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Conserved domains on  [gi|21222767|ref|NP_628546|]
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serine-threonine protein kinase [Streptomyces coelicolor A3(2)]

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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 ...
22-265 5.70e-42

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: 151.98  E-value: 5.70e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  22 YRLAARLGAGGMGRVYL-SHTRGGRPVAIKVVRSELADDatfRRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLY 100
Cdd:cd05122   2 FEILEKIGKGGFGEVYKaRHKRTGKEVAIKVIKLESKEK---KEKIINEIQILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 101 VPGPSLAGAV-ARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGISlaADSTAHTATGT 178
Cdd:cd05122  79 CSGGSLKDLLkSTNQTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTSDGEvKLIDFGLS--AQLSDTKARNT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 179 TIGTPQYMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIVHSEP----DLSELPERLRDLLGRCLA 254
Cdd:cd05122 157 MVGTPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPYSELPPMKALFKIATNGPpglrNPEKWSDEFKDFLKKCLQ 236
                       250
                ....*....|.
gi 21222767 255 TAPEERATPAE 265
Cdd:cd05122 237 KNPEKRPTAEQ 247
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
22-268 5.23e-48

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


:

Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 168.86  E-value: 5.23e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767     22 YRLAARLGAGGMGRVYLS-HTRGGRPVAIKVVRSELADDatFRRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLY 100
Cdd:smart00220   1 YEILEKLGEGSFGKVYLArDKKTGKLVAIKVIKKKKIKK--DRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767    101 VPGPSLAGAVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGisLAADSTAHTATGTT 179
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHvKLADFG--LARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767    180 IGTPQYMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIV-----HSEPDLSELPERLRDLLGRCLA 254
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIgkpkpPFPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....
gi 21222767    255 TAPEERATPAEIVE 268
Cdd:smart00220 237 KDPEKRLTAEEALQ 250
 
Name Accession Description Interval E-value
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
22-265 5.70e-42

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: 151.98  E-value: 5.70e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  22 YRLAARLGAGGMGRVYL-SHTRGGRPVAIKVVRSELADDatfRRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLY 100
Cdd:cd05122   2 FEILEKIGKGGFGEVYKaRHKRTGKEVAIKVIKLESKEK---KEKIINEIQILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 101 VPGPSLAGAV-ARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGISlaADSTAHTATGT 178
Cdd:cd05122  79 CSGGSLKDLLkSTNQTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTSDGEvKLIDFGLS--AQLSDTKARNT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 179 TIGTPQYMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIVHSEP----DLSELPERLRDLLGRCLA 254
Cdd:cd05122 157 MVGTPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPYSELPPMKALFKIATNGPpglrNPEKWSDEFKDFLKKCLQ 236
                       250
                ....*....|.
gi 21222767 255 TAPEERATPAE 265
Cdd:cd05122 237 KNPEKRPTAEQ 247
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
44-165 6.69e-09

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: 54.53  E-value: 6.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767    44 GRPVAIKV-----VRSELADDATFRRRFGREITAARRVK--GAYTAELIDADPDGTPpwLATLYVPGPSLAGAVARSGpl 116
Cdd:TIGR03724  17 GLKAVIKErvpksYRHPELDERIRRERTRNEARLLSRARkaGVNTPVVYDVDPDNKT--IVMEYIEGKPLKDVIEEGN-- 92
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 21222767   117 pvpavLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGPRVIDFGIS 165
Cdd:TIGR03724  93 -----DELLREIGRLVGKLHKAGIVHGDLTTSNIIVRDDKLYLIDFGLG 136
COG3642 COG3642
Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]
44-165 2.34e-08

Mn2+-dependent serine/threonine protein kinase [Signal transduction mechanisms]


Pssm-ID: 226168  Cd Length: 204  Bit Score: 53.06  E-value: 2.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  44 GRPVAIKV-----VRSELADDATFRRRFGREITAARRVK--GAYTAELIDADPDGTPPWLAtlYVPGPSLAGAVARSGPL 116
Cdd:COG3642  19 GLPAVVKEripkrYRHPELDEKLRRERTRREARILAKAReaGVPVPIVYDVDPDNGLIVME--YIEGELLKDALEEARPD 96
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 21222767 117 pvpavlwLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGPRVIDFGIS 165
Cdd:COG3642  97 -------LLREVGRLVGKLHKAGIVHGDLTTSNIILSGGRIYFIDFGLG 138
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
59-165 1.36e-06

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 47.98  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767   59 DATFRRRfgREITAARRVKGAYTA-----ELIDADPDGTPpwLATLYVPGPSLAGAVARSGPLpvpaVLWLMAGVAEALQ 133
Cdd:PRK14879  38 DERIRRE--RTRREARIMSRARKAgvnvpAVYFVDPENFI--IVMEYIEGEPLKDLINSNGME----ELELSREIGRLVG 109
                         90       100       110
                 ....*....|....*....|....*....|..
gi 21222767  134 AIHAAGIVHRDLKPANVLLAADGPRVIDFGIS 165
Cdd:PRK14879 110 KLHSAGIIHGDLTTSNMILSGGKIYLIDFGLA 141
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
105-271 1.82e-06

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: 47.01  E-value: 1.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767    105 SLAGAV-ARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGprvidfgiSLAADSTAhtatgTTIGTP 183
Cdd:smart00750   2 SLADILeVRGRPLNEEEIWAVCLQCLGALRELHRQAKSGNILLTWDGLLKLDG--------SVAFKTPE-----QSRPDP 68
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767    184 QYMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGD-------------GPAATVLYRIVHSEPDLSELpeRLRDLLG 250
Cdd:smart00750  69 YFMAPEVIQGQSYTEKADIYSLGITLYEALDYELPYNEerelsaileillnGMPADDPRDRSNLEGVSAAR--SFEDFMR 146
                          170       180
                   ....*....|....*....|.
gi 21222767    251 RCLATAPEERATPAEIVEWCR 271
Cdd:smart00750 147 LCASRLPQRREAANHYLAHCR 167
Kdo pfam06293
Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to ...
72-162 7.82e-04

Lipopolysaccharide kinase (Kdo/WaaP) family; These lipopolysaccharide kinases are related to protein kinases pfam00069. This family includes waaP (rfaP) gene product is required for the addition of phosphate to O-4 of the first heptose residue of the lipopolysaccharide (LPS) inner core region. It has previously been shown that WaaP is necessary for resistance to hydrophobic and polycationic antimicrobials in Escherichia coli and that it is required for virulence in invasive strains of S. enterica.


Pssm-ID: 253661  Cd Length: 206  Bit Score: 39.65  E-value: 7.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767    72 AARRVKGAYTAELIDADPDGTPP---WLATLYVPGPSLAGAVARSgplpvpavlwlmagVAEALQAIHAAGIVHRDLKPA 148
Cdd:pfam06293  82 GAVKVGGEYQADLLTERLEGAQDlvtWLAQWADPAEELRRALWRA--------------VGRLIARMHRAGVNHTDLNAH 147
                          90
                  ....*....|....*...
gi 21222767   149 NVLL--AADGPRV--IDF 162
Cdd:pfam06293 148 NILLdtGEGGFKVwlIDF 165
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
22-268 5.23e-48

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 168.86  E-value: 5.23e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767     22 YRLAARLGAGGMGRVYLS-HTRGGRPVAIKVVRSELADDatFRRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLY 100
Cdd:smart00220   1 YEILEKLGEGSFGKVYLArDKKTGKLVAIKVIKKKKIKK--DRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767    101 VPGPSLAGAVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGisLAADSTAHTATGTT 179
Cdd:smart00220  79 CEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHvKLADFG--LARQLDPGEKLTTF 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767    180 IGTPQYMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIV-----HSEPDLSELPERLRDLLGRCLA 254
Cdd:smart00220 157 VGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIgkpkpPFPPPEWDISPEAKDLIRKLLV 236
                          250
                   ....*....|....
gi 21222767    255 TAPEERATPAEIVE 268
Cdd:smart00220 237 KDPEKRLTAEEALQ 250
Pkinase pfam00069
Protein kinase domain;
22-268 5.83e-48

Protein kinase domain;


Pssm-ID: 249558 [Multi-domain]  Cd Length: 260  Bit Score: 168.96  E-value: 5.83e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767    22 YRLAARLGAGGMGRVYLSHTRG-GRPVAIKVVRSELADDaTFRRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLY 100
Cdd:pfam00069   1 YELLRKLGSGSFGTVYKAKHKGtGKIVAVKILKKRSEKS-KKDQTARREIRILRRLSHPNIVRLIDAFEDKDHLYLVMEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767   101 VPGPSLAGAVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADG-PRVIDFGISLAADSTAHTATgTT 179
Cdd:pfam00069  80 CEGGDLFDYLSRGGPLSEDEAKKIALQILRGLEYLHSNGIIHRDLKPENILLDENGvVKIADFGLAKKLTKSSSSLT-TF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767   180 IGTPQYMAPEQ-ASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIVH--------SEPDLSELPERLRDLLG 250
Cdd:pfam00069 159 VGTPEYMAPEVlLGGNGYGPKVDVWSLGVILYELLTGKPPFSGESILDQLQLIRRilgpplefDEPKSDSGSEEAKDLIK 238
                         250
                  ....*....|....*...
gi 21222767   251 RCLATAPEERATPAEIVE 268
Cdd:pfam00069 239 KCLNKDPSKRPTAEEILQ 256
SPS1 COG0515
Serine/threonine protein kinase [General function prediction only / Signal transduction ...
21-268 1.07e-37

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: 142.96  E-value: 1.07e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  21 GYRLAARLGAGGMGRVYLSHTRggRPVAIKVVRSELADDATFRRRFGREITAARRVKGA-YTAELIDADPDGTPPWLATL 99
Cdd:COG0515   1 SYRILRKLGEGSFGEVYLARDR--KLVALKVLAKKLESKSKEVERFLREIQILASLNHPpNIVKLYDFFQDEGSLYLVME 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 100 YVPGPSLA---GAVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGPRV--IDFGISLAAD----- 169
Cdd:COG0515  79 YVDGGSLEdllKKIGRKGPLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVVklIDFGLAKLLPdpgst 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 170 STAHTATGTTIGTPQYMAPEQA---SAGAITAATDVFSLGQTAAFAALGKP---LYGDGPAATVLYRIVHSEPD------ 237
Cdd:COG0515 159 SSIPALPSTSVGTPGYMAPEVLlglSLAYASSSSDIWSLGITLYELLTGLPpfeGEKNSSATSQTLKIILELPTpslasp 238
                       250       260       270
                ....*....|....*....|....*....|....*.
gi 21222767 238 -----LSELPERLRDLLGRCLATAPEERATPAEIVE 268
Cdd:COG0515 239 lspsnPELISKAASDLLKKLLAKDPKNRLSSSSDLS 274
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
44-288 7.52e-29

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: 121.11  E-value: 7.52e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767     44 GRPVAIKVVRSELADDATFRRRFGREITAARRVKGAYTAELIDADPDGTPPWLATL-YVPGPSLAGAVARSGPLPVPAVL 122
Cdd:TIGR03903    3 GHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPPGLLFAVFeYVPGRTLREVLAADGALPAGETG 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767    123 WLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGPR----VIDFGISL------AADSTAHTATGTTIGTPQYMAPEQAS 192
Cdd:TIGR03903   83 RLMLQVLDALACAHNQGIVHRDLKPQNIMVSQTGVRphakVLDFGIGTllpgvrDADVATLTRTTEVLGTPTYCAPEQLR 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767    193 AGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRivHSEPDLSELPE-----RLRDLLGRCLATAPEERATPAEIV 267
Cdd:TIGR03903  163 GEPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQ--QLSPVDVSLPPwiaghPLGQVLRKALNKDPRQRAASAPAL 240
                          250       260
                   ....*....|....*....|.
gi 21222767    268 EWCRRELGRDGGEGAGPAGWR 288
Cdd:TIGR03903  241 AERFRALELCALVGILRMGEG 261
pknD PRK13184
serine/threonine-protein kinase; Reviewed
22-206 1.52e-21

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 97.92  E-value: 1.52e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767   22 YRLAARLGAGGMGRVYLSHTRG-GRPVAIKVVRSELADDATFRRRFGRE--ITAARRVKG---AYTAElidadPDGTPPW 95
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVcSRRVALKKIREDLSENPLLKKRFLREakIAADLIHPGivpVYSIC-----SDGDPVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767   96 LATLYVPG---PSLAGAVARSGPLP--------VPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGPRVI-DFG 163
Cdd:PRK13184  79 YTMPYIEGytlKSLLKSVWQKESLSkelaektsVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVIlDWG 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  164 ISLAAD-----------------STAHTATGTTIGTPQYMAPEQASAGAITAATDVFSLG 206
Cdd:PRK13184 159 AAIFKKleeedlldidvdernicYSSMTIPGKIVGTPDYMAPERLLGVPASESTDIYALG 218
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
27-291 1.74e-12

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 67.54  E-value: 1.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767   27 RLGAGGMGRVY-LSHTRGGRPVAIKVVRSELADdaTFRRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLYVPGPS 105
Cdd:PLN00034  81 RIGSGAGGTVYkVIHRPTGRLYALKVIYGNHED--TVRRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGS 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  106 LAGAVARSGPLPVPAVLWLMAGVAealqAIHAAGIVHRDLKPANVLL-AADGPRVIDFGISLAADSTAHTATgTTIGTPQ 184
Cdd:PLN00034 159 LEGTHIADEQFLADVARQILSGIA----YLHRRHIVHRDIKPSNLLInSAKNVKIADFGVSRILAQTMDPCN-SSVGTIA 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  185 YMAPEQASA----GAITA-ATDVFSLGQTAAFAALGK---PLYGDGPAATVLYRIVHSEPdlSELP----ERLRDLLGRC 252
Cdd:PLN00034 234 YMSPERINTdlnhGAYDGyAGDIWSLGVSILEFYLGRfpfGVGRQGDWASLMCAICMSQP--PEAPatasREFRHFISCC 311
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 21222767  253 LATAPEERATPAEIVEWcRRELGRDGGEGAGPAGWREIA 291
Cdd:PLN00034 312 LQREPAKRWSAMQLLQH-PFILRAQPGQGQGGPNLHQLL 349
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
28-260 3.21e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 63.68  E-value: 3.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767   28 LGAGGMGRVYLSHTRG-GRPVAIKVVRSELADDATFRRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLYVPGPSL 106
Cdd:PTZ00263  26 LGTGSFGRVRIAKHKGtGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEFVVGGEL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  107 AGAVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGisLAADSTAHTAtgTTIGTPQY 185
Cdd:PTZ00263 106 FTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHvKVTDFG--FAKKVPDRTF--TLCGTPEY 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 21222767  186 MAPEQASAGAITAATDVFSLG-QTAAFAALGKPLYGDGPAATvLYRIVHSE---PDLSElpERLRDLLGRCLATAPEER 260
Cdd:PTZ00263 182 LAPEVIQSKGHGKAVDWWTMGvLLYEFIAGYPPFFDDTPFRI-YEKILAGRlkfPNWFD--GRARDLVKGLLQTDHTKR 257
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
22-206 1.96e-10

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 61.40  E-value: 1.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767   22 YRLAARLGAGGMGRVYLSHTRGG---RPVAIKVVrseladdaTFRRRFGREITAARRVKGAYTAELIDAdpdgtPPWLAT 98
Cdd:PHA03207  94 YNILSSLTPGSEGEVFVCTKHGDeqrKKVIVKAV--------TGGKTPGREIDILKTISHRAIINLIHA-----YRWKST 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767   99 LYVPGP----SLAGAVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGPRVI-DFGIslAADSTAH 173
Cdd:PHA03207 161 VCMVMPkykcDLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLgDFGA--ACKLDAH 238
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 21222767  174 TATGTT---IGTPQYMAPEQASAGAITAATDVFSLG 206
Cdd:PHA03207 239 PDTPQCygwSGTLETNSPELLALDPYCAKTDIWSAG 274
 
Name Accession Description Interval E-value
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; Protein Kinases (PKs), STE family, catalytic ...
22-265 5.70e-42

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: 151.98  E-value: 5.70e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  22 YRLAARLGAGGMGRVYL-SHTRGGRPVAIKVVRSELADDatfRRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLY 100
Cdd:cd05122   2 FEILEKIGKGGFGEVYKaRHKRTGKEVAIKVIKLESKEK---KEKIINEIQILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 101 VPGPSLAGAV-ARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGISlaADSTAHTATGT 178
Cdd:cd05122  79 CSGGSLKDLLkSTNQTLTESQIAYVCKELLKGLEYLHSNGIIHRDIKAANILLTSDGEvKLIDFGLS--AQLSDTKARNT 156
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 179 TIGTPQYMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIVHSEP----DLSELPERLRDLLGRCLA 254
Cdd:cd05122 157 MVGTPYWMAPEVINGKPYDYKADIWSLGITAIELAEGKPPYSELPPMKALFKIATNGPpglrNPEKWSDEFKDFLKKCLQ 236
                       250
                ....*....|.
gi 21222767 255 TAPEERATPAE 265
Cdd:cd05122 237 KNPEKRPTAEQ 247
PKc cd00180
Catalytic domain of Protein Kinases; Protein Kinases (PKs), catalytic (c) domain. PKs catalyze ...
28-268 1.72e-39

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: 143.53  E-value: 1.72e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  28 LGAGGMGRVYLSHTRG-GRPVAIKVVRSElaDDATFRRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLYVPGPSL 106
Cdd:cd00180   1 LGEGGFGTVYLARDKKtGKKVAIKIIKKE--DSSSLLEELLREIEILKKLNHPNIVKLYGVFEDENHLYLVMEYCEGGSL 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 107 AGAVAR-SGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGPRV--IDFGISLAADSTAHTATgTTIGTP 183
Cdd:cd00180  79 KDLLKEnEGKLSEDEILRILLQILEGLEYLHSNGIIHRDLKPENILLDSDNGKVklADFGLSKLLTSDKSLLK-TIVGTP 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 184 QYMAPEQA-SAGAITAATDVFSLGqtaafaalgkplygdgpaaTVLYrivhsepdlsELPErLRDLLGRCLATAPEERAT 262
Cdd:cd00180 158 AYMAPEVLlGKGYYSEKSDIWSLG-------------------VILY----------ELPE-LKDLIRKMLQKDPEKRPS 207

                ....*.
gi 21222767 263 PAEIVE 268
Cdd:cd00180 208 AKEILE 213
STKc_MAPKKK cd06606
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein Kinase ...
22-265 1.20e-36

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: 136.92  E-value: 1.20e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  22 YRLAARLGAGGMGRVYLSHTRG-GRPVAIKVVRSELADDATFRRrFGREITAARRVK--------GAYTAELIDadpdgt 92
Cdd:cd06606   2 WTRGELLGRGSFGSVYLALDKDtGELMAVKSVELSGDSEEELEA-LEREIRILSSLQhpnivryyGSERDEEKN------ 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  93 ppwlaTL-----YVPGPSLAGAVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGprVI---DFGI 164
Cdd:cd06606  75 -----TLnifleYVSGGSLSSLLKKFGKLPEPVIRKYTRQILEGLAYLHSNGIVHRDIKGANILVDSDG--VVklaDFGC 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 165 S-LAADSTAHTATGTTIGTPQYMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGD-GPAATVLYRIVHSE--PDLSE 240
Cdd:cd06606 148 AkRLGDIETGEGTGSVRGTPYWMAPEVIRGEEYGRAADIWSLGCTVIEMATGKPPWSElGNPMAALYKIGSSGepPEIPE 227
                       250       260
                ....*....|....*....|....*.
gi 21222767 241 -LPERLRDLLGRCLATAPEERATPAE 265
Cdd:cd06606 228 hLSEEAKDFLRKCLRRDPKKRPTADE 253
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Protein Serine/Threonine Kinases; ...
22-265 1.87e-30

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: 119.28  E-value: 1.87e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  22 YRLAARLGAGGMGRVYLS-HTRGGRPVAIKVVRSElADDATFRRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLY 100
Cdd:cd06627   2 YQLGDLIGRGAFGVVYKGlNLETGDFVAIKQISLE-KIKEEALKSIMQEIDLLKNLKHPNIVKYIGSIETSDSLYIILEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 101 VPGPSLAGAVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGprVI---DFGISLAADSTAHTATg 177
Cdd:cd06627  81 AENGSLRQIIKKFGPFPESLVAVYVYQVLQGLAYLHEQGVIHRDIKAANILTTKDG--VVklaDFGVATKLNDVSKDDA- 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 178 TTIGTPQYMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIVhsEPDLSELPER----LRDLLGRCL 253
Cdd:cd06627 158 SVVGTPYWMAPEVIEMSGASTASDIWSLGCTVIELLTGNPPYYDLNPMAALFRIV--QDDHPPLPEGispeLKDFLMQCF 235
                       250
                ....*....|..
gi 21222767 254 ATAPEERATPAE 265
Cdd:cd06627 236 QKDPNLRPTAKQ 247
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity MAP kinase kinases and similar proteins; Protein ...
28-265 7.86e-28

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: 112.30  E-value: 7.86e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  28 LGAGGMGRVYLS-HTRGGRPVAIKVVRseLADDATFRRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLYVPGPSL 106
Cdd:cd06623   9 LGQGSSGVVYKVrHKPTGKIYALKKIH--VDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 107 AGAVARSGPLPVPAVLWLMAGVAEALQAIHA-AGIVHRDLKPANVLLAADG-PRVIDFGISLAADSTAhTATGTTIGTPQ 184
Cdd:cd06623  87 ADLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGeVKIADFGISKVLENTL-DQCNTFVGTVT 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 185 YMAPEQASAGAITAATDVFSLGQTAAFAALGK-PLYGDGPA--ATVLYRIVHSEPdlSELPER-----LRDLLGRCLATA 256
Cdd:cd06623 166 YMSPERIQGESYSYAADIWSLGLTLLECALGKfPFLPPGQPsfFELMQAICDGPP--PSLPAEefspeFRDFISACLQKD 243

                ....*....
gi 21222767 257 PEERATPAE 265
Cdd:cd06623 244 PKKRPSAAE 252
STKc_Nek cd08215
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A-related ...
22-266 9.40e-27

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: 109.12  E-value: 9.40e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  22 YRLAARLGAGGMGRVYL-SHTRGGRPVAIKVVR-SELADDAtfRRRFGREITAARRVKGAYTAELIDADPDGTppwlaTL 99
Cdd:cd08215   2 YEIIKQIGKGSFGKVYLvRRKSDGKLYVLKEIDlSNMSEKE--REDALNEVKILKKLNHPNIIKYYESFEEKG-----KL 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 100 -----YVPGPSLAGAV----ARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGprVI---DFGISLA 167
Cdd:cd08215  75 civmeYADGGDLSQKIkkqkKEGKPFPEEQILDWFVQLCLALKYLHSRKILHRDIKPQNIFLTSNG--LVklgDFGISKV 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 168 ADSTAHTATgTTIGTPQYMAPEQASAGAITAATDVFSLG----QtaaFAALGKPLYGDGPAAtVLYRIVHSE--PDLSEL 241
Cdd:cd08215 153 LSSTVDLAK-TVVGTPYYLSPELCQNKPYNYKSDIWSLGcvlyE---LCTLKHPFEGENLLE-LALKILKGQypPIPSQY 227
                       250       260
                ....*....|....*....|....*
gi 21222767 242 PERLRDLLGRCLATAPEERATPAEI 266
Cdd:cd08215 228 SSELRNLVSSLLQKDPEERPSIAQI 252
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Protein Serine/Threonine Kinases; Serine/threonine ...
22-266 2.33e-26

Catalytic domain of Fungal Nak1-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), Nak1 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nak1 subfamily is part of a 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 Schizosaccharomyces pombe Nak1, Saccharomyces cerevisiae Kic1p (kinase that interacts with Cdc31p) and related proteins. Nak1 (also known as 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.


Pssm-ID: 132991 [Multi-domain]  Cd Length: 277  Bit Score: 108.29  E-value: 2.33e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  22 YRLAARLGAGGMGRVYLS-HTRGGRPVAIKVVRSELADDATfrRRFGREItaarrvkgAYTAELIDADP----------- 89
Cdd:cd06917   3 YQRLELIGRGAYGAVYRGkHVPTGRVVALKIINLDTPDDDV--SDIQREV--------ALLSQLRQSQPpnitkyygsyl 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  90 DGTPPWLATLYVPGPSLAgAVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGpRVI--DFGISLA 167
Cdd:cd06917  73 KGPRLWIIMEYAEGGSVR-TLMKAGPIAEKYISVIIREVLVALKYIHKVGVIHRDIKAANILVTNTG-NVKlcDFGVAAL 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 168 ADSTAHTATgTTIGTPQYMAPEQASAG-AITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIVHSEPdlSELPER-- 244
Cdd:cd06917 151 LNQNSSKRS-TFVGTPYWMAPEVITEGkYYDTKADIWSLGITIYEMATGNPPYSDVDAFRAMMLIPKSKP--PRLEDNgy 227
                       250       260
                ....*....|....*....|....*
gi 21222767 245 ---LRDLLGRCLATAPEERATPAEI 266
Cdd:cd06917 228 sklLREFVAACLDEEPKERLSAEEL 252
STKc_MEKK1_plant cd06632
Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine ...
28-268 4.05e-26

Catalytic domain of the Protein Serine/Threonine Kinase, Plant MAP/ERK kinase kinase 1; Serine/threonine kinases (STKs), plant MAP/ERK kinase kinase 1 (MEKK1)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The plant MEKK1 subfamily is part of a 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 plant mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs or MAP3Ks) including Arabidopsis thaliana MEKK1 and MAPKKK3. MEKK1 is a MAPKKK 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. 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.


Pssm-ID: 132963 [Multi-domain]  Cd Length: 258  Bit Score: 107.12  E-value: 4.05e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  28 LGAGGMGRVYLSHTRG-GRPVAIKVVrSELADDATFR---RRFGREITAARRVKGAYTAELIDADPDGTPPWLATLYVPG 103
Cdd:cd06632   8 LGSGSFGSVYEGLNLDdGDFFAVKEV-SLADDGQTGQeavKQLEQEIALLSKLQHPNIVQYLGTEREEDNLYIFLELVPG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 104 PSLAGAVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGisLAADSTAHTATGTTIGT 182
Cdd:cd06632  87 GSLAKLLKKYGSFPEPVIRLYTRQILLGLEYLHDRNTVHRDIKGANILVDTNGVvKLADFG--MAKQVVEFSFAKSFKGS 164
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 183 PQYMAPEQ-ASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIVHSePDLSELPERL----RDLLGRCLATAP 257
Cdd:cd06632 165 PYWMAPEViAQQGGYGLAADIWSLGCTVLEMATGKPPWSQLEGVAAVFKIGRS-KELPPIPDHLsdeaKDFILKCLQRDP 243
                       250
                ....*....|.
gi 21222767 258 EERATPAEIVE 268
Cdd:cd06632 244 SLRPTAAELLE 254
STKc_AGC cd05123
Catalytic domain of AGC family Protein Serine/Threonine Kinases; Serine/Threonine Kinases ...
28-267 6.10e-26

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: 106.45  E-value: 6.10e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  28 LGAGGMGRVYL-SHTRGGRPVAIKVVRSEL-----ADDATFRRRFGREitaarRVKgaytaelidadpdgtPPWLATL-- 99
Cdd:cd05123   1 LGKGSFGKVLLvRKKDTGKLYAMKVLKKKKiikrkEVEHTLTERNILS-----RIN---------------HPFIVKLhy 60
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 100 -------------YVPGPSLAGAVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGPRVI-DFGIS 165
Cdd:cd05123  61 afqteeklylvleYAPGGELFSHLSKEGRFSEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDADGHIKLtDFGLA 140
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 166 lAADSTAHTATGTTIGTPQYMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIVHSEPDLSE-LPER 244
Cdd:cd05123 141 -KELSSEGSRTNTFCGTPEYLAPEVLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAEDRKEIYEKILKDPLRFPEfLSPE 219
                       250       260
                ....*....|....*....|....*
gi 21222767 245 LRDLLGRCLATAPEER--ATPAEIV 267
Cdd:cd05123 220 ARDLISGLLQKDPTKRlgSGGAEEI 244
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Protein Serine/Threonine ...
22-262 9.57e-26

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: 106.55  E-value: 9.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  22 YRLAARLGAGGMGRVYLSHTRG-GRPVAIKVVRSELADDATFRrrFGREITAARRVKGAYTAELIDADPDGTPPWLATLY 100
Cdd:cd06609   3 FTLLECIGKGSFGEVYKAIDKRtNQVVAIKVIDLEEAEDEIED--IQQEIQFLSQCRSPYITKYYGSFLKGSKLWIIMEY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 101 VPGPSLAGaVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGISLAADSTAhTATGTT 179
Cdd:cd06609  81 CGGGSCLD-LLKPGKLDETYIAFILREVLLGLEYLHEEGKIHRDIKAANILLSEEGDvKLADFGVSGQLTSTM-SKRNTF 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 180 IGTPQYMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIVHSEPDLSELP---ERLRDLLGRCLATA 256
Cdd:cd06609 159 VGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLEGNkfsKPFKDFVSLCLNKD 238

                ....*.
gi 21222767 257 PEERAT 262
Cdd:cd06609 239 PKERPS 244
STKc_SLK_like cd06611
Catalytic domain of Ste20-like kinase-like Protein Serine/Threonine Kinases; Serine/threonine ...
15-268 5.82e-25

Catalytic domain of Ste20-like kinase-like Protein Serine/Threonine Kinases; Serine/threonine kinases (STKs), Ste20-like kinase (SLK)-like subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SLK-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 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 (HEK) cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 104.44  E-value: 5.82e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  15 DPRTVagYRLAARLGAGGMGRVYLSHTRG-GRPVAIKVVR----SELADdatfrrrFGREITAARRVKGAYTAELIDA-- 87
Cdd:cd06611   2 NPNDI--WEIIGELGDGAFGKVYKAQHKEtGLFAAAKIIQieseEELED-------FMVEIDILSECKHPNIVGLYEAyf 72
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  88 -DPDgtpPWLATLYVPGPSLAGAVARSG-PLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGI 164
Cdd:cd06611  73 yENK---LWILIEFCDGGALDSIMLELErGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDvKLADFGV 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 165 SLAADSTAHTATgTTIGTPQYMAP-----EQASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIVHSEPDLS 239
Cdd:cd06611 150 SAKNKSTLQKRD-TFIGTPYWMAPevvacETFKDNPYDYKADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEPPTL 228
                       250       260       270
                ....*....|....*....|....*....|...
gi 21222767 240 ELPER----LRDLLGRCLATAPEERATPAEIVE 268
Cdd:cd06611 229 DQPSKwsssFNDFLKSCLVKDPDDRPTAAELLK 261
STKc_PAK cd06614
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase; Serine ...
14-268 1.01e-23

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: 100.75  E-value: 1.01e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  14 DDPRTVagYRLAARLGAGGMGRVYLSHTRG-GRPVAIKVVRseLADDAtfRRRFGREITAARRVKGAYTAELIDADPDGT 92
Cdd:cd06614  15 GDPREL--YKNLEKIGEGASGEVYKATDRAtGKEVAIKKMR--LRKQN--KELIINEILIMKDCKHPNIVDYYDSYLVGD 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  93 PPWLATLYVPGPSLAGAVARSG-PLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGIslAADS 170
Cdd:cd06614  89 ELWVVMEYMDGGSLTDIITQNFvRMNEPQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSvKLADFGF--AAQL 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 171 TAHTATGTTI-GTPQYMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIVHSE-PDLSElPER---- 244
Cdd:cd06614 167 TKEKSKRNSVvGTPYWMAPEVIKRKDYGPKVDIWSLGIMCIEMAEGEPPYLREPPLRALFLITTKGiPPLKN-PEKwspe 245
                       250       260
                ....*....|....*....|....
gi 21222767 245 LRDLLGRCLATAPEERATPAEIVE 268
Cdd:cd06614 246 FKDFLNKCLVKDPEKRPSAEELLQ 269
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; Serine/Threonine ...
22-265 2.40e-23

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; Serine/Threonine Kinases (STKs), Cell Cycle-Related Kinase (CCRK) p42 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173736 [Multi-domain]  Cd Length: 286  Bit Score: 99.67  E-value: 2.40e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  22 YRLAARLGAGGMGRVYLSHTRG-GRPVAIKVVrseladdaTFRRRFG-------REITAARRVKGAYTAELIDADPDGTP 93
Cdd:cd07832   2 YKILGRIGEGAHGIVFKAKDREtGETVALKKV--------ALRRLEGgipnqalREIKALQACQHPYVVKLLDVFPHGSG 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  94 PWLATLYVPgPSLAGAVA-RSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGISLAADST 171
Cdd:cd07832  74 FVLVMEYMP-SDLSEVLRdEERPLPEAQVKSYMRMLLKGVAYMHANGIMHRDLKPANLLISADGVlKIADFGLARLFSEE 152
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 172 AHTATGTTIGTPQYMAPEQA-SAGAITAATDVFSLGqtAAFAAL--GKPLY-GDGPAATVLYRI-------------VHS 234
Cdd:cd07832 153 EPRLYSHQVATRWYRAPELLyGARKYDPGVDLWAVG--CIFAELlnGSPLFpGENDIEQLAIVFrtlgtpneetwpgLTS 230
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 21222767 235 EPDLSEL------PERLR-----------DLLGRCLATAPEERATPAE 265
Cdd:cd07832 231 LPDYNKItfpeskPIPLEeifpdaspealDLLKGLLVYDPSKRLSAAE 278
STKc_MST1_2 cd06612
Catalytic domain of the Protein Serine/Threonine Kinases, Mammalian Ste20-like protein kinase ...
22-268 7.15e-23

Catalytic domain of the Protein Serine/Threonine Kinases, Mammalian Ste20-like protein kinase 1 and 2; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 1 (MST1) and MST2 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST1/2 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. 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 (a MAPK kinase) and MEKK1 (a MAPK kinase kinase) by acting as a MAPK kinase kinase kinase (MAPKKKK). 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.


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 97.72  E-value: 7.15e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  22 YRLAARLGAGGMGRVYLS-HTRGGRPVAIKVVRSELADDAtfrrrFGREITAARRVKGAYTAELIDADPDGTPPWLATLY 100
Cdd:cd06612   5 FDILEKLGEGSYGSVYKAiHKETGQVVAIKVVPVEEDLQE-----IIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEY 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 101 VPGPSLAGAV-ARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADG-PRVIDFGISLAADSTAHTAtGT 178
Cdd:cd06612  80 CGAGSVSDIMkITNKTLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGqAKLADFGVSGQLTDTMAKR-NT 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 179 TIGTPQYMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIVHSEPDLSELPER----LRDLLGRCLA 254
Cdd:cd06612 159 VIGTPFWMAPEVIQEIGYNNKADIWSLGITAIEMAEGKPPYSDIHPMRAIFMIPNKPPPTLSDPEKwspeFNDFVKKCLV 238
                       250
                ....*....|....
gi 21222767 255 TAPEERATPAEIVE 268
Cdd:cd06612 239 KDPEERPSAIQLLQ 252
STKc_STK25-YSK1 cd06642
Catalytic domain of the Protein Serine/Threonine Kinase, STK25 or Yeast Sps1/Ste20-related ...
27-268 1.94e-22

Catalytic domain of the Protein Serine/Threonine Kinase, STK25 or Yeast Sps1/Ste20-related kinase 1; Serine/threonine kinases (STKs), STK25 subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The STK25 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). STK25 is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may play a role 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.


Pssm-ID: 132973 [Multi-domain]  Cd Length: 277  Bit Score: 97.04  E-value: 1.94e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  27 RLGAGGMGRVYLS-HTRGGRPVAIKVVRSELADDATfrRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLYVPGPS 105
Cdd:cd06642  11 RIGKGSFGEVYKGiDNRTKEVVAIKIIDLEEAEDEI--EDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 106 lAGAVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGISLAADSTaHTATGTTIGTPQ 184
Cdd:cd06642  89 -ALDLLKPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDvKLADFGVAGQLTDT-QIKRNTFVGTPF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 185 YMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRI-VHSEPDLS-ELPERLRDLLGRCLATAPEERAT 262
Cdd:cd06642 167 WMAPEVIKQSAYDFKADIWSLGITAIELAKGEPPNSDLHPMRVLFLIpKNSPPTLEgQYSKPFKEFVEACLNKDPRFRPT 246

                ....*.
gi 21222767 263 PAEIVE 268
Cdd:cd06642 247 AKELLK 252
PKc_MAPKK_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity MAP kinase kinases; Protein kinases (PKs) ...
11-267 3.96e-22

Catalytic domain of fungal Byr1-like dual-specificity MAP kinase kinases; Protein kinases (PKs), MAP kinase kinase (MAPKK) subfamily, fungal Byr1-like 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 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 MAPKKK 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.


Pssm-ID: 132951 [Multi-domain]  Cd Length: 284  Bit Score: 96.02  E-value: 3.96e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  11 LQGDDPRTVAgyrlaaRLGAGGMGRVYL-SHTRGGRPVAIKVVRSElaDDATFRRRFGREITAARRVKGAYTAELIDA-- 87
Cdd:cd06620   2 LRNEDLETIS------DLGAGNGGSVSKvKHIPTGTVMAKKVVHIG--AKSSVRKQILRELQIMHECRSPYIVSFYGAfl 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  88 -DPDGTppwLATLYVPGPSLAGAVARSGPLPVPAVLWLMAGVAEALQAIH-AAGIVHRDLKPANVLLAADGP-RVIDFGI 164
Cdd:cd06620  74 nENNIC---MCMEFMDCGSLDRIYKKGGPIPVEILGKIAVAVVEGLTYLYnVHRIMHRDIKPSNILVNSRGQiKLCDFGV 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 165 S-LAADSTAHTATGTTIgtpqYMAPEQASAGAITAATDVFSLGQTAAFAALGK------PLYGDGPAATV-----LYRIV 232
Cdd:cd06620 151 SgELINSIADTFVGTST----YMSPERIQGGKYTVKSDVWSLGISIIELALGKfpfafsNIDDDGQDDPMgildlLQQIV 226
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 21222767 233 HSEPDL---SELPERLRDLLGRCLATAPEERATPAEIV 267
Cdd:cd06620 227 QEPPPRlpsSDFPEDLRDFVDACLLKDPTERPTPQQLC 264
STKc_MST4 cd06640
Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; ...
27-268 7.40e-22

Catalytic domain of the Protein Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; Serine/threonine kinases (STKs), mammalian Ste20-like protein kinase 4 (MST4) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MST4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 95.12  E-value: 7.40e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  27 RLGAGGMGRVYLS-HTRGGRPVAIKVVRSELADDATfrRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLYVPGPS 105
Cdd:cd06640  11 RIGKGSFGEVFKGiDNRTQQVVAIKIIDLEEAEDEI--EDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGS 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 106 lAGAVARSGPLPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGISLAADSTaHTATGTTIGTPQ 184
Cdd:cd06640  89 -ALDLLRAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDvKLADFGVAGQLTDT-QIKRNTFVGTPF 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 185 YMAPEQASAGAITAATDVFSLGQTAAFAALGKPLYGDGPAATVLYRIVHSEPD--LSELPERLRDLLGRCLATAPEERAT 262
Cdd:cd06640 167 WMAPEVIQQSAYDSKADIWSLGITAIELAKGEPPNSDMHPMRVLFLIPKNNPPtlTGEFSKPFKEFIDACLNKDPSFRPT 246

                ....*.
gi 21222767 263 PAEIVE 268
Cdd:cd06640 247 AKELLK 252
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
28-268 9.90e-22

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: 94.69  E-value: 9.90e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  28 LGAGGMGRVYL-SHTRGGRPVAIKVVRSELadDATFRRRFGREITAARRVKGAYTAELIDADPDGTPPWLATLYVPGPSL 106
Cdd:cd06605   9 LGAGNSGVVSKvLHRPTGKIMAVKTIRLEI--NEAIQKQILRELDILHKCNSPYIVGFYGAFYNNGDISICMEYMDGGSL 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 107 AGAVAR-SGPLPVPAVLWLMAGVAEALQAIHAA-GIVHRDLKPANVLLAADGP-RVIDFGIS-LAADSTAhtatGTTIGT 182
Cdd:cd06605  87 DKILKEvQGRIPERILGKIAVAVLKGLTYLHEKhKIIHRDVKPSNILVNSRGQiKLCDFGVSgQLVNSLA----KTFVGT 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767 183 PQYMAPEQASAGAITAATDVFSLGQTAAFAALGK---PLYGDGPAA--TVLYRIVHSEPDL---SELPERLRDLLGRCLA 254
Cdd:cd06605 163 SSYMAPERIQGNDYSVKSDIWSLGLSLIELATGRfpyPPENDPPDGifELLQYIVNEPPPRlpsGKFSPDFQDFVNLCLI 242
                       250
                ....*....|....
gi 21222767 255 TAPEERATPAEIVE 268
Cdd:cd06605 243 KDPRERPSYKELLE 256
STKc_OSR1_SPAK cd06610
Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and ...
22-268 1.02e-21

Catalytic domain of the Protein Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; Serine/threonine kinases (STKs), oxidative stress response kinase (OSR1) and Ste20-related proline alanine-rich kinase (SPAK) subfamily, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The OSR1 and SPAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. 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.


Pssm-ID: 173726 [Multi-domain]  Cd Length: 267  Bit Score: 94.35  E-value: 1.02e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  22 YRLAARLGAGGMGRVYLSHTR-GGRPVAIKVVrsELADDATFRRRFGREITAAR-----RVKGAYTAELIdadpdGTPPW 95
Cdd:cd06610   3 YELIEVIGVGATAVVYAAICLpNNEKVAIKRI--DLEKCQTSVDELRKEVQAMSqcnhpNVVKYYTSFVV-----GDELW 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21222767  96 LATLYVPGPSLAGAVARSGP---LPVPAVLWLMAGVAEALQAIHAAGIVHRDLKPANVLLAADGP-RVIDFGIS--LAAD 169
Cdd:cd06610  76 LVMPYLSGGSLLDIMKSSYPrggLDEAIIATVLKEVLKGLEYLHSNGQIHRDIKAGNILLGEDGSvKIADFGVSasLADG 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|