513 732 YAFGILFWYICSGSI 746
Cdd:cd14087  185 WAVGVIAYILLSGTM 199
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
553-809 3.45e-11

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


Pssm-ID: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 64.99  E-value: 3.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLcDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSlPKHERLVDLHGSVIDYNYgggssvavLL 632
Cdd:cd14152    3 ELGELIGQGRWGKVHR-GRWHGEVAIRLLEIDGNNQDHLKLFKKEVMNYRQ-TRHENVVLFMGACMHPPH--------LA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERL--HRDLYTGL---KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDkQNRAKITDLGFCKpeamMSG 707
Cdd:cd14152   73 IITSFckGRTLYSFVrdpKTSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLKSKNVFYD-NGKVVITDFGLFG----ISG 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 SIV------------GTPIHMAPELF----TGK------YDNSVDVYAFGILfWYICSGSiKLPeaFERCASKDHLWnNV 765
Cdd:cd14152  148 VVQegrrenelklphDWLCYLAPEIVremtPGKdedclpFSKAADVYAFGTI-WYELQAR-DWP--LKNQPAEALIW-QI 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 564380513 766 RRGTRPERLPV---FDEECWQLMEACWDGDPSKRPLLGIVQPILRSI 809
Cdd:cd14152  223 GSGEGMKQVLTtisLGKEVTEILSACWAFDLEERPSFTLLMDMLEKL 269
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
561-744 4.60e-11

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 64.11  E-value: 4.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 561 GQYGVVYLCDNWGGH--FPCalKSVvppDEKHWNdlALEF--HY-MRslpKHERLVDLHGSVidynyggGSSVAVLLIME 635
Cdd:PHA03390  27 GKFGKVSVLKHKPTQklFVQ--KII---KAKNFN--AIEPmvHQlMK---DNPNFIKLYYSV-------TTLKGHVLIMD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RLHR-DLYTGLKAGLSL---ETRLqIALDVVEGIRFLHSQGLVHRDIKLKNVLLD-KQNRAKITDLGFCKpeammsgsIV 710
Cdd:PHA03390  90 YIKDgDLFDLLKKEGKLseaEVKK-IIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKDRIYLCDYGLCK--------II 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564380513 711 GTP-------IHMAPELFTGK-YDNSVDVYAFGILFWYICSG 744
Cdd:PHA03390 161 GTPscydgtlDYFSPEKIKGHnYDVSFDWWAVGVLTYELLTG 202
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
556-796 4.61e-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: 64.42  E-value: 4.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCdNWGGHFpCALKSVVPPDEKHWndlALEFH-YMRSLPKHERLVDLHGSVIDynyGGGSSVAVLLIM 634
Cdd:cd14144    1 RSVGKGRYGEVWKG-KWRGEK-VAVKIFFTTEEASW---FRETEiYQTVLMRHENILGFIAADIK---GTGSWTQLYLIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 ErLHRD--LYTGLKAG-LSLETRLQIALDVVEGIRFLHS-----QG---LVHRDIKLKNVLLDKQNRAKITDLGFC---K 700
Cdd:cd14144   73 D-YHENgsLYDFLRGNtLDTQSMLKLAYSAACGLAHLHTeifgtQGkpaIAHRDIKSKNILVKKNGTCCIADLGLAvkfI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 701 PEA----MMSGSIVGTPIHMAPELFTGKYDNS-------VDVYAFGILFWYI---C-SGSI----KLPeaFERCASKDHL 761
Cdd:cd14144  152 SETnevdLPPNTRVGTKRYMAPEVLDESLNRNhfdaykmADMYSFGLVLWEIarrCiSGGIveeyQLP--YYDAVPSDPS 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 564380513 762 WNNVRRGTRPERL-PVF-----DEECW----QLMEACWDGDPSKR 796
Cdd:cd14144  230 YEDMRRVVCVERRrPSIpnrwsSDEVLrtmsKLMSECWAHNPAAR 274
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
658-797 5.23e-11

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: 64.29  E-value: 5.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLV---HRDIKLKNVLL-------DKQNRA-KITDLGFCKP-EAMMSGSIVGTPIHMAPELF-TGK 724
Cdd:cd14145  110 AVQIARGMNYLHCEAIVpviHRDLKSSNILIlekvengDLSNKIlKITDFGLAREwHRTTKMSAAGTYAWMAPEVIrSSM 189
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564380513 725 YDNSVDVYAFGILFWYICSGSIKLpEAFERCASKDHLWNNVRRGTRPERLPvfdEECWQLMEACWDGDPSKRP 797
Cdd:cd14145  190 FSKGSDVWSYGVLLWELLTGEVPF-RGIDGLAVAYGVAMNKLSLPIPSTCP---EPFARLMEDCWNPDPHSRP 258
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
558-827 5.37e-11

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: 64.66  E-value: 5.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVY----LCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDynygggSSVAV--- 630
Cdd:cd05108   15 LGSGAFGTVYkglwIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLT------STVQLitq 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 ------LLIMERLHRDLYTGlkaglslETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---- 700
Cdd:cd05108   89 lmpfgcLLDYVREHKDNIGS-------QYLLNWCVQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKllga 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 701 --PEAMMSGSIVgtPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSGSIKlpeAFERCASKDhLWNNVRRGTRPERLPV 776
Cdd:cd05108  162 eeKEYHAEGGKV--PIKwMALEsILHRIYTHQSDVWSYGVTVWELMTFGSK---PYDGIPASE-ISSILEKGERLPQPPI 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564380513 777 FDEECWQLMEACWDGDPSKRP----LLG-------------IVQPILRSIMDRLCKCDSERPSR---GLDD 827
Cdd:cd05108  236 CTIDVYMIMVKCWMIDADSRPkfreLIIefskmardpqrylVIQGDERMHLPSPTDSNFYRALMdeeDMDD 306
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
556-796 5.37e-11

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1a, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 64.29  E-value: 5.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLcDNWGGHfPCALKSVVPPDEKHWndlaleFH----YMRSLPKHERLVDLHGSVIDynyGGGSSVAVL 631
Cdd:cd14220    1 RQIGKGRYGEVWM-GKWRGE-KVAVKVFFTTEEASW------FReteiYQTVLMRHENILGFIAADIK---GTGSWTQLY 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMErLHRD--LYTGLKAGlSLETR--LQIALDVVEGIRFLHSQ--------GLVHRDIKLKNVLLDKQNRAKITDLGFC 699
Cdd:cd14220   70 LITD-YHENgsLYDFLKCT-TLDTRalLKLAYSAACGLCHLHTEiygtqgkpAIAHRDLKSKNILIKKNGTCCIADLGLA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 700 KPEAMMSGSI-------VGTPIHMAPELFTGKYDNS-------VDVYAFGILFWYIC----SGSI----KLPeaFERCAS 757
Cdd:cd14220  148 VKFNSDTNEVdvplntrVGTKRYMAPEVLDESLNKNhfqayimADIYSFGLIIWEMArrcvTGGIveeyQLP--YYDMVP 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 564380513 758 KDHLWNNVR-----RGTRPERLPVFD-EEC----WQLMEACWDGDPSKR 796
Cdd:cd14220  226 SDPSYEDMRevvcvKRLRPTVSNRWNsDEClravLKLMSECWAHNPASR 274
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
556-799 5.66e-11

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: 63.88  E-value: 5.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLcDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSlPKHERLVDLHGSVIDYNYG------GGSSva 629
Cdd:cd14150    6 KRIGTGSFGTVFR-GKWHGDVAVKILKVTEPTPEQLQAFKNEMQVLRK-TRHVNILLFMGFMTRPNFAiitqwcEGSS-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 vllimerLHRDLYTgLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGS- 708
Cdd:cd14150   82 -------LYRHLHV-TETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLATVKTRWSGSq 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 709 ----IVGTPIHMAPELF----TGKYDNSVDVYAFGILFWYICSGSikLPeaFERCASKDHLWNNVRRGTRPERLPVFDEE 780
Cdd:cd14150  154 qveqPSGSILWMAPEVIrmqdTNPYSFQSDVYAYGVVLYELMSGT--LP--YSNINNRDQIIFMVGRGYLSPDLSKLSSN 229
                        250       260
                 ....*....|....*....|...
gi 564380513 781 CWQLMEA----CWDGDPSKRPLL 799
Cdd:cd14150  230 CPKAMKRllidCLKFKREERPLF 252
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
558-797 7.20e-11

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: 63.44  E-value: 7.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVvpPDEKHWNDLAL-EFHYMRSLPKH-----ERLVDLHGSVIDYNYgggssvaVL 631
Cdd:cd14133    7 LGKGTFGQVVKCYDLLTGEEVALKII--KNNKDYLDQSLdEIRLLELLNKKdkadkYHIVRLKDVFYFKNH-------LC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLHRDLYTGLK----AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA--KITDLGFCKPEAMM 705
Cdd:cd14133   78 IVFELLSQNLYEFLKqnkfQYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCqiKIIDFGSSCFLTQR 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 706 SGSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGSIKLPEAFErcasKDHLWNNVR-RGTRPERL----PVFDE 779
Cdd:cd14133  158 LYSYIQSRYYRAPEVILGlPYDEKIDMWSLGCILAELYTGEPLFPGASE----VDQLARIIGtIGIPPAHMldqgKADDE 233
                        250
                 ....*....|....*...
gi 564380513 780 ECWQLMEACWDGDPSKRP 797
Cdd:cd14133  234 LFVDFLKKLLEIDPKERP 251
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
630-796 8.44e-11

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: 63.53  E-value: 8.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIME----RLHrdLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PEA 703
Cdd:cd05605   78 VLTIMNggdlKFH--IYNMGNPGFEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVeiPEG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 MMSGSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGsiKLPeaFErcASKDHL-WNNVRRGTRPERLPV---FD 778
Cdd:cd05605  156 ETIRGRVGTVGYMAPEVVKNeRYTFSPDWWGLGCLIYEMIEG--QAP--FR--ARKEKVkREEVDRRVKEDQEEYsekFS 229
                        170
                 ....*....|....*...
gi 564380513 779 EECWQLMEACWDGDPSKR 796
Cdd:cd05605  230 EEAKSICSQLLQKDPKTR 247
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
556-797 8.50e-11

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: 63.61  E-value: 8.50e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDnwggHFPCAL---KSVVPPDEKH--WNDLALEFHYMRSLpKHERLVDLHGSvidYNYGGGSSVAV 630
Cdd:cd06620   11 KDLGAGNGGSVSKVL----HIPTGTimaKKVIHIDAKSsvRKQILRELQILHEC-HSPYIVSFYGA---FLNENNNIIIC 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQ-GLVHRDIKLKNVLLDKQNRAKITDLGFCKpEAMMS--G 707
Cdd:cd06620   83 MEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGVSG-ELINSiaD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 SIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGsiKLPEAFERCASK---------DHLWNNVRRgtRPERLP-- 775
Cdd:cd06620  162 TFVGTSTYMSPERIQGgKYSVKSDVWSLGLSIIELALG--EFPFAGSNDDDDgyngpmgilDLLQRIVNE--PPPRLPkd 237
                        250       260
                 ....*....|....*....|...
gi 564380513 776 -VFDEECWQLMEACWDGDPSKRP 797
Cdd:cd06620  238 rIFPKDLRDFVDRCLLKDPRERP 260
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
557-797 1.02e-10

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


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 63.07  E-value: 1.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHwNDLALEFHYMRSLpKHERLVDLhgsvIDyNYGGGSSVAVLLIMER 636
Cdd:cd14113   14 ELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKR-DQVTHELGVLQSL-QHPQLVGL----LD-TFETPTSYILVLEMAD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 637 LHRDLYTGLKAGLSLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDK---QNRAKITDLGfckpEAMMSGS---- 708
Cdd:cd14113   87 QGRLLDYVVRWGNLTEEKIRFYLrEILEALQYLHNCRIAHLDLKPENILVDQslsKPTIKLADFG----DAVQLNTtyyi 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 709 --IVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSG-SIKLPEAFER-CAS--------KDHLWNNVRRGTRperlp 775
Cdd:cd14113  163 hqLLGSPEFAAPEIILGNpVSLTSDLWSIGVLTYVLLSGvSPFLDESVEEtCLNicrldfsfPDDYFKGVSQKAK----- 237
                        250       260
                 ....*....|....*....|..
gi 564380513 776 vfDEECWQLmeacwDGDPSKRP 797
Cdd:cd14113  238 --DFVCFLL-----QMDPAKRP 252
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
661-796 1.03e-10

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: 63.04  E-value: 1.03e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF---CKPEAMMSGSiVGTPIHMAPELFTGK-YDNS-VDVYAFG 735
Cdd:cd14081  110 IISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMaslQPEGSLLETS-CGSPHYACPEVIKGEkYDGRkADIWSCG 188
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564380513 736 ILFWYICSGsiKLPeaFERcASKDHLWNNVRRGT--RPERLPvfdEECWQLMEACWDGDPSKR 796
Cdd:cd14081  189 VILYALLVG--ALP--FDD-DNLRQLLEKVKRGVfhIPHFIS---PDAQDLLRRMLEVNPEKR 243
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
656-797 1.09e-10

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


Pssm-ID: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 63.21  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALDVVEGIRFLHSQ-GLVHRDIKLKNVLLDKQNRAKITDLGfckpeamMSGSIV---------GTPIHMAPELFTGK- 724
Cdd:cd06617  107 KIAVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFG-------ISGYLVdsvaktidaGCKPYMAPERINPEl 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 725 ----YDNSVDVYAFGILFWYICSGsiKLPEA-----FERCaskdhlwNNVRRGTRPeRLPV--FDEECWQLMEACWDGDP 793
Cdd:cd06617  180 nqkgYDVKSDVWSLGITMIELATG--RFPYDswktpFQQL-------KQVVEEPSP-QLPAekFSPEFQDFVNKCLKKNY 249

                 ....
gi 564380513 794 SKRP 797
Cdd:cd06617  250 KERP 253
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
558-749 1.12e-10

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: 63.57  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLcdnwgghfpcaLKSVVPPDEKHwndlaleFHYMRSLPK------------HER--LVDL-HGSVIDYNY 622
Cdd:cd05582    3 LGQGSFGKVFL-----------VRKITGPDAGT-------LYAMKVLKKatlkvrdrvrtkMERdiLADVnHPFIVKLHY 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 623 GGGSSVAVLLIMERLHR-DLYTGL-KAGLSLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC 699
Cdd:cd05582   65 AFQTEGKLYLILDFLRGgDLFTRLsKEVMFTEEDVKFYLaELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLS 144
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564380513 700 KpEAMMSG----SIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGSikLP 749
Cdd:cd05582  145 K-ESIDHEkkaySFCGTVEYMAPEVVNRRgHTQSADWWSFGVLMFEMLTGS--LP 196
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
652-797 1.15e-10

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


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 63.04  E-value: 1.15e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 652 ETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC------KPEAMMSG-----------------S 708
Cdd:cd14222   90 QQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSrliveeKKKPPPDKpttkkrtlrkndrkkryT 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 709 IVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGSIKLPEAFERCASkdhLWNNVR---RGTRPERLPvfdEECWQL 784
Cdd:cd14222  170 VVGNPYWMAPEMLNGKsYDEKVDIFSFGIVLCEIIGQVYADPDCLPRTLD---FGLNVRlfwEKFVPKDCP---PAFFPL 243
                        170
                 ....*....|...
gi 564380513 785 MEACWDGDPSKRP 797
Cdd:cd14222  244 AAICCRLEPDSRP 256
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
661-796 1.22e-10

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


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 62.86  E-value: 1.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQ--NRAKITDLGFCKPEAMMS--GSIVGTPIHMAPELFTGK-YDNSV-DVYAF 734
Cdd:cd14662  105 LISGVSYCHSMQICHRDLKLENTLLDGSpaPRLKICDFGYSKSSVLHSqpKSTVGTPAYIAPEVLSRKeYDGKVaDVWSC 184
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564380513 735 GILFWYICSGSIklpeAFERCASKDHLWNNVRR-----GTRPERLPVfDEECWQLMEACWDGDPSKR 796
Cdd:cd14662  185 GVTLYVMLVGAY----PFEDPDDPKNFRKTIQRimsvqYKIPDYVRV-SQDCRHLLSRIFVANPAKR 246
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
661-741 1.24e-10

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: 62.77  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVL---LDKQNRAKITDLGFCKPEA--MMSgSIVGTPIHMAPELFTGK-YDNSVDVYAF 734
Cdd:cd14083  110 VLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSKMEDsgVMS-TACGTPGYVAPEVLAQKpYGKAVDCWSI 188

                 ....*..
gi 564380513 735 GILFwYI 741
Cdd:cd14083  189 GVIS-YI 194
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
557-736 1.59e-10

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: 62.74  E-value: 1.59e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGS---------VIDYNYGGgss 627
Cdd:cd06643   12 ELGDGAFGKVYKAQNKETGILAAAKVIDTKSEEELEDYMVEIDILASC-DHPNIVKLLDAfyyennlwiLIEFCAGG--- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 vAVLLIMERLHRDLytglkaglsLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA--- 703
Cdd:cd06643   88 -AVDAVMLELERPL---------TEPQIRVVCkQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVSAKNTrtl 157
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564380513 704 MMSGSIVGTPIHMAPELF---TGK---YDNSVDVYAFGI 736
Cdd:cd06643  158 QRRDSFIGTPYWMAPEVVmceTSKdrpYDYKADVWSLGV 196
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
657-797 1.60e-10

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 63.69  E-value: 1.60e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 657 IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMM---SGSIVGTPIHMAPE-----LFTGKYDNS 728
Cdd:PLN00034 173 VARQILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILAQTmdpCNSSVGTIAYMSPErintdLNHGAYDGY 252
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380513 729 V-DVYAFG--ILFWYICsgsiKLPEAFERCASKDHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:PLN00034 253 AgDIWSLGvsILEFYLG----RFPFGVGRQGDWASLMCAICMSQPPEAPATASREFRHFISCCLQREPAKRW 320
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
557-744 1.62e-10

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: 62.53  E-value: 1.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLC--DNWGGHFPCalkSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaVLLIM 634
Cdd:cd14111   10 EKARGRFGVIRRCreNATGKNFPA---KIVPYQAEEKQGVLQEYEILKSL-HHERIMALHEAYITPRY-------LVLIA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 ErlhrdlYTGLKAGL-SLETRLQIALD--------VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMM 705
Cdd:cd14111   79 E------FCSGKELLhSLIDRFRYSEDdvvgylvqILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPL 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564380513 706 S----GSIVGTPIHMAPELFTGKYDNS-VDVYAFGILFWYICSG 744
Cdd:cd14111  153 SlrqlGRRTGTLEYMAPEMVKGEPVGPpADIWSIGVLTYIMLSG 196
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
547-736 1.71e-10

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: 62.76  E-value: 1.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 547 LLHRKPK----LGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSV----- 617
Cdd:cd06645    4 LSRRNPQedfeLIQRIGSGTYGDVYKARNVNTGELAAIKVIKLEPGEDFAVVQQEIIMMKDC-KHSNIVAYFGSYlrrdk 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 618 --IDYNYGGGSSVavllimerlhRDLYTgLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITD 695
Cdd:cd06645   83 lwICMEFCGGGSL----------QDIYH-VTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLAD 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564380513 696 LGFckpEAMMSGSI------VGTPIHMAPELFT----GKYDNSVDVYAFGI 736
Cdd:cd06645  152 FGV---SAQITATIakrksfIGTPYWMAPEVAAverkGGYNQLCDIWAVGI 199
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
541-736 1.72e-10

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: 62.72  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 541 RSLQDVLLH--RKP----KLGQELGRGQYGVVYLcdnwGGHFPC---ALKSVVPPDEKHWNDLALEFHYMRSLPKHERLV 611
Cdd:cd06636    1 RSLDDIDLSalRDPagifELVEVVGNGTYGQVYK----GRHVKTgqlAAIKVMDVTEDEEEEIKLEINMLKKYSHHRNIA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 612 DLHGSVIDYNYGGGSSvAVLLIMERLH----RDLYTGLKAGLSLETRLQ-IALDVVEGIRFLHSQGLVHRDIKLKNVLLD 686
Cdd:cd06636   77 TYYGAFIKKSPPGHDD-QLWLVMEFCGagsvTDLVKNTKGNALKEDWIAyICREILRGLAHLHAHKVIHRDIKGQNVLLT 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564380513 687 KQNRAKITDLGFCKPEAMMSG---SIVGTPIHMAPELFT------GKYDNSVDVYAFGI 736
Cdd:cd06636  156 ENAEVKLVDFGVSAQLDRTVGrrnTFIGTPYWMAPEVIAcdenpdATYDYRSDIWSLGI 214
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
657-797 1.80e-10

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 62.33  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 657 IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC--KPEAMMSGSIVGTPIHMAPELFTGKYDNSVDVYAF 734
Cdd:cd14050  105 ILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVveLDKEDIHDAQEGDPRYMAPELLQGSFTKAADIFSL 184
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564380513 735 GI-LFWYICsgSIKLPEAFErcaskdhLWNNVRRGTRPER-LPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd14050  185 GItILELAC--NLELPSGGD-------GWHQLRQGYLPEEfTAGLSPELRSIIKLMMDPDPERRP 240
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
648-780 1.85e-10

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: 62.61  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 648 GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC--KPEAMMSGSIVGTPIHMAPELFTGK- 724
Cdd:cd05607  100 GIEMERVIFYSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAveVKEGKPITQRAGTNGYMAPEILKEEs 179
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 725 YDNSVDVYAFGILFWYICSGSIKLPEAFERCASKDhlwnnVRRGTRPERL----PVFDEE 780
Cdd:cd05607  180 YSYPVDWFAMGCSIYEMVAGRTPFRDHKEKVSKEE-----LKRRTLEDEVkfehQNFTEE 234
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
649-797 2.00e-10

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 62.48  E-value: 2.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 649 LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP----------EAMMsgsivgtPIH-MA 717
Cdd:cd05046  114 LSTKQKVALCTQIALGMDHLSNARFVHRDLAARNCLVSSQREVKVSLLSLSKDvynseyyklrNALI-------PLRwLA 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 718 PE-LFTGKYDNSVDVYAFGILFWYICSgSIKLP-------EAFERCASKDHLWnnvrrgTRPERLPvfdEECWQLMEACW 789
Cdd:cd05046  187 PEaVQEDDFSTKSDVWSFGVLMWEVFT-QGELPfyglsdeEVLNRLQAGKLEL------PVPEGCP---SRLYKLMTRCW 256

                 ....*...
gi 564380513 790 DGDPSKRP 797
Cdd:cd05046  257 AVNPKDRP 264
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
614-739 2.31e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 62.97  E-value: 2.31e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 614 HGSVIDYNYGGGSSVAVLLIMERLHRDLYTGLKAG---LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNR 690
Cdd:PHA03209 116 HPSVIRMKDTLVSGAITCMVLPHYSSDLYTYLTKRsrpLPIDQALIIEKQILEGLRYLHAQRIIHRDVKTENIFINDVDQ 195
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564380513 691 AKITDLGF--CKPEAMMSGSIVGTPIHMAPE-LFTGKYDNSVDVYAFGILFW 739
Cdd:PHA03209 196 VCIGDLGAaqFPVVAPAFLGLAGTVETNAPEvLARDKYNSKADIWSAGIVLF 247
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
556-797 2.32e-10

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


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 62.39  E-value: 2.32e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVY-----LCDNWGGHFPCALKSVvppDEKHWNDLALEFHY---MRSLPKHERLVDLHGSVID-------Y 620
Cdd:cd05048   11 EELGEGAFGKVYkgellGPSSEESAISVAIKTL---KENASPKTQQDFRReaeLMSDLQHPNIVCLLGVCTKeqpqcmlF 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 621 NYGGGSSVAVLLIMERLHRDL-----YTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITD 695
Cdd:cd05048   88 EYMAHGDLHEFLVRHSPHSDVgvssdDDGTASSLDQSDFLHIAIQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTVKISD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 696 LGFCKP------EAMMSGSIVgtPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSGSIKLPEAFercaSKDHLWNNVRr 767
Cdd:cd05048  168 FGLSRDiyssdyYRVQSKSLL--PVRwMPPEaILYGKFTTESDVWSFGVVLWEIFSYGLQPYYGY----SNQEVIEMIR- 240
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 564380513 768 gtrpER--LPVfDEEC----WQLMEACWDGDPSKRP 797
Cdd:cd05048  241 ----SRqlLPC-PEDCparvYSLMVECWHEIPSRRP 271
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
595-821 2.40e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 63.48  E-value: 2.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 595 ALEFHYMRSLpKHERLVDLHGSvIDYNYgggssvAVLLIMERLHRDLYTGL--KAGLSLETRLQIALDVVEGIRFLHSQG 672
Cdd:PHA03212 131 ATEAHILRAI-NHPSIIQLKGT-FTYNK------FTCLILPRYKTDLYCYLaaKRNIAICDILAIERSVLRAIQYLHENR 202
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 673 LVHRDIKLKNVLLDKQNRAKITDLG-FCKPEAMMSGSI---VGTPIHMAPELFT-GKYDNSVDVYAFGILFWYICSGSIK 747
Cdd:PHA03212 203 IIHRDIKAENIFINHPGDVCLGDFGaACFPVDINANKYygwAGTIATNAPELLArDPYGPAVDIWSAGIVLFEMATCHDS 282
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 748 LpeaFER------CASKDHLWNNVRR-GTRPERLPVfdeecwqlmeacwdgDPskrpllgivQPILRSIMDRLCKCDSER 820
Cdd:PHA03212 283 L---FEKdgldgdCDSDRQIKLIIRRsGTHPNEFPI---------------DA---------QANLDEIYIGLAKKSSRK 335

                 .
gi 564380513 821 P 821
Cdd:PHA03212 336 P 336
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
556-736 2.48e-10

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: 62.34  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKsVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSVavLLIME 635
Cdd:cd06638   24 ETIGKGTYGKVFKVLNKKNGSKAAVK-ILDPIHDIDEEIEAEYNILKALSDHPNVVKFYGMYYKKDVKNGDQL--WLVLE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RLH----RDLYTG-LKAGLSLETRL--QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMM 705
Cdd:cd06638  101 LCNggsvTDLVKGfLKRGERMEEPIiaYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSaqlTSTRLR 180
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 564380513 706 SGSIVGTPIHMAPELFT------GKYDNSVDVYAFGI 736
Cdd:cd06638  181 RNTSVGTPFWMAPEVIAceqqldSTYDARCDVWSLGI 217
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
553-797 2.64e-10

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: 62.36  E-value: 2.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVVP---PDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNygggssvA 629
Cdd:cd08229   27 RIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIfdlMDAKARADCIKEIDLLKQL-NHPNVIKYYASFIEDN-------E 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHRDLYTGLKAGLSLETRL-------QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG---FC 699
Cdd:cd08229   99 LNIVLELADAGDLSRMIKHFKKQKRLipektvwKYFVQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGlgrFF 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 700 KPEAMMSGSIVGTPIHMAPE-LFTGKYDNSVDVYAFGILFWYICSgsikLPEAFErcASKDHLWNNVRRGTRPERLPV-- 776
Cdd:cd08229  179 SSKTTAAHSLVGTPYYMSPErIHENGYNFKSDIWSLGCLLYEMAA----LQSPFY--GDKMNLYSLCKKIEQCDYPPLps 252
                        250       260
                 ....*....|....*....|...
gi 564380513 777 --FDEECWQLMEACWDGDPSKRP 797
Cdd:cd08229  253 dhYSEELRQLVNMCINPDPEKRP 275
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
655-797 2.77e-10

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: 61.96  E-value: 2.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 655 LQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK------PEAMMSGSIVgtPIH-MAPE-LFTGKYD 726
Cdd:cd05109  112 LNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARlldideTEYHADGGKV--PIKwMALEsILHRRFT 189
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564380513 727 NSVDVYAFGILFWYICSGSIKLPEAFERCASKDHLwnnvRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05109  190 HQSDVWSYGVTVWELMTFGAKPYDGIPAREIPDLL----EKGERLPQPPICTIDVYMIMVKCWMIDSECRP 256
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
656-744 2.85e-10

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: 61.83  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALDVVEGIRFLHSQGLVHRDIKLKNVLLD---KQNRAKITDLGFCKPEAM-MSGSIVGTPIHMAPELFTGK-YDNSVD 730
Cdd:cd14169  105 QLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFGLSKIEAQgMLSTACGTPGYVAPELLEQKpYGKAVD 184
                         90
                 ....*....|....
gi 564380513 731 VYAFGILFWYICSG 744
Cdd:cd14169  185 VWAIGVISYILLCG 198
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
660-749 2.87e-10

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: 62.74  E-value: 2.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQ-GLVHRDIKLKNVLLDKQNRAKITDLGFCKpEAMMSGSIV----GTPIHMAPELFT-GKYDNSVDVYA 733
Cdd:cd05594  133 EIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCK-EGIKDGATMktfcGTPEYLAPEVLEdNDYGRAVDWWG 211
                         90
                 ....*....|....*.
gi 564380513 734 FGILFWYICSGsiKLP 749
Cdd:cd05594  212 LGVVMYEMMCG--RLP 225
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
658-796 2.93e-10

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: 62.07  E-value: 2.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF-C-----KPEAMmsgsiVGTPIHMAPELFTG--KYDNSV 729
Cdd:cd05606  104 AAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLaCdfskkKPHAS-----VGTHGYMAPEVLQKgvAYDSSA 178
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564380513 730 DVYAFGILFWYICSGSiklpEAFERCASKDHLWNNVRRGTRPERLP-VFDEECWQLMEACWDGDPSKR 796
Cdd:cd05606  179 DWFSLGCMLYKLLKGH----SPFRQHKTKDKHEIDRMTLTMNVELPdSFSPELKSLLEGLLQRDVSKR 242
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
553-806 3.10e-10

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


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 62.01  E-value: 3.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLcDNWGGHFPCALKSVvPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVidynygggSSVAVLL 632
Cdd:cd05071   12 RLEVKLGQGCFGEVWM-GTWNGTTRVAIKTL-KPGTMSPEAFLQEAQVMKKL-RHEKLVQLYAVV--------SEEPIYI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERLHR-DLYTGLKAGLSLETRL----QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---PEAM 704
Cdd:cd05071   81 VTEYMSKgSLLDFLKGEMGKYLRLpqlvDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARlieDNEY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 705 MSGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS-GSIKLPEAFERcaskdHLWNNVRRGTRPERLPVFDEEC 781
Cdd:cd05071  161 TARQGAKFPIKwTAPEaALYGRFTIKSDVWSFGILLTELTTkGRVPYPGMVNR-----EVLDQVERGYRMPCPPECPESL 235
                        250       260
                 ....*....|....*....|....*
gi 564380513 782 WQLMEACWDGDPSKRPLLGIVQPIL 806
Cdd:cd05071  236 HDLMCQCWRKEPEERPTFEYLQAFL 260
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
649-797 3.34e-10

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


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 61.97  E-value: 3.34e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 649 LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG---------FCKPE--AMMsgsivgtPIH-M 716
Cdd:cd05051  128 LSYGTLLYMATQIASGMKYLESLNFVHRDLATRNCLVGPNYTIKIADFGmsrnlysgdYYRIEgrAVL-------PIRwM 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 717 APELF-TGKYDNSVDVYAFGILFWYICSGSIKLPeaFERCASKDHLWNN---VRRGTRPERL---PVFDEECWQLMEACW 789
Cdd:cd05051  201 AWESIlLGKFTTKSDVWAFGVTLWEILTLCKEQP--YEHLTDEQVIENAgefFRDDGMEVYLsrpPNCPKEIYELMLECW 278

                 ....*...
gi 564380513 790 DGDPSKRP 797
Cdd:cd05051  279 RRDEEDRP 286
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
556-745 3.38e-10

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: 61.73  E-value: 3.38e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLAL-EFHYMRSLpKHERLVDLHgSVIDynygggSSVAVLLIM 634
Cdd:cd07836    6 EKLGEGTYATVYKGRNRTTGEIVALKEIHLDAEEGTPSTAIrEISLMKEL-KHENIVRLH-DVIH------TENKLMLVF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 ERLHRDL--YT---GLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKPEAMM 705
Cdd:cd07836   78 EYMDKDLkkYMdthGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGlaraFGIPVNTF 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564380513 706 SGSIVgTPIHMAPELFTGK--YDNSVDVYAFGILFWYICSGS 745
Cdd:cd07836  158 SNEVV-TLWYRAPDVLLGSrtYSTSIDIWSVGCIMAEMITGR 198
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
553-744 3.76e-10

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: 61.42  E-value: 3.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVvppDEKHWNDLALEFHYMRSLPKHERLVdlHGSVID-YNYGGGSSVaVL 631
Cdd:cd14186    4 KVLNLLGKGSFACVYRARSLHTGLEVAIKMI---DKKAMQKAGMVQRVRNEVEIHCQLK--HPSILElYNYFEDSNY-VY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIME-----RLHRDLYTGLKAGLSLETRlQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMS 706
Cdd:cd14186   78 LVLEmchngEMSRYLKNRKKPFTEDEAR-HFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPH 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564380513 707 G---SIVGTPIHMAPELFT-GKYDNSVDVYAFGILFWYICSG 744
Cdd:cd14186  157 EkhfTMCGTPNYISPEIATrSAHGLESDVWSLGCMFYTLLVG 198
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
545-813 3.77e-10

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: 61.87  E-value: 3.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 545 DVLLHRKP-KLGQELGRGQYGVV---YLCDNWGGHFPCALKSVVPPD--EKHWNDLALEFHYMRSLpKHERLVDLHGSVI 618
Cdd:cd14204    1 DVMIDRNLlSLGKVLGEGEFGSVmegELQQPDGTNHKVAVKTMKLDNfsQREIEEFLSEAACMKDF-NHPNVIRLLGVCL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 619 DYNYGGGSSVAVLLIMER---LHRDL-YTGLKAG---LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA 691
Cdd:cd14204   80 EVGSQRIPKPMVILPFMKygdLHSFLlRSRLGSGpqhVPLQTLLKFMIDIALGMEYLSSRNFLHRDLAARNCMLRDDMTV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 692 KITDLGFCKP----EAMMSGSIVGTPIH------MAPELFTGKydnsVDVYAFGILFWYICSGSIKLPEAFERCASKDHL 761
Cdd:cd14204  160 CVADFGLSKKiysgDYYRQGRIAKMPVKwiavesLADRVYTVK----SDVWAFGVTMWEIATRGMTPYPGVQNHEIYDYL 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564380513 762 WNNVRRGTRPERLpvfdEECWQLMEACWDGDPSKRPLLGIVQPILRSIMDRL 813
Cdd:cd14204  236 LHGHRLKQPEDCL----DELYDIMYSCWRSDPTDRPTFTQLRENLEKLLESL 283
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
553-813 4.14e-10

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: 61.23  E-value: 4.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLcdnwgGHF--------PCALKSVVP-PDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIdynyg 623
Cdd:cd05033    7 TIEKVIGGGEFGEVCS-----GSLklpgkkeiDVAIKTLKSgYSDKQRLDFLTEASIMGQF-DHPNVIRLEGVVT----- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 624 ggSSVAVLLIMERL-HRDLYTGLK---AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC 699
Cdd:cd05033   76 --KSRPVMIVTEYMeNGSLDKFLRendGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 700 K----PEA---MMSGSIvgtPIH-MAPELFT-GKYDNSVDVYAFGILFWYICSGSIKlpeAFERCASKDHLwNNVRRGTR 770
Cdd:cd05033  154 RrledSEAtytTKGGKI---PIRwTAPEAIAyRKFTSASDVWSFGIVMWEVMSYGER---PYWDMSNQDVI-KAVEDGYR 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 564380513 771 ---PERLPvfdEECWQLMEACWDGDPSKRPLLGIVqpilRSIMDRL 813
Cdd:cd05033  227 lppPMDCP---SALYQLMLDCWQKDRNERPTFSQI----VSTLDKM 265
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
656-798 4.27e-10

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 61.52  E-value: 4.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALDVVEGIRFLHSQGLVHRDIKLKNVL---LDKQN--RAKITDLGFCKpEAMMSGS--IVGTPIHMAPELFTG-KYDN 727
Cdd:cd14067  118 KIAYQIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQEhiNIKLSDYGISR-QSFHEGAlgVEGTPGYQAPEIRPRiVYDE 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 728 SVDVYAFGILFWYICSGsiklpeafERCASKDH---LWNNVRRGTRP-----ERLPVFdeeCWQ-LMEACWDGDPSKRPL 798
Cdd:cd14067  197 KVDMFSYGMVLYELLSG--------QRPSLGHHqlqIAKKLSKGIRPvlgqpEEVQFF---RLQaLMMECWDTKPEKRPL 265
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
645-797 4.39e-10

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: 61.63  E-value: 4.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 645 LKAGLSLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPEL 720
Cdd:cd06641   93 LEPGPLDETQIATILrEILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAgqlTDTQIKRN*FVGTPFWMAPEV 172
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564380513 721 F-TGKYDNSVDVYAFGILFWYICSGSiklPEAFERCASKDHLWnnVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd06641  173 IkQSAYDSKADIWSLGITAIELARGE---PPHSELHPMKVLFL--IPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRP 245
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
551-805 4.77e-10

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: 62.36  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQ-----ELGRGQYGVVYLCDNWGGHFPCALKsVVPPDEKHWNDlalEFHYMR------SLPKHERLVDLHGSVID 619
Cdd:cd05600    7 RLKLSDfqiltQVGQGGYGSVFLARKKDTGEICALK-IMKKKVLFKLN---EVNHVLterdilTTTNSPWLVKLLYAFQD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 620 YNYgggssvaVLLIMERL----HRDLYTGLKAGLSLETRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITD 695
Cdd:cd05600   83 PEN-------VYLAMEYVpggdFRTLLNNSGILSEEHARFYIA-EMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 696 LGFCK----PEAMMS------------------------------------GSIVGTPIHMAPELFTGK-YDNSVDVYAF 734
Cdd:cd05600  155 FGLASgtlsPKKIESmkirleevkntafleltakerrniyramrkedqnyaNSVVGSPDYMAPEVLRGEgYDLTVDYWSL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 735 G-ILFWYIC-----SGSiklpeafercaSKDHLWNNVRRGTRPERLPVFDE---------ECWQLMEACWDgDPSKRplL 799
Cdd:cd05600  235 GcILFECLVgfppfSGS-----------TPNETWANLYHWKKTLQRPVYTDpdlefnlsdEAWDLITKLIT-DPQDR--L 300

                 ....*.
gi 564380513 800 GIVQPI 805
Cdd:cd05600  301 QSPEQI 306
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
557-738 4.84e-10

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: 61.43  E-value: 4.84e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDL-AL-EFHYMRSLpKHERLVDLHGSVIDYNYGGGSSvAVLLIM 634
Cdd:cd07840    6 QIGEGTYGQVYKARNKKTGELVALKKIRMENEKEGFPItAIrEIKLLQKL-DHPNVVRLKEIVTSKGSAKYKG-SIYMVF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 ERLHRDLytglkAGLSLETRLQIALDVV--------EGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKPE 702
Cdd:cd07840   84 EYMDHDL-----TGLLDNPEVKFTESQIkcymkqllEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFGlarpYTKEN 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564380513 703 AMMSGSIVGTPIHMAPELFTG--KYDNSVDVYAFGILF 738
Cdd:cd07840  159 NADYTNRVITLWYRPPELLLGatRYGPEVDMWSVGCIL 196
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
560-797 5.09e-10

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


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 60.79  E-value: 5.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 560 RGQYGVVYLCDNWGGHFPCALKsVVPPDEKHWNDLALEFHYmrslpKHERLVDLHGSVI-------DYNYGGGSSVavll 632
Cdd:cd13995   14 RGAFGKVYLAQDTKTKKRMACK-LIPVEQFKPSDVEIQACF-----RHENIAELYGALLweetvhlFMEAGEGGSV---- 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 iMERLHrdlytglKAGLSLETRL-QIALDVVEGIRFLHSQGLVHRDIKLKNVLLdKQNRAKITDLGFC---KPEAMMSGS 708
Cdd:cd13995   84 -LEKLE-------SCGPMREFEIiWVTKHVLKGLDFLHSKNIIHHDIKPSNIVF-MSTKAVLVDFGLSvqmTEDVYVPKD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 709 IVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGSIKLPEAFERCASKDHLWNNVRRGTRPERLPvfdEEC----WQ 783
Cdd:cd13995  155 LRGTEIYMSPEVILCRgHNTKADIYSLGATIIHMQTGSPPWVRRYPRSAYPSYLYIIHKQAPPLEDIA---QDCspamRE 231
                        250
                 ....*....|....
gi 564380513 784 LMEACWDGDPSKRP 797
Cdd:cd13995  232 LLEAALERNPNHRS 245
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
642-797 5.18e-10

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


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 61.31  E-value: 5.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 642 YTGLKAGLSLETR--LQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGT----PIH 715
Cdd:cd05043  104 LSEANNPQALSTQqlVHMALQIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALSRDLFPMDYHCLGDnenrPIK 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 716 -MAPELFTGK-YDNSVDVYAFGILFWYICSGSiKLPEA----FErcaskdhLWNNVRRGTR---PERLPvfdEECWQLME 786
Cdd:cd05043  184 wMSLESLVNKeYSSASDVWSFGVLLWELMTLG-QTPYVeidpFE-------MAAYLKDGYRlaqPINCP---DELFAVMA 252
                        170
                 ....*....|.
gi 564380513 787 ACWDGDPSKRP 797
Cdd:cd05043  253 CCWALDPEERP 263
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
592-737 5.18e-10

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: 61.81  E-value: 5.18e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 592 NDLALEFHYMRSlpkherlvDLHgSVIDYNygggssvavllIMERLHRD--LYTGLKAglsletrlqialdvvegIRFLH 669
Cdd:cd07852   82 KDIYLVFEYMET--------DLH-AVIRAN-----------ILEDIHKQyiMYQLLKA-----------------LKYLH 124
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380513 670 SQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSI--------VGTPIHMAPELFTG--KYDNSVDVYAFG-IL 737
Cdd:cd07852  125 SGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQLEEDDenpvltdyVATRWYRAPEILLGstRYTKGVDMWSVGcIL 203
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
553-799 5.30e-10

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: 61.02  E-value: 5.30e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLA------LEFHYMRSL---PKHE---RLVDLHGSVIDY 620
Cdd:cd14101    3 TMGNLLGKGGFGTVYAGHRISDGLQVAIKQISRNRVQQWSKLPgvnpvpNEVALLQSVgggPGHRgviRLLDWFEIPEGF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 621 nygggssvavLLIMER-LH-RDLYTGLKAGLSLETRL--QIALDVVEGIRFLHSQGLVHRDIKLKNVLLD-KQNRAKITD 695
Cdd:cd14101   83 ----------LLVLERpQHcQDLFDYITERGALDESLarRFFKQVVEAVQHCHSKGVVHRDIKDENILVDlRTGDIKLID 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 696 LGfckpeammSGSIV---------GTPIHMAPE-LFTGKYDN-SVDVYAFGILFWYICSGSIKLPEAFERCASKDHLwnn 764
Cdd:cd14101  153 FG--------SGATLkdsmytdfdGTRVYSPPEwILYHQYHAlPATVWSLGILLYDMVCGDIPFERDTDILKAKPSF--- 221
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564380513 765 vrrgtrpeRLPVfDEECWQLMEACWDGDPSKRPLL 799
Cdd:cd14101  222 --------NKRV-SNDCRSLIRSCLAYNPSDRPSL 247
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
557-797 6.27e-10

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: 61.02  E-value: 6.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLCDNWGGHFPCALKSV-VPPDEKHWNDLALEfhymrslpkherLVDLHGSVIDY--NYGGGSSV--AVL 631
Cdd:cd06622    8 ELGKGNYGSVYKVLHRPTGVTMAMKEIrLELDESKFNQIIME------------LDILHKAVSPYivDFYGAFFIegAVY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLHRDLYTGLKAGLSLETRL------QIALDVVEGIRFLHSQ-GLVHRDIKLKNVLLDKQNRAKITDLGFC-KPEA 703
Cdd:cd06622   76 MCMEYMDAGSLDKLYAGGVATEGIpedvlrRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSgNLVA 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 MMSGSIVGTPIHMAPELFTG-------KYDNSVDVYAFGILFWYICSGSIKL-PEAFERCASKdhlWNNVRRGTRPERLP 775
Cdd:cd06622  156 SLAKTNIGCQSYMAPERIKSggpnqnpTYTVQSDVWSLGLSILEMALGRYPYpPETYANIFAQ---LSAIVDGDPPTLPS 232
                        250       260
                 ....*....|....*....|..
gi 564380513 776 VFDEECWQLMEACWDGDPSKRP 797
Cdd:cd06622  233 GYSDDAQDFVAKCLNKIPNRRP 254
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
597-743 6.45e-10

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: 61.13  E-value: 6.45e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 597 EFHYMRSLPKHERLVDLHGSVIDYNYGggsSVAvlLIMERLHRDLY---TGLKAGLSLETRLQIALDVVEGIRFLHSQGL 673
Cdd:cd07831   47 EIQALRRLSPHPNILRLIEVLFDRKTG---RLA--LVFELMDMNLYeliKGRKRPLPEKRVKNYMYQLLKSLDHMHRNGI 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 674 VHRDIKLKNVLLdKQNRAKITDLGFCKpeammsgSIVGTPIHM---------APE--LFTGKYDNSVDVYAFGILFWYIC 742
Cdd:cd07831  122 FHRDIKPENILI-KDDILKLADFGSCR-------GIYSKPPYTeyistrwyrAPEclLTDGYYGPKMDIWAVGCVFFEIL 193

                 .
gi 564380513 743 S 743
Cdd:cd07831  194 S 194
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
668-796 7.50e-10

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: 61.05  E-value: 7.50e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 668 LHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK---PEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICS 743
Cdd:cd05585  110 LHKFNVIYRDLKPENILLDYTGHIALCDFGLCKlnmKDDDKTNTFCGTPEYLAPELLLGHgYTKAVDWWTLGVLLYEMLT 189
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564380513 744 GsikLPEAFercaskDHLWNNVRRG--TRPERLP-VFDEECWQLMEACWDGDPSKR 796
Cdd:cd05585  190 G---LPPFY------DENTNEMYRKilQEPLRFPdGFDRDAKDLLIGLLNRDPTKR 236
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
662-737 7.80e-10

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 61.17  E-value: 7.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 662 VEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG-FCKPEAMM---SGSIVGTPIHMAPELFT-------GKYDNSVD 730
Cdd:cd05601  112 VLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGsAAKLSSDKtvtSKMPVGTPDYIAPEVLTsmnggskGTYGVECD 191

                 ....*..
gi 564380513 731 VYAFGIL 737
Cdd:cd05601  192 WWSLGIV 198
pknD PRK13184
serine/threonine-protein kinase PknD;
645-741 8.61e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 62.48  E-value: 8.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 645 LKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----------------FCKPEAMMS-- 706
Cdd:PRK13184 106 LAEKTSVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGaaifkkleeedlldidVDERNICYSsm 185
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564380513 707 ---GSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYI 741
Cdd:PRK13184 186 tipGKIVGTPDYMAPERLLGvPASESTDIYALGVILYQM 224
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
645-797 8.66e-10

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: 60.46  E-value: 8.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 645 LKAGLSLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPEL 720
Cdd:cd06642   93 LKPGPLEETYIATILrEILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAgqlTDTQIKRNTFVGTPFWMAPEV 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 721 F-TGKYDNSVDVYAFGILfwyicsgSIKLPEAfERCASKDH---LWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKR 796
Cdd:cd06642  173 IkQSAYDFKADIWSLGIT-------AIELAKG-EPPNSDLHpmrVLFLIPKNSPPTLEGQHSKPFKEFVEACLNKDPRFR 244

                 .
gi 564380513 797 P 797
Cdd:cd06642  245 P 245
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
629-808 8.76e-10

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


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 60.34  E-value: 8.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 AVLLIMER-----LHRDLyTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP-- 701
Cdd:cd05115   77 ALMLVMEMasggpLNKFL-SGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSKAlg 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 --EAMMSGSIVGT-PIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS------GSIKLPEAFercaskdhlwNNVRRGTR 770
Cdd:cd05115  156 adDSYYKARSAGKwPLKwYAPEcINFRKFSSRSDVWSYGVTMWEAFSygqkpyKKMKGPEVM----------SFIEQGKR 225
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564380513 771 PERLPVFDEECWQLMEACWDGDPSKRPLLGIVQPILRS 808
Cdd:cd05115  226 MDCPAECPPEMYALMSDCWIYKWEDRPNFLTVEQRMRT 263
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
554-738 9.61e-10

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: 60.63  E-value: 9.61e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDlalEFHYMRSLPKHERLVDLHGSVIDYNYGGGSsvavlLI 633
Cdd:cd14132   22 IIRKIGRGKYSEVFEGINIGNNEKVVIKVLKPVKKKKIKR---EIKILQNLRGGPNIVKLLDVVKDPQSKTPS-----LI 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERL-HRDLYTgLKAGLSLE------TRLQIALDvvegirFLHSQGLVHRDIKLKNVLLDKQNRA-KITDLG---FCKPe 702
Cdd:cd14132   94 FEYVnNTDFKT-LYPTLTDYdiryymYELLKALD------YCHSKGIMHRDVKPHNIMIDHEKRKlRLIDWGlaeFYHP- 165
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564380513 703 aMMSGSI-VGTPIHMAPELFTG--KYDNSVDVYAFGILF 738
Cdd:cd14132  166 -GQEYNVrVASRYYKGPELLVDyqYYDYSLDMWSLGCML 203
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
651-797 1.04e-09

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


Pssm-ID: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 60.21  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 651 LETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN-RAKITDLGFCKPEAMMS---------------GSIVGTPI 714
Cdd:cd14049  119 VDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHGSDiHVRIGDFGLACPDILQDgndsttmsrlnglthTSGVGTCL 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 715 HMAPELFTG-KYDNSVDVYAFGILFwyicsgsIKLPEAFERCASKDHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDP 793
Cdd:cd14049  199 YAAPEQLEGsHYDFKSDMYSIGVIL-------LELFQPFGTEMERAEVLTQLRNGQIPKSLCKRWPVQAKYIKLLTSTEP 271

                 ....
gi 564380513 794 SKRP 797
Cdd:cd14049  272 SERP 275
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
648-744 1.06e-09

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: 60.36  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 648 GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA---KITDLGFCKP--EAMMSGSIVGTPIHMAPELF- 721
Cdd:cd14038   97 GLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGEQRlihKIIDLGYAKEldQGSLCTSFVGTLQYLAPELLe 176
                         90       100
                 ....*....|....*....|...
gi 564380513 722 TGKYDNSVDVYAFGILFWYICSG 744
Cdd:cd14038  177 QQKYTVTVDYWSFGTLAFECITG 199
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
659-797 1.07e-09

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


Pssm-ID: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 60.00  E-value: 1.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 659 LDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNrAKITDLGFCK--PEAM--MSGSIVGTPIHMAPELFTGKYDNSV--DVY 732
Cdd:cd14163  108 RQLVEAIRYCHGCGVAHRDLKCENALLQGFT-LKLTDFGFAKqlPKGGreLSQTFCGSTAYAAPEVLQGVPHDSRkgDIW 186
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564380513 733 AFG-ILFWYICSgsiKLPeaFERCASKDHLWNNVRRGTRPERLPVfDEECWQLMEACWDGDPSKRP 797
Cdd:cd14163  187 SMGvVLYVMLCA---QLP--FDDTDIPKMLCQQQKGVSLPGHLGV-SRTCQDLLKRLLEPDMVLRP 246
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
553-812 1.12e-09

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


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 60.02  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLcDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSlPKHERLVDLHGSVIdynygggsSVAVLL 632
Cdd:cd14153    3 EIGELIGKGRFGQVYH-GRWHGEVAIRLIDIERDNEEQLKAFKREVMAYRQ-TRHENVVLFMGACM--------SPPHLA 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERL--HRDLYTGL---KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDkQNRAKITDLG-FCKPEAMMS 706
Cdd:cd14153   73 IITSLckGRTLYSVVrdaKVVLDVNKTRQIAQEIVKGMGYLHAKGILHKDLKSKNVFYD-NGKVVITDFGlFTISGVLQA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 707 GS-------IVGTPIHMAPELFTG----------KYDNSVDVYAFGILfWYICSGSiKLPeaFERCASKDHLWnNVRRGT 769
Cdd:cd14153  152 GRredklriQSGWLCHLAPEIIRQlspeteedklPFSKHSDVFAFGTI-WYELHAR-EWP--FKTQPAEAIIW-QVGSGM 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564380513 770 RPERLPV-FDEECWQLMEACWDGDPSKRPLLGIVQPILRSIMDR 812
Cdd:cd14153  227 KPNLSQIgMGKEISDILLFCWAYEQEERPTFSKLMEMLEKLPKR 270
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
553-738 1.20e-09

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 60.41  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVY--LCDNWGGHfpCALKSVVPPDEKhwnDL----AL-EFHYMRSLpKHERLVDLHGSVIDYNYG-G 624
Cdd:cd07866   11 EILGKLGEGTFGEVYkaRQIKTGRV--VALKKILMHNEK---DGfpitALrEIKILKKL-KHPNVVPLIDMAVERPDKsK 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 625 GSSVAVLLIMERLHRDLytglkAGLsLET---RLQ------IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITD 695
Cdd:cd07866   85 RKRGSVYMVTPYMDHDL-----SGL-LENpsvKLTesqikcYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIAD 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564380513 696 LGF------CKPEAMMSG--------SIVGTPIHMAPELFTG--KYDNSVDVYAFGILF 738
Cdd:cd07866  159 FGLarpydgPPPNPKGGGgggtrkytNLVVTRWYRPPELLLGerRYTTAVDIWGIGCVF 217
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
553-797 1.35e-09

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: 59.76  E-value: 1.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYL-CDNWGGHFpcALKSVV--PPD----EKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYN---- 621
Cdd:cd06631    4 KKGNVLGKGAYGTVYCgLTSTGQLI--AVKQVEldTSDkekaEKEYEKLQEEVDLLKTL-KHVNIVGYLGTCLEDNvvsi 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 622 ---YGGGSSVAVLL-----IMERLHRdLYTGlkaglsletrlQIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKI 693
Cdd:cd06631   81 fmeFVPGGSIASILarfgaLEEPVFC-RYTK-----------QI----LEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKL 144
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 694 TDLGFCKPEAM---------MSGSIVGTPIHMAPELF--TGkYDNSVDVYAFGILFWYICSGsiKLPEA-FERCASKDHL 761
Cdd:cd06631  145 IDFGCAKRLCInlssgsqsqLLKSMRGTPYWMAPEVIneTG-HGRKSDIWSIGCTVFEMATG--KPPWAdMNPMAAIFAI 221
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 564380513 762 WNnvRRGTRPeRLPV-FDEECWQLMEACWDGDPSKRP 797
Cdd:cd06631  222 GS--GRKPVP-RLPDkFSPEARDFVHACLTRDQDERP 255
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
656-738 1.39e-09

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: 59.61  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALdvveGIRFLHSQGLVHRDIKLKNVLLDKQNRA--KITDLGFC---KPEAMMSgSIVGTPIHMAPELFTGK-YDNSV 729
Cdd:cd14121  103 QLAS----ALQFLREHNISHMDLKPQNLLLSSRYNPvlKLADFGFAqhlKPNDEAH-SLRGSPLYMAPEMILKKkYDARV 177
                         90
                 ....*....|
gi 564380513 730 DVYAFG-ILF 738
Cdd:cd14121  178 DLWSVGvILY 187
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
658-796 1.42e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 60.46  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF-CKPEAMMSGSIVGTPIHMAPELFTG--KYDNSVDVYAF 734
Cdd:cd05633  114 ATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLaCDFSKKKPHASVGTHGYMAPEVLQKgtAYDSSADWFSL 193
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564380513 735 GILFWYICSGSiklpEAFERCASKD-HLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKR 796
Cdd:cd05633  194 GCMLFKLLRGH----SPFRQHKTKDkHEIDRMTLTVNVELPDSFSPELKSLLEGLLQRDVSKR 252
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
558-796 1.50e-09

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: 59.76  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLcDNWGGHfPCALKSVVPPDEKHWNDLAlEFhYMRSLPKHERLVdlhGSVIDYNYGGGSSVAVLLIME-R 636
Cdd:cd14143    3 IGKGRFGEVWR-GRWRGE-DVAVKIFSSREERSWFREA-EI-YQTVMLRHENIL---GFIAADNKDNGTWTQLWLVSDyH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 637 LHRDLYTGL-KAGLSLETRLQIALDVVEGIRFLH-----SQG---LVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSG 707
Cdd:cd14143   76 EHGSLFDYLnRYTVTVEGMIKLALSIASGLAHLHmeivgTQGkpaIAHRDLKSKNILVKKNGTCCIADLGLAVRHDSATD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 SI-------VGTPIHMAPELFtgkyDNSV-----------DVYAFGILFWYI---CS-GSI----KLPEAFERCA--SKD 759
Cdd:cd14143  156 TIdiapnhrVGTKRYMAPEVL----DDTInmkhfesfkraDIYALGLVFWEIarrCSiGGIhedyQLPYYDLVPSdpSIE 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 564380513 760 HLWNNV-RRGTRPErLPVFDEEC------WQLMEACWDGDPSKR 796
Cdd:cd14143  232 EMRKVVcEQKLRPN-IPNRWQSCealrvmAKIMRECWYANGAAR 274
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
553-741 1.66e-09

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: 59.74  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSV----VPPdeKHWNDLALEFHYMRSLpKHERLVDLHGS---------VID 619
Cdd:cd14086    4 DLKEELGKGAFSVVRRCVQKSTGQEFAAKIIntkkLSA--RDHQKLEREARICRLL-KHPNIVRLHDSiseegfhylVFD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 620 YNYGGGssvavlLIMERLHRDLYTGLKAGLSLEtrlQIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKQNR---AKITDL 696
Cdd:cd14086   81 LVTGGE------LFEDIVAREFYSEADASHCIQ---QI----LESVNHCHQNGIVHRDLKPENLLLASKSKgaaVKLADF 147
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564380513 697 GFCkpeAMMSGS------IVGTPIHMAPE-LFTGKYDNSVDVYAFGILFwYI 741
Cdd:cd14086  148 GLA---IEVQGDqqawfgFAGTPGYLSPEvLRKDPYGKPVDIWACGVIL-YI 195
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
558-738 1.84e-09

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: 59.61  E-value: 1.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVY-LCDNWGGHFpCALKSV--------VPPDekhwndlAL-EFHYMRSLpKHERLVDLHGSVIDYNygggss 627
Cdd:cd07835    7 IGEGTYGVVYkARDKLTGEI-VALKKIrletedegVPST-------AIrEISLLKEL-NHPNIVRLLDVVHSEN------ 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 vAVLLIMERLHRDL--YTGLKAGLSLETRL------QIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG-- 697
Cdd:cd07835   72 -KLYLVFEFLDLDLkkYMDSSPLTGLDPPLiksylyQL----LQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGla 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564380513 698 --FCKPEAMMSGSIVgTPIHMAPELFTG--KYDNSVDVYAFGILF 738
Cdd:cd07835  147 raFGVPVRTYTHEVV-TLWYRAPEILLGskHYSTPVDIWSVGCIF 190
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
594-797 1.87e-09

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: 59.56  E-value: 1.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 594 LALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaVLLIMERLHR----DLYTGLKAGLSLETRLQIAlDVVEGIRFLH 669
Cdd:cd14187   54 MSMEIAIHRSL-AHQHVVGFHGFFEDNDF-------VYVVLELCRRrsllELHKRRKALTEPEARYYLR-QIILGCQYLH 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 670 SQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP---EAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGs 745
Cdd:cd14187  125 RNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKveyDGERKKTLCGTPNYIAPEVLSKKgHSFEVDIWSIGCIMYTLLVG- 203
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564380513 746 iKLPeaFE-RCASKDHLWNNVRRGTRPERL-PVfdeeCWQLMEACWDGDPSKRP 797
Cdd:cd14187  204 -KPP--FEtSCLKETYLRIKKNEYSIPKHInPV----AASLIQKMLQTDPTARP 250
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
558-738 1.92e-09

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: 59.87  E-value: 1.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVppDEKHWNDLAL-EFHYMRSLPKHERLvDLHGSV--IDYNYGGGSsvaVLLIM 634
Cdd:cd14210   21 LGKGSFGQVVKCLDHKTGQLVAIKIIR--NKKRFHQQALvEVKILKHLNDNDPD-DKHNIVryKDSFIFRGH---LCIVF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 ERLHRDLYTGLKA----GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA--KITDLGfckpeammSGS 708
Cdd:cd14210   95 ELLSINLYELLKSnnfqGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPSKSsiKVIDFG--------SSC 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 564380513 709 IVGTPIHM--------APELFTG-KYDNSVDVYAFG-ILF 738
Cdd:cd14210  167 FEGEKVYTyiqsrfyrAPEVILGlPYDTAIDMWSLGcILA 206
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
553-809 1.98e-09

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: 59.27  E-value: 1.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVV---PPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYN-------Y 622
Cdd:cd08228    5 QIEKKIGRGQFSEVYRATCLLDRKPVALKKVQifeMMDAKARQDCVKEIDLLKQL-NHPNVIKYLDSFIEDNelnivleL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 623 GGGSSVAVLLIMERLHRDLytglkagLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG---FC 699
Cdd:cd08228   84 ADAGDLSQMIKYFKKQKRL-------IPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGlgrFF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 700 KPEAMMSGSIVGTPIHMAPE-LFTGKYDNSVDVYAFGILFWYICSgsikLPEAFErcASKDHLWNNVRRGTRPERLPV-- 776
Cdd:cd08228  157 SSKTTAAHSLVGTPYYMSPErIHENGYNFKSDIWSLGCLLYEMAA----LQSPFY--GDKMNLFSLCQKIEQCDYPPLpt 230
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564380513 777 --FDEECWQLMEACWDGDPSKRPLLGIVQPILRSI 809
Cdd:cd08228  231 ehYSEKLRELVSMCIYPDPDQRPDIGYVHQIAKQM 265
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
558-735 2.01e-09

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: 59.82  E-value: 2.01e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLAL--EFHYMRSLpKHERLVDLHGSVIDYNYG---GGSSVAVLL 632
Cdd:cd07864   15 IGEGTYGQVYKAKDKDTGELVALKKVRLDNEKEGFPITAirEIKILRQL-NHRSVVNLKEIVTDKQDAldfKKDKGAFYL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERLHRDLYTGLKAGL---SLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKPEAMM 705
Cdd:cd07864   94 VFEYMDHDLMGLLESGLvhfSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFGlarlYNSEESRP 173
                        170       180       190
                 ....*....|....*....|....*....|..
gi 564380513 706 SGSIVGTPIHMAPELFTG--KYDNSVDVYAFG 735
Cdd:cd07864  174 YTNKVITLWYRPPELLLGeeRYGPAIDVWSCG 205
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
554-799 2.11e-09

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: 59.27  E-value: 2.11e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLcDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSlPKHERLVDLHGSVIDYN------YGGGSS 627
Cdd:cd14149   16 LSTRIGSGSFGTVYK-GKWHGDVAVKILKVVDPTPEQFQAFRNEVAVLRK-TRHVNILLFMGYMTKDNlaivtqWCEGSS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 vavllimerLHRDLYTgLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSG 707
Cdd:cd14149   94 ---------LYKHLHV-QETKFQMFQLIDIARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVKSRWSG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 S-----IVGTPIHMAPELFTGKYDN----SVDVYAFGILFWYICSGsiKLPeaFERCASKDHLWNNVRRGTRPERLPVFD 778
Cdd:cd14149  164 SqqveqPTGSILWMAPEVIRMQDNNpfsfQSDVYSYGIVLYELMTG--ELP--YSHINNRDQIIFMVGRGYASPDLSKLY 239
                        250       260
                 ....*....|....*....|....*
gi 564380513 779 EECWQLMEA----CWDGDPSKRPLL 799
Cdd:cd14149  240 KNCPKAMKRlvadCIKKVKEERPLF 264
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
653-738 2.12e-09

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: 60.02  E-value: 2.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 653 TRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC-------KPEAMMSGSIVGTPIHMAPELF--TG 723
Cdd:cd05598  103 ARFYIA-ELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCtgfrwthDSKYYLAHSLVGTPNYIAPEVLlrTG 181
                         90
                 ....*....|....*.
gi 564380513 724 kYDNSVDVYAFG-ILF 738
Cdd:cd05598  182 -YTQLCDWWSVGvILY 196
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
661-746 2.29e-09

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


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 59.06  E-value: 2.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGS-----IVGTPIHMAPELFT-GKYDNSVDVYAF 734
Cdd:cd14070  112 LVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYSdpfstQCGSPAYAAPELLArKKYGPKVDVWSI 191
                         90
                 ....*....|..
gi 564380513 735 GILFWYICSGSI 746
Cdd:cd14070  192 GVNMYAMLTGTL 203
STKc_BMPR1b cd14219
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs ...
550-796 2.30e-09

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IB; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1b, also called Activin receptor-Like Kinase 6 (ALK6), functions as a receptor for bone morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Mutations in BMPR1b that led to inhibition of chondrogenesis can cause Brachydactyly (BD) type A2, a dominant hand malformation characterized by shortening and lateral deviation of the index fingers. A point mutation in the BMPR1b kinase domain is also associated with the Booroola phenotype, characterized by precocious differentiation of ovarian follicles. BMPR1b belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1b, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271121 [Multi-domain]  Cd Length: 305  Bit Score: 59.68  E-value: 2.30e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 550 RKPKLGQELGRGQYGVVYLcDNWGGHfPCALKSVVPPDEKHWndLALEFHYMRSLPKHERLVDLHGSVIDynyGGGSSVA 629
Cdd:cd14219    5 KQIQMVKQIGKGRYGEVWM-GKWRGE-KVAVKVFFTTEEASW--FRETEIYQTVLMRHENILGFIAADIK---GTGSWTQ 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMErLHRD--LYTGLKAG-LSLETRLQIALDVVEGIRFLHSQ--------GLVHRDIKLKNVLLDKQNRAKITDLGF 698
Cdd:cd14219   78 LYLITD-YHENgsLYDYLKSTtLDTKAMLKLAYSSVSGLCHLHTEifstqgkpAIAHRDLKSKNILVKKNGTCCIADLGL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 699 CKPEAMMSGSI-------VGTPIHMAPELFTGKYDNS-------VDVYAFGILFWYIC----SGSI----KLPeaFERCA 756
Cdd:cd14219  157 AVKFISDTNEVdippntrVGTKRYMPPEVLDESLNRNhfqsyimADMYSFGLILWEVArrcvSGGIveeyQLP--YHDLV 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 564380513 757 SKDHLWNNVRRGTRPERL-PVF-----DEECW----QLMEACWDGDPSKR 796
Cdd:cd14219  235 PSDPSYEDMREIVCIKRLrPSFpnrwsSDECLrqmgKLMTECWAHNPASR 284
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
652-797 2.35e-09

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: 59.05  E-value: 2.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 652 ETRL-QIALDVVEGIRFLHSQ-GLVHRDIKLKNVLLDKQNRAKITDLGFCK---PEAMMSGSIVGTPIHMAPELFTGK-Y 725
Cdd:cd08528  112 EDRIwNIFVQMVLALRYLHKEkQIVHRDLKPNNIMLGEDDKVTITDFGLAKqkgPESSKMTSVVGTILYSCPEIVQNEpY 191
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564380513 726 DNSVDVYAFGILFWYICSGSiklPEAFERC----ASKDhlwnnVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd08528  192 GEKADIWALGCILYQMCTLQ---PPFYSTNmltlATKI-----VEAEYEPLPEGMYSDDITFVIRSCLTPDPEARP 259
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
551-739 2.78e-09

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: 59.49  E-value: 2.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQELGRGQYGVVY--LCDNWGGHfpCALKSV---VPPDEkhwnDLAL-EFHYMRSLP-KHERLVDLHGSVIDYN-- 621
Cdd:cd13977    1 KYSLIREVGRGSYGVVYeaVVRRTGAR--VAVKKIrcnAPENV----ELALrEFWALSSIQrQHPNVIQLEECVLQRDgl 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 622 -----YGGGSSVAVLLIMErlhrdlyTGLKAGLSLETR----LQIALDVVEG---------------------------I 665
Cdd:cd13977   75 aqrmsHGSSKSDLYLLLVE-------TSLKGERCFDPRsacyLWFVMEFCDGgdmneyllsrrpdrqtntsfmlqlssaL 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 666 RFLHSQGLVHRDIKLKNVLLDKQNRA---KITDLGFCK--------PEAMMS------GSIVGTPIHMAPELFTGKYDNS 728
Cdd:cd13977  148 AFLHRNQIVHRDLKPDNILISHKRGEpilKVADFGLSKvcsgsglnPEEPANvnkhflSSACGSDFYMAPEVWEGHYTAK 227
                        250
                 ....*....|.
gi 564380513 729 VDVYAFGILFW 739
Cdd:cd13977  228 ADIFALGIIIW 238
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
662-803 2.88e-09

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


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 59.28  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 662 VEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC-KPEAMMSGS----IVGTPIHMAPELFTGKYDNS------VD 730
Cdd:cd14141  112 IPGLKDGHKPAIAHRDIKSKNVLLKNNLTACIADFGLAlKFEAGKSAGdthgQVGTRRYMAPEVLEGAINFQrdaflrID 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 731 VYAFGILFWYI---CSGS------IKLPeaFERCASKDHLWNNVRRGTRPERLPVFDEECWQ----------LMEACWDG 791
Cdd:cd14141  192 MYAMGLVLWELasrCTASdgpvdeYMLP--FEEEVGQHPSLEDMQEVVVHKKKRPVLRECWQkhagmamlceTIEECWDH 269
                        170
                 ....*....|..
gi 564380513 792 DPSKRPLLGIVQ 803
Cdd:cd14141  270 DAEARLSAGCVE 281
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
661-796 2.96e-09

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: 59.09  E-value: 2.96e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLL-DKQNRAKITDLGFCK----PEA-MMSGSIVGTPIHMAPELFTGK-YDNSVDVYA 733
Cdd:cd14094  118 ILEALRYCHDNNIIHRDVKPHCVLLaSKENSAPVKLGGFGVaiqlGESgLVAGGRVGTPHFMAPEVVKREpYGKPVDVWG 197
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564380513 734 FGILFWYICSGsiKLPeafeRCASKDHLWNNVRRGT---RPERLPVFDEECWQLMEACWDGDPSKR 796
Cdd:cd14094  198 CGVILFILLSG--CLP----FYGTKERLFEGIIKGKykmNPRQWSHISESAKDLVRRMLMLDPAER 257
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
659-741 3.00e-09

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: 58.87  E-value: 3.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 659 LDVVEGIRFLH-SQGLVHRDIKLKNVLLDKQNRAKITDLGFC-------KPEAMMSGSIVGTPI-------HMAPELFTG 723
Cdd:cd14011  121 LQISEALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCisseqatDQFPYFREYDPNLPPlaqpnlnYLAPEYILS 200
                         90
                 ....*....|....*....
gi 564380513 724 K-YDNSVDVYAFGILFWYI 741
Cdd:cd14011  201 KtCDPASDMFSLGVLIYAI 219
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
554-753 3.19e-09

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 59.39  E-value: 3.19e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWGGHFPCALKSV--------VPPDEKHWNDLALEFHYMRSLP-----KHERLVDLHGSVIDY 620
Cdd:PTZ00024  13 KGAHLGEGTYGKVEKAYDTLTGKIVAIKKVkiieisndVTKDRQLVGMCGIHFTTLRELKimneiKHENIMGLVDVYVEG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 621 NYgggssvaVLLIMERLHRDLytglKAGLSLETRLQ------IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKIT 694
Cdd:PTZ00024  93 DF-------INLVMDIMASDL----KKVVDRKIRLTesqvkcILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIA 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380513 695 DLGFC------------------KPEAMMSGSIVgTPIHMAPELFTG--KYDNSVDVYAFGILFWYICSGSIKLPEAFE 753
Cdd:PTZ00024 162 DFGLArrygyppysdtlskdetmQRREEMTSKVV-TLWYRAPELLMGaeKYHFAVDMWSVGCIFAELLTGKPLFPGENE 239
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
658-797 3.29e-09

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: 58.53  E-value: 3.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN---RAKITDLGFCKPEAMMSGSIVGTPIH----MAPEL--FTGKYDNS 728
Cdd:cd14012  110 TLQLLEALEYLHRNGVVHKSLHAGNVLLDRDAgtgIVKLTDYSLGKTLLDMCSRGSLDEFKqtywLPPELaqGSKSPTRK 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380513 729 VDVYAFGILFWYICSGSiklpEAFERCASKDHLWNNVrrgtrperlpVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd14012  190 TDVWDLGLLFLQMLFGL----DVLEKYTSPNPVLVSL----------DLSASLQDFLSKCLSLDPKKRP 244
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
597-797 3.41e-09

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: 58.87  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 597 EFHYMRSLpKHERLVDLHGSV-IDYNygggSSVAVLLIMErlHRDLYTGLKAGLSL---ETRLqIALDVVEGIRFL--HS 670
Cdd:cd13990   54 EYEIHKSL-DHPRIVKLYDVFeIDTD----SFCTVLEYCD--GNDLDFYLKQHKSIperEARS-IIMQVVSALKYLneIK 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 671 QGLVHRDIKLKNVLLDKQN---RAKITDLGFCK---PEAMMSGSI------VGTPIHMAPELF-TG----KYDNSVDVYA 733
Cdd:cd13990  126 PPIIHYDLKPGNILLHSGNvsgEIKITDFGLSKimdDESYNSDGMeltsqgAGTYWYLPPECFvVGktppKISSKVDVWS 205
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564380513 734 FGILFWYICSGsiKLPEAFERCA---SKDHLWNNVRRGTRPERlPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd13990  206 VGVIFYQMLYG--RKPFGHNQSQeaiLEENTILKATEVEFPSK-PVVSSEAKDFIRRCLTYRKEDRP 269
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
557-758 3.41e-09

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: 58.39  E-value: 3.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLCDNWGGHFPCALKsVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIdynygggSSVAVLLIMER 636
Cdd:cd14110   10 EINRGRFSVVRQCEEKRSGQMLAAK-IIPYKPEDKQLVLREYQVLRRL-SHPRIAQLHSAYL-------SPRHLVLIEEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 637 ------LH----RDLYTGLKAGLSLEtrlqialDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP----E 702
Cdd:cd14110   81 csgpelLYnlaeRNSYSEAEVTDYLW-------QILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPfnqgK 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564380513 703 AMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSG----SIKLPEAFERCASK 758
Cdd:cd14110  154 VLMTDKKGDYVETMAPELLEGQgAGPQTDIWAIGVTAFIMLSAdypvSSDLNWERDRNIRK 214
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
661-767 3.58e-09

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: 58.50  E-value: 3.58e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLD---KQNRAKITDLGFCKPEAMMSGSIVGTPIHMAPELFT-GKYDNSVDVYAFGI 736
Cdd:cd14088  108 VLEAVAYLHSLKIVHRNLKLENLVYYnrlKNSKIVISDFHLAKLENGLIKEPCGTPEYLAPEVVGrQRYGRPVDCWAIGV 187
                         90       100       110
                 ....*....|....*....|....*....|.
gi 564380513 737 LFWYICSGSIKLPEAFERCASKDHLWNNVRR 767
Cdd:cd14088  188 IMYILLSGNPPFYDEAEEDDYENHDKNLFRK 218
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
556-797 3.64e-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: 58.79  E-value: 3.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGH------FP----------CALKSVVPPDEKHW-NDLALEFHYMRSLpKHERLVDLHGSVI 618
Cdd:cd05096   11 EKLGEGQFGEVHLCEVVNPQdlptlqFPfnvrkgrpllVAVKILRPDANKNArNDFLKEVKILSRL-KDPNIIRLLGVCV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 619 DynygggsSVAVLLIMERL----------HRDLYTGLKAG------------LSLETRLQIALDVVEGIRFLHSQGLVHR 676
Cdd:cd05096   90 D-------EDPLCMITEYMengdlnqflsSHHLDDKEENGndavppahclpaISYSSLLHVALQIASGMKYLSSLNFVHR 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 677 DIKLKNVLLDKQNRAKITDLGFCKpeAMMSGS---IVGT---PIH-MAPE-LFTGKYDNSVDVYAFGILFWYICS----- 743
Cdd:cd05096  163 DLATRNCLVGENLTIKIADFGMSR--NLYAGDyyrIQGRavlPIRwMAWEcILMGKFTTASDVWAFGVTLWEILMlckeq 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564380513 744 --GSIKLPEAFERCAskdHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05096  241 pyGELTDEQVIENAG---EFFRDQGRQVYLFRPPPCPQGLYELMLQCWSRDCRERP 293
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
554-798 3.78e-09

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: 58.34  E-value: 3.78e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWGGHFPCALKSVVppdEKHWNDLALEFHYMRSLPKHERLvdLHGSVID-YNYGGGSSvAVLL 632
Cdd:cd14117   10 IGRPLGKGKFGNVYLAREKQSKFIVALKVLF---KSQIEKEGVEHQLRREIEIQSHL--RHPNILRlYNYFHDRK-RIYL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERLHR-DLYTGL-KAGLSLETRLQIALD-VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF-CKPEAMMSGS 708
Cdd:cd14117   84 ILEYAPRgELYKELqKHGRFDEQRTATFMEeLADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWsVHAPSLRRRT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 709 IVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSG-----SIKLPEAFERCASKD------------HLWNNVRRGTR 770
Cdd:cd14117  164 MCGTLDYLPPEMIEGRtHDEKVDLWCIGVLCYELLVGmppfeSASHTETYRRIVKVDlkfppflsdgsrDLISKLLRYHP 243
                        250       260
                 ....*....|....*....|....*...
gi 564380513 771 PERLPVFdeecwQLMEACWDGDPSKRPL 798
Cdd:cd14117  244 SERLPLK-----GVMEHPWVKANSRRVL 266
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
617-744 4.37e-09

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: 59.64  E-value: 4.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 617 VIDYnYGGGSSVAVLLIME-RLHRDLytglkaglsleTRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITD 695
Cdd:cd05624  150 VMDY-YVGGDLLTLLSKFEdKLPEDM-----------ARFYIG-EMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLAD 216
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 564380513 696 LGFC----KPEAMMSGSIVGTPIHMAPELF------TGKYDNSVDVYAFGILFWYICSG 744
Cdd:cd05624  217 FGSClkmnDDGTVQSSVAVGTPDYISPEILqamedgMGKYGPECDWWSLGVCMYEMLYG 275
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
558-700 5.22e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 59.09  E-value: 5.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWG--GHFPCALKSVVPPdekhwNDLALEFHYMRSLPkherlvdlHGSVID--YNYGGGSSVAvlLI 633
Cdd:PHA03207 100 LTPGSEGEVFVCTKHGdeQRKKVIVKAVTGG-----KTPGREIDILKTIS--------HRAIINliHAYRWKSTVC--MV 164
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERLHRDLYTGL--KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG-FCK 700
Cdd:PHA03207 165 MPKYKCDLFTYVdrSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGaACK 234
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
606-737 5.39e-09

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: 58.30  E-value: 5.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 606 KHERLVDLHGsvidYNYGGGSSVAVLLIM------ERLHRDlytGLKAGLSLETRLQIALDVVEGIRFLH--SQGLVHRD 677
Cdd:cd14159   50 RHPNIVDLAG----YSAQQGNYCLIYVYLpngsleDRLHCQ---VSCPCLSWSQRLHVLLGTARAIQYLHsdSPSLIHGD 122
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380513 678 IKLKNVLLDKQNRAKITDLG---FCK--PEAMMSGSIV------GTPIHMAPE-LFTGKYDNSVDVYAFGIL 737
Cdd:cd14159  123 VKSSNILLDAALNPKLGDFGlarFSRrpKQPGMSSTLArtqtvrGTLAYLPEEyVKTGTLSVEIDVYSFGVV 194
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
553-797 5.74e-09

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


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 57.67  E-value: 5.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLA------LEFHYMRSLPKHERLVDlhgSVIDYNYGGGS 626
Cdd:cd14100    3 QVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVSEWGELPngtrvpMEIVLLKKVGSGFRGVI---RLLDWFERPDS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 627 SVavlLIMERLH--RDLYTGL--KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLD-KQNRAKITDLGfckP 701
Cdd:cd14100   80 FV---LVLERPEpvQDLFDFIteRGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFG---S 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 EAMMSGSIV----GTPIHMAPEL--FTGKYDNSVDVYAFGILFWYICSGSIKLPEAFErcaskdhlwnnVRRGTRPERLP 775
Cdd:cd14100  154 GALLKDTVYtdfdGTRVYSPPEWirFHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEE-----------IIRGQVFFRQR 222
                        250       260
                 ....*....|....*....|..
gi 564380513 776 VfDEECWQLMEACWDGDPSKRP 797
Cdd:cd14100  223 V-SSECQHLIKWCLALRPSDRP 243
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
669-803 6.45e-09

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


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 58.12  E-value: 6.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 669 HSQGLVHRDIKLKNVLLDKQNRAKITDLGFC------KPEAMMSGSiVGTPIHMAPELFTGKYDNS------VDVYAFGI 736
Cdd:cd14140  120 HKPAIAHRDFKSKNVLLKNDLTAVLADFGLAvrfepgKPPGDTHGQ-VGTRRYMAPEVLEGAINFQrdsflrIDMYAMGL 198
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 737 LFWYICS------GSIK---LPeaFERCASKDHLWNNVRRGTRPERL-PVFdEECW-------QL---MEACWDGDPSKR 796
Cdd:cd14140  199 VLWELVSrckaadGPVDeymLP--FEEEIGQHPSLEDLQEVVVHKKMrPVF-KDHWlkhpglaQLcvtIEECWDHDAEAR 275

                 ....*..
gi 564380513 797 PLLGIVQ 803
Cdd:cd14140  276 LSAGCVE 282
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
556-744 6.46e-09

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: 58.11  E-value: 6.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVvppdEKHWNDLALEFHYMRSLPKHERLVDLHGSvidynYGGGSSVAVLLIME 635
Cdd:cd14175    7 ETIGVGSYSVCKRCVHKATNMEYAVKVI----DKSKRDPSEEIEILLRYGQHPNIITLKDV-----YDDGKHVYLVTELM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 R--------LHRDLYTGLKAGLSLETrlqialdVVEGIRFLHSQGLVHRDIKLKNVL-LDKQNRA---KITDLGFCKPEA 703
Cdd:cd14175   78 RggelldkiLRQKFFSEREASSVLHT-------ICKTVEYLHSQGVVHRDLKPSNILyVDESGNPeslRICDFGFAKQLR 150
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564380513 704 MMSGSIVgTPIH----MAPELFTGK-YDNSVDVYAFGILFWYICSG 744
Cdd:cd14175  151 AENGLLM-TPCYtanfVAPEVLKRQgYDEGCDIWSLGILLYTMLAG 195
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
660-736 6.55e-09

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: 58.54  E-value: 6.55e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC----KPEAMMSGSIVGTPIHMAPELFT-----GKYDNSVD 730
Cdd:cd05596  133 EVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCmkmdKDGLVRSDTAVGTPDYISPEVLKsqggdGVYGRECD 212

                 ....*.
gi 564380513 731 VYAFGI 736
Cdd:cd05596  213 WWSVGV 218
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
554-744 6.77e-09

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: 57.91  E-value: 6.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDynygggssvaVLLI 633
Cdd:cd14085    7 IESELGRGATSVVYRCRQKGTQKPYAVKKLKKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTE----------ISLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MErlhrdLYTG-------LKAGLSLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLL-DKQNRA--KITDLGFCK-- 700
Cdd:cd14085   77 LE-----LVTGgelfdriVEKGYYSERDAADAVkQILEAVAYLHENGIVHRDLKPENLLYaTPAPDAplKIADFGLSKiv 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564380513 701 PEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSG 744
Cdd:cd14085  152 DQQVTMKTVCGTPGYCAPEILRGCaYGPEVDMWSVGVITYILLCG 196
PK_GC-2D cd14043
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-2D; The pseudokinase domain ...
654-797 7.24e-09

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


Pssm-ID: 270945 [Multi-domain]  Cd Length: 267  Bit Score: 57.42  E-value: 7.24e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 654 RLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFckPEAMMSGSIVGTP------IHMAPELF-----T 722
Cdd:cd14043   99 KSSLLLDLIKGMRYLHHRGIVHGRLKSRNCVVDGRFVLKITDYGY--NEILEAQNLPLPEpapeelLWTAPELLrdprlE 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 723 GKYDNSVDVYAFGILFW-YICSG----SIKLP--EAFERCASKDHLwnnVRRGTRPERLPVfdeECWQLMEACWDGDPSK 795
Cdd:cd14043  177 RRGTFPGDVFSFAIIMQeVIVRGapycMLGLSpeEIIEKVRSPPPL---CRPSVSMDQAPL---ECIQLMKQCWSEAPER 250

                 ..
gi 564380513 796 RP 797
Cdd:cd14043  251 RP 252
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
601-741 7.62e-09

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: 57.30  E-value: 7.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 601 MRSLPKHERLVDLHG---------SVID-Y-NYGGGSSvAVLLIMERL-----------HRDL-YTGLKAGlsletrlQI 657
Cdd:cd14089   34 LRDNPKARREVELHWrasgcphivRIIDvYeNTYQGRK-CLLVVMECMeggelfsriqeRADSaFTEREAA-------EI 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLL-DKQNRA--KITDLGFCKpEAMMSGSIVG---TPIHMAPE-LFTGKYDNSVD 730
Cdd:cd14089  106 MRQIGSAVAHLHSMNIAHRDLKPENLLYsSKGPNAilKLTDFGFAK-ETTTKKSLQTpcyTPYYVAPEvLGPEKYDKSCD 184
                        170
                 ....*....|.
gi 564380513 731 VYAFGILFwYI 741
Cdd:cd14089  185 MWSLGVIM-YI 194
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
656-797 7.73e-09

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


Pssm-ID: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 57.58  E-value: 7.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA-MMSGSIVGTPIHMAPELFTG-KYDNSVDVYA 733
Cdd:cd06619   99 RIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVnSIAKTYVGTNAYMAPERISGeQYGIHSDVWS 178
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564380513 734 FGILFWYICSGSIKLPEAFERCASKDHL-WNNVRRGTRPERLPV--FDEECWQLMEACWDGDPSKRP 797
Cdd:cd06619  179 LGISFMELALGRFPYPQIQKNQGSLMPLqLLQCIVDEDPPVLPVgqFSEKFVHFITQCMRKQPKERP 245
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
630-765 8.03e-09

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: 58.50  E-value: 8.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA---MMS 706
Cdd:cd07876  101 VYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACtnfMMT 180
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380513 707 GSIVgTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGSIKLpeafercASKDHL--WNNV 765
Cdd:cd07876  181 PYVV-TRYYRAPEVILGmGYKENVDIWSVGCIMGELVKGSVIF-------QGTDHIdqWNKV 234
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
549-719 8.31e-09

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: 57.61  E-value: 8.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 549 HRKPKLGQeLGRGQYGVVYLCDNWGGHFpCALKSV--VPPDEKHWNDLALEFHYMRSLPKHERLVDLhgsvIDYNYGGGS 626
Cdd:cd14131    1 KPYEILKQ-LGKGGSSKVYKVLNPKKKI-YALKRVdlEGADEQTLQSYKNEIELLKKLKGSDRIIQL----YDYEVTDED 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 627 SVaVLLIMERLHRDLYTGLK----AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKqNRAKITDLGFCK-- 700
Cdd:cd14131   75 DY-LYMVMECGEIDLATILKkkrpKPIDPNFIRYYWKQMLEAVHTIHEEGIVHSDLKPANFLLVK-GRLKLIDFGIAKai 152
                        170       180
                 ....*....|....*....|..
gi 564380513 701 PE---AMMSGSIVGTPIHMAPE 719
Cdd:cd14131  153 QNdttSIVRDSQVGTLNYMSPE 174
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
661-746 9.41e-09

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: 58.22  E-value: 9.41e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAM-----MSGSIVgTPIHMAPELFTG--KYDNSVDVYA 733
Cdd:cd07853  112 ILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEPdeskhMTQEVV-TQYYRAPEILMGsrHYTSAVDIWS 190
                         90
                 ....*....|...
gi 564380513 734 FGILFWYICSGSI 746
Cdd:cd07853  191 VGCIFAELLGRRI 203
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
635-796 9.46e-09

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: 57.74  E-value: 9.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 ERLHRDLYTGLKAGLSLETRLQ------------IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN---RAKITDLGFC 699
Cdd:cd14179   73 DQLHTFLVMELLKGGELLERIKkkqhfseteashIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDESdnsEIKIIDFGFA 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 700 K---PEAMMSGSIVGTPIHMAPELFT-GKYDNSVDVYAFGILFWYICSGSIKLpEAFER---CASKDHLWNNVRRGTRPe 772
Cdd:cd14179  153 RlkpPDNQPLKTPCFTLHYAAPELLNyNGYDESCDLWSLGVILYTMLSGQVPF-QCHDKsltCTSAEEIMKKIKQGDFS- 230
                        170       180       190
                 ....*....|....*....|....*....|..
gi 564380513 773 rlpvFDEECWQ--------LMEACWDGDPSKR 796
Cdd:cd14179  231 ----FEGEAWKnvsqeakdLIQGLLTVDPNKR 258
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
652-797 9.69e-09

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: 56.91  E-value: 9.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 652 ETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKPEAmMSGSIVGTPIHMAPELFTG-KYD 726
Cdd:cd08219  100 DTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGsarlLTSPGA-YACTYVGTPYYVPPEIWENmPYN 178
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564380513 727 NSVDVYAFGILFWYICSgsikLPEAFErCASKDHLWNNVRRGT-RPerLPV-FDEECWQLMEACWDGDPSKRP 797
Cdd:cd08219  179 NKSDIWSLGCILYELCT----LKHPFQ-ANSWKNLILKVCQGSyKP--LPShYSYELRSLIKQMFKRNPRSRP 244
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
556-776 1.03e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 58.98  E-value: 1.03e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513  556 QELGRGQYGVVYLCDN--------WGGHFPCALKsvvppdEKHWNDLALEFHYMRSLpKHERLVdlhgSVIDyNYGGGSS 627
Cdd:PTZ00266   19 KKIGNGRFGEVFLVKHkrtqeffcWKAISYRGLK------EREKSQLVIEVNVMREL-KHKNIV----RYID-RFLNKAN 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513  628 VAVLLIME-----RLHRDLYTGLKAGLSLETR--LQIALDVVEGIRFLHS-------QGLVHRDIKLKNVLLDKQNR--- 690
Cdd:PTZ00266   87 QKLYILMEfcdagDLSRNIQKCYKMFGKIEEHaiVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTGIRhig 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513  691 --------------AKITDLGFCKPEAM--MSGSIVGTPIHMAPELF---TGKYDNSVDVYAFGILFWYICSGsiKLPea 751
Cdd:PTZ00266  167 kitaqannlngrpiAKIGDFGLSKNIGIesMAHSCVGTPYYWSPELLlheTKSYDDKSDMWALGCIIYELCSG--KTP-- 242
                         250       260
                  ....*....|....*....|....*
gi 564380513  752 FERCASKDHLWNNVRRGtrPErLPV 776
Cdd:PTZ00266  243 FHKANNFSQLISELKRG--PD-LPI 264
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
661-813 1.06e-08

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: 57.18  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-----PEAMMSGSIVGTPIH-MAPELFT-GKYDNSVDVYA 733
Cdd:cd05066  115 IASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRvleddPEAAYTTRGGKIPIRwTAPEAIAyRKFTSASDVWS 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 734 FGILFWYICSGSiklPEAFERCASKDHLwNNVRRGTR---PERLPVfdeECWQLMEACWDGDPSKRPLLG-IVqpilrSI 809
Cdd:cd05066  195 YGIVMWEVMSYG---ERPYWEMSNQDVI-KAIEEGYRlpaPMDCPA---ALHQLMLDCWQKDRNERPKFEqIV-----SI 262

                 ....
gi 564380513 810 MDRL 813
Cdd:cd05066  263 LDKL 266
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
558-744 1.14e-08

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: 57.14  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVvppDEKHWNDLALEFHYMRSLPkheRLVDLHGSVIDYNYgggssvaVLLIMErl 637
Cdd:cd13991   14 IGRGSFGEVHRMEDKQTGFQCAVKKV---RLEVFRAEELMACAGLTSP---RVVPLYGAVREGPW-------VNIFMD-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 638 hrdlytgLKAGLSL-----------ETR-LQIALDVVEGIRFLHSQGLVHRDIKLKNVLL-DKQNRAKITDLGFCK---- 700
Cdd:cd13991   79 -------LKEGGSLgqlikeqgclpEDRaLHYLGQALEGLEYLHSRKILHGDVKADNVLLsSDGSDAFLCDFGHAEcldp 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564380513 701 ----PEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSG 744
Cdd:cd13991  152 dglgKSLFTGDYIPGTETHMAPEVVLGKpCDAKVDVWSSCCMMLHMLNG 200
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
658-744 1.14e-08

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: 57.34  E-value: 1.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PEAMMSGSIVGTPIHMAPELFTG-KYDNSVDVYAF 734
Cdd:cd05630  108 AAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVhvPEGQTIKGRVGTVGYMAPEVVKNeRYTFSPDWWAL 187
                         90
                 ....*....|
gi 564380513 735 GILFWYICSG 744
Cdd:cd05630  188 GCLLYEMIAG 197
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
554-809 1.26e-08

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: 56.97  E-value: 1.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWG-----GHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDynygggsSV 628
Cdd:cd05093    9 LKRELGEGAFGKVFLAECYNlcpeqDKILVAVKTLKDASDNARKDFHREAELLTNL-QHEHIVKFYGVCVE-------GD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 AVLLIMERL-HRDLYTGLKAG---------------LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAK 692
Cdd:cd05093   81 PLIMVFEYMkHGDLNKFLRAHgpdavlmaegnrpaeLTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 693 ITDLGFCK----PEAMMSGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSGSiKLPeafERCASKDHLWNNVR 766
Cdd:cd05093  161 IGDFGMSRdvysTDYYRVGGHTMLPIRwMPPEsIMYRKFTTESDVWSLGVVLWEIFTYG-KQP---WYQLSNNEVIECIT 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 564380513 767 RGTRPERLPVFDEECWQLMEACWDGDPSKRPLLGIVQPILRSI 809
Cdd:cd05093  237 QGRVLQRPRTCPKEVYDLMLGCWQREPHMRLNIKEIHSLLQNL 279
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
630-744 1.28e-08

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: 57.29  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIME--RLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PEAMM 705
Cdd:cd05632   80 VLTIMNggDLKFHIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVkiPEGES 159
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564380513 706 SGSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSG 744
Cdd:cd05632  160 IRGRVGTVGYMAPEVLNNqRYTLSPDYWGLGCLIYEMIEG 199
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
553-736 1.36e-08

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: 57.04  E-value: 1.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSV-VPPDEKHwnDLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSvAVL 631
Cdd:cd06637    9 ELVELVGNGTYGQVYKGRHVKTGQLAAIKVMdVTGDEEE--EIKQEINMLKKYSHHRNIATYYGAFIKKNPPGMDD-QLW 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLH----RDLYTGLKAG-LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMS 706
Cdd:cd06637   86 LVMEFCGagsvTDLIKNTKGNtLKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTV 165
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564380513 707 G---SIVGTPIHMAPELFT------GKYDNSVDVYAFGI 736
Cdd:cd06637  166 GrrnTFIGTPYWMAPEVIAcdenpdATYDFKSDLWSLGI 204
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
558-738 1.37e-08

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: 57.54  E-value: 1.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLC-DNWGGHfPCALKSVVPPDEkhwnDLAL------EFHYMRSLpKHERLVDLH-----GSVIDYNyggg 625
Cdd:cd07834    8 IGSGAYGVVCSAyDKRTGR-KVAIKKISNVFD----DLIDakrilrEIKILRHL-KHENIIGLLdilrpPSPEEFN---- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 626 ssvAVLLIMERLHRDLYTGLKAGLSL-ETRLQ-IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FC 699
Cdd:cd07834   78 ---DVYIVTELMETDLHKVIKSPQPLtDDHIQyFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGlargVD 154
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564380513 700 KPEA--MMSGSIVgTPIHMAPELFTG--KYDNSVDVYAFGILF 738
Cdd:cd07834  155 PDEDkgFLTEYVV-TRWYRAPELLLSskKYTKAIDIWSVGCIF 196
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
555-797 1.41e-08

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 56.72  E-value: 1.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 555 GQELGRGQYGVVYL-----CDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYgggssva 629
Cdd:cd05037    4 HEHLGQGTFTNIYDgilreVGDGRVQEVEVLLKVLDSDHRDISESFFETASLMSQISHKHLVKLYGVCVADEN------- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 vLLIMERLHR---DLYTGL-KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNR------AKITDLGFc 699
Cdd:cd05037   77 -IMVQEYVRYgplDKYLRRmGNNVPLSWKLQVAKQLASALHYLEDKKLIHGNVRGRNILLAREGLdgyppfIKLSDPGV- 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 700 kPEAMMSGSIVGTPIH-MAPELFTG---KYDNSVDVYAFGILFWYICSGSiklPEAFERCASKDHLwnnvRRGTRPERLP 775
Cdd:cd05037  155 -PITVLSREERVDRIPwIAPECLRNlqaNLTIAADKWSFGTTLWEICSGG---EEPLSALSSQEKL----QFYEDQHQLP 226
                        250       260
                 ....*....|....*....|...
gi 564380513 776 VFD-EECWQLMEACWDGDPSKRP 797
Cdd:cd05037  227 APDcAELAELIMQCWTYEPTKRP 249
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
644-822 1.43e-08

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 56.66  E-value: 1.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 644 GLKAGLSlETRL-QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF---CKPEAMMSGSivGTPIHMAPE 719
Cdd:cd14052   98 GLLGRLD-EFRVwKILVELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFGMatvWPLIRGIERE--GDREYIAPE 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 720 -LFTGKYDNSVDVYAFGILFWYIcSGSIKLPEAFERcaskdhlWNNVRRG--TRPERLPVFDEECWQLMEACWDGDPSKR 796
Cdd:cd14052  175 iLSEHMYDKPADIFSLGLILLEA-AANVVLPDNGDA-------WQKLRSGdlSDAPRLSSTDLHSASSPSSNPPPDPPNM 246
                        170       180
                 ....*....|....*....|....*..
gi 564380513 797 PLLGivQPILRsIMDRLCKCDSE-RPS 822
Cdd:cd14052  247 PILS--GSLDR-VVRWMLSPEPDrRPT 270
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
554-751 1.49e-08

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: 56.65  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWGGHFPCALKSVvppDEKHWNDLALE--FHYMR--SLPKHERLVDLHgSVIDynygggSSVA 629
Cdd:cd14074    7 LEETLGRGHFAVVKLARHVFTGEKVAVKVI---DKTKLDDVSKAhlFQEVRcmKLVQHPNVVRLY-EVID------TQTK 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHR-DLY---TGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLL-DKQNRAKITDLGFC---KP 701
Cdd:cd14074   77 LYLILELGDGgDMYdyiMKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSnkfQP 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 564380513 702 EAMMSGSiVGTPIHMAPELFTG-KYDN-SVDVYAFGILFWYICSGSIKLPEA 751
Cdd:cd14074  157 GEKLETS-CGSLAYSAPEILLGdEYDApAVDIWSLGVILYMLVCGQPPFQEA 207
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
630-749 1.76e-08

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: 57.10  E-value: 1.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHRDLYTGLKAG--LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK------P 701
Cdd:cd07859   79 IYVVFELMESDLHQVIKANddLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARvafndtP 158
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564380513 702 EAMMSGSIVGTPIHMAPEL---FTGKYDNSVDVYAFGILFWYICSGSIKLP 749
Cdd:cd07859  159 TAIFWTDYVATRWYRAPELcgsFFSKYTPAIDIWSIGCIFAEVLTGKPLFP 209
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
630-809 1.92e-08

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: 56.54  E-value: 1.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIME--RLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK--PEAMM 705
Cdd:cd05631   78 VLTIMNggDLKFHIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVqiPEGET 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 706 SGSIVGTPIHMAPELFTG-KYDNSVDVYAFGILFWYICSGSIKLPEAFERcASKDHLWNNVRRGTRpERLPVFDEECWQL 784
Cdd:cd05631  158 VRGRVGTVGYMAPEVINNeKYTFSPDWWGLGCLIYEMIQGQSPFRKRKER-VKREEVDRRVKEDQE-EYSEKFSEDAKSI 235
                        170       180       190
                 ....*....|....*....|....*....|....
gi 564380513 785 MEACWDGDPSKRplLGIV---------QPILRSI 809
Cdd:cd05631  236 CRMLLTKNPKER--LGCRgngaagvkqHPIFKNI 267
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
556-744 1.99e-08

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 56.91  E-value: 1.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFP-CALKSVVPPD---EKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssvaVL 631
Cdd:PTZ00426  36 RTLGTGSFGRVILATYKNEDFPpVAIKRFEKSKiikQKQVDHVFSERKILNYI-NHPFCVNLYGSFKDESY-------LY 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIME-RLHRDLYTGLKAGLSLETRLQI--ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGS 708
Cdd:PTZ00426 108 LVLEfVIGGEFFTFLRRNKRFPNDVGCfyAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDTRTYT 187
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 564380513 709 IVGTPIHMAPE-LFTGKYDNSVDVYAFGILFWYICSG 744
Cdd:PTZ00426 188 LCGTPEYIAPEiLLNVGHGKAADWWTLGIFIYEILVG 224
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
660-811 2.08e-08

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


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 56.45  E-value: 2.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLV-HRDIKLKNVLLDKQNRAKITDLGFckpEAMMSGSIVGTPIH--------MAPELFTGKYDNSV- 729
Cdd:cd14042  111 DIVKGMHYLHDSEIKsHGNLKSSNCVVDSRFVLKITDFGL---HSFRSGQEPPDDSHayyakllwTAPELLRDPNPPPPg 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 730 ----DVYAFGILF---------WYICSGSIKLPEAFERCaskdhlwnnVRRGTRPERLPVFDEECW-----QLMEACWDG 791
Cdd:cd14042  188 tqkgDVYSFGIILqeiatrqgpFYEEGPDLSPKEIIKKK---------VRNGEKPPFRPSLDELECpdevlSLMQRCWAE 258
                        170       180
                 ....*....|....*....|
gi 564380513 792 DPSKRPLLGIVQPILRSIMD 811
Cdd:cd14042  259 DPEERPDFSTLRNKLKKLNK 278
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
551-742 2.16e-08

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: 56.18  E-value: 2.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDL-ALEFHYMRSLpKHERLVDLHGsviDYNygggSSVA 629
Cdd:cd14095    1 KYDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKCKGKEHMiENEVAILRRV-KHPNIVQLIE---EYD----TDTE 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHR-DLYTGLKAGLSLETRLQIAL--DVVEGIRFLHSQGLVHRDIKLKNVLL----DKQNRAKITDLGFCK-- 700
Cdd:cd14095   73 LYLVMELVKGgDLFDAITSSTKFTERDASRMvtDLAQALKYLHSLSIVHRDIKPENLLVveheDGSKSLKLADFGLATev 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 564380513 701 PEAMMsgSIVGTPIHMAPELF--TGkYDNSVDVYAFG-ILFWYIC 742
Cdd:cd14095  153 KEPLF--TVCGTPTYVAPEILaeTG-YGLKVDIWAAGvITYILLC 194
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
558-797 2.79e-08

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


Pssm-ID: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 55.87  E-value: 2.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPP-----DEKHwndlALEFHYMRS-LPKHERLVDLHGS-------VIDYNYGG 624
Cdd:cd14051    8 IGSGEFGSVYKCINRLDGCVYAIKKSKKPvagsvDEQN----ALNEVYAHAvLGKHPHVVRYYSAwaeddhmIIQNEYCN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 625 GSSvavllimerLHRDLYTGLKAGLSL-ETRL-QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC--- 699
Cdd:cd14051   84 GGS---------LADAISENEKAGERFsEAELkDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPVSSEEEEEdfe 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 700 ----KPEAMMSGSIVGTPIH----------------MAPELFTGKYDN--SVDVYAFGILFWYICSGSIkLPEAFERcas 757
Cdd:cd14051  155 geedNPESNEVTYKIGDLGHvtsisnpqveegdcrfLANEILQENYSHlpKADIFALALTVYEAAGGGP-LPKNGDE--- 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 564380513 758 kdhlWNNVRRGTRPeRLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd14051  231 ----WHEIRQGNLP-PLPQCSPEFNELLRSMIHPDPEKRP 265
PTKc_IGF-1R cd05062
Catalytic domain of the Protein Tyrosine Kinase, Insulin-like Growth Factor-1 Receptor; PTKs ...
631-805 2.88e-08

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


Pssm-ID: 133193 [Multi-domain]  Cd Length: 277  Bit Score: 55.81  E-value: 2.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLHR-DLYTGLK------------AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG 697
Cdd:cd05062   85 LVIMELMTRgDLKSYLRslrpemennpvqAPPSLKKMIQMAGEIADGMAYLNANKFVHRDLAARNCMVAEDFTVKIGDFG 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 698 FCK----PEAMMSGSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSgsikLPEAFERCASKDHLWNNVRRG--- 768
Cdd:cd05062  165 MTRdiyeTDYYRKGGKGLLPVRwMSPEsLKDGVFTTYSDVWSFGVVLWEIAT----LAEQPYQGMSNEQVLRFVMEGgll 240
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 564380513 769 TRPERLPvfdEECWQLMEACWDGDPSKRP-LLGIVQPI 805
Cdd:cd05062  241 DKPDNCP---DMLFELMRMCWQYNPKMRPsFLEIISSI 275
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
555-742 3.08e-08

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: 55.63  E-value: 3.08e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 555 GQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHW--NDLALEFHYMRSLpKHERLVDLHgSVIDynygggSSVAVLL 632
Cdd:cd14097    6 GRKLGQGSFGVVIEATHKETQTKWAIKKINREKAGSSavKLLEREVDILKHV-NHAHIIHLE-EVFE------TPKRMYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERLH----RDLYTGLKAGLSLETRlQIALDVVEGIRFLHSQGLVHRDIKLKNVLL--------DKQNrAKITDLGFC- 699
Cdd:cd14097   78 VMELCEdgelKELLLRKGFFSENETR-HIIQSLASAVAYLHKNDIVHRDLKLENILVkssiidnnDKLN-IKVTDFGLSv 155
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564380513 700 ----KPEAMMSGSiVGTPIHMAPELFTGK-YDNSVDVYAFG-ILFWYIC 742
Cdd:cd14097  156 qkygLGEDMLQET-CGTPIYMAPEVISAHgYSQQCDIWSIGvIMYMLLC 203
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
659-828 3.56e-08

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 56.80  E-value: 3.56e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 659 LDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP-EAMMSGSI----VGTPIHMAPELFTGK-YDNSVDVY 732
Cdd:PTZ00283 150 IQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMyAATVSDDVgrtfCGTPYYVAPEIWRRKpYSKKADMF 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 733 AFGILFWYIcsgsIKLPEAFERcASKDHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP--------------- 797
Cdd:PTZ00283 230 SLGVLLYEL----LTLKRPFDG-ENMEEVMHKTLAGRYDPLPPSISPEMQEIVTALLSSDPKRRPssskllnmpicklfi 304
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564380513 798 --LLGIVQP-----------ILRSIMD--RLCKCDSERPSRGLDDS 828
Cdd:PTZ00283 305 sgLLEIVQTqpgfsgplrdtISRQIQQtkQLLQVERRRIVRQMEES 350
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
553-745 3.86e-08

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: 55.41  E-value: 3.86e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLC--DNWGGHFpcALKSVVPPDEKHW------NDLALEFHYMRSLpKHERLVDLHgSVIDynygg 624
Cdd:cd14194    8 DTGEELGSGQFAVVKKCreKSTGLQY--AAKFIKKRRTKSSrrgvsrEDIEREVSILKEI-QHPNVITLH-EVYE----- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 625 gSSVAVLLIMERLHR-DLYTGL--KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN----RAKITDLG 697
Cdd:cd14194   79 -NKTDVILILELVAGgELFDFLaeKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNvpkpRIKIIDFG 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564380513 698 FCkpEAMMSG----SIVGTPIHMAPELFTgkYDN---SVDVYAFGILFWYICSGS 745
Cdd:cd14194  158 LA--HKIDFGnefkNIFGTPEFVAPEIVN--YEPlglEADMWSIGVITYILLSGA 208
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
653-796 4.11e-08

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: 55.49  E-value: 4.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 653 TRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAM------------------MSGSIVGTPI 714
Cdd:cd05609  102 ARMYFA-ETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLSKIGLMslttnlyeghiekdtrefLDKQVCGTPE 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 715 HMAPELFTGK-YDNSVDVYAFGILFWYICSGSIKL----PEA-FERCASKDHLWnnvrrgtrPERLPVFDEECWQLMEAC 788
Cdd:cd05609  181 YIAPEVILRQgYGKPVDWWAMGIILYEFLVGCVPFfgdtPEElFGQVISDEIEW--------PEGDDALPDDAQDLITRL 252

                 ....*...
gi 564380513 789 WDGDPSKR 796
Cdd:cd05609  253 LQQNPLER 260
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
657-797 4.35e-08

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


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 55.77  E-value: 4.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 657 IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpeAMMSGS---IVGT---PIH-MAPE-LFTGKYDNS 728
Cdd:cd05095  136 MAAQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKIADFGMSR--NLYSGDyyrIQGRavlPIRwMSWEsILLGKFTTA 213
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 564380513 729 VDVYAFGILFWYICSGSIKLPeaFERCASKDHLWNN---VRRGTRPERLP---VFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05095  214 SDVWAFGVTLWETLTFCREQP--YSQLSDEQVIENTgefFRDQGRQTYLPqpaLCPDSVYKLMLSCWRRDTKDRP 286
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
601-744 4.44e-08

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: 55.81  E-value: 4.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 601 MRSLPKHERLVDLHgsvidynYGGGSSVAVLLIMErLHRDLYTGLKA---------GLSLETRLQ--------------I 657
Cdd:cd14170   35 LQDCPKARREVELH-------WRASQCPHIVRIVD-VYENLYAGRKCllivmecldGGELFSRIQdrgdqaftereaseI 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLL-DKQNRA--KITDLGFCKpEAMMSGSIVG---TPIHMAPELF-TGKYDNSVD 730
Cdd:cd14170  107 MKSIGEAIQYLHSINIAHRDVKPENLLYtSKRPNAilKLTDFGFAK-ETTSHNSLTTpcyTPYYVAPEVLgPEKYDKSCD 185
                        170
                 ....*....|....
gi 564380513 731 VYAFGILFWYICSG 744
Cdd:cd14170  186 MWSLGVIMYILLCG 199
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
658-796 4.85e-08

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: 55.82  E-value: 4.85e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF-CKPEAMMSGSIVGTPIHMAPELFTG--KYDNSVDVYAF 734
Cdd:cd14223  109 AAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLaCDFSKKKPHASVGTHGYMAPEVLQKgvAYDSSADWFSL 188
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564380513 735 GILFWYICSGSiklpEAFERCASKDHLWNNVRRGTRPERLP-VFDEECWQLMEACWDGDPSKR 796
Cdd:cd14223  189 GCMLFKLLRGH----SPFRQHKTKDKHEIDRMTLTMAVELPdSFSPELRSLLEGLLQRDVNRR 247
STKc_TTBK cd14017
Catalytic domain of the Serine/Threonine protein kinase, Tau-Tubulin Kinase; STKs catalyze the ...
553-700 5.04e-08

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: 54.96  E-value: 5.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKsvVPPDEKHWNDLALEFHYMRSLPKHE---RLVDLhGSVIDYNYgggssva 629
Cdd:cd14017    3 KVVKKIGGGGFGEIYKVRDVVDGEEVAMK--VESKSQPKQVLKMEVAVLKKLQGKPhfcRLIGC-GRTERYNY------- 72
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380513 630 vlLIMERLHRDLYTGLKA----GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLL----DKQNRAKITDLGFCK 700
Cdd:cd14017   73 --IVMTLLGPNLAELRRSqprgKFSVSTTLRLGIQILKAIEDIHEVGFLHRDVKPSNFAIgrgpSDERTVYILDFGLAR 149
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
632-737 5.10e-08

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 56.44  E-value: 5.10e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLHRDLYTGLKAGLSLETRLQI---ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG-FCKPEAMMSG 707
Cdd:PHA03211 237 LVLPKYRSDLYTYLGARLRPLGLAQVtavARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFGaACFARGSWST 316
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564380513 708 ----SIVGTPIHMAPELFTGK-YDNSVDVYAFGIL 737
Cdd:PHA03211 317 pfhyGIAGTVDTNAPEVLAGDpYTPSVDIWSAGLV 351
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
558-796 5.12e-08

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: 55.46  E-value: 5.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVY---LCDNWGGHF-PCALKsVVPPDEKH-WNDlALEFHYMRSLpKHERLVDLHGSVIDynyGGGSSVAVLL 632
Cdd:cd14055    3 VGKGRFAEVWkakLKQNASGQYeTVAVK-IFPYEEYAsWKN-EKDIFTDASL-KHENILQFLTAEER---GVGLDRQYWL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IME-----RLHRDLYTGLkagLSLETRLQIALDVVEGIRFLHS----QGL-----VHRDIKLKNVLLDKQNRAKITDLGF 698
Cdd:cd14055   77 ITAyhengSLQDYLTRHI---LSWEDLCKMAGSLARGLAHLHSdrtpCGRpkipiAHRDLKSSNILVKNDGTCVLADFGL 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 699 C-------KPEAMMSGSIVGTPIHMAPELFTGKYD-------NSVDVYAFGILFWYICS--------GSIKLP---EAFE 753
Cdd:cd14055  154 AlrldpslSVDELANSGQVGTARYMAPEALESRVNledlesfKQIDVYSMALVLWEMASrceasgevKPYELPfgsKVRE 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 564380513 754 RcASKDHLWNNVRRG-TRPErLPvfdeECW---QLMEA-------CWDGDPSKR 796
Cdd:cd14055  234 R-PCVESMKDLVLRDrGRPE-IP----DSWlthQGMCVlcdtiteCWDHDPEAR 281
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
664-765 5.40e-08

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: 55.50  E-value: 5.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 664 GIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA---MMSGSIVgTPIHMAPELFTG-KYDNSVDVYAFGILFW 739
Cdd:cd07850  114 GIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGtsfMMTPYVV-TRYYRAPEVILGmGYKENVDIWSVGCIMG 192
                         90       100
                 ....*....|....*....|....*...
gi 564380513 740 YICSGSIKLPeafercaSKDHL--WNNV 765
Cdd:cd07850  193 EMIRGTVLFP-------GTDHIdqWNKI 213
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
660-744 5.44e-08

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: 56.17  E-value: 5.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMS-GSIVGTPIHMAPELFT-----GKYDNSVD 730
Cdd:cd05622  180 EVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmkmNKEGMVRcDTAVGTPDYISPEVLKsqggdGYYGRECD 259
                         90
                 ....*....|....
gi 564380513 731 VYAFGILFWYICSG 744
Cdd:cd05622  260 WWSVGVFLYEMLVG 273
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
558-744 7.19e-08

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: 54.58  E-value: 7.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGS---------VIDYNYGGGssv 628
Cdd:cd14192   12 LGGGRFGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKNEINIMNQL-NHVNLIQLYDAfesktnltlIMEYVDGGE--- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 avllIMERLHRDLYTGLKAGLSLETRlqialDVVEGIRFLHSQGLVHRDIKLKNVLLDKQ--NRAKITDLGFC---KPEA 703
Cdd:cd14192   88 ----LFDRITDESYQLTELDAILFTR-----QICEGVHYLHQHYILHLDLKPENILCVNStgNQIKIIDFGLArryKPRE 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564380513 704 MMSGSIvGTPIHMAPELFTGKYDN-SVDVYAFGILFWYICSG 744
Cdd:cd14192  159 KLKVNF-GTPEFLAPEVVNYDFVSfPTDMWSVGVITYMLLSG 199
PK_GC-C cd14044
Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain ...
649-809 7.44e-08

Pseudokinase domain of the membrane Guanylate Cyclase receptor, GC-C; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-C binds and is activated by the intestinal hormones, guanylin (GN) and uroguanylin (UGN), which are secreted after salty meals to inhibit sodium absorption and induce the secretion of chloride, bicarbonate, and water. GN and UGN are also present in the kidney, where they induce increased salt and water secretion. This prevents the development of hypernatremia and hypervolemia after ingestion of high amounts of salt. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-C subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270946 [Multi-domain]  Cd Length: 271  Bit Score: 54.51  E-value: 7.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 649 LSLETRLQIALDVVEGIRFLHSQGL-VHRDIKLKNVLLDKQNRAKITDLGfCKPEAMMSGSIVGTPIHMAPELFTGKYDn 727
Cdd:cd14044  106 MDWEFKISVMYDIAKGMSYLHSSKTeVHGRLKSTNCVVDSRMVVKITDFG-CNSILPPSKDLWTAPEHLRQAGTSQKGD- 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 728 svdVYAFGILFWYIcsgsIKLPEAFERCASKDHLWNNVR----RGTRPERLPVFDE-------ECWQLMEACWDGDPSKR 796
Cdd:cd14044  184 ---VYSYGIIAQEI----ILRKETFYTAACSDRKEKIYRvqnpKGMKPFRPDLNLEsagererEVYGLVKNCWEEDPEKR 256
                        170
                 ....*....|...
gi 564380513 797 PLLGIVQPILRSI 809
Cdd:cd14044  257 PDFKKIENTLAKI 269
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
655-806 7.87e-08

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK 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: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 54.42  E-value: 7.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 655 LQIALDVVEGIRFLHS-QGLVHR-DIKLKNVLLDKQNRAKI----TDLGFCKPEAMMSgsivgtPIHMAPELFTGKYDN- 727
Cdd:cd14057   97 VKFALDIARGMAFLHTlEPLIPRhHLNSKHVMIDEDMTARInmadVKFSFQEPGKMYN------PAWMAPEALQKKPEDi 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 728 ---SVDVYAFGILFWYICSGSIKLPE-AFERCASKDHLwnnvrRGTRPERLPVFDEECWQLMEACWDGDPSKRPLLGIVQ 803
Cdd:cd14057  171 nrrSADMWSFAILLWELVTREVPFADlSNMEIGMKIAL-----EGLRVTIPPGISPHMCKLMKICMNEDPGKRPKFDMIV 245

                 ...
gi 564380513 804 PIL 806
Cdd:cd14057  246 PIL 248
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
660-744 8.36e-08

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: 55.39  E-value: 8.36e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC----KPEAMMSGSIVGTPIHMAPELFT-----GKYDNSVD 730
Cdd:cd05621  159 EVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGTCmkmdETGMVHCDTAVGTPDYISPEVLKsqggdGYYGRECD 238
                         90
                 ....*....|....
gi 564380513 731 VYAFGILFWYICSG 744
Cdd:cd05621  239 WWSVGVFLFEMLVG 252
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
661-796 8.92e-08

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: 54.67  E-value: 8.92e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLL---DKQNRAKITDLGFCKPEA---MMSgSIVGTPIHMAPELFTGK-YDNSVDVYA 733
Cdd:cd14168  117 VLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKMEGkgdVMS-TACGTPGYVAPEVLAQKpYSKAVDCWS 195
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564380513 734 FGILFWYICSGsikLPEAFERCASKdhLWNNVRRGTRPERLPVFD---EECWQLMEACWDGDPSKR 796
Cdd:cd14168  196 IGVIAYILLCG---YPPFYDENDSK--LFEQILKADYEFDSPYWDdisDSAKDFIRNLMEKDPNKR 256
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
630-765 1.04e-07

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: 55.05  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA---MMS 706
Cdd:cd07875  104 VYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGtsfMMT 183
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380513 707 GSIVgTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGSIKLPeafercaSKDHL--WNNV 765
Cdd:cd07875  184 PYVV-TRYYRAPEVILGMgYKENVDIWSVGCIMGEMIKGGVLFP-------GTDHIdqWNKV 237
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
558-742 1.05e-07

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: 54.44  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYGGGSSVAVLLIMERL 637
Cdd:cd14036    8 IAEGGFAFVYEAQDVGTGKEYALKRLLSNEEEKNKAIIQEINFMKKLSGHPNIVQFCSAASIGKEESDQGQAEYLLLTEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 638 HR----DLYTGLKAG--LSLETRLQIALDVVEGIRFLHSQG--LVHRDIKLKNVLLDKQNRAKITDLGFCKPEA------ 703
Cdd:cd14036   88 CKgqlvDFVKKVEAPgpFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGSATTEAhypdys 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 564380513 704 -------MMSGSI--VGTPIHMAPELFTgKYDN-----SVDVYAFGILFWYIC 742
Cdd:cd14036  168 wsaqkrsLVEDEItrNTTPMYRTPEMID-LYSNypigeKQDIWALGCILYLLC 219
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
661-744 1.19e-07

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: 54.25  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVL-LDKQ---NRAKITDLGFCKPEAMMSGSIVgTPIH----MAPELFTGK-YDNSVDV 731
Cdd:cd14178  106 ITKTVEYLHSQGVVHRDLKPSNILyMDESgnpESIRICDFGFAKQLRAENGLLM-TPCYtanfVAPEVLKRQgYDAACDI 184
                         90
                 ....*....|...
gi 564380513 732 YAFGILFWYICSG 744
Cdd:cd14178  185 WSLGILLYTMLAG 197
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
617-736 1.25e-07

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: 54.28  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 617 VIDYnYGGGSSVAVLLIME-RLHRDLytglkaglsleTRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITD 695
Cdd:cd05597   79 VMDY-YCGGDLLTLLSKFEdRLPEEM-----------ARFYLA-EMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLAD 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564380513 696 LGFC----KPEAMMSGSIVGTPIHMAPELF------TGKYDNSVDVYAFGI 736
Cdd:cd05597  146 FGSClklrEDGTVQSSVAVGTPDYISPEILqamedgKGRYGPECDWWSLGV 196
STKc_VRK cd14015
Catalytic domain of the Serine/Threonine protein kinase, Vaccinia Related Kinase; STKs ...
550-698 1.30e-07

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


Pssm-ID: 270917 [Multi-domain]  Cd Length: 300  Bit Score: 54.21  E-value: 1.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 550 RKPKLGQELGRGQYGVVYL-CDNWGGHFPCALKSVVPPDEKHWNDLALEFH-YMRSLPKHE-------RLVDLHGsvIDY 620
Cdd:cd14015   10 RQWKLGKSIGQGGFGEIYLaSDDSTLSVGKDAKYVVKIEPHSNGPLFVEMNfYQRVAKPEMikkwmkaKKLKHLG--IPR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 621 NYGGGSSVAV-----LLIMERLHRDLYTGLKAG---LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDK---QN 689
Cdd:cd14015   88 YIGSGSHEYKgekyrFLVMPRFGRDLQKIFEKNgkrFPEKTVLQLALRILDVLEYIHENGYVHADIKASNLLLGFgknKD 167

                 ....*....
gi 564380513 690 RAKITDLGF 698
Cdd:cd14015  168 QVYLVDYGL 176
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
630-765 1.66e-07

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: 54.32  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA---MMS 706
Cdd:cd07874   97 VYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGtsfMMT 176
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380513 707 GSIVgTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGSIKLPeafercaSKDHL--WNNV 765
Cdd:cd07874  177 PYVV-TRYYRAPEVILGMgYKENVDIWSVGCIMGEMVRHKILFP-------GRDYIdqWNKV 230
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
661-745 1.72e-07

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: 53.39  E-value: 1.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPE-LFTGKYDNSVDVYAFGI 736
Cdd:cd14189  110 IISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAarlEPPEQRKKTICGTPNYLAPEvLLRQGHGPESDVWSLGC 189

                 ....*....
gi 564380513 737 LFWYICSGS 745
Cdd:cd14189  190 VMYTLLCGN 198
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
556-797 1.83e-07

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: 53.36  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKsVVPPDEKHWNDLALEFHYMRSLpKHERLVDLhgsvIDYNYGGGSSVAVLLIM- 634
Cdd:cd14107    8 EEIGRGTFGFVKRVTHKGNGECCAAK-FIPLRSSTRARAFQERDILARL-SHRRLTCL----LDQFETRKTLILILELCs 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 635 -ERLHRDLYtglKAGLSLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA--KITDLGFCK--PEAMMSGS 708
Cdd:cd14107   82 sEELLDRLF---LKGVVTEAEVKLYIqQVLEGIGYLHGMNILHLDIKPDNILMVSPTREdiKICDFGFAQeiTPSEHQFS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 709 IVGTPIHMAPELFTGK-YDNSVDVYAFGILFwYICSgSIKLPEAFErcaSKDHLWNNVRRGTRPERLPVF---DEECWQL 784
Cdd:cd14107  159 KYGSPEFVAPEIVHQEpVSAATDIWALGVIA-YLSL-TCHSPFAGE---NDRATLLNVAEGVVSWDTPEIthlSEDAKDF 233
                        250
                 ....*....|...
gi 564380513 785 MEACWDGDPSKRP 797
Cdd:cd14107  234 IKRVLQPDPEKRP 246
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
554-745 1.91e-07

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: 53.42  E-value: 1.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDnwgghfpcalksvvppDEKHWNDLALEFHYMRSLPKH---------ERLVD-----LHGSVID 619
Cdd:cd14196    9 IGEELGSGQFAIVKKCR----------------EKSTGLEYAAKFIKKRQSRASrrgvsreeiEREVSilrqvLHPNIIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 620 YNYGGGSSVAVLLIMERLHR-DLYTGL--KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN----RAK 692
Cdd:cd14196   73 LHDVYENRTDVVLILELVSGgELFDFLaqKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNipipHIK 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 564380513 693 ITDLGFCK--PEAMMSGSIVGTPIHMAPELFTgkYDN---SVDVYAFGILFWYICSGS 745
Cdd:cd14196  153 LIDFGLAHeiEDGVEFKNIFGTPEFVAPEIVN--YEPlglEADMWSIGVITYILLSGA 208
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
631-797 1.93e-07

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


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 53.42  E-value: 1.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLHRDlytglkaGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK----PEAMMS 706
Cdd:cd05111   95 LLDHVRQHRG-------SLGPQLLLNWCVQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADllypDDKKYF 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 707 GSIVGTPIH-MAPE-LFTGKYDNSVDVYAFGILFWYICSGSIKlPEAFERCASKDHLWNNVRRGTRPERLPVfdeECWQL 784
Cdd:cd05111  168 YSEAKTPIKwMALEsIHFGKYTHQSDVWSYGVTVWEMMTFGAE-PYAGMRLAEVPDLLEKGERLAQPQICTI---DVYMV 243
                        170
                 ....*....|...
gi 564380513 785 MEACWDGDPSKRP 797
Cdd:cd05111  244 MVKCWMIDENIRP 256
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
656-746 2.00e-07

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: 53.72  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALDVVEGIRFLHSQGLVHRDIKLKNVLL-DKQNRA--KITDLGFCKPEAMMSGSIvGTPI----HMAPELF-TGKYDN 727
Cdd:cd14180  105 QLMRSLVSAVSFMHEAGVVHRDLKPENILYaDESDGAvlKVIDFGFARLRPQGSRPL-QTPCftlqYAAPELFsNQGYDE 183
                         90
                 ....*....|....*....
gi 564380513 728 SVDVYAFGILFWYICSGSI 746
Cdd:cd14180  184 SCDLWSLGVILYTMLSGQV 202
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
556-738 2.01e-07

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: 53.59  E-value: 2.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSV-VPPDEKHWNDLAL-EFHYMRSLpKHERLVDLHGSVIdynygggSSVAVLLI 633
Cdd:cd07839    6 EKIGEGTYGTVFKAKNRETHEIVALKRVrLDDDDEGVPSSALrEICLLKEL-KHKNIVRLYDVLH-------SDKKLTLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERLHRDL---YTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK----PEAMMS 706
Cdd:cd07839   78 FEYCDQDLkkyFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARafgiPVRCYS 157
                        170       180       190
                 ....*....|....*....|....*....|....
gi 564380513 707 GSIVgTPIHMAPELFTGK--YDNSVDVYAFGILF 738
Cdd:cd07839  158 AEVV-TLWYRPPDVLFGAklYSTSIDMWSAGCIF 190
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
617-797 2.20e-07

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 54.25  E-value: 2.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 617 VIDYNYGGGSSVAvllIMERLHRDL-YTGLKAGLsLETRLQIALDVVegirflHSQGLVHRDIKLKNVLLDKQNRAKITD 695
Cdd:PTZ00267 143 IMEYGSGGDLNKQ---IKQRLKEHLpFQEYEVGL-LFYQIVLALDEV------HSRKMMHRDLKSANIFLMPTGIIKLGD 212
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 696 LGFCKPEA-----MMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYIcsgsIKLPEAFERCASKDHLWNNVRRGT 769
Cdd:PTZ00267 213 FGFSKQYSdsvslDVASSFCGTPYYLAPELWERKrYSKKADMWSLGVILYEL----LTLHRPFKGPSQREIMQQVLYGKY 288
                        170       180
                 ....*....|....*....|....*...
gi 564380513 770 RPERLPVFDeECWQLMEACWDGDPSKRP 797
Cdd:PTZ00267 289 DPFPCPVSS-GMKALLDPLLSKNPALRP 315
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
559-738 2.30e-07

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: 53.44  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 559 GRGQYGVVYLC--DNWGGHFPCALKSVVPpDEKHWNDLAL----EFHYMRSLpKHERLVDLHGSVIDYNYGggssvAVLL 632
Cdd:cd07842    9 GRGTYGRVYKAkrKNGKDGKEYAIKKFKG-DKEQYTGISQsacrEIALLREL-KHENVVSLVEVFLEHADK-----SVYL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 633 IMERLHRDLYTGLK-----AGLSLETRL--QIALDVVEGIRFLHSQGLVHRDIKLKNVLL----DKQNRAKITDLGFC-- 699
Cdd:cd07842   82 LFDYAEHDLWQIIKfhrqaKRVSIPPSMvkSLLWQILNGIHYLHSNWVLHRDLKPANILVmgegPERGVVKIGDLGLArl 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 564380513 700 -----KPEAMMSGSIVgTPIHMAPELFTGK--YDNSVDVYAFGILF 738
Cdd:cd07842  162 fnaplKPLADLDPVVV-TIWYRAPELLLGArhYTKAIDIWAIGCIF 206
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
558-749 2.36e-07

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: 53.51  E-value: 2.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEK--HWNDLALEFHYMRSLpKHERLVDL------HGSVIDYNygggssvA 629
Cdd:cd07877   25 VGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSiiHAKRTYRELRLLKHM-KHENVIGLldvftpARSLEEFN-------D 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHRDLYTGLKAGLSLETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGS 708
Cdd:cd07877   97 VYLVTHLMGADLNNIVKCQKLTDDHVQFLIyQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTG 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564380513 709 IVGTPIHMAPELFTG--KYDNSVDVYAFGILFWYICSGSIKLP 749
Cdd:cd07877  177 YVATRWYRAPEIMLNwmHYNQTVDIWSVGCIMAELLTGRTLFP 219
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
558-719 2.38e-07

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: 52.61  E-value: 2.38e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGS---------VIDYNYGGGssv 628
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKCRKAKDREDVRNEIEIMNQL-RHPRLLQLYDAfetpremvlVMEYVAGGE--- 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 avllIMERLHRDLYTGLKAGLSLETRlQIaldvVEGIRFLHSQGLVHRDIKLKNVLLDKQ--NRAKITDLGFC------K 700
Cdd:cd14103   77 ----LFERVVDDDFELTERDCILFMR-QI----CEGVQYMHKQGILHLDLKPENILCVSRtgNQIKIIDFGLArkydpdK 147
                        170
                 ....*....|....*....
gi 564380513 701 PEAMMsgsiVGTPIHMAPE 719
Cdd:cd14103  148 KLKVL----FGTPEFVAPE 162
STKc_CK1_gamma cd14126
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1 gamma; STKs catalyze ...
553-746 2.43e-07

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


Pssm-ID: 271028 [Multi-domain]  Cd Length: 288  Bit Score: 53.20  E-value: 2.43e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKsvVPPDEKHWNDLALEFHYMRSLPKHERLVDLH--GSVIDYNygggssvav 630
Cdd:cd14126    3 RVGKKIGCGNFGELRLGKNLYNNEHVAIK--LEPMKSRAPQLHLEYRFYKLLGQAEGLPQVYyfGPCGKYN--------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 631 LLIMERLH---RDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAK-----ITDLGFCK-- 700
Cdd:cd14126   72 AMVLELLGpslEDLFDLCDRTFSLKTVLMIAIQLISRIEYVHSKHLIYRDVKPENFLIGRQSTKKqhvihIIDFGLAKey 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564380513 701 --PEAMM------SGSIVGTPIHMAPELFTGKYDNSV-DVYAFGILFWYICSGSI 746
Cdd:cd14126  152 idPETNKhipyreHKSLTGTARYMSINTHLGKEQSRRdDLEALGHMFMYFLRGSL 206
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
656-758 2.46e-07

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: 53.19  E-value: 2.46e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNR---AKITDLGF---CK-----------PEAMmsgSIVGTPIHMAP 718
Cdd:cd14090  104 LVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspVKICDFDLgsgIKlsstsmtpvttPELL---TPVGSAEYMAP 180
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564380513 719 E---LFTG---KYDNSVDVYAFGILFWYICSGsikLPEAFERCASK 758
Cdd:cd14090  181 EvvdAFVGealSYDKRCDLWSLGVILYIMLCG---YPPFYGRCGED 223
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
551-744 2.62e-07

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: 52.73  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQELGRGQYGVVYLC--DNWGGHFpcALKSVVPPD---EKHWndLALEFHYMRSLpKHERLVDLHGSVidynyggG 625
Cdd:cd14184    2 KYKIGKVIGDGNFAVVKECveRSTGKEF--ALKIIDKAKccgKEHL--IENEVSILRRV-KHPNIIMLIEEM-------D 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 626 SSVAVLLIMERLHR-DLYTGLKAGLSLETRLQIAL--DVVEGIRFLHSQGLVHRDIKLKNVLL----DKQNRAKITDLGF 698
Cdd:cd14184   70 TPAELYLVMELVKGgDLFDAITSSTKYTERDASAMvyNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGL 149
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 564380513 699 CKPEAMMSGSIVGTPIHMAPELF--TGkYDNSVDVYAFGILFWYICSG 744
Cdd:cd14184  150 ATVVEGPLYTVCGTPTYVAPEIIaeTG-YGLKVDIWAAGVITYILLCG 196
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
556-738 2.66e-07

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: 53.19  E-value: 2.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSV-VPPDEKHWNDLAL-EFHYMRSLpKHERLVDLHGSVIDYNygggssvAVLLI 633
Cdd:cd07861    6 EKIGEGTYGVVYKGRNKKTGQIVAMKKIrLESEEEGVPSTAIrEISLLKEL-QHPNIVCLEDVLMQEN-------RLYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERLHRDL---YTGLKAGLSLETRL--QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKPEAM 704
Cdd:cd07861   78 FEFLSMDLkkyLDSLPKGKYMDAELvkSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGlaraFGIPVRV 157
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 564380513 705 MSGSIVgTPIHMAPELFTG--KYDNSVDVYAFGILF 738
Cdd:cd07861  158 YTHEVV-TLWYRAPEVLLGspRYSTPVDIWSIGTIF 192
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
553-744 2.91e-07

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: 53.49  E-value: 2.91e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSVvppdEKHWNDLALEFHYMRSLPKHERLVDLHGSvidynYGGGSSVAVL- 631
Cdd:cd14176   22 EVKEDIGVGSYSVCKRCIHKATNMEFAVKII----DKSKRDPTEEIEILLRYGQHPNIITLKDV-----YDDGKYVYVVt 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 -------LIMERLHRDLYTGLKAGLSLETrlqialdVVEGIRFLHSQGLVHRDIKLKNVL-LDKQNRA---KITDLGFCK 700
Cdd:cd14176   93 elmkggeLLDKILRQKFFSEREASAVLFT-------ITKTVEYLHAQGVVHRDLKPSNILyVDESGNPesiRICDFGFAK 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564380513 701 PEAMMSGSIVgTPIH----MAPELFTGK-YDNSVDVYAFGILFWYICSG 744
Cdd:cd14176  166 QLRAENGLLM-TPCYtanfVAPEVLERQgYDAACDIWSLGVLLYTMLTG 213
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
661-750 3.05e-07

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: 52.66  E-value: 3.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKpeAMMSGSIV----GTPIHMAPELFTGK-YDNS-VDVYAF 734
Cdd:cd14079  111 IISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSN--IMRDGEFLktscGSPNYAAPEVISGKlYAGPeVDVWSC 188
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564380513 735 GI-------------------LFWYICSGSIKLPE 750
Cdd:cd14079  189 GVilyallcgslpfddehipnLFKKIKSGIYTIPS 223
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
661-779 3.25e-07

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: 52.32  E-value: 3.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC---KPEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGI 736
Cdd:cd14188  110 IVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAarlEPLEHRRRTICGTPNYLSPEVLNKQgHGCESDIWALGC 189
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 564380513 737 LFWYICSG-----SIKLPEAFeRC-------------ASKDHLWNNVRRGTrPERLPVFDE 779
Cdd:cd14188  190 VMYTMLLGrppfeTTNLKETY-RCirearyslpssllAPAKHLIASMLSKN-PEDRPSLDE 248
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
661-744 3.26e-07

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: 52.71  E-value: 3.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVL-LDKQNRA---KITDLGFCKPEAMMSGSIVgTPIH----MAPE-LFTGKYDNSVDV 731
Cdd:cd14177  107 ITKTVDYLHCQGVVHRDLKPSNILyMDDSANAdsiRICDFGFAKQLRGENGLLL-TPCYtanfVAPEvLMRQGYDAACDI 185
                         90
                 ....*....|...
gi 564380513 732 YAFGILFWYICSG 744
Cdd:cd14177  186 WSLGVLLYTMLAG 198
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
655-797 3.36e-07

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 52.76  E-value: 3.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 655 LQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK----PEAMMSGSIVGTPIH-MAPE-LFTGKYDNS 728
Cdd:cd05110  112 LNWCVQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARllegDEKEYNADGGKMPIKwMALEcIHYRKFTHQ 191
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380513 729 VDVYAFGILFWYICSGSIKLPEAFERCASKDHLwnnvRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05110  192 SDVWSYGVTIWELMTFGGKPYDGIPTREIPDLL----EKGERLPQPPICTIDVYMVMVKCWMIDADSRP 256
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
597-746 3.55e-07

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: 52.88  E-value: 3.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 597 EFHYMRSLpKHERLVDLHGSVIDYNygggsSVAVLLIMERL-HRDLYTGLKA-----GLSLETRLQIALDVVEGIRFLHS 670
Cdd:cd13988   41 EFEVLKKL-NHKNIVKLFAIEEELT-----TRHKVLVMELCpCGSLYTVLEEpsnayGLPESEFLIVLRDVVAGMNHLRE 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 671 QGLVHRDIKLKNVLL----DKQNRAKITDLGFCKpEAMMSG---SIVGTPIHMAPELF--------TGK-YDNSVDVYAF 734
Cdd:cd13988  115 NGIVHRDIKPGNIMRvigeDGQSVYKLTDFGAAR-ELEDDEqfvSLYGTEEYLHPDMYeravlrkdHQKkYGATVDLWSI 193
                        170
                 ....*....|..
gi 564380513 735 GILFWYICSGSI 746
Cdd:cd13988  194 GVTFYHAATGSL 205
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
553-745 3.75e-07

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: 52.31  E-value: 3.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHFPCALKSV-----------VPPDEkhwndLALEFHYMRSLpKHERLVDLHgSVIDyn 621
Cdd:cd14195    8 EMGEELGSGQFAIVRKCREKGTGKEYAAKFIkkrrlsssrrgVSREE-----IEREVNILREI-QHPNIITLH-DIFE-- 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 622 ygggSSVAVLLIMERLHR-DLYTGL--KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN----RAKIT 694
Cdd:cd14195   79 ----NKTDVVLILELVSGgELFDFLaeKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNvpnpRIKLI 154
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 564380513 695 DLGFC-KPEAMMS-GSIVGTPIHMAPELFTgkYDN---SVDVYAFGILFWYICSGS 745
Cdd:cd14195  155 DFGIAhKIEAGNEfKNIFGTPEFVAPEIVN--YEPlglEADMWSIGVITYILLSGA 208
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
656-744 4.13e-07

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: 52.69  E-value: 4.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALDVVEGIRFLHSQGLVHRDIKLKNVLL---DKQNRAKITDLGFC--KPEAMMSGSIVGTPIHMAPELF-----TGKY 725
Cdd:cd14092  103 RIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFArlKPENQPLKTPCFTLPYAAPEVLkqalsTQGY 182
                         90
                 ....*....|....*....
gi 564380513 726 DNSVDVYAFGILFWYICSG 744
Cdd:cd14092  183 DESCDLWSLGVILYTMLSG 201
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
630-738 4.66e-07

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: 52.23  E-value: 4.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHRDLYTGL---KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FCKPE 702
Cdd:cd07843   81 IYMVMEYVEHDLKSLMetmKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGlareYGSPL 160
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 564380513 703 AMMSgSIVGTPIHMAPELFTG--KYDNSVDVYAFGILF 738
Cdd:cd07843  161 KPYT-QLVVTLWYRAPELLLGakEYSTAIDMWSVGCIF 197
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
661-738 4.67e-07

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: 52.53  E-value: 4.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQ-NRAKITDLG----FCKPEAMMSGSIVgTPIHMAPELFTG--KYDNSVDVYA 733
Cdd:cd07837  118 LCKGVAHCHSHGVMHRDLKPQNLLVDKQkGLLKIADLGlgraFTIPIKSYTHEIV-TLWYRAPEVLLGstHYSTPVDMWS 196

                 ....*
gi 564380513 734 FGILF 738
Cdd:cd07837  197 VGCIF 201
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
556-749 4.84e-07

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: 52.30  E-value: 4.84e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVY-----LCDNWgghfpCALKSVVPPDEKHWNDLAL-EFHYMRSLpKHERLVDLHGSVidynyggGSSVA 629
Cdd:cd07872   12 EKLGEGTYATVFkgrskLTENL-----VALKEIRLEHEEGAPCTAIrEVSLLKDL-KHANIVTLHDIV-------HTDKS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHRDLYTGLKAGLSLETRLQIAL---DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK----PE 702
Cdd:cd07872   79 LTLVFEYLDKDLKQYMDDCGNIMSMHNVKIflyQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARaksvPT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564380513 703 AMMSGSIVgTPIHMAPELFTG--KYDNSVDVYAFGILFWYICSGSIKLP 749
Cdd:cd07872  159 KTYSNEVV-TLWYRPPDVLLGssEYSTQIDMWGVGCIFFEMASGRPLFP 206
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
557-796 5.75e-07

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: 51.45  E-value: 5.75e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLCDnwgghfpcaLKSVVPPDEKHWNDLALEFHYMRSLPKH-----ERLVDLHGS--VIDYNYGGGSSVA 629
Cdd:cd14019    8 KIGEGTFSSVYKAE---------DKLHDLYDRNKGRLVALKHIYPTSSPSRilnelECLERLGGSnnVSGLITAFRNEDQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERL-HRDLYTGLKAGLSLETR-----LQIALdvvegiRFLHSQGLVHRDIKLKNVLLDKQNR-AKITDLGFCKPE 702
Cdd:cd14019   79 VVAVLPYIeHDDFRDFYRKMSLTDIRiylrnLFKAL------KHVHSFGIIHRDVKPGNFLYNRETGkGVLVDFGLAQRE 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 703 AM---MSGSIVGTPIHMAPE-LFtgKYDN---SVDVYAFGILFWYICSGsiKLPeAFERCASKDHLwnnvrrgtrPERLP 775
Cdd:cd14019  153 EDrpeQRAPRAGTRGFRAPEvLF--KCPHqttAIDIWSAGVILLSILSG--RFP-FFFSSDDIDAL---------AEIAT 218
                        250       260
                 ....*....|....*....|..
gi 564380513 776 VF-DEECWQLMEACWDGDPSKR 796
Cdd:cd14019  219 IFgSDEAYDLLDKLLELDPSKR 240
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
558-749 5.87e-07

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDKL5 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 51.92  E-value: 5.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDE-KHWNDLAL-EFHYMRSLpKHERLVDLHGSVIDYnyggGSSVAVLLIME 635
Cdd:cd07848    9 VGEGAYGVVLKCRHKETKEIVAIKKFKDSEEnEEVKETTLrELKMLRTL-KQENIVELKEAFRRR----GKLYLVFEYVE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGS----IVG 711
Cdd:cd07848   84 KNMLELLEEMPNGVPPEKVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNAnyteYVA 163
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564380513 712 TPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGSIKLP 749
Cdd:cd07848  164 TRWYRSPELLLGApYGKAVDMWSVGCILGELSDGQPLFP 202
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
661-749 5.89e-07

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: 52.36  E-value: 5.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK-PEAMMSGsIVGTPIHMAPELFTG--KYDNSVDVYAFGIL 737
Cdd:cd07878  127 LLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARqADDEMTG-YVATRWYRAPEIMLNwmHYNQTVDIWSVGCI 205
                         90
                 ....*....|..
gi 564380513 738 FWYICSGSIKLP 749
Cdd:cd07878  206 MAELLKGKALFP 217
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
654-809 5.97e-07

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


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 51.78  E-value: 5.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 654 RLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGT------PIHMAPELFTGKY-- 725
Cdd:cd14045  105 RFSFATDIARGMAYLHQHKIYHGRLKSSNCVIDDRWVCKIADYGLTTYRKEDGSENASGyqqrlmQVYLPPENHSNTDte 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 726 -DNSVDVYAFGILFWYICSGSIKLPeafERCASKDHLW----NNVRRGTRPERLPVfDEECWQLMEACWDGDPSKRPLLG 800
Cdd:cd14045  185 pTQATDVYSYAIILLEIATRNDPVP---EDDYSLDEAWcpplPELISGKTENSCPC-PADYVELIRRCRKNNPAQRPTFE 260

                 ....*....
gi 564380513 801 IVQPILRSI 809
Cdd:cd14045  261 QIKKTLHKI 269
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
556-744 6.27e-07

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: 51.82  E-value: 6.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVIDYNygggssvAVLLIME 635
Cdd:cd14114    8 EELGTGAFGVVHRCTERATGNNFAAKFIMTPHESDKETVRKEIQIMNQL-HHPKLINLHDAFEDDN-------EMVLILE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RLHR-DLYTGLKA---GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLD--KQNRAKITDLGFC---KPEAMMS 706
Cdd:cd14114   80 FLSGgELFERIAAehyKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLAthlDPKESVK 159
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564380513 707 GSiVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSG 744
Cdd:cd14114  160 VT-TGTAEFAAPEIVEREpVGFYTDMWAVGVLSYVLLSG 197
PHA02988 PHA02988
hypothetical protein; Provisional
649-797 7.52e-07

hypothetical protein; Provisional


Pssm-ID: 165291 [Multi-domain]  Cd Length: 283  Bit Score: 51.67  E-value: 7.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 649 LSLETRLQIALDVVEGIRFLH-SQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSIVGTPIHMAPELFT---GK 724
Cdd:PHA02988 119 LSFKTKLDMAIDCCKGLYNLYkYTNKPYKNLTSVSFLVTENYKLKIICHGLEKILSSPPFKNVNFMVYFSYKMLNdifSE 198
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564380513 725 YDNSVDVYAFGILFWYICSGSIklpeAFERCASKDhLWNNVRRGTRPERLPVfdeECWQLM----EACWDGDPSKRP 797
Cdd:PHA02988 199 YTIKDDIYSLGVVLWEIFTGKI----PFENLTTKE-IYDLIINKNNSLKLPL---DCPLEIkcivEACTSHDSIKRP 267
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
660-763 9.48e-07

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: 51.57  E-value: 9.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNR---AKITDL---------GFCKPeamMSGSIVGTPI----HMAPELF-- 721
Cdd:cd14173  108 DIASALDFLHNKGIAHRDLKPENILCEHPNQvspVKICDFdlgsgiklnSDCSP---ISTPELLTPCgsaeYMAPEVVea 184
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 564380513 722 ----TGKYDNSVDVYAFGILFWYICSGsikLPEAFERCASkDHLWN 763
Cdd:cd14173  185 fneeASIYDKRCDLWSLGVILYIMLSG---YPPFVGRCGS-DCGWD 226
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
554-744 1.13e-06

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: 50.95  E-value: 1.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 554 LGQELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEK------HWNDLALEFHYMRSLpKHERLVDLHgSVIDynygggSS 627
Cdd:cd14105    9 IGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKasrrgvSREDIEREVSILRQV-LHPNIITLH-DVFE------NK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 628 VAVLLIMERLHR-DLYTGL--KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN----RAKITDLGFCK 700
Cdd:cd14105   81 TDVVLILELVAGgELFDFLaeKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENIMLLDKNvpipRIKLIDFGLAH 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564380513 701 --PEAMMSGSIVGTPIHMAPELFTgkYDN---SVDVYAFGILFWYICSG 744
Cdd:cd14105  161 kiEDGNEFKNIFGTPEFVAPEIVN--YEPlglEADMWSIGVITYILLSG 207
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
656-745 1.15e-06

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: 51.18  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALDVVEGIRFLHSQGLVHRDIKLKNVLL---DKQNRAKITDLGF---------CKPeamMSGSIVGTPI----HMAP- 718
Cdd:cd14174  104 RVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDLgsgvklnsaCTP---ITTPELTTPCgsaeYMAPe 180
                         90       100       110
                 ....*....|....*....|....*....|..
gi 564380513 719 --ELFTGK---YDNSVDVYAFGILFWYICSGS 745
Cdd:cd14174  181 vvEVFTDEatfYDKRCDLWSLGVILYIMLSGY 212
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
610-738 1.36e-06

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: 51.39  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 610 LVDLHGSVIDYNYgggssvaVLLIMERL-HRDLYTGL-KAGLSLE--TRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLL 685
Cdd:cd05629   63 VVSLYYSFQDAQY-------LYLIMEFLpGGDLMTMLiKYDTFSEdvTRFYMA-ECVLAIEAVHKLGFIHRDIKPDNILI 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 686 DKQNRAKITDLGFC--------------------------------------------------KPEAMMSGSIVGTPIH 715
Cdd:cd05629  135 DRGGHIKLSDFGLStgfhkqhdsayyqkllqgksnknridnrnsvavdsinltmsskdqiatwkKNRRLMAYSTVGTPDY 214
                        170       180
                 ....*....|....*....|....*
gi 564380513 716 MAPELFTGK-YDNSVDVYAFG-ILF 738
Cdd:cd05629  215 IAPEIFLQQgYGQECDWWSLGaIMF 239
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
625-761 1.48e-06

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: 50.51  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 625 GSSVAVLLimerlhrDLYTGLKAGLSLETRLQIALdvveGIRFLHSQGLVHRDIKLKNVLLDKQ-NRAKITDLGFCKPEA 703
Cdd:cd06630   87 GGSVASLL-------SKYGAFSENVIINYTLQILR----GLAYLHDNQIIHRDLKGANLLVDSTgQRLRIADFGAAARLA 155
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 564380513 704 -------MMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGsiKLPeaFERCASKDHL 761
Cdd:cd06630  156 skgtgagEFQGQLLGTIAFMAPEVLRGEqYGRSCDVWSVGCVIIEMATA--KPP--WNAEKISNHL 217
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
660-744 1.69e-06

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: 50.38  E-value: 1.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 660 DVVEGIRFLHSQGLVHRDIKLKNVLL-DKQNRAKITDLGFCKPEAMMSG---SIVGTPIHMAPELF--TGkYDNSVDVYA 733
Cdd:cd14183  112 NLASAIKYLHSLNIVHRDIKPENLLVyEHQDGSKSLKLGDFGLATVVDGplyTVCGTPTYVAPEIIaeTG-YGLKVDIWA 190
                         90
                 ....*....|.
gi 564380513 734 FGILFWYICSG 744
Cdd:cd14183  191 AGVITYILLCG 201
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
617-744 1.84e-06

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: 51.17  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 617 VIDYnYGGGSSVAVLLIME-RLHRDLytglkaglsleTRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITD 695
Cdd:cd05623  150 VMDY-YVGGDLLTLLSKFEdRLPEDM-----------ARFYLA-EMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLAD 216
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 696 LGFCKpEAMMSGSI-----VGTPIHMAPELF------TGKYDNSVDVYAFGILFWYICSG 744
Cdd:cd05623  217 FGSCL-KLMEDGTVqssvaVGTPDYISPEILqamedgKGKYGPECDWWSLGVCMYEMLYG 275
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
661-744 1.85e-06

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: 50.32  E-value: 1.85e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQN---RAKITDLGFCKpeaMMSGS-----IVGTPIHMAPELFTgkYD---NSV 729
Cdd:cd14197  120 ILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKIVDFGLSR---ILKNSeelreIMGTPEYVAPEILS--YEpisTAT 194
                         90
                 ....*....|....*
gi 564380513 730 DVYAFGILFWYICSG 744
Cdd:cd14197  195 DMWSIGVLAYVMLTG 209
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
654-744 2.07e-06

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: 50.65  E-value: 2.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 654 RLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP---EAMMSGSIVGTPIHMAPELFTGK--YDNS 728
Cdd:cd05586   99 KFYIA-ELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKAdltDNKTTNTFCGTTEYLAPEVLLDEkgYTKM 177
                         90
                 ....*....|....*.
gi 564380513 729 VDVYAFGILFWYICSG 744
Cdd:cd05586  178 VDFWSLGVLVFEMCCG 193
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
658-746 2.25e-06

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: 50.14  E-value: 2.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 658 ALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG---FCKPEAMMSgSIVGTPIHMAPELFTGK-YDN-SVDVY 732
Cdd:cd14077  119 ARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGlsnLYDPRRLLR-TFCGSLYFAAPELLQAQpYTGpEVDVW 197
                         90
                 ....*....|....
gi 564380513 733 AFGILFWYICSGSI 746
Cdd:cd14077  198 SFGVVLYVLVCGKV 211
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
553-750 2.62e-06

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: 49.93  E-value: 2.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVvyLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRS----LPKHERLVDLHGSVIDYNYGGGSSV 628
Cdd:cd14020    7 RLGQGSSASVYRV--SSGRGADQPTSALKEFQLDHQGSQESGDYGFAKERAaleqLQGHRNIVTLYGVFTNHYSANVPSR 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 AVLLIM--ERLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA-KITDLGFCKPEAMM 705
Cdd:cd14020   85 CLLLELldVSVSELLLRSSNQGCSMWMIQHCARDVLEALAFLHHEGYVHADLKPRNILWSAEDECfKLIDFGLSFKEGNQ 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 564380513 706 SGSIVGTPIHMAPEL------------FTGKYDNSVDVYAFGILFWYICSGsIKLPE 750
Cdd:cd14020  165 DVKYIQTDGYRAPEAelqnclaqaglqSETECTSAVDLWSLGIVLLEMFSG-MKLKH 220
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
558-796 3.03e-06

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: 49.93  E-value: 3.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVvppdEKhwNDLALEFHYMR--------SLPKHERLVDLHGS---------VIDY 620
Cdd:cd05574    9 LGKGDVGRVYLVRLKGTGKLFAMKVL----DK--EEMIKRNKVKRvltereilATLDHPFLPTLYASfqtsthlcfVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 621 NYGGgssvavllimeRLHRDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLL--------------- 685
Cdd:cd05574   83 CPGG-----------ELFRLLQKQPGKRLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLhesghimltdfdlsk 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 686 -----------------DKQNRAKITDLGFCKPEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSGSIk 747
Cdd:cd05574  152 qssvtpppvrkslrkgsRRSSVKSIEKETFVAEPSARSNSFVGTEEYIAPEVIKGDgHGSAVDWWTLGILLYEMLYGTT- 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564380513 748 lPeaFeRCASKDHLWNNV--RRGTRPERLPVfDEECWQLMEACWDGDPSKR 796
Cdd:cd05574  231 -P--F-KGSNRDETFSNIlkKELTFPESPPV-SSEAKDLIRKLLVKDPSKR 276
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
632-797 3.11e-06

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: 49.71  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLHRDLYTGLKAGLSLETR-------LQIALDVVEGIRFLHSQG-LVHRDIKLKNVLLDKQNRA-KITDLGFCKP- 701
Cdd:cd14001   83 LAMEYGGKSLNDLIEERYEAGLGpfpaatiLKVALSIARALEYLHNEKkILHGDIKSGNVLIKGDFESvKLCDFGVSLPl 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 -EAMMSGS-----IVGTPIHMAPELFTGKYD--NSVDVYAFGILFWYICSGSI-----------KLPEAFERCASKDHLW 762
Cdd:cd14001  163 tENLEVDSdpkaqYVGTEPWKAKEALEEGGVitDKADIFAYGLVLWEMMTLSVphlnlldieddDEDESFDEDEEDEEAY 242
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 564380513 763 NNvRRGTRP-ERLPVFDEECWQLME---ACWDGDPSKRP 797
Cdd:cd14001  243 YG-TLGTRPaLNLGELDDSYQKVIElfyACTQEDPKDRP 280
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
661-738 3.14e-06

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: 50.07  E-value: 3.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLL----DKQNRAKITDLGFC-------KPEAMMSGSIVgTPIHMAPELFTG--KYDN 727
Cdd:cd07867  118 ILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFArlfnsplKPLADLDPVVV-TFWYRAPELLLGarHYTK 196
                         90
                 ....*....|.
gi 564380513 728 SVDVYAFGILF 738
Cdd:cd07867  197 AIDIWAIGCIF 207
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
551-797 3.62e-06

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: 49.45  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQELGRGQYGVVY--LCDNWGGHFPCALKSVVPPDEKhwNDLALEFHYMRSLpKHERLVDLHGSVIDYNYgggssv 628
Cdd:cd14112    4 RFSFGSEIFRGRFSVIVkaVDSTTETDAHCAVKIFEVSDEA--SEAVREFESLRTL-QHENVQRLIAAFKPSNF------ 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 aVLLIMERLHRDLYTGLKAGlSLETRLQIAL---DVVEGIRFLHSQGLVHRDIKLKNVLLD--KQNRAKITDLGFCKPEA 703
Cdd:cd14112   75 -AYLVMEKLQEDVFTRFSSN-DYYSEEQVATtvrQILDALHYLHFKGIAHLDVQPDNIMFQsvRSWQVKLVDFGRAQKVS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 704 MMSGSIVGTPIHMA-PELFTGKYDNSV--DVYAFGILFWYICSGSIKLPEAFERCASKDHLWNNVRrgTRPERLPV-FDE 779
Cdd:cd14112  153 KLGKVPVDGDTDWAsPEFHNPETPITVqsDIWGLGVLTFCLLSGFHPFTSEYDDEEETKENVIFVK--CRPNLIFVeATQ 230
                        250
                 ....*....|....*...
gi 564380513 780 ECWQLMEACWDGDPSKRP 797
Cdd:cd14112  231 EALRFATWALKKSPTRRM 248
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
556-749 4.07e-06

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: 49.69  E-value: 4.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGSVidynyggGSSVAVLLIME 635
Cdd:cd07869   11 EKLGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAIREASLLKGLKHANIVLLHDII-------HTKETLTLVFE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RLHRDLYTGLK---AGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMSGSI--- 709
Cdd:cd07869   84 YVHTDLCQYMDkhpGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLARAKSVPSHTYsne 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564380513 710 VGTPIHMAPELFTG--KYDNSVDVYAFGILFWYICSGSIKLP 749
Cdd:cd07869  164 VVTLWYRPPDVLLGstEYSTCLDMWGVGCIFVEMIQGVAAFP 205
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
656-736 4.41e-06

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 49.29  E-value: 4.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALDVVEGIRFL-HSQGLVHRDIKLKNVLLDKQNRAKITDLGfckpeamMSGSIV---------GTPIHMAPELFT--- 722
Cdd:cd06618  118 KMTVSIVKALHYLkEKHGVIHRDVKPSNILLDESGNVKLCDFG-------ISGRLVdskaktrsaGCAAYMAPERIDppd 190
                         90
                 ....*....|....*
gi 564380513 723 -GKYDNSVDVYAFGI 736
Cdd:cd06618  191 nPKYDIRADVWSLGI 205
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
558-744 4.59e-06

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: 49.67  E-value: 4.59e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLAlefhYMRSlpKHERLVDLHGS-VIDYNYGGGSSVAVLLIMER 636
Cdd:cd05627   10 IGRGAFGEVRLVQKKDTGHIYAMKILRKADMLEKEQVA----HIRA--ERDILVEADGAwVVKMFYSFQDKRNLYLIMEF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 637 L-HRDLYTGLKAGLSL---ETRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFC------------- 699
Cdd:cd05627   84 LpGGDMMTLLMKKDTLseeATQFYIA-ETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCtglkkahrtefyr 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380513 700 -------------------------KPEAMMSGSIVGTPIHMAPELF--TGkYDNSVDVYAFGILFWYICSG 744
Cdd:cd05627  163 nlthnppsdfsfqnmnskrkaetwkKNRRQLAYSTVGTPDYIAPEVFmqTG-YNKLCDWWSLGVIMYEMLIG 233
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
661-738 4.64e-06

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: 49.67  E-value: 4.64e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLL----DKQNRAKITDLGFC-------KPEAMMSGSIVgTPIHMAPELFTG--KYDN 727
Cdd:cd07868  133 ILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIADMGFArlfnsplKPLADLDPVVV-TFWYRAPELLLGarHYTK 211
                         90
                 ....*....|.
gi 564380513 728 SVDVYAFGILF 738
Cdd:cd07868  212 AIDIWAIGCIF 222
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
659-797 5.22e-06

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


Pssm-ID: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 48.87  E-value: 5.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 659 LDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA-------------------KITDLGFCkpeAMMSGSIV--GTPIHMA 717
Cdd:cd14138  116 LQVARGLKYIHSMSLVHMDIKPSNIFISRTSIPnaaseegdedewasnkvifKIGDLGHV---TRVSSPQVeeGDSRFLA 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 718 PELFTGKYDN--SVDVYAFGILFWyICSGSIKLPEAFERcaskdhlWNNVRRGTRPeRLP-VFDEECWQLMEACWDGDPS 794
Cdd:cd14138  193 NEVLQENYTHlpKADIFALALTVV-CAAGAEPLPTNGDQ-------WHEIRQGKLP-RIPqVLSQEFLDLLKVMIHPDPE 263

                 ...
gi 564380513 795 KRP 797
Cdd:cd14138  264 RRP 266
STKc_CK1_delta_epsilon cd14125
Catalytic domain of the Serine/Threonine protein kinases, Casein Kinase 1 delta and epsilon; ...
551-700 5.61e-06

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


Pssm-ID: 271027 [Multi-domain]  Cd Length: 275  Bit Score: 48.90  E-value: 5.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 551 KPKLGQELGRGQYGVVYLCDNW--GGHFPCALKSVvppDEKHwNDLALEFHYMRSL------PKherlVDLHGSVIDYNy 622
Cdd:cd14125    1 KYRLGRKIGSGSFGDIYLGTNIqtGEEVAIKLESV---KTKH-PQLLYESKLYKILqggvgiPN----VRWYGVEGDYN- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 623 gggssvavLLIMERLH---RDLYTGLKAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLL---DKQNRAKITDL 696
Cdd:cd14125   72 --------VMVMDLLGpslEDLFNFCSRKFSLKTVLMLADQMISRIEYVHSKNFIHRDIKPDNFLMglgKKGNLVYIIDF 143

                 ....
gi 564380513 697 GFCK 700
Cdd:cd14125  144 GLAK 147
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
556-744 7.90e-06

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: 48.40  E-value: 7.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVvppdEKHWNDLALEFHYMRSLPKHERLVDLHGSVIDYNYgggssvaVLLIME 635
Cdd:cd14091    6 EEIGKGSYSVCKRCIHKATGKEYAVKII----DKSKRDPSEEIEILLRYGQHPNIITLRDVYDDGNS-------VYLVTE 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 636 RLhrdlytglKAGLSLETRLQ-----------IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA----KITDLGFCK 700
Cdd:cd14091   75 LL--------RGGELLDRILRqkffsereasaVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDpeslRICDFGFAK 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 564380513 701 PEAMMSGSIVgTPIH----MAPE-LFTGKYDNSVDVYAFGILFWYICSG 744
Cdd:cd14091  147 QLRAENGLLM-TPCYtanfVAPEvLKKQGYDAACDIWSLGVLLYTMLAG 194
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
558-744 7.96e-06

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: 48.37  E-value: 7.96e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGS---------VIDYNYGGGssv 628
Cdd:cd14193   12 LGGGRFGQVHKCEEKSSGLKLAAKIIKARSQKEKEEVKNEIEVMNQL-NHANLIQLYDAfesrndivlVMEYVDGGE--- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 avllIMERLHRDLYTglkagLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLL--DKQNRAKITDLGFC---KPEA 703
Cdd:cd14193   88 ----LFDRIIDENYN-----LTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCvsREANQVKIIDFGLArryKPRE 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 564380513 704 MMSGSIvGTPIHMAPELFTGKYDN-SVDVYAFGILFWYICSG 744
Cdd:cd14193  159 KLRVNF-GTPEFLAPEVVNYEFVSfPTDMWSLGVIAYMLLSG 199
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
556-815 8.00e-06

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: 48.42  E-value: 8.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYL-CDNWGGHFpCALKSVVPPDEKHWNDLAL-EFHYMRSLpKHERLVDLHGSVidynyggGSSVAVLLI 633
Cdd:cd07870    6 EKLGEGSYATVYKgISRINGQL-VALKVISMKTEEGVPFTAIrEASLLKGL-KHANIVLLHDII-------HTKETLTFV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERLHRDLYTGL---KAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEAMMS---G 707
Cdd:cd07870   77 FEYMHTDLAQYMiqhPGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSIPSqtyS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 708 SIVGTPIHMAPELFTG--KYDNSVDVYAFGILFWYICSGSIKLPEAFERCASKDHLWNNVRRGTRP-----ERLPVFDEE 780
Cdd:cd07870  157 SEVVTLWYRPPDVLLGatDYSSALDIWGAGCIFIEMLQGQPAFPGVSDVFEQLEKIWTVLGVPTEDtwpgvSKLPNYKPE 236
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 564380513 781 cWQLMEACwdgdpskrpllgivqPILRSIMDRLCK 815
Cdd:cd07870  237 -WFLPCKP---------------QQLRVVWKRLSR 255
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
556-685 8.99e-06

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: 48.86  E-value: 8.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVvpPDEKHWNDLAL-EFHYMR-------SLPKHERLVDLhgsVIDYNYGGGSS 627
Cdd:cd14218   16 RKLGWGHFSTVWLCWDIQRKRFVALKVV--KSAVHYTETAVdEIKLLKcvrdsdpSDPKRETIVQL---IDDFKISGVNG 90
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 564380513 628 VAVLLIMERL-HRDLYTGLKA---GLSLETRLQIALDVVEGIRFLHSQ-GLVHRDIKLKNVLL 685
Cdd:cd14218   91 VHVCMVLEVLgHQLLKWIIKSnyqGLPLPCVKSILRQVLQGLDYLHTKcKIIHTDIKPENILM 153
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
646-749 9.07e-06

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: 48.51  E-value: 9.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 646 KAGLSLETRL-QIALDVVEGIRFLHSQ-GLVHRDIKLKNVLLDKQNRAKITDLGFC-KPEAMMSGSIVGTPIHMAPELFT 722
Cdd:cd06650   96 KAGRIPEQILgKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSgQLIDSMANSFVGTRSYMSPERLQ 175
                         90       100
                 ....*....|....*....|....*...
gi 564380513 723 GK-YDNSVDVYAFGILFWYICSGSIKLP 749
Cdd:cd06650  176 GThYSVQSDIWSMGLSLVEMAVGRYPIP 203
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
657-697 1.10e-05

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


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 45.90  E-value: 1.10e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 564380513 657 IALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG 697
Cdd:cd13968   96 IMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
630-735 1.10e-05

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: 48.44  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHRDLYTGLKAG-LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP-EAMMSG 707
Cdd:cd07851   95 VYLVTHLMGADLNNIVKCQkLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHtDDEMTG 174
                         90       100       110
                 ....*....|....*....|....*....|
gi 564380513 708 sIVGTPIHMAPE--LFTGKYDNSVDVYAFG 735
Cdd:cd07851  175 -YVATRWYRAPEimLNWMHYNQTVDIWSVG 203
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
556-797 1.12e-05

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: 48.13  E-value: 1.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKH-WNDLAL-EFHYMRSLpKHERLVDL----HGSVIDYNYGGGSsva 629
Cdd:cd07865   18 AKIGQGTFGEVFKARHRKTGQIVALKKVLMENEKEgFPITALrEIKILQLL-KHENVVNLieicRTKATPYNRYKGS--- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 630 VLLIMERLHRDLytglkAGLSLETRLQIALDVV--------EGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKP 701
Cdd:cd07865   94 IYLVFEFCEHDL-----AGLLSNKNVKFTLSEIkkvmkmllNGLYYIHRNKILHRDMKAANILITKDGVLKLADFGLARA 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 702 EAM--------MSGSIVgTPIHMAPELFTGK--YDNSVDVYAFGIL---FW-------------------YICsGSIKlP 749
Cdd:cd07865  169 FSLaknsqpnrYTNRVV-TLWYRPPELLLGErdYGPPIDMWGAGCImaeMWtrspimqgnteqhqltlisQLC-GSIT-P 245
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 564380513 750 EAFERCASKDhLWNNVR-----RGTRPERLPVF--DEECWQLMEACWDGDPSKRP 797
Cdd:cd07865  246 EVWPGVDKLE-LFKKMElpqgqKRKVKERLKPYvkDPYALDLIDKLLVLDPAKRI 299
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
556-738 1.25e-05

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 47.89  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLCDNWGGHFPCALKSVV--PPDEKHWNDLALEFHYMRSLpKHERLVDLHGSVidynyggGSSVAVLLI 633
Cdd:PLN00009   8 EKIGEGTYGVVYKARDRVTNETIALKKIRleQEDEGVPSTAIREISLLKEM-QHGNIVRLQDVV-------HSEKRLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 634 MERLHRDLYTGLKAGLSLETRLQIA----LDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA-KITDLG----FCKPEAM 704
Cdd:PLN00009  80 FEYLDLDLKKHMDSSPDFAKNPRLIktylYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNAlKLADFGlaraFGIPVRT 159
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 564380513 705 MSGSIVgTPIHMAPELFTGK--YDNSVDVYAFGILF 738
Cdd:PLN00009 160 FTHEVV-TLWYRAPEILLGSrhYSTPVDIWSVGCIF 194
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
656-736 1.26e-05

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: 48.20  E-value: 1.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALDVVEGIRFL---HSqgLVHRDIKLKNVLLDKQNRAKITDLGFC-KPEAMMSGSIVGTPIHMAPELFTG-KYDNSVD 730
Cdd:cd06615  103 KISIAVLRGLTYLrekHK--IMHRDVKPSNILVNSRGEIKLCDFGVSgQLIDSMANSFVGTRSYMSPERLQGtHYTVQSD 180

                 ....*.
gi 564380513 731 VYAFGI 736
Cdd:cd06615  181 IWSLGL 186
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
652-744 1.64e-05

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: 47.95  E-value: 1.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 652 ETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK------------------------------- 700
Cdd:cd05610  104 EMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSKvtlnrelnmmdilttpsmakpkndysrtpgq 183
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 701 ------------------PEAMMSGS-------IVGTPIHMAPELFTGK-YDNSVDVYAFGILFWYICSG 744
Cdd:cd05610  184 vlslisslgfntptpyrtPKSVRRGAarvegerILGTPDYLAPELLLGKpHGPAVDWWALGVCLFEFLTG 253
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
556-745 1.67e-05

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: 47.22  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 556 QELGRGQYGVVYLC--DNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLPKHERLVDLHGS-------VIDYNYGGGS 626
Cdd:cd14198   14 KELGRGKFAVVRQCisKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAKSNPRVVNLHEVyettseiILILEYAAGG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 627 SVAVLLIMERLHRdlytglkagLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN---RAKITDLGFCKP-- 701
Cdd:cd14198   94 EIFNLCVPDLAEM---------VSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYplgDIKIVDFGMSRKig 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 564380513 702 EAMMSGSIVGTPIHMAPELFTgkYD---NSVDVYAFGILFWYICSGS 745
Cdd:cd14198  165 HACELREIMGTPEYLAPEILN--YDpitTATDMWNIGVIAYMLLTHE 209
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
617-744 1.73e-05

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: 48.11  E-value: 1.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 617 VIDYNYGGGSSVAVLLIMERL-HRDLYTGLKAGLSL---ETRLQIAlDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAK 692
Cdd:cd05628   63 VVKMFYSFQDKLNLYLIMEFLpGGDMMTLLMKKDTLteeETQFYIA-ETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVK 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 693 ITDLGFC--------------------------------------KPEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYA 733
Cdd:cd05628  142 LSDFGLCtglkkahrtefyrnlnhslpsdftfqnmnskrkaetwkRNRRQLAFSTVGTPDYIAPEVFMQTgYNKLCDWWS 221
                        170
                 ....*....|.
gi 564380513 734 FGILFWYICSG 744
Cdd:cd05628  222 LGVIMYEMLIG 232
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
620-797 1.76e-05

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


Pssm-ID: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 47.49  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 620 YNYGGGSSVAVLLIMERLHRDLYTGLKAG-LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQN----RAKIT 694
Cdd:cd14018  105 NPSGLGHNRTLFLVMKNYPCTLRQYLWVNtPSYRLARVMILQLLEGVDHLVRHGIAHRDLKSDNILLELDFdgcpWLVIA 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 695 DLGFCKPEAMM------SGSIV---GTPIHMAPELFTG------KYDNS-VDVYAFGILFWYIcsgsIKLPEAFERcASK 758
Cdd:cd14018  185 DFGCCLADDSIglqlpfSSWYVdrgGNACLMAPEVSTAvpgpgvVINYSkADAWAVGAIAYEI----FGLSNPFYG-LGD 259
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 564380513 759 DHLWNnvrRGTRPERLPVFDEEC----WQLMEACWDGDPSKRP 797
Cdd:cd14018  260 TMLES---RSYQESQLPALPSAVppdvRQVVKDLLQRDPNKRV 299
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
632-737 1.78e-05

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 48.15  E-value: 1.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLHRDLYTGLKAG--------LSLETRlQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG----FC 699
Cdd:PHA03210 240 MITQKYDFDLYSFMYDEafdwkdrpLLKQTR-AIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGtampFE 318
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 564380513 700 KPEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVYAFGIL 737
Cdd:PHA03210 319 KEREAFDYGWVGTVATNSPEILAGDgYCEITDIWSCGLI 357
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
553-737 1.87e-05

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: 47.78  E-value: 1.87e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 553 KLGQELGRGQYGVVYLCDNWGGHF--PCALKSVVPP-DEKHWNDLAL-EFHYMRSLPKHERLVDLHGS--VIDYNYGGgs 626
Cdd:cd07857    3 ELIKELGQGAYGIVCSARNAETSEeeTVAIKKITNVfSKKILAKRALrELKLLRHFRGHKNITCLYDMdiVFPGNFNE-- 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 627 svaVLLIMERLHRDLYTGLKAGLSL-ETRLQIAL-DVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLG------- 697
Cdd:cd07857   81 ---LYLYEELMEADLHQIIRSGQPLtDAHFQSFIyQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFGlargfse 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564380513 698 -FCKPEAMMSGsIVGTPIHMAPELFTG--KYDNSVDVYAFG-IL 737
Cdd:cd07857  158 nPGENAGFMTE-YVATRWYRAPEIMLSfqSYTKAIDVWSVGcIL 200
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
649-738 1.92e-05

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


Pssm-ID: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 47.40  E-value: 1.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 649 LSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRaKITDLGFCKPEAMMSGSIV-----GTPIHMAPELFTG 723
Cdd:cd13974  129 LSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTR-KITITNFCLGKHLVSEDDLlkdqrGSPAYISPDVLSG 207
                         90
                 ....*....|....*...
gi 564380513 724 K-Y-DNSVDVYAFG-ILF 738
Cdd:cd13974  208 KpYlGKPSDMWALGvVLF 225
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
661-744 2.27e-05

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: 46.96  E-value: 2.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLL---DKQNRAKITDLGFCK--PEAMMSGSIVGTPIHMAPELFTgkYDN---SVDVY 732
Cdd:cd14106  117 ILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGISRviGEGEEIREILGTPDYVAPEILS--YEPislATDMW 194
                         90
                 ....*....|..
gi 564380513 733 AFGILFWYICSG 744
Cdd:cd14106  195 SIGVLTYVLLTG 206
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
664-738 2.36e-05

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: 47.37  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 664 GIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCKPEA----MMSGSIVgTPIHMAPELF--TGKYDNSVDVYAFGIL 737
Cdd:cd07858  120 GLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLARTTSekgdFMTEYVV-TRWYRAPELLlnCSEYTTAIDVWSVGCI 198

                 .
gi 564380513 738 F 738
Cdd:cd07858  199 F 199
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
632-735 2.80e-05

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: 47.24  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 632 LIMERLHRDLYTGLKA----GLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRA--KITDLGfckpEAMM 705
Cdd:cd14212   79 IVFELLGVNLYELLKQnqfrGLSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDSPeiKLIDFG----SACF 154
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 564380513 706 SGSIVGTPI----HMAPELFTG-KYDNSVDVYAFG 735
Cdd:cd14212  155 ENYTLYTYIqsrfYRSPEVLLGlPYSTAIDMWSLG 189
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
621-738 3.18e-05

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: 46.98  E-value: 3.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 621 NYGGGSSVAVLL-IMER-LHRDLYTGlkAGLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGF 698
Cdd:cd07855   78 PYADFKDVYVVLdLMESdLHHIIHSD--QPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGM 155
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 564380513 699 CKpeAMMSGSI---------VGTPIHMAPELF--TGKYDNSVDVYAFGILF 738
Cdd:cd07855  156 AR--GLCTSPEehkyfmteyVATRWYRAPELMlsLPEYTQAIDMWSVGCIF 204
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
557-697 3.36e-05

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: 46.80  E-value: 3.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 557 ELGRGQYGVVYLC-DNWGGHFpCALKsvVPPDEKHWNDLAL-EFHYMRSL----PKHE------RLVDlhgsviDYNYGG 624
Cdd:cd14136   17 KLGWGHFSTVWLCwDLQNKRF-VALK--VVKSAQHYTEAALdEIKLLKCVreadPKDPgrehvvQLLD------DFKHTG 87
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380513 625 GSSVAVLLIMERLHRDLYTGLKA----GLSLETRLQIALDVVEGIRFLHSQ-GLVHRDIKLKNVLLDKQN-RAKITDLG 697
Cdd:cd14136   88 PNGTHVCMVFEVLGPNLLKLIKRynyrGIPLPLVKKIARQVLQGLDYLHTKcGIIHTDIKPENVLLCISKiEVKIADLG 166
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
656-697 3.47e-05

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: 46.66  E-value: 3.47e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 564380513 656 QIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQNR-AKITDLG 697
Cdd:cd14013  124 SIMRQILVALRKLHSTGIVHRDVKPQNIIVSEGDGqFKIIDLG 166
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
655-744 3.95e-05

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: 46.15  E-value: 3.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 655 LQIALDVVEGIRFLHSQGLVHRDIKLKNVLLDKQ--NRAKITDLGFCKpEAMMSGS---IVGTPIHMAPELFTGK-YDNS 728
Cdd:cd14191  103 IKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKtgTKIKLIDFGLAR-RLENAGSlkvLFGTPEFVAPEVINYEpIGYA 181
                         90
                 ....*....|....*.
gi 564380513 729 VDVYAFGILFWYICSG 744
Cdd:cd14191  182 TDMWSIGVICYILVSG 197
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
558-744 4.57e-05

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: 46.07  E-value: 4.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 558 LGRGQYGVVYLCDNWGGHFPCALKSVVPPDEKHWNDLALEFHYMRSLpKHERLVDLHGSV---------IDYNYGGGssv 628
Cdd:cd14190   12 LGGGKFGKVHTCTEKRTGLKLAAKVINKQNSKDKEMVLLEIQVMNQL-NHRNLIQLYEAIetpneivlfMEYVEGGE--- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 629 avllIMERLHRDLYTglkagLSLETRLQIALDVVEGIRFLHSQGLVHRDIKLKNVLL--DKQNRAKITDLGFC---KPEA 703
Cdd:cd14190   88 ----LFERIVDEDYH-----LTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCvnRTGHQVKIIDFGLArryNPRE 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 564380513 704 MMSGSIvGTPIHMAPELFTgkYD---NSVDVYAFGILFWYICSG 744
Cdd:cd14190  159 KLKVNF-GTPEFLSPEVVN--YDqvsFPTDMWSMGVITYMLLSG 199
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
661-797 5.79e-05

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


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 45.63  E-value: 5.79e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLLDKQNRAKITDLGFCK------PEAMMSGSIVGT-PIH-MAPELFT-GKYDNSVDV 731
Cdd:cd05065  115 IAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRfleddtSDPTYTSSLGGKiPIRwTAPEAIAyRKFTSASDV 194
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 564380513 732 YAFGILFWYICSGSiklpeafERC---ASKDHLWNNVRRGTRPERLPVFDEECWQLMEACWDGDPSKRP 797
Cdd:cd05065  195 WSYGIVMWEVMSYG-------ERPywdMSNQDVINAIEQDYRLPPPMDCPTALHQLMLDCWQKDRNLRP 256
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
547-685 5.95e-05

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: 46.18  E-value: 5.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 547 LLHRKPKLGQELGRGQYGVVYLCDNWGGHFPCALKSVvpPDEKHWNDLAL-EFHYMRSL-------PKHERLVDLhgsVI 618
Cdd:cd14216    7 LFNGRYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVV--KSAEHYTETALdEIKLLKSVrnsdpndPNREMVVQL---LD 81
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 564380513 619 DYNYGGGSSVAVLLIMERL-HRDLYTGLKA---GLSLETRLQIALDVVEGIRFLHSQ-GLVHRDIKLKNVLL 685
Cdd:cd14216   82 DFKISGVNGTHICMVFEVLgHHLLKWIIKSnyqGLPLPCVKKIIRQVLQGLDYLHTKcRIIHTDIKPENILL 153
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
661-742 6.40e-05

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: 45.89  E-value: 6.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 661 VVEGIRFLHSQGLVHRDIKLKNVLL-----------------DKQN----------------RAKITDLGFCK---PEAM 704
Cdd:cd14096  115 VASAVKYLHEIGVVHRDIKPENLLFepipfipsivklrkaddDETKvdegefipgvggggigIVKLADFGLSKqvwDSNT 194
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 564380513 705 MSGsiVGTPIHMAPELFTGK-YDNSVDVYAFG-ILFWYIC 742
Cdd:cd14096  195 KTP--CGTVGYTAPEVVKDErYSKKVDMWALGcVLYTLLC 232
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
656-749 6.69e-05

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: 45.81  E-value: 6.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564380513 656 QIALDVVEGIRFLHSQ-GLVHRDIKLKNVLLDKQNRAKITDLGFC-KPEAMMSGSIVGTPIHMAPELFTGK-YDNSVDVY 732
Cdd:cd06649  107 KVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGVSgQLIDSMANSFVGTRSYMSPERLQGThYSVQSDIW 186
                         90
                 ....*....|....*..
gi 564380513 733 AFGILFWYICSGSIKLP 749
Cdd:cd06649  187 SMGLSLVELAIGRYPIP 203
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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