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Conserved domains on  [gi|111222708|ref|YP_713502|]
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serine/threonine protein kinase [Frankia alni ACN14a]

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List of domain hits

Name Accession Description Interval E-value
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
78-266 1.94e-39

Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The STE family is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). 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), MAPK kinase kinases (MAPKKKs), or MAPK kinase kinase 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.


:

Pssm-ID: 173659 [Multi-domain]  Cd Length: 253  Bit Score: 145.81  E-value: 1.94e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGR-LPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDG 156
Cdd:cd05122   56 HPNIVKYYGSYLKKDELWIVMEFCSGGSLKDLLKSTNQtLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTSDG 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 157 QARLTDFGIAVTEGDATLTEagTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPL-AILAAVVED 235
Cdd:cd05122  136 EVKLIDFGLSAQLSDTKARN--TMVGTPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPYSELPPMkALFKIATNG 213
                        170       180       190
                 ....*....|....*....|....*....|....
gi 111222708 236 R---RRPFQHSGPLRGILTELLDSDPARRPSLAE 266
Cdd:cd05122  214 PpglRNPEKWSDEFKDFLKKCLQKNPEKRPTAEQ 247
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
41-267 4.49e-53

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 184.27  E-value: 4.49e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708    41 RRVAIKEVRRPAVASPA-----ERAVLSErvlrearaaarLRHPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGR 115
Cdd:smart00220  25 KLVAIKVIKKKKIKKDRerilrEIKILKK-----------LKHPNIVRLYDVFEDEDKLYLVMEYCEGGDLFDLLKKRGR 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708   116 LPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDGQARLTDFGIAVTEGDATLTeaGTLVGSPAYIAPERARGA 195
Cdd:smart00220  94 LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKL--TTFVGTPEYMAPEVLLGK 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 111222708   196 RVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAVVEDRRRPFQH-----SGPLRGILTELLDSDPARRPSLAEA 267
Cdd:smart00220 172 GYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPpewdiSPEAKDLIRKLLVKDPEKRLTAEEA 248
 
Name Accession Description Interval E-value
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
78-266 1.94e-39

Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The STE family is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). 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), MAPK kinase kinases (MAPKKKs), or MAPK kinase kinase 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.


Pssm-ID: 173659 [Multi-domain]  Cd Length: 253  Bit Score: 145.81  E-value: 1.94e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGR-LPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDG 156
Cdd:cd05122   56 HPNIVKYYGSYLKKDELWIVMEFCSGGSLKDLLKSTNQtLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTSDG 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 157 QARLTDFGIAVTEGDATLTEagTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPL-AILAAVVED 235
Cdd:cd05122  136 EVKLIDFGLSAQLSDTKARN--TMVGTPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPYSELPPMkALFKIATNG 213
                        170       180       190
                 ....*....|....*....|....*....|....
gi 111222708 236 R---RRPFQHSGPLRGILTELLDSDPARRPSLAE 266
Cdd:cd05122  214 PpglRNPEKWSDEFKDFLKKCLQKNPEKRPTAEQ 247
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
83-166 8.52e-09

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 54.91  E-value: 8.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  83 TVYDVlDTDDHTwIVMEYVDGTSLAELIrAAGRLPALEVAR-IGVSLAyaleAAHRGGVVHRDVKPGNVLVTnDGQARLT 161
Cdd:PRK14879  65 AVYFV-DPENFI-IVMEYIEGEPLKDLI-NSNGMEELELSReIGRLVG----KLHSAGIIHGDLTTSNMILS-GGKIYLI 136

                 ....*
gi 111222708 162 DFGIA 166
Cdd:PRK14879 137 DFGLA 141
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
83-166 1.55e-08

Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated with Kae1 (kinase-associated endopeptidase 1) in the Archaea. In many Archaeal genomes, Kae1 and Bud32 are fused. The complex is homologous to the Kae1 and Bud32 subunits of the eukaryotic KEOPS complex, an apparently ancient protein kinase-containing molecular machine [Unknown function, General].


Pssm-ID: 234331  Cd Length: 199  Bit Score: 53.76  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708   83 TVYDVlDTDDHTwIVMEYVDGTSLAELIRAAGrlpaLEVAR-IGVSLAyaleAAHRGGVVHRDVKPGNVLVTNDgQARLT 161
Cdd:TIGR03724  63 VVYDV-DPDNKT-IVMEYIEGKPLKDVIEEGN----DELLReIGRLVG----KLHKAGIVHGDLTTSNIIVRDD-KLYLI 131

                  ....*
gi 111222708  162 DFGIA 166
Cdd:TIGR03724 132 DFGLG 136
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
105-273 9.47e-08

kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to the C-terminal protein kinase catalytic fold (C lobe). Its presence at the N terminus of signalling proteins and the absence of the active-site residues in the catalytic and activation loops suggest that it folds independently and is likely to be non-catalytic. The occurrence of KIND only in metazoa implies that it has evolved from the catalytic protein kinase domain into an interaction domain possibly by keeping the substrate-binding features


Pssm-ID: 214801  Cd Length: 176  Bit Score: 51.25  E-value: 9.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708   105 SLAELIRAAGR-LPALEVArigvslAYALEAAHRGGVVHRDVKPGNVLVTNDGQARLtdfgiavtEGDATLTEAGTLVGS 183
Cdd:smart00750   2 SLADILEVRGRpLNEEEIW------AVCLQCLGALRELHRQAKSGNILLTWDGLLKL--------DGSVAFKTPEQSRPD 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708   184 PAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAVVEDRRRPFQHSGP-----------LRGILTE 252
Cdd:smart00750  68 PYFMAPEVIQGQSYTEKADIYSLGITLYEALDYELPYNEERELSAILEILLNGMPADDPRDRsnlegvsaarsFEDFMRL 147
                          170       180
                   ....*....|....*....|.
gi 111222708   253 LLDSDPARRPSLAEARGRLRE 273
Cdd:smart00750 148 CASRLPQRREAANHYLAHCRA 168
AarF COG0661
Predicted unusual protein kinase [General function prediction only]
96-165 1.06e-06

Predicted unusual protein kinase [General function prediction only]


Pssm-ID: 223733  Cd Length: 517  Bit Score: 50.39  E-value: 1.06e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 111222708  96 IVMEYVDGTSL--AELIRAAGRLPAlEVARIGVSlAYaLEAAHRGGVVHRDVKPGNVLVTNDGQARLTDFGI 165
Cdd:COG0661  243 LTMEWIDGIKIsdIAALKSAGIDRK-ELAELLVR-AF-LRQLLRDGFFHADPHPGNILVRSDGRIVLLDFGI 311
PHA02882 PHA02882
putative serine/threonine kinase; Provisional
121-166 1.48e-03

putative serine/threonine kinase; Provisional


Pssm-ID: 165211  Cd Length: 294  Bit Score: 39.93  E-value: 1.48e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*.
gi 111222708 121 VARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDGQARLTDFGIA 166
Cdd:PHA02882 128 IKNIMKDMLTTLEYIHEHGISHGDIKPENIMVDGNNRGYIIDYGIA 173
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
139-261 1.77e-03

Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. These proteins have a typical bilobed protein kinase fold, but lack catalytic actvity.


Pssm-ID: 258671  Cd Length: 289  Bit Score: 39.32  E-value: 1.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  139 GVVHRDVKPGNVLVTNDGQARLTDFGIAVTEGDatlteAGTLVGSPAYIAPERARGARVGA---------AGDVWGLGAT 209
Cdd:pfam14531 166 GLVHGDFRPDNFFLDQKGGVFLGGFTALVRAGT-----KVVVSEVDVAFAPPELFASRGYTgkntttmthKTDAWQLGLV 240
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 111222708  210 LFTAVEGVPPFQGEGPLAILAAvveDRRRPFQHSGPLRGILTELLDSDPARR 261
Cdd:pfam14531 241 IYRIWCLRLPFTLDTPEGGSEW---KFGRCVNMPEPVKALLAGFLNRSQEAR 289
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
41-267 4.49e-53

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 184.27  E-value: 4.49e-53
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708    41 RRVAIKEVRRPAVASPA-----ERAVLSErvlrearaaarLRHPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGR 115
Cdd:smart00220  25 KLVAIKVIKKKKIKKDRerilrEIKILKK-----------LKHPNIVRLYDVFEDEDKLYLVMEYCEGGDLFDLLKKRGR 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708   116 LPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDGQARLTDFGIAVTEGDATLTeaGTLVGSPAYIAPERARGA 195
Cdd:smart00220  94 LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKL--TTFVGTPEYMAPEVLLGK 171
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 111222708   196 RVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAVVEDRRRPFQH-----SGPLRGILTELLDSDPARRPSLAEA 267
Cdd:smart00220 172 GYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPpewdiSPEAKDLIRKLLVKDPEKRLTAEEA 248
Pkinase pfam00069
Protein kinase domain;
40-267 1.32e-49

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 174.36  E-value: 1.32e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708   40 RRRVAIKEVRRPAVASPAERAVLSE-RVLREARaaarlrHPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGRLPA 118
Cdd:pfam00069  24 GKIVAVKILKKRSEKSKKDQTARREiRILRRLS------HPNIVRLIDAFEDKDHLYLVMEYCEGGDLFDYLSRGGPLSE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  119 LEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDGQARLTDFGIAVTeGDATLTEAGTLVGSPAYIAPERARGAR-V 197
Cdd:pfam00069  98 DEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGVVKIADFGLAKK-LTKSSSSLTTFVGTPEYMAPEVLLGGNgY 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 111222708  198 GAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAVVEDRRRPFQHSGP--------LRGILTELLDSDPARRPSLAEA 267
Cdd:pfam00069 177 GPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRILGPPLEFDEPksdsgseeAKDLIKKCLNKDPSKRPTAEEI 254
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
40-267 2.29e-33

Serine/threonine protein kinase [General function prediction only / Signal transduction mechanisms / Transcription / DNA replication, recombination, and repair]


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 131.79  E-value: 2.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  40 RRRVAIKEVRRPAVASPAERA-VLSERvlreARAAARLRHPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRA---AGR 115
Cdd:COG0515   22 RKLVALKVLAKKLESKSKEVErFLREI----QILASLNHPPNIVKLYDFFQDEGSLYLVMEYVDGGSLEDLLKKigrKGP 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 116 LPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVT-NDGQARLTDFGIAVTEGDATLT-----EAGTLVGSPAYIAP 189
Cdd:COG0515   98 LSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDrDGRVVKLIDFGLAKLLPDPGSTssipaLPSTSVGTPGYMAP 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 190 ERARG---ARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAVVE--------DRRRPFQHSGP------LRGILTE 252
Cdd:COG0515  178 EVLLGlslAYASSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLKiilelptpSLASPLSPSNPeliskaASDLLKK 257
                        250
                 ....*....|....*
gi 111222708 253 LLDSDPARRPSLAEA 267
Cdd:COG0515  258 LLAKDPKNRLSSSSD 272
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
78-261 5.39e-26

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 109.14  E-value: 5.39e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGRLPAlEVARI-GVSLAYALEAAHRGGVVHRDVKPGNVLVTNDG 156
Cdd:PTZ00263  77 HPFIVNMMCSFQDENRVYFLLEFVVGGELFTHLRKAGRFPN-DVAKFyHAELVLAFEYLHSKDIIYRDLKPENLLLDNKG 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 157 QARLTDFGIAVTEGDATLteagTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAVVEDR 236
Cdd:PTZ00263 156 HVKVTDFGFAKKVPDRTF----TLCGTPEYLAPEVIQSKGHGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGR 231
                        170       180
                 ....*....|....*....|....*.
gi 111222708 237 RR-PFQHSGPLRGILTELLDSDPARR 261
Cdd:PTZ00263 232 LKfPNWFDGRARDLVKGLLQTDHTKR 257
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
42-274 2.92e-20

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


Pssm-ID: 234389 [Multi-domain]  Cd Length: 1266  Bit Score: 94.91  E-value: 2.92e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708    42 RVAIKEVRRPAVASPAERAvlseRVLREARAAARLRHPGLVTVYDVLDT-DDHTWIVMEYVDGTSLAELIRAAGRLPALE 120
Cdd:TIGR03903    5 EVAIKLLRTDAPEEEHQRA----RFRRETALCARLYHPNIVALLDSGEApPGLLFAVFEYVPGRTLREVLAADGALPAGE 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708   121 VARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDG---QARLTDFGIA-----VTEGD-ATLTEAGTLVGSPAYIAPER 191
Cdd:TIGR03903   81 TGRLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGvrpHAKVLDFGIGtllpgVRDADvATLTRTTEVLGTPTYCAPEQ 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708   192 ARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAIL---AAVVEDRRRPFQHSGPLRGILTELLDSDPARRPSLAEA- 267
Cdd:TIGR03903  161 LRGEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILyqqLSPVDVSLPPWIAGHPLGQVLRKALNKDPRQRAASAPAl 240

                   ....*..
gi 111222708   268 RGRLREI 274
Cdd:TIGR03903  241 AERFRAL 247
pknD PRK13184
serine/threonine-protein kinase; Reviewed
36-261 6.54e-19

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 90.21  E-value: 6.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  36 DTLLRRRVAIKEVRRPAvaspAERAVLSERVLREARAAARLRHPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGR 115
Cdd:PRK13184  23 DPVCSRRVALKKIREDL----SENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPYIEGYTLKSLLKSVWQ 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 116 LPAL--EVA---------RIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDGQARLTDFGIAVT-------EGD------ 171
Cdd:PRK13184  99 KESLskELAektsvgaflSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGAAIFkkleeedLLDidvder 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 172 ----ATLTEAGTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAIlaaVVEDRRRPFQHSGPLR 247
Cdd:PRK13184 179 nicySSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKI---SYRDVILSPIEVAPYR 255
                        250       260
                 ....*....|....*....|.
gi 111222708 248 GILTEL-------LDSDPARR 261
Cdd:PRK13184 256 EIPPFLsqiamkaLAVDPAER 276
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
78-266 6.81e-15

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 75.25  E-value: 6.81e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLaELIRAAGRLPALEVAR-IGVSLAYAleaaHRGGVVHRDVKPGNVLVTNDG 156
Cdd:PLN00034 131 HPNVVKCHDMFDHNGEIQVLLEFMDGGSL-EGTHIADEQFLADVARqILSGIAYL----HRRHIVHRDIKPSNLLINSAK 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 157 QARLTDFGIAVTEGDaTLTEAGTLVGSPAYIAPERA-----RGARVGAAGDVWGLGATLFTAVEGVPPF----QGEGPLA 227
Cdd:PLN00034 206 NVKIADFGVSRILAQ-TMDPCNSSVGTIAYMSPERIntdlnHGAYDGYAGDIWSLGVSILEFYLGRFPFgvgrQGDWASL 284
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 111222708 228 ILAAVVEDR-RRPFQHSGPLRGILTELLDSDPARRPSLAE 266
Cdd:PLN00034 285 MCAICMSQPpEAPATASREFRHFISCCLQREPAKRWSAMQ 324
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
78-207 3.11e-13

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 69.11  E-value: 3.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGRLPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVT-NDG 156
Cdd:PHA03390  68 NPNFIKLYYSVTTLKGHVLIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDrAKD 147
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 111222708 157 QARLTDFGIAVTEGdATLTEAGTLVgspaYIAPERARGARVGAAGDVWGLG 207
Cdd:PHA03390 148 RIYLCDYGLCKIIG-TPSCYDGTLD----YFSPEKIKGHNYDVSFDWWAVG 193
PRK07764 PRK07764
DNA polymerase III subunits gamma and tau; Validated
307-525 1.18e-04

DNA polymerase III subunits gamma and tau; Validated


Pssm-ID: 236090 [Multi-domain]  Cd Length: 824  Bit Score: 44.21  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 307 GGAAPPPASNVSPAAPPSAAGTPAPTGRPGLADRPDGADQPGPVGPAGLDAGASWAARPGSAGEPGQAAAAGPAAASEGG 386
Cdd:PRK07764 593 GAAGGEGPPAPASSGPPEEAARPAAPAAPAAPAAPAPAGAAAAPAEASAAPAPGVAAPEHHPKHVAVPDASDGGDGWPAK 672
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 387 GLDAAGSGAGGRvdaagsgaaggldaAASGGDRAAPRRDPAAPRDHPDGPARRRRIAVLAGVAAVVIAAVAIVLGLVLAG 466
Cdd:PRK07764 673 AGGAAPAAPPPA--------------PAPAAPAAPAGAAPAQPAPAPAATPPAGQADDPAAQPPQAAQGASAPSPAADDP 738
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 111222708 467 GGSPGSPVAAATTSPATAAPTPAPRSSATATAGSKPSPTTSPSATGPTPAGTPSAPSTA 525
Cdd:PRK07764 739 VPLPPEPDDPPDPAGAPAQPPPPPAPAPAAAPAAAPPPSPPSEEEEMAEDDAPSMDDED 797
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
256-586 1.50e-04

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 43.62  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  256 SDPARRPSLAEARGRLREIADRLEETDHTLDGTLVEIPQLGPDGPDGANGLGGAAPPPASnvSPAAPPSAAGTPAPTGRP 335
Cdd:PHA03307   62 CDRFEPPTGPPPGPGTEAPANESRSTPTWSLSTLAPASPAREGSPTPPGPSSPDPPPPTP--PPASPPPSPAPDLSEMLR 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  336 GLADRPDGADQPGPVGPAGLDAGASWAARPGSAGEP---GQAAAAGPAAASEGGGLDAAGSGAGGRVDAAGSGAAGGLDA 412
Cdd:PHA03307  140 PVGSPGPPPAASPPAAGASPAAVASDAASSRQAALPlssPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASS 219
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  413 AASGGDRAAPRRDPAAPRDHPDGPARRRRIAVLAGVAAVVIAAVAIVLGLVLAGGGSPGSPVAAATTSPATAAPTPAPRS 492
Cdd:PHA03307  220 PAPAPGRSAADDAGASSSDSSSSESSGCGWGPENECPLPRPAPITLPTRIWEASGWNGPSSRPGPASSSSSPRERSPSPS 299
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  493 SATATAGSKPSPTTSPSATGPTPAGTPSAPSTASPAVSSAGDNLGALIPDTTDPAEAPDGYTTHRDSSGWSAALPAGWRT 572
Cdd:PHA03307  300 PSSPGSGPAPSSPRASSSSSSSRESSSSSTSSSSESSRGAAVSPGPSPSRSPSPSRPPPPADPSSPRKRPRPSRAPSSPA 379
                         330
                  ....*....|....
gi 111222708  573 SERGNGRVITTAPS 586
Cdd:PHA03307  380 ASAGRPTRRRARAA 393
 
Name Accession Description Interval E-value
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
78-266 1.94e-39

Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The STE family is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). 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), MAPK kinase kinases (MAPKKKs), or MAPK kinase kinase 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.


Pssm-ID: 173659 [Multi-domain]  Cd Length: 253  Bit Score: 145.81  E-value: 1.94e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGR-LPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDG 156
Cdd:cd05122   56 HPNIVKYYGSYLKKDELWIVMEFCSGGSLKDLLKSTNQtLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTSDG 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 157 QARLTDFGIAVTEGDATLTEagTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPL-AILAAVVED 235
Cdd:cd05122  136 EVKLIDFGLSAQLSDTKARN--TMVGTPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPYSELPPMkALFKIATNG 213
                        170       180       190
                 ....*....|....*....|....*....|....
gi 111222708 236 R---RRPFQHSGPLRGILTELLDSDPARRPSLAE 266
Cdd:cd05122  214 PpglRNPEKWSDEFKDFLKKCLQKNPEKRPTAEQ 247
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
78-266 9.60e-38

Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), (Cdc7)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Cdc7-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. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) epsilon, and related proteins. 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. 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.


Pssm-ID: 173731 [Multi-domain]  Cd Length: 254  Bit Score: 141.23  E-value: 9.60e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGRLPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDGQ 157
Cdd:cd06627   58 HPNIVKYIGSIETSDSLYIILEYAENGSLRQIIKKFGPFPESLVAVYVYQVLQGLAYLHEQGVIHRDIKAANILTTKDGV 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 158 ARLTDFGIAVTEGDATLTEAgTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAVVEDRR 237
Cdd:cd06627  138 VKLADFGVATKLNDVSKDDA-SVVGTPYWMAPEVIEMSGASTASDIWSLGCTVIELLTGNPPYYDLNPMAALFRIVQDDH 216
                        170       180       190
                 ....*....|....*....|....*....|.
gi 111222708 238 RPFQH--SGPLRGILTELLDSDPARRPSLAE 266
Cdd:cd06627  217 PPLPEgiSPELKDFLMQCFQKDPNLRPTAKQ 247
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
57-261 1.86e-36

Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), AGC (Protein Kinases A, G and C) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The AGC 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 (PI3K). 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. AGC kinases regulate many cellular processes including division, growth, survival, metabolism, motility, and differentiation. Many are implicated in the development of various human diseases.


Pssm-ID: 173660 [Multi-domain]  Cd Length: 250  Bit Score: 137.27  E-value: 1.86e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  57 AERAVLSErvlrearaaarLRHPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGRLPALEVARIGVSLAYALEAAH 136
Cdd:cd05123   42 TERNILSR-----------INHPFIVKLHYAFQTEEKLYLVLEYAPGGELFSHLSKEGRFSEERARFYAAEIVLALEYLH 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 137 RGGVVHRDVKPGNVLVTNDGQARLTDFGIAvTEGDATLTEAGTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEG 216
Cdd:cd05123  111 SLGIIYRDLKPENILLDADGHIKLTDFGLA-KELSSEGSRTNTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTG 189
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 111222708 217 VPPFQGEGPLAILAAVVEDRRR-PFQHSGPLRGILTELLDSDPARR 261
Cdd:cd05123  190 KPPFYAEDRKEIYEKILKDPLRfPEFLSPEARDLISGLLQKDPTKR 235
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
78-266 7.65e-36

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase (Nek) family, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek 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. 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.


Pssm-ID: 173755 [Multi-domain]  Cd Length: 258  Bit Score: 135.70  E-value: 7.65e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGR----LPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVT 153
Cdd:cd08215   58 HPNIIKYYESFEEKGKLCIVMEYADGGDLSQKIKKQKKegkpFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLT 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 154 NDGQARLTDFGIAvTEGDATLTEAGTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAVV 233
Cdd:cd08215  138 SNGLVKLGDFGIS-KVLSSTVDLAKTVVGTPYYLSPELCQNKPYNYKSDIWSLGCVLYELCTLKHPFEGENLLELALKIL 216
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 111222708 234 EDRRRPF--QHSGPLRGILTELLDSDPARRPSLAE 266
Cdd:cd08215  217 KGQYPPIpsQYSSELRNLVSSLLQKDPEERPSIAQ 251
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
41-267 3.39e-35

Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. 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. PKs make up a large family of serine/threonine kinases, protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation, about 95%, 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 550 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.


Pssm-ID: 173623 [Multi-domain]  Cd Length: 215  Bit Score: 132.75  E-value: 3.39e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  41 RRVAIKEVRRPAVASPAERA-----VLSERvlrearaaarlRHPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRA-AG 114
Cdd:cd00180   19 KKVAIKIIKKEDSSSLLEELlreieILKKL-----------NHPNIVKLYGVFEDENHLYLVMEYCEGGSLKDLLKEnEG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 115 RLPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTND-GQARLTDFGIAVTEGDATLTEaGTLVGSPAYIAPERAR 193
Cdd:cd00180   88 KLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDnGKVKLADFGLSKLLTSDKSLL-KTIVGTPAYMAPEVLL 166
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 111222708 194 GAR-VGAAGDVWGLGATLFTAVEgvppfqgegplailaavvedrrrpfqhsgpLRGILTELLDSDPARRPSLAEA 267
Cdd:cd00180  167 GKGyYSEKSDIWSLGVILYELPE------------------------------LKDLIRKMLQKDPEKRPSAKEI 211
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine ...
78-262 1.01e-32

Catalytic domain of Microtubule-associated serine/threonine kinase-like proteins; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. The MAST kinase subfamily includes MAST kinases, MAST-like (MASTL) kinases, 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 also contains an insert relative to MAST kinases like MASTL. 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. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively.


Pssm-ID: 173670 [Multi-domain]  Cd Length: 265  Bit Score: 127.36  E-value: 1.01e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGRLPAlEVARIGVS-LAYALEAAHRGGVVHRDVKPGNVLVTNDG 156
Cdd:cd05579   52 SPYVVKLYYSFQGKKNLYLVMEYLPGGDLASLLENVGSLDE-DVARIYIAeIVLALEYLHSNGIIHRDLKPDNILIDSNG 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 157 QARLTDFGIA-------VTEGDATLTEAGTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAIL 229
Cdd:cd05579  131 HLKLTDFGLSkvglvrrQINLNDDEKEDKRIVGTPDYIAPEVILGQGHSKTVDWWSLGCILYEFLVGIPPFHGETPEEIF 210
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 111222708 230 AAVVEDRRRP---FQHSGPLRGILTELLDSDPARRP 262
Cdd:cd05579  211 QNILNGKIEWpedVEVSDEAIDLISKLLVPDPEKRL 246
STKc_PAK cd06614
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine ...
78-267 1.42e-32

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine/threonine kinases (STKs), p21-activated kinase (PAK) subfamily, 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 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.


Pssm-ID: 173728 [Multi-domain]  Cd Length: 286  Bit Score: 127.33  E-value: 1.42e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIR-AAGRLPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDG 156
Cdd:cd06614   74 HPNIVDYYDSYLVGDELWVVMEYMDGGSLTDIITqNFVRMNEPQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDG 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 157 QARLTDFGIAvtegdATLTEAG----TLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAV 232
Cdd:cd06614  154 SVKLADFGFA-----AQLTKEKskrnSVVGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLREPPLRALFLI 228
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 111222708 233 VEDRRRPFQH----SGPLRGILTELLDSDPARRPSLAEA 267
Cdd:cd06614  229 TTKGIPPLKNpekwSPEFKDFLNKCLVKDPEKRPSAEEL 267
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
78-220 1.90e-32

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase Kinase; Serine/threonine kinases (STKs), mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAPKKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173724 [Multi-domain]  Cd Length: 260  Bit Score: 126.52  E-value: 1.90e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDV-LDTDDHTW-IVMEYVDGTSLAELIRAAGRLPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTND 155
Cdd:cd06606   58 HPNIVRYYGSeRDEEKNTLnIFLEYVSGGSLSSLLKKFGKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVDSD 137
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 111222708 156 GQARLTDFGIAVTEGDATLTEA-GTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPF 220
Cdd:cd06606  138 GVVKLADFGCAKRLGDIETGEGtGSVRGTPYWMAPEVIRGEEYGRAADIWSLGCTVIEMATGKPPW 203
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
78-266 1.95e-31

Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, Plant MAPKKs and similar proteins, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising of the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK). 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.


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 123.47  E-value: 1.95e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGRLPALEVARIGVSLAYALEAAHRG-GVVHRDVKPGNVLVTNDG 156
Cdd:cd06623   58 SPYVVKCYGAFYKEGEISIVLEYMDGGSLADLLKKVGKIPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKG 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 157 QARLTDFGIAVTEgDATLTEAGTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQ---GEGPLAILAAVV 233
Cdd:cd06623  138 EVKIADFGISKVL-ENTLDQCNTFVGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLppgQPSFFELMQAIC 216
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 111222708 234 ED---RRRPFQHSGPLRGILTELLDSDPARRPSLAE 266
Cdd:cd06623  217 DGpppSLPAEEFSPEFRDFISACLQKDPKKRPSAAE 252
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
78-266 1.50e-30

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, catalytic (c) domain. PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. The MAPKK 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. The mitogen-activated protein (MAP) kinase signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAP kinase (MAPK), which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPK kinase kinase (MAPKKK or MKKK or MAP3K). MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. 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.


Pssm-ID: 173723 [Multi-domain]  Cd Length: 265  Bit Score: 121.27  E-value: 1.50e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELI-RAAGRLPALEVARIGVSLAYALEAAHRG-GVVHRDVKPGNVLVTND 155
Cdd:cd06605   58 SPYIVGFYGAFYNNGDISICMEYMDGGSLDKILkEVQGRIPERILGKIAVAVLKGLTYLHEKhKIIHRDVKPSNILVNSR 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 156 GQARLTDFGIAvteGDATLTEAGTLVGSPAYIAPERARGARVGAAGDVWGLGATLFT-AVEGVP-PFQGEGPLAI---LA 230
Cdd:cd06605  138 GQIKLCDFGVS---GQLVNSLAKTFVGTSSYMAPERIQGNDYSVKSDIWSLGLSLIElATGRFPyPPENDPPDGIfelLQ 214
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 111222708 231 AVV-EDRRRPFQH--SGPLRGILTELLDSDPARRPSLAE 266
Cdd:cd06605  215 YIVnEPPPRLPSGkfSPDFQDFVNLCLIKDPRERPSYKE 253
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine ...
79-261 2.28e-30

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; Serine/Threonine Kinases (STKs), Microtubule-associated serine/threonine (MAST) kinase subfamily, fungal Rim15-like kinases, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MAST kinase subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173702 [Multi-domain]  Cd Length: 260  Bit Score: 120.28  E-value: 2.28e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  79 PGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGRLPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDGQA 158
Cdd:cd05611   57 PYVAKLYYSFQSKDYLYLVMEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHL 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 159 RLTDFGiavtegdatLTEAGTL----VGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAVVE 234
Cdd:cd05611  137 KLTDFG---------LSRNGLEnkkfVGTPDYLAPETILGVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILS 207
                        170       180       190
                 ....*....|....*....|....*....|..
gi 111222708 235 DR----RRPFQHSGP-LRGILTELLDSDPARR 261
Cdd:cd05611  208 RRinwpEEVKEFCSPeAVDLINRLLCMDPAKR 239
STKc_Nek2 cd08217
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
78-266 5.78e-29

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 2; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 2 (Nek2) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173757 [Multi-domain]  Cd Length: 265  Bit Score: 116.58  E-value: 5.78e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYD-VLDTDDHT-WIVMEYVDGTSLAELIRAA----GRLPALEVARIGVSLAYALEAAHRGG-----VVHRDVK 146
Cdd:cd08217   58 HPNIVRYYDrIIDRSNQTlYIVMEYCEGGDLAQLIQKCkkerKYIEEEFIWRILTQLLLALYECHNRSdpgntVLHRDLK 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 147 PGNVLVTNDGQARLTDFGIAVTEGDATlTEAGTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEG-- 224
Cdd:cd08217  138 PANIFLDANNNVKLGDFGLAKILGHDS-SFAKTYVGTPYYMSPEQLNHMSYDEKSDIWSLGCLIYELCALSPPFTARNql 216
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 111222708 225 PLAILAAVVEDRRRPFQHSGPLRGILTELLDSDPARRPSLAE 266
Cdd:cd08217  217 QLASKIKEGKFRRIPYRYSSELNEVIKSMLNVDPDKRPSTEE 258
STKc_PKA cd05580
Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine ...
78-261 1.81e-28

Catalytic domain of the Protein Serine/Threonine Kinase, cAMP-dependent protein kinase; Serine/Threonine Kinases (STKs), cAMP-dependent protein kinase (PKA) subfamily, catalytic (c) subunit. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKA subfamily is part of a 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). This subfamily is composed of the cAMP-dependent proteins kinases, PKA and PRKX. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic (C) 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 C 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.


Pssm-ID: 173671 [Multi-domain]  Cd Length: 290  Bit Score: 115.72  E-value: 1.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGRLPaLEVARI-GVSLAYALEAAHRGGVVHRDVKPGNVLVTNDG 156
Cdd:cd05580   60 HPFLVNLYGSFQDDSNLYLVMEYVPGGELFSHLRKSGRFP-EPVARFyAAQVVLALEYLHSLDIVYRDLKPENLLLDSDG 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 157 QARLTDFGIAVTEGDATLteagTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAVVEDR 236
Cdd:cd05580  139 YIKITDFGFAKRVKGRTY----TLCGTPEYLAPEIILSKGYGKAVDWWALGILIYEMLAGYPPFFDDNPIQIYEKILEGK 214
                        170       180
                 ....*....|....*....|....*.
gi 111222708 237 RR-PFQHSGPLRGILTELLDSDPARR 261
Cdd:cd05580  215 VRfPSFFSPDAKDLIRNLLQVDLTKR 240
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
37-272 3.30e-28

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related kinase 9; Serine/Threonine Kinases (STKs), Never In Mitosis gene A (NIMA)-related kinase 9 (Nek9) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek9 subfamily is one 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 protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173761 [Multi-domain]  Cd Length: 256  Bit Score: 114.08  E-value: 3.30e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  37 TLLRRR-----VAIKEVRRPAVASPAERAVLSERVLREARAaarlrHPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELI- 110
Cdd:cd08221   17 TLYRRTeddslVVWKEVNLTRLSEKERRDALNEIVILSLLQ-----HPNIIAYYNHFMDDNTLLIEMEYANGGTLYDKIv 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 111 -RAAGRLPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDGQARLTDFGIAVTEGDATLTeAGTLVGSPAYIAP 189
Cdd:cd08221   92 rQKGQLFEEEMVLWYLFQIVSAVSYIHKAGILHRDIKTLNIFLTKAGLIKLGDFGISKILGSEYSM-AETVVGTPYYMSP 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 190 ERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAVVEDRRRPF--QHSGPLRGILTELLDSDPARRPSLAEA 267
Cdd:cd08221  171 ELCQGVKYNFKSDIWALGCVLYELLTLKRTFDATNPLNLVVKIVQGNYTPVvsVYSSELISLVHSLLQQDPEKRPTADEV 250

                 ....*
gi 111222708 268 RGRLR 272
Cdd:cd08221  251 LDQPL 255
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine ...
95-263 3.54e-28

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 3 (MST3)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST3-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. 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.


Pssm-ID: 132940 [Multi-domain]  Cd Length: 274  Bit Score: 114.25  E-value: 3.54e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  95 WIVMEYVDGTSLAELIRAaGRLPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDGQARLTDFGIAvTEGDATL 174
Cdd:cd06609   75 WIIMEYCGGGSCLDLLKP-GKLDETYIAFILREVLLGLEYLHEEGKIHRDIKAANILLSEEGDVKLADFGVS-GQLTSTM 152
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 175 TEAGTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAIL-------AAVVEDRrrpfQHSGPLR 247
Cdd:cd06609  153 SKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLflipknnPPSLEGN----KFSKPFK 228
                        170
                 ....*....|....*.
gi 111222708 248 GILTELLDSDPARRPS 263
Cdd:cd06609  229 DFVSLCLNKDPKERPS 244
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine ...
78-266 6.87e-28

Catalytic domain of the Protein Serine/Threonine Kinase, MAP/ERK kinase kinase 4; Serine/threonine kinases (STKs), MAP/ERK kinase kinase 4 (MEKK4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MEKK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. MEKK4 is a mitogen-activated protein kinase (MAPK) kinase kinase (MAPKKK or MKKK or MAP3K), that 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. MEKK4 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.


Pssm-ID: 132957 [Multi-domain]  Cd Length: 264  Bit Score: 113.20  E-value: 6.87e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGRLPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDGQ 157
Cdd:cd06626   58 HPNLVKYYGVEVHREKVYIFMEYCSGGTLEELLEHGRILDEHVIRVYTLQLLEGLAYLHSHGIVHRDIKPANIFLDHNGV 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 158 ARLTDFGIAVTEGDATLTEAG---TLVGSPAYIAPERARGARV---GAAGDVWGLGATLFTAVEGVPPFQG-EGPLAILA 230
Cdd:cd06626  138 IKLGDFGCAVKLKNNTTTMGEevqSLAGTPAYMAPEVITGGKGkghGRAADIWSLGCVVLEMATGKRPWSElDNEFQIMF 217
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 111222708 231 AVVEDRRRPF----QHSGPLRGILTELLDSDPARRPSLAE 266
Cdd:cd06626  218 HVGAGHKPPIpdslQLSPEGKDFLDRCLESDPKKRPTASE 257
STKc_PAK_II cd06648
Catalytic domain of the Protein Serine/Threonine Kinase, Group II p21-activated kinase; Serine ...
78-266 6.92e-28

Catalytic domain of the Protein Serine/Threonine Kinase, Group II p21-activated kinase; Serine/threonine kinases (STKs), p21-activated kinase (PAK) subfamily, Group II, 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. 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.


Pssm-ID: 132979 [Multi-domain]  Cd Length: 285  Bit Score: 113.69  E-value: 6.92e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIrAAGRLPALEVARIGVSLAYALEAAHRGGVVHRDVKPGNVLVTNDGQ 157
Cdd:cd06648   75 HPNIVEMYSSYLVGDELWVVMEFLEGGALTDIV-THTRMNEEQIATVCLAVLKALSFLHAQGVIHRDIKSDSILLTSDGR 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 158 ARLTDFGIAvtegdATLTEA----GTLVGSPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAVV 233
Cdd:cd06648  154 VKLSDFGFC-----AQVSKEvprrKSLVGTPYWMAPEVISRLPYGTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIR 228
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 111222708 234 EDRRRPFQH----SGPLRGILTELLDSDPARRPSLAE 266
Cdd:cd06648  229 DNLPPKLKNlhkvSPRLRSFLDRMLVRDPAQRATAAE 265
STKc_PKC cd05570
Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase C; Serine/Threonine ...
78-261 4.66e-27

Catalytic domain of the Protein Serine/Threonine Kinase, Protein Kinase C; Serine/Threonine Kinases (STKs), Protein Kinase C (PKC) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173661 [Multi-domain]  Cd Length: 318  Bit Score: 112.09  E-value: 4.66e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGRLPaLEVARI-GVSLAYALEAAHRGGVVHRDVKPGNVLVTNDG 156
Cdd:cd05570   55 HPFLTQLHSCFQTKDRLFFVMEYVNGGDLMFHIQRSGRFD-EPRARFyAAEIVLGLQFLHERGIIYRDLKLDNVLLDSEG 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708 157 QARLTDFGIA---VTEGDATLTEAGTlvgsPAYIAPERARGARVGAAGDVWGLGATLFTAVEGVPPFQGEGPLAILAAVV 233
Cdd:cd05570  134 HIKIADFGMCkegILGGVTTSTFCGT----PDYIAPEILSYQPYGPAVDWWALGVLLYEMLAGQSPFEGDDEDELFQSIL 209
                        170       180
                 ....*....|....*....|....*....
gi 111222708 234 EDR-RRPFQHSGPLRGILTELLDSDPARR 261
Cdd:cd05570  210 EDEvRYPRWLSKEAKSILKSFLTKNPEKR 238
STKc_PDK1 cd05581
Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; ...
78-272 2.92e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; Serine/Threonine Kinases (STKs), Phosphoinositide-dependent kinase 1 (PDK1) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PDK1 subfamily is part of a 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). 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. PDK1 is essential for normal embryo development and is important in regulating cell volume.


Pssm-ID: 173672 [Multi-domain]  Cd Length: 280  Bit Score: 108.82  E-value: 2.92e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 111222708  78 HPGLVTVYDVLDTDDHTWIVMEYVDGTSLAELIRAAGRLPaLEVARIGVS-LAYALEAAHRGGVVHRDVKPGNVLVTNDG 156