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Conserved domains on  [gi|118468993|ref|YP_889750|]
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serine/threonine protein kinase [Mycobacterium smegmatis str. MC2 155]

Protein Classification

STKc_PknB_like and Lpp-LpqN domain-containing protein (domain architecture ID 10883830)

STKc_PknB_like and Lpp-LpqN domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-276 7.60e-96

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


:

Pssm-ID: 270916  Cd Length: 260  Bit Score: 297.96  E-value: 7.60e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  11 GFTIVRLVGTGGMGEVYLAKHPRLPREDALKVLPISVSADDEFRQRFIREADMAATLWHPHIVGVHDRGEFEGRLWISMD 90
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  91 YVDGHDAARLLHDKYPkgMPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVTEkhgtKRRIMLTDFGIARRTDDvN 170
Cdd:cd14014   81 YVEGGSLADLLRERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTE----DGRVKLTDFGIARALGD-S 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993 171 GLTSTNITVGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSHSNPAVVISHHLNSPPPKLGDTKPALAK-LD 249
Cdd:cd14014  154 GLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPaLD 233
                        250       260
                 ....*....|....*....|....*..
gi 118468993 250 SVMAKALAKDAKDRFDTCHDFAVALAE 276
Cdd:cd14014  234 AIILRALAKDPEERPQSAAELLAALRA 260
Lpp-LpqN pfam10738
Probable lipoprotein LpqN; This family is conserved in Mycobacteriaceae and is likely to be a ...
448-616 2.49e-70

Probable lipoprotein LpqN; This family is conserved in Mycobacteriaceae and is likely to be a lipoprotein.


:

Pssm-ID: 313855  Cd Length: 171  Bit Score: 227.89  E-value: 2.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  448 AYTIADYIRDNKISETPVHRGDPNTPELTMPTPPGWADAGTRTPAWAYSAIV-NDPASPTDPPSVISLISKLDGNVDPEK 526
Cdd:pfam10738   2 SGTIADYLESNGVTETPVAPGDPGAPTIDLPTPPGWEPAGDPNPPDAYGVIAdTDPGSGGYPPNAVLLVSKLTGDFDPAK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  527 LLEFAPNELQNLTEWEPIGGvTRSNLSGFPSVQLGGSYLKDGKRRAITQKTVVVDIPSGIYVLQINADSLYRDFGALVDV 606
Cdd:pfam10738  82 AIEHAPVDAQNLPGFRPTDG-STADLGGFPSSQIEGTYDLDGMTLATAQRTVIITGGDGRYLVQLNVTGLEDQAVALADA 160
                         170
                  ....*....|
gi 118468993  607 NKAIDKEATI 616
Cdd:pfam10738 161 TEAIDNGFTV 170
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-276 7.60e-96

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


Pssm-ID: 270916  Cd Length: 260  Bit Score: 297.96  E-value: 7.60e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  11 GFTIVRLVGTGGMGEVYLAKHPRLPREDALKVLPISVSADDEFRQRFIREADMAATLWHPHIVGVHDRGEFEGRLWISMD 90
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  91 YVDGHDAARLLHDKYPkgMPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVTEkhgtKRRIMLTDFGIARRTDDvN 170
Cdd:cd14014   81 YVEGGSLADLLRERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTE----DGRVKLTDFGIARALGD-S 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993 171 GLTSTNITVGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSHSNPAVVISHHLNSPPPKLGDTKPALAK-LD 249
Cdd:cd14014  154 GLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPaLD 233
                        250       260
                 ....*....|....*....|....*..
gi 118468993 250 SVMAKALAKDAKDRFDTCHDFAVALAE 276
Cdd:cd14014  234 AIILRALAKDPEERPQSAAELLAALRA 260
Lpp-LpqN pfam10738
Probable lipoprotein LpqN; This family is conserved in Mycobacteriaceae and is likely to be a ...
448-616 2.49e-70

Probable lipoprotein LpqN; This family is conserved in Mycobacteriaceae and is likely to be a lipoprotein.


Pssm-ID: 313855  Cd Length: 171  Bit Score: 227.89  E-value: 2.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  448 AYTIADYIRDNKISETPVHRGDPNTPELTMPTPPGWADAGTRTPAWAYSAIV-NDPASPTDPPSVISLISKLDGNVDPEK 526
Cdd:pfam10738   2 SGTIADYLESNGVTETPVAPGDPGAPTIDLPTPPGWEPAGDPNPPDAYGVIAdTDPGSGGYPPNAVLLVSKLTGDFDPAK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  527 LLEFAPNELQNLTEWEPIGGvTRSNLSGFPSVQLGGSYLKDGKRRAITQKTVVVDIPSGIYVLQINADSLYRDFGALVDV 606
Cdd:pfam10738  82 AIEHAPVDAQNLPGFRPTDG-STADLGGFPSSQIEGTYDLDGMTLATAQRTVIITGGDGRYLVQLNVTGLEDQAVALADA 160
                         170
                  ....*....|
gi 118468993  607 NKAIDKEATI 616
Cdd:pfam10738 161 TEAIDNGFTV 170
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-264 1.18e-56

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 194.29  E-value: 1.18e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993    12 FTIVRLVGTGGMGEVYLAKHPRLPREDALKVlpISVSADDEFRQRFIREADMAATLWHPHIVGVHDRGEFEGRLWISMDY 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKV--IKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993    92 VDGHDAARLLHDKypKGMPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVTEKHgtkrRIMLTDFGIARRTDDvNG 171
Cdd:smart00220  79 CEGGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG----HVKLADFGLARQLDP-GE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993   172 LTSTniTVGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSHSNPAVVISHHLNSPPPKLGDTKPAL-AKLDS 250
Cdd:smart00220 152 KLTT--FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDIsPEAKD 229
                          250
                   ....*....|....
gi 118468993   251 VMAKALAKDAKDRF 264
Cdd:smart00220 230 LIRKLLVKDPEKRL 243
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
11-270 1.52e-47

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 173.00  E-value: 1.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  11 GFTIVRLVGTGGMGEVYLAKHPRLPredALKVLPISVSADDEFRQRFIREADMAATL-WHPHIVGVHDRGEFEGRLWISM 89
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARDRKLV---ALKVLAKKLESKSKEVERFLREIQILASLnHPPNIVKLYDFFQDEGSLYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  90 DYVDGHDAARLLHDKYPKG-MPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVTEKhgtKRRIMLTDFGIARRTDD 168
Cdd:COG0515   78 EYVDGGSLEDLLKKIGRKGpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRD---GRVVKLIDFGLAKLLPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993 169 ----VNGLTSTNITVGSMSYTSPEQLMGQPL---DGRADQYSLAATAYRLLTGAPPF----SHSNPAVVISHHLNSPPPK 237
Cdd:COG0515  155 pgstSSIPALPSTSVGTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFegekNSSATSQTLKIILELPTPS 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 118468993 238 L------GDTKPALAKLDSVMAKALAKDAKDRF----DTCHDF 270
Cdd:COG0515  235 LasplspSNPELISKAASDLLKKLLAKDPKNRLssssDLSHDL 277
Pkinase pfam00069
Protein kinase domain;
12-263 8.39e-40

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 146.97  E-value: 8.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993   12 FTIVRLVGTGGMGEVYLAKHPRLPREDALKVLPISvSADDEFRQRFIREADMAATLWHPHIVGVHDRGEFEGRLWISMDY 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKE-KIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993   92 VDGHDAARLLHDKypKGMPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVtEKHGTkrrIMLTDFGIARRtddVNG 171
Cdd:pfam00069  80 VEGGSLFDLLSEK--GAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILI-DEDGN---LKITDFGLARQ---LNS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  172 LTSTNITVGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSHSNPAVVISHHL----NSPPPklgDTKPALAK 247
Cdd:pfam00069 151 GSSLTSFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIdqdfDSPRP---SSISEEAK 227
                         250
                  ....*....|....*.
gi 118468993  248 ldSVMAKALAKDAKDR 263
Cdd:pfam00069 228 --DLLKKLLKKDPSKR 241
pknD PRK13184
serine/threonine-protein kinase; Reviewed
12-281 1.46e-29

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 124.50  E-value: 1.46e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  12 FTIVRLVGTGGMGEVYLAKHPRLPREDALKVLPISVSADDEFRQRFIREADMAATLWHPHIVGVH---DRGEFegrLWIS 88
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYsicSDGDP---VYYT 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  89 MDYVDGHDAARLLHDKYPK-GMPADdvVEIVTAVGDAL----------DYAHQRQLLHRDVKPANILVtekhGTKRRIML 157
Cdd:PRK13184  81 MPYIEGYTLKSLLKSVWQKeSLSKE--LAEKTSVGAFLsifhkicatiEYVHSKGVLHRDLKPDNILL----GLFGEVVI 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993 158 TDFGIARRTD-----------DVNGLTSTNIT-----VGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSHS 221
Cdd:PRK13184 155 LDWGAAIFKKleeedlldidvDERNICYSSMTipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRK 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993 222 NPAVVISHHLNSPPPKLGDTKPALAKLDSVMAKALAKDAKDRFDTCHDFAVALAEANKGD 281
Cdd:PRK13184 235 KGRKISYRDVILSPIEVAPYREIPPFLSQIAMKALAVDPAERYSSVQELKQDLEPHLQGS 294
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
39-263 6.57e-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: 274846  Cd Length: 1266  Bit Score: 123.03  E-value: 6.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993    39 ALKVLPISVSADDEFRQRFIREADMAATLWHPHIVGVHDRGEFE-GRLWISMDYVDGHDAARLLHDKYPkgMPADDVVEI 117
Cdd:TIGR03903    7 AIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEAPpGLLFAVFEYVPGRTLREVLAADGA--LPAGETGRL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993   118 VTAVGDALDYAHQRQLLHRDVKPANILVTEKhGTKRRIMLTDFGIAR-----RTDDVNGLTSTNITVGSMSYTSPEQLMG 192
Cdd:TIGR03903   85 MLQVLDALACAHNQGIVHRDLKPQNIMVSQT-GVRPHAKVLDFGIGTllpgvRDADVATLTRTTEVLGTPTYCAPEQLRG 163
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118468993   193 QPLDGRADQYSLAATAYRLLTGAPPFSHSNPAVVISHHLNSPPPKLgdtKPALA--KLDSVMAKALAKDAKDR 263
Cdd:TIGR03903  164 EPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSPVDVSL---PPWIAghPLGQVLRKALNKDPRQR 233
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-276 7.60e-96

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


Pssm-ID: 270916  Cd Length: 260  Bit Score: 297.96  E-value: 7.60e-96
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  11 GFTIVRLVGTGGMGEVYLAKHPRLPREDALKVLPISVSADDEFRQRFIREADMAATLWHPHIVGVHDRGEFEGRLWISMD 90
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  91 YVDGHDAARLLHDKYPkgMPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVTEkhgtKRRIMLTDFGIARRTDDvN 170
Cdd:cd14014   81 YVEGGSLADLLRERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTE----DGRVKLTDFGIARALGD-S 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993 171 GLTSTNITVGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSHSNPAVVISHHLNSPPPKLGDTKPALAK-LD 249
Cdd:cd14014  154 GLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPaLD 233
                        250       260
                 ....*....|....*....|....*..
gi 118468993 250 SVMAKALAKDAKDRFDTCHDFAVALAE 276
Cdd:cd14014  234 AIILRALAKDPEERPQSAAELLAALRA 260
Lpp-LpqN pfam10738
Probable lipoprotein LpqN; This family is conserved in Mycobacteriaceae and is likely to be a ...
448-616 2.49e-70

Probable lipoprotein LpqN; This family is conserved in Mycobacteriaceae and is likely to be a lipoprotein.


Pssm-ID: 313855  Cd Length: 171  Bit Score: 227.89  E-value: 2.49e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  448 AYTIADYIRDNKISETPVHRGDPNTPELTMPTPPGWADAGTRTPAWAYSAIV-NDPASPTDPPSVISLISKLDGNVDPEK 526
Cdd:pfam10738   2 SGTIADYLESNGVTETPVAPGDPGAPTIDLPTPPGWEPAGDPNPPDAYGVIAdTDPGSGGYPPNAVLLVSKLTGDFDPAK 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  527 LLEFAPNELQNLTEWEPIGGvTRSNLSGFPSVQLGGSYLKDGKRRAITQKTVVVDIPSGIYVLQINADSLYRDFGALVDV 606
Cdd:pfam10738  82 AIEHAPVDAQNLPGFRPTDG-STADLGGFPSSQIEGTYDLDGMTLATAQRTVIITGGDGRYLVQLNVTGLEDQAVALADA 160
                         170
                  ....*....|
gi 118468993  607 NKAIDKEATI 616
Cdd:pfam10738 161 TEAIDNGFTV 170
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-264 1.18e-56

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 194.29  E-value: 1.18e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993    12 FTIVRLVGTGGMGEVYLAKHPRLPREDALKVlpISVSADDEFRQRFIREADMAATLWHPHIVGVHDRGEFEGRLWISMDY 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKV--IKKKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993    92 VDGHDAARLLHDKypKGMPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVTEKHgtkrRIMLTDFGIARRTDDvNG 171
Cdd:smart00220  79 CEGGDLFDLLKKR--GRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDG----HVKLADFGLARQLDP-GE 151
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993   172 LTSTniTVGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSHSNPAVVISHHLNSPPPKLGDTKPAL-AKLDS 250
Cdd:smart00220 152 KLTT--FVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDIsPEAKD 229
                          250
                   ....*....|....
gi 118468993   251 VMAKALAKDAKDRF 264
Cdd:smart00220 230 LIRKLLVKDPEKRL 243
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
11-270 1.52e-47

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 173.00  E-value: 1.52e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  11 GFTIVRLVGTGGMGEVYLAKHPRLPredALKVLPISVSADDEFRQRFIREADMAATL-WHPHIVGVHDRGEFEGRLWISM 89
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARDRKLV---ALKVLAKKLESKSKEVERFLREIQILASLnHPPNIVKLYDFFQDEGSLYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  90 DYVDGHDAARLLHDKYPKG-MPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVTEKhgtKRRIMLTDFGIARRTDD 168
Cdd:COG0515   78 EYVDGGSLEDLLKKIGRKGpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRD---GRVVKLIDFGLAKLLPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993 169 ----VNGLTSTNITVGSMSYTSPEQLMGQPL---DGRADQYSLAATAYRLLTGAPPF----SHSNPAVVISHHLNSPPPK 237
Cdd:COG0515  155 pgstSSIPALPSTSVGTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFegekNSSATSQTLKIILELPTPS 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 118468993 238 L------GDTKPALAKLDSVMAKALAKDAKDRF----DTCHDF 270
Cdd:COG0515  235 LasplspSNPELISKAASDLLKKLLAKDPKNRLssssDLSHDL 277
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
12-263 1.35e-43

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


Pssm-ID: 270692  Cd Length: 254  Bit Score: 157.75  E-value: 1.35e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  12 FTIVRLVGTGGMGEVYLAKHPRLPREDALKVLPISVSADdefRQRFIREADMAATLWHPHIVGVHDRGEFEGRLWISMDY 91
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKEK---KESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  92 VDGHDAARLLhDKYPKGMPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVTEKHGTKrrimLTDFGIARRtddVNG 171
Cdd:cd05122   79 CSGGSLKDLL-KNTNKTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVK----LIDFGLSAQ---LSD 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993 172 LTSTNITVGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSHSNPAVVISHHLNSPPPKLGDTKPALAKLDSV 251
Cdd:cd05122  151 GKTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPGLRNPKKWSKEFKDF 230
                        250
                 ....*....|..
gi 118468993 252 MAKALAKDAKDR 263
Cdd:cd05122  231 LKKCLQKDPEKR 242
Pkinase pfam00069
Protein kinase domain;
12-263 8.39e-40

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 146.97  E-value: 8.39e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993   12 FTIVRLVGTGGMGEVYLAKHPRLPREDALKVLPISvSADDEFRQRFIREADMAATLWHPHIVGVHDRGEFEGRLWISMDY 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKE-KIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993   92 VDGHDAARLLHDKypKGMPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVtEKHGTkrrIMLTDFGIARRtddVNG 171
Cdd:pfam00069  80 VEGGSLFDLLSEK--GAFSEREAKFIMKQILEGLEYLHSNGIIHRDLKPENILI-DEDGN---LKITDFGLARQ---LNS 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  172 LTSTNITVGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSHSNPAVVISHHL----NSPPPklgDTKPALAK 247
Cdd:pfam00069 151 GSSLTSFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIdqdfDSPRP---SSISEEAK 227
                         250
                  ....*....|....*.
gi 118468993  248 ldSVMAKALAKDAKDR 263
Cdd:pfam00069 228 --DLLKKLLKKDPSKR 241
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
11-263 1.81e-37

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek family is composed of 11 different mammalian members (Nek1-11) with similarity to the catalytic domain of Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants that were prevented from entering mitosis. Neks contain a conserved N-terminal catalytic domain and a more divergent C-terminal regulatory region of various sizes and structures. They are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270855  Cd Length: 258  Bit Score: 140.68  E-value: 1.81e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  11 GFTIVRLVGTGGMGEVYLAKHprlpRED----ALKVLPISVSADDEfRQRFIREADMAATLWHPHIVGVHDRGEFEGRLW 86
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRR----KSDgklyVLKEIDLSNMSEKE-REEALNEVKLLSKLKHPNIVKYYESFEENGKLC 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  87 ISMDYVDGHDAARLLHDKYPKG--MPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVTEKHgtkrRIMLTDFGIAR 164
Cdd:cd08215   76 IVMEYADGGDLAQKIKKQKKKGqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDG----VVKLGDFGISK 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993 165 RTDDVNGLTSTniTVGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSHSNPAVVISHHLNSPPPKLgdtkPA 244
Cdd:cd08215  152 VLESTTDLAKT--VVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPI----PS 225
                        250       260
                 ....*....|....*....|.
gi 118468993 245 L--AKLDSVMAKALAKDAKDR 263
Cdd:cd08215  226 QysSELRDLVNSMLQKDPEKR 246
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
19-211 3.68e-36

Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. PKs make up a large family of serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins. Majority of protein phosphorylation occurs on serine residues while only 1% occurs on tyrosine residues. Protein phosphorylation is a mechanism by which a wide variety of cellular proteins, such as enzymes and membrane channels, are reversibly regulated in response to certain stimuli. PKs often function as components of signal transduction pathways in which one kinase activates a second kinase, which in turn, may act on other kinases; this sequential action transmits a signal from the cell surface to target proteins, which results in cellular responses. The PK family is one of the largest known protein families with more than 100 homologous yeast enzymes and more than 500 human proteins. A fraction of PK family members are pseudokinases that lack crucial residues for catalytic activity. The mutiplicity of kinases allows for specific regulation according to substrate, tissue distribution, and cellular localization. PKs regulate many cellular processes including proliferation, division, differentiation, motility, survival, metabolism, cell-cycle progression, cytoskeletal rearrangement, immunity, and neuronal functions. Many kinases are implicated in the development of various human diseases including different types of cancer. The PK family is part of a larger superfamily that includes the catalytic domains of RIO kinases, aminoglycoside phosphotransferase, choline kinase, phosphoinositide 3-kinase (PI3K), and actin-fragmin kinase.


Pssm-ID: 270622  Cd Length: 215  Bit Score: 135.48  E-value: 3.68e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  19 GTGGMGEVYLAKHPRLPREDALKVLPISVSadDEFRQRFIREADMAATLWHPHIVGVHDRGEFEGRLWISMDYVDGHDAA 98
Cdd:cd00180    2 GKGSFGKVYKARDKETGKKVAVKVIPKEKL--KKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  99 RLLhDKYPKGMPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVTEkhgtKRRIMLTDFGIARRTDDVNGLTSTNIT 178
Cdd:cd00180   80 DLL-KENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDS----DGTVKLADFGLAKDLDSDDSLLKTTGG 154
                        170       180       190
                 ....*....|....*....|....*....|...
gi 118468993 179 VGSMSYTSPEQLMGQPLDGRADQYSLAATAYRL 211
Cdd:cd00180  155 TTPPYYAPPELLGGRYYGPKVDIWSLGVILYEL 187
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
12-224 1.50e-33

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


Pssm-ID: 270687  Cd Length: 258  Bit Score: 129.52  E-value: 1.50e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  12 FTIVRLVGTGGMGEVYLAKHPRLPREDALKVLPISvSADDEFRQRFIREADMAATLWHPHIVGVHDRGEFEGRLWISMDY 91
Cdd:cd05117    2 YELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKK-KLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  92 VDGHDaarlLHDKYPKG--MPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVTEKHGTKrRIMLTDFGIARRTDDV 169
Cdd:cd05117   81 CTGGE----LFDRIVKKgsFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKDPDS-PIKIIDFGLAKIFEEG 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 118468993 170 NGLTStniTVGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSHSNPA 224
Cdd:cd05117  156 EKLKT---VCGTPYYVAPEVLKGKGYGKKCDIWSLGVILYILLCGYPPFYGETEQ 207
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
12-263 1.23e-31

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


Pssm-ID: 270783  Cd Length: 258  Bit Score: 124.17  E-value: 1.23e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  12 FTIVRLVGTGGMGEVYLAKHPRLPREDALKVLPISVSADDEFRQrFIREADMAATLWHPHIVGVHDRGEFEGRLWISMDY 91
Cdd:cd06606    2 WKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEA-LEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  92 VDGHDAARLLhDKYPKgMPaDDVVEIVTA-VGDALDYAHQRQLLHRDVKPANILVTEKhgtkRRIMLTDFGIARRTDDVN 170
Cdd:cd06606   81 VPGGSLASLL-KKFGK-LP-EPVVRKYTRqILEGLEYLHSNGIVHRDIKGANILVDSD----GVVKLADFGCAKRLAEIA 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993 171 GLTSTNITVGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSH-SNPAVVISH--HLNSPPPkLGDTKPALAK 247
Cdd:cd06606  154 TGEGTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSElGNPVAALFKigSSGEPPP-IPEHLSEEAK 232
                        250
                 ....*....|....*.
gi 118468993 248 ldSVMAKALAKDAKDR 263
Cdd:cd06606  233 --DFLRKCLQRDPKKR 246
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
12-234 2.70e-31

Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK36, also called Fused (or Fu) kinase, is involved in the Hedgehog signaling pathway. It is activated by the Smoothened (SMO) signal transducer, resulting in the stabilization of GLI transcription factors and the phosphorylation of SUFU to facilitate the nuclear accumulation of GLI. In Drosophila, Fused kinase is maternally required for proper segmentation during embryonic development and for the development of legs and wings during the larval stage. In mice, STK36 is not necessary for embryonic development, although mice deficient in STK36 display growth retardation postnatally. The STK36 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270904  Cd Length: 253  Bit Score: 123.13  E-value: 2.70e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  12 FTIVRLVGTGGMGEVYLAKHPRLPREDALKVLPISVSADDEFRQrFIREADMAATLWHPHIVGVHDRGEFEGRLWISMDY 91
Cdd:cd14002    3 YHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRN-LRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  92 VDGhDAARLLHDKypKGMPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVtekhGTKRRIMLTDFGIARrTDDVNG 171
Cdd:cd14002   82 AQG-ELFQILEDD--GTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILI----GKGGVVKLCDFGFAR-AMSCNT 153
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118468993 172 LTSTNITvGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSHSNPAVVISHHLNSP 234
Cdd:cd14002  154 LVLTSIK-GTPLYMAPELVQEQPYDHTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDP 215
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
12-222 1.59e-30

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


Pssm-ID: 270905  Cd Length: 252  Bit Score: 121.09  E-value: 1.59e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  12 FTIVRLVGTGGMGEVYLAKHPRLPREDALKVLPISVSADDEFRqRFIREADMAATLWHPHIVGVHDRGEFEGRLWISMDY 91
Cdd:cd14003    2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEE-KIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  92 VDGHDaarlLHDK-YPKG-MPADDVVEIVTAVGDALDYAHQRQLLHRDVKPANILVTEKHgtkrRIMLTDFGIARRTDDV 169
Cdd:cd14003   81 ASGGE----LFDYiVNNGrLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNG----NLKIIDFGLSNEFRGG 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 118468993 170 NGLTStniTVGSMSYTSPEQLMGQPLDGR-ADQYSLAATAYRLLTGAPPFSHSN 222
Cdd:cd14003  153 SLLKT---FCGTPAYAAPEVLLGRKYDGPkADVWSLGVILYAMLTGYLPFDDDN 203
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
12-263 6.52e-30

Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and similar proteins; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. Members of this group include MAPKKs from plants, kinetoplastids, alveolates, and mycetozoa. The MAPKK, LmxPK4, from Leishmania mexicana, is important in differentiation and virulence. Dictyostelium discoideum MEK1 is required for proper chemotaxis; MEK1 null mutants display severe defects in cell polarization and directional movement. Plants contain multiple MAPKKs like other eukaryotes. The Arabidopsis genome encodes for 10 MAPKKs while poplar and rice contain 13 MAPKKs each. The functions of these proteins have not been fully elucidated. There is evidence to suggest that MAPK cascades are involved in plant stress responses. In Arabidopsis, MKK3 plays a role in pathogen signaling; MKK2 is involved in cold and salt stress signaling; MKK4/MKK5 participates in innate immunity; and MKK7 regulates basal and systemic acquired resistance. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132954  Cd Length: 264  Bit Score: 119.62  E-value: 6.52e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  12 FTIVRLVGTGGMGEVYLAKHPRLPREDALKVlpISVSADDEFRQRFIREADMAATLWHPHIVGVHdrGEF--EGRLWISM 89
Cdd:cd06623    3 LERVKVLGQGSSGVVYKVRHKPTGKIYALKK--IHVDGDEEFRKQLLRELKTLRSCESPYVVKCY--GAFykEGEISIVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  90 DYVDGHDAARLLhdKYPKGMPADDVVEIVTAVGDALDYAHQ-RQLLHRDVKPANILVTekhgTKRRIMLTDFGIARRTDD 168
Cdd:cd06623   79 EYMDGGSLADLL--KKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLIN----SKGEVKIADFGISKVLEN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993 169 VNGLTSTNitVGSMSYTSPEQLMGQPLDGRADQYSLAATAYRLLTGAPPFSHSNPAVVIS---HHLNSPPPKLgDTKPAL 245
Cdd:cd06623  153 TLDQCNTF--VGTVTYMSPERIQGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFElmqAICDGPPPSL-PAEEFS 229
                        250
                 ....*....|....*...
gi 118468993 246 AKLDSVMAKALAKDAKDR 263
Cdd:cd06623  230 PEFRDFISACLQKDPKKR 247
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
12-270 7.11e-30

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


Pssm-ID: 132943  Cd Length: 256  Bit Score: 119.29  E-value: 7.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  12 FTIVRLVGTGGMGEVYLAKHPRLPREDALKVLPIsvsadDEFRQRFIREADMAATLWHPHIVGVHDRGEFEGRLWISMDY 91
Cdd:cd06612    5 FDILEKLGEGSYGSVYKAIHKETGQVVAIKVVPV-----EEDLQEIIKEISILKQCDSPYIVKYYGSYFKNTDLWIVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118468993  92 VDG---HDAARLLHdkypKGMPADDVVEIVTAVGDAL