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Conserved domains on  [gi|118472741|ref|YP_885582|]
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serine/threonine protein kinase [Mycobacterium smegmatis str. MC2 155]

Protein Classification

serine/threonine protein kinase (domain architecture ID 10195858)

serine/threonine protein kinase catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

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 ...
11-278 2.13e-99

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: 307.21  E-value: 2.13e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  11 GYTVERMLGSGGMGEVYLAQHPRLPRHDALKVLRANISADPAYVERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMD 90
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  91 FVDGTDASRLLHDRYPdgMPVPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILISDGDhgerRILLGDFGVARDLGDSa 170
Cdd:cd14014   81 YVEGGSLADLLRERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG----RVKLTDFGIARALGDS- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 171 gnGLTATNMTVGTAAYAAPEQLMGLELDGRADQYSLAATAYHLLTGGPLFENSNPAVVIGQHLNAPPPALGDSRPELAP- 249
Cdd:cd14014  154 --GLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPa 231
                        250       260
                 ....*....|....*....|....*....
gi 118472741 250 LDAALSRALAKNPDDRFATCTDFANALEH 278
Cdd:cd14014  232 LDAIILRALAKDPEERPQSAAELLAALRA 260
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-278 2.13e-99

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: 307.21  E-value: 2.13e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  11 GYTVERMLGSGGMGEVYLAQHPRLPRHDALKVLRANISADPAYVERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMD 90
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  91 FVDGTDASRLLHDRYPdgMPVPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILISDGDhgerRILLGDFGVARDLGDSa 170
Cdd:cd14014   81 YVEGGSLADLLRERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG----RVKLTDFGIARALGDS- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 171 gnGLTATNMTVGTAAYAAPEQLMGLELDGRADQYSLAATAYHLLTGGPLFENSNPAVVIGQHLNAPPPALGDSRPELAP- 249
Cdd:cd14014  154 --GLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPa 231
                        250       260
                 ....*....|....*....|....*....
gi 118472741 250 LDAALSRALAKNPDDRFATCTDFANALEH 278
Cdd:cd14014  232 LDAIILRALAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-279 2.97e-56

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 193.13  E-value: 2.97e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741    12 YTVERMLGSGGMGEVYLAQHPRLPRHDALKVLRanISADPAYVERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMDF 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741    92 VDGTDASRLLHDRYPdgMPVPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILISDGDHgerrILLGDFGVARDLGDSag 171
Cdd:smart00220  79 CEGGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH----VKLADFGLARQLDPG-- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741   172 nglTATNMTVGTAAYAAPEQLMGLELDGRADQYSLAATAYHLLTGGPLFENSNPAVVIGQHLNAPPPALGDSRPELAPlD 251
Cdd:smart00220 151 ---EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISP-E 226
                          250       260       270
                   ....*....|....*....|....*....|
gi 118472741   252 AA--LSRALAKNPDDRFatctDFANALEHP 279
Cdd:smart00220 227 AKdlIRKLLVKDPEKRL----TAEEALQHP 252
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
11-297 2.80e-49

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 178.01  E-value: 2.80e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  11 GYTVERMLGSGGMGEVYLAQHPRLPrhdALKVLRANISADPAYVERFNKEADLAAKL-WHPHIVGIHDRGKHRNRLWISM 89
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARDRKLV---ALKVLAKKLESKSKEVERFLREIQILASLnHPPNIVKLYDFFQDEGSLYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  90 DFVDGTDASRLLHDRYPDG-MPVPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILIsdgDHGERRILLGDFGVARDLGD 168
Cdd:COG0515   78 EYVDGGSLEDLLKKIGRKGpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILL---DRDGRVVKLIDFGLAKLLPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 169 --SAGNGLTATNMTVGTAAYAAPEQLMGLEL---DGRADQYSLAATAYHLLTGGPLFENSNPAVVIGQHL--------NA 235
Cdd:COG0515  155 pgSTSSIPALPSTSVGTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLkiilelptPS 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118472741 236 PPPALGDSRPELAPLDAA--LSRALAKNPDDRFATCTDFANALEHPQNHAATMTAPVPSPNDVP 297
Cdd:COG0515  235 LASPLSPSNPELISKAASdlLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSA 298
Pkinase pfam00069
Protein kinase domain;
12-279 3.84e-36

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 136.96  E-value: 3.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741   12 YTVERMLGSGGMGEVYLAQHPRLPRHDALKVLRANiSADPAYVERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMDF 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKE-KIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741   92 VDGTDasrlLHDRYPDGMPVPE--VLDIVKAVAAALDYAHGRGLLHRDVKPANILISdgDHGErrILLGDFGVARDLGDS 169
Cdd:pfam00069  80 VEGGS----LFDLLSEKGAFSEreAKFIMKQILEGLEYLHSNGIIHRDLKPENILID--EDGN--LKITDFGLARQLNSG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  170 agnglTATNMTVGTAAYAAPEQLMGLELDGRADQYSLAATAYHLLTGGPLFENSNPAVVIGQHLNAP--PPALGDSRPEL 247
Cdd:pfam00069 152 -----SSLTSFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDfdSPRPSSISEEA 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 118472741  248 APLdaaLSRALAKNPDDRFaTCTDfanALEHP 279
Cdd:pfam00069 227 KDL---LKKLLKKDPSKRL-TATE---ALQHP 251
pknD PRK13184
serine/threonine-protein kinase; Reviewed
12-277 2.42e-34

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 139.52  E-value: 2.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  12 YTVERMLGSGGMGEVYLAQHPRLPRHDALKVLRANISADPAYVERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMDF 91
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  92 VDGTDASRLLHD-RYPDGMP--------VPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILIsdGDHGERRILlgDFGV 162
Cdd:PRK13184  84 IEGYTLKSLLKSvWQKESLSkelaektsVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILL--GLFGEVVIL--DWGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 163 AR-------DLGDSAGN--GLTATNMT-----VGTAAYAAPEQLMGLELDGRADQYSLAATAYHLLTGGPLFENSNPAVV 228
Cdd:PRK13184 160 AIfkkleeeDLLDIDVDerNICYSSMTipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKI 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 118472741 229 IGQHLNAPPPALGDSRpELAP-LDAALSRALAKNPDDRFATCTDFANALE 277
Cdd:PRK13184 240 SYRDVILSPIEVAPYR-EIPPfLSQIAMKALAVDPAERYSSVQELKQDLE 288
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
39-274 8.37e-26

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: 113.40  E-value: 8.37e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741    39 ALKVLRANISADPAYVERFNKEADLAAKLWHPHIVGIHDRGK-HRNRLWISMDFVDGTDASRLLHDRYPdgMPVPEVLDI 117
Cdd:TIGR03903    7 AIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDSGEaPPGLLFAVFEYVPGRTLREVLAADGA--LPAGETGRL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741   118 VKAVAAALDYAHGRGLLHRDVKPANILISDGDhGERRILLGDFGVAR---DLGDSAGNGLTATNMTVGTAAYAAPEQLMG 194
Cdd:TIGR03903   85 MLQVLDALACAHNQGIVHRDLKPQNIMVSQTG-VRPHAKVLDFGIGTllpGVRDADVATLTRTTEVLGTPTYCAPEQLRG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741   195 LELDGRADQYSLAATAYHLLTGGPLFENSNPAVVIGQHLN----APPPALgdsrpELAPLDAALSRALAKNPDDRFATCT 270
Cdd:TIGR03903  164 EPVTPNSDLYAWGLIFLECLTGQRVVQGASVAEILYQQLSpvdvSLPPWI-----AGHPLGQVLRKALNKDPRQRAASAP 238

                   ....
gi 118472741   271 DFAN 274
Cdd:TIGR03903  239 ALAE 242
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
11-278 2.13e-99

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: 307.21  E-value: 2.13e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  11 GYTVERMLGSGGMGEVYLAQHPRLPRHDALKVLRANISADPAYVERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMD 90
Cdd:cd14014    1 RYRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  91 FVDGTDASRLLHDRYPdgMPVPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILISDGDhgerRILLGDFGVARDLGDSa 170
Cdd:cd14014   81 YVEGGSLADLLRERGP--LPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDG----RVKLTDFGIARALGDS- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 171 gnGLTATNMTVGTAAYAAPEQLMGLELDGRADQYSLAATAYHLLTGGPLFENSNPAVVIGQHLNAPPPALGDSRPELAP- 249
Cdd:cd14014  154 --GLTQTGSVLGTPAYMAPEQARGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLNPDVPPa 231
                        250       260
                 ....*....|....*....|....*....
gi 118472741 250 LDAALSRALAKNPDDRFATCTDFANALEH 278
Cdd:cd14014  232 LDAIILRALAKDPEERPQSAAELLAALRA 260
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
12-279 2.97e-56

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


Pssm-ID: 214567  Cd Length: 254  Bit Score: 193.13  E-value: 2.97e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741    12 YTVERMLGSGGMGEVYLAQHPRLPRHDALKVLRanISADPAYVERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMDF 91
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIK--KKKIKKDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEY 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741    92 VDGTDASRLLHDRYPdgMPVPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILISDGDHgerrILLGDFGVARDLGDSag 171
Cdd:smart00220  79 CEGGDLFDLLKKRGR--LSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGH----VKLADFGLARQLDPG-- 150
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741   172 nglTATNMTVGTAAYAAPEQLMGLELDGRADQYSLAATAYHLLTGGPLFENSNPAVVIGQHLNAPPPALGDSRPELAPlD 251
Cdd:smart00220 151 ---EKLTTFVGTPEYMAPEVLLGKGYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFKKIGKPKPPFPPPEWDISP-E 226
                          250       260       270
                   ....*....|....*....|....*....|
gi 118472741   252 AA--LSRALAKNPDDRFatctDFANALEHP 279
Cdd:smart00220 227 AKdlIRKLLVKDPEKRL----TAEEALQHP 252
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
11-297 2.80e-49

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589  Cd Length: 384  Bit Score: 178.01  E-value: 2.80e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  11 GYTVERMLGSGGMGEVYLAQHPRLPrhdALKVLRANISADPAYVERFNKEADLAAKL-WHPHIVGIHDRGKHRNRLWISM 89
Cdd:COG0515    1 SYRILRKLGEGSFGEVYLARDRKLV---ALKVLAKKLESKSKEVERFLREIQILASLnHPPNIVKLYDFFQDEGSLYLVM 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  90 DFVDGTDASRLLHDRYPDG-MPVPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILIsdgDHGERRILLGDFGVARDLGD 168
Cdd:COG0515   78 EYVDGGSLEDLLKKIGRKGpLSESEALFILAQILSALEYLHSKGIIHRDIKPENILL---DRDGRVVKLIDFGLAKLLPD 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 169 --SAGNGLTATNMTVGTAAYAAPEQLMGLEL---DGRADQYSLAATAYHLLTGGPLFENSNPAVVIGQHL--------NA 235
Cdd:COG0515  155 pgSTSSIPALPSTSVGTPGYMAPEVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLkiilelptPS 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118472741 236 PPPALGDSRPELAPLDAA--LSRALAKNPDDRFATCTDFANALEHPQNHAATMTAPVPSPNDVP 297
Cdd:COG0515  235 LASPLSPSNPELISKAASdlLKKLLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDLLKPDDSA 298
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
12-279 5.49e-37

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: 139.26  E-value: 5.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  12 YTVERMLGSGGMGEVYLAQHPRLPRHDALKVLraNISADPAYvERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMDF 91
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKI--NLESKEKK-ESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  92 VDGTDASRLLHDRypdGMPVPE--VLDIVKAVAAALDYAHGRGLLHRDVKPANILISdgDHGErrILLGDFGVARDLGDS 169
Cdd:cd05122   79 CSGGSLKDLLKNT---NKTLTEqqIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLT--SDGE--VKLIDFGLSAQLSDG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 170 agnglTATNMTVGTAAYAAPEQLMGLELDGRADQYSLAATAYHLLTGGPLFENSNPA---VVIGQHlnaPPPALGDSRPE 246
Cdd:cd05122  152 -----KTRNTFVGTPYWMAPEVIQGKPYGFKADIWSLGITAIEMAEGKPPYSELPPMkalFLIATN---GPPGLRNPKKW 223
                        250       260       270
                 ....*....|....*....|....*....|...
gi 118472741 247 LAPLDAALSRALAKNPDDRfATCTDFanaLEHP 279
Cdd:cd05122  224 SKEFKDFLKKCLQKDPEKR-PTAEQL---LKHP 252
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
18-279 5.75e-37

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: 137.79  E-value: 5.75e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  18 LGSGGMGEVYLAQHPRLPRHDALKVLraNISADPAYVERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMDFVDGTDA 97
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVI--PKEKLKKLLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  98 SRLLhDRYPDGMPVPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILISDGDHgerrILLGDFGVARDLGDSagNGLTAT 177
Cdd:cd00180   79 KDLL-KENKGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGT----VKLADFGLAKDLDSD--DSLLKT 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 178 NMTVGTAAYAAPEQLMGLELDGRADQYSLAATAYhlltggplfensnpavvigqhlnapppalgdsrpELAPLDAALSRA 257
Cdd:cd00180  152 TGGTTPPYYAPPELLGGRYYGPKVDIWSLGVILY----------------------------------ELEELKDLIRRM 197
                        250       260
                 ....*....|....*....|..
gi 118472741 258 LAKNPDDRFatctDFANALEHP 279
Cdd:cd00180  198 LQYDPKKRP----SAKELLEHL 215
Pkinase pfam00069
Protein kinase domain;
12-279 3.84e-36

Protein kinase domain;


Pssm-ID: 306557  Cd Length: 253  Bit Score: 136.96  E-value: 3.84e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741   12 YTVERMLGSGGMGEVYLAQHPRLPRHDALKVLRANiSADPAYVERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMDF 91
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKE-KIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEY 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741   92 VDGTDasrlLHDRYPDGMPVPE--VLDIVKAVAAALDYAHGRGLLHRDVKPANILISdgDHGErrILLGDFGVARDLGDS 169
Cdd:pfam00069  80 VEGGS----LFDLLSEKGAFSEreAKFIMKQILEGLEYLHSNGIIHRDLKPENILID--EDGN--LKITDFGLARQLNSG 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  170 agnglTATNMTVGTAAYAAPEQLMGLELDGRADQYSLAATAYHLLTGGPLFENSNPAVVIGQHLNAP--PPALGDSRPEL 247
Cdd:pfam00069 152 -----SSLTSFVGTPWYMAPEVLRGNPYGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEKIIDQDfdSPRPSSISEEA 226
                         250       260       270
                  ....*....|....*....|....*....|..
gi 118472741  248 APLdaaLSRALAKNPDDRFaTCTDfanALEHP 279
Cdd:pfam00069 227 KDL---LKKLLKKDPSKRL-TATE---ALQHP 251
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
11-265 2.44e-35

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: 134.51  E-value: 2.44e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  11 GYTVERMLGSGGMGEVYLAQHPRLPRHDALKVLR-ANISADpayvERFN--KEADLAAKLWHPHIVGIHDRGKHRNRLWI 87
Cdd:cd08215    1 KYEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDlSNMSEK----EREEalNEVKLLSKLKHPNIVKYYESFEENGKLCI 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  88 SMDFVDGTDASRLLHDRYPDGMPVPE--VLDIVKAVAAALDYAHGRGLLHRDVKPANILISDGDHgerrILLGDFGVARD 165
Cdd:cd08215   77 VMEYADGGDLAQKIKKQKKKGQPFPEeqILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGV----VKLGDFGISKV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 166 LGDSagngLTATNMTVGTAAYAAPEQLMGLELDGRADQYSLAATAYHLLTGGPLFENSNPAVVIGQHLNAPPPALGDSR- 244
Cdd:cd08215  153 LEST----TDLAKTVVGTPYYLSPELCENKPYNYKSDIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPPIPSQYs 228
                        250       260
                 ....*....|....*....|.
gi 118472741 245 PELAPLdaaLSRALAKNPDDR 265
Cdd:cd08215  229 SELRDL---VNSMLQKDPEKR 246
pknD PRK13184
serine/threonine-protein kinase; Reviewed
12-277 2.42e-34

serine/threonine-protein kinase; Reviewed


Pssm-ID: 183880  Cd Length: 932  Bit Score: 139.52  E-value: 2.42e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  12 YTVERMLGSGGMGEVYLAQHPRLPRHDALKVLRANISADPAYVERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMDF 91
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFLREAKIAADLIHPGIVPVYSICSDGDPVYYTMPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  92 VDGTDASRLLHD-RYPDGMP--------VPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILIsdGDHGERRILlgDFGV 162
Cdd:PRK13184  84 IEGYTLKSLLKSvWQKESLSkelaektsVGAFLSIFHKICATIEYVHSKGVLHRDLKPDNILL--GLFGEVVIL--DWGA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 163 AR-------DLGDSAGN--GLTATNMT-----VGTAAYAAPEQLMGLELDGRADQYSLAATAYHLLTGGPLFENSNPAVV 228
Cdd:PRK13184 160 AIfkkleeeDLLDIDVDerNICYSSMTipgkiVGTPDYMAPERLLGVPASESTDIYALGVILYQMLTLSFPYRRKKGRKI 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 118472741 229 IGQHLNAPPPALGDSRpELAP-LDAALSRALAKNPDDRFATCTDFANALE 277
Cdd:PRK13184 240 SYRDVILSPIEVAPYR-EIPPfLSQIAMKALAVDPAERYSSVQELKQDLE 288
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
14-265 2.73e-31

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: General Control Non-derepressible-2 (GCN2) which is activated during amino acid or serum starvation; protein kinase regulated by RNA (PKR) which is activated by double stranded RNA; heme-regulated inhibitor kinase (HRI) which is activated under heme-deficient conditions; and PKR-like endoplasmic reticulum kinase (PERK) which is activated when misfolded proteins accumulate in the ER. The EIF2AK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270898  Cd Length: 273  Bit Score: 123.94  E-value: 2.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  14 VERMLGSGGMGEVYLAQHPRLPRHDALKVLRANISAD-PAYVERfnkEADLAAKLWHPHIVGIHDRGKHRNRLWISMDFV 92
Cdd:cd13996   10 EIELLGSGGFGSVYKVRNKVDGVTYAIKKIRLTEKSSaSEKVLR---EVKALAKLNHPNIVRYYTAWVEEPPLYIQMELC 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  93 DGTDASRLLHDR--YPDGMpVPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILISDGDhgeRRILLGDFGVARDLGD-- 168
Cdd:cd13996   87 EGGTLRDWIDRRnsSSKND-RKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDD---LQVKIGDFGLATSIGNqk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 169 -------SAGNGLTATNMT-VGTAAYAAPEQLMGLELDGRADQYSLAATAYHLL-TGGPLFENSNpavVIGQHLNAP-PP 238
Cdd:cd13996  163 relnnlnNNNNGNTSNNSVgIGTPLYASPEQLDGENYNEKADIYSLGIILFEMLhPFKTAMERST---ILTDLRNGIlPE 239
                        250       260
                 ....*....|....*....|....*..
gi 118472741 239 ALGDSRPELAPLdaaLSRALAKNPDDR 265
Cdd:cd13996  240 SFKAKHPKEADL---IQSLLSKNPEER 263
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
12-279 1.56e-30

Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of MST3, MST4, STK25, Schizosaccharomyces pombe Nak1 and Sid1, Saccharomyces cerevisiae sporulation-specific protein 1 (SPS1), and related proteins. Nak1 is required by fission yeast for polarizing the tips of actin cytoskeleton and is involved in cell growth, cell separation, cell morphology and cell-cycle progression. Sid1 is a component in the septation initiation network (SIN) signaling pathway, and plays a role in cytokinesis. SPS1 plays a role in regulating proteins required for spore wall formation. MST4 plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. STK25 may play a role in the regulation of cell migration and polarization. The MST3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270786  Cd Length: 274  Bit Score: 121.58  E-value: 1.56e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  12 YTVERMLGSGGMGEVYLAQHPRLPRHDALKVLRANISADPayVERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMDF 91
Cdd:cd06609    3 FTLLERIGKGSFGEVYKGIDKRTNQVVAIKVIDLEEAEDE--IEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  92 VDGTDASRLLHdryPDGMPVPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILIS-DGDhgerrILLGDFGVARDLGDSa 170
Cdd:cd06609   81 CGGGSVLDLLK---PGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSeEGD-----VKLADFGVSGQLTST- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 171 gngLTATNMTVGTAAYAAPEQLMGLELDGRADQYSLAATAYHLLTGGPLFENSNPAVVIGQHLNAPPPALGD---SRpel 247
Cdd:cd06609  152 ---MSKRNTFVGTPFWMAPEVIKQSGYDEKADIWSLGITAIELAKGEPPLSDLHPMRVLFLIPKNNPPSLEGnkfSK--- 225
                        250       260       270
                 ....*....|....*....|....*....|..
gi 118472741 248 aPLDAALSRALAKNPDDRfATCTDFanaLEHP 279
Cdd:cd06609  226 -PFKDFVELCLNKDPKER-PSAKEL---LKHK 252
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
11-234 5.36e-30

Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. TSSK6, also called SSTK, is expressed at the head of elongated sperm. TSSK1/TSSK2 double knock-out and TSSK6 null mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270982  Cd Length: 262  Bit Score: 119.98  E-value: 5.36e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  11 GYTVERMLGSGGMGEVYLAQ--HPRLPRHDALKVLRANIsADPAYVERF-NKEADLAAKLWHPHIVGIHDRGKHRNRLWI 87
Cdd:cd14080    1 GYRLGKTIGEGSYSKVKLAEytKSGLKEKVACKIIDKKK-APKDFLEKFlPRELEILRKLRHPNIIQVYSIFERGSKVFI 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  88 SMDFVDGTDasrLL-HDRYPDGMPVPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILISDGDHgerrILLGDFGVARDL 166
Cdd:cd14080   80 FMEYAEHGD---LLeYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNN----VKLSDFGFARLC 152
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118472741 167 GDSAGNGLTATnmTVGTAAYAAPEQLMGLELDGR-ADQYSLAATAYHLLTGGPLFENSNPAVVIGQHLN 234
Cdd:cd14080  153 PDDDGDVLSKT--FCGSAAYAAPEILQGIPYDPKkYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQN 219
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
12-279 7.88e-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: 119.16  E-value: 7.88e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  12 YTVERMLGSGGMGEVYLAQHPRLPRHDALKVL-RANISADPayVERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMD 90
Cdd:cd14003    2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIdKSKLKEEI--EEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  91 FVDGTDasrlLHDR-YPDG-MPVPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILIsDGDHgerRILLGDFGVARdlgD 168
Cdd:cd14003   80 YASGGE----LFDYiVNNGrLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILL-DKNG---NLKIIDFGLSN---E 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 169 SAGNGLTATnmTVGTAAYAAPEQLMGLELDGR-ADQYSLAATAYHLLTGGPLFENSNPAVVIGQHLNAPPPalgdsRPEL 247
Cdd:cd14003  149 FRGGSLLKT--FCGTPAYAAPEVLLGRKYDGPkADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYP-----IPSH 221
                        250       260       270
                 ....*....|....*....|....*....|....
gi 118472741 248 APLDAA--LSRALAKNPDDRFATctdfANALEHP 279
Cdd:cd14003  222 LSPDARdlIRRMLVVDPSKRITI----EEILNHP 251
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
12-279 2.82e-29

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: 117.62  E-value: 2.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  12 YTVERMLGSGGMGEVYLAQHPRLPRHDALKVLRANiSADPAYVERFNKEADLAAKLWHPHIVGIHDRGKHRNRLWISMDF 91
Cdd:cd06606    2 WKKGELLGKGSFGSVYLALNLDTGELMAVKEVELS-GDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741  92 VDGTDASRLLhDRYPdGMPVPEVLDIVKAVAAALDYAHGRGLLHRDVKPANILISDGDhgerRILLGDFGVARDLGDSAG 171
Cdd:cd06606   81 VPGGSLASLL-KKFG-KLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDG----VVKLADFGCAKRLAEIAT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118472741 172 NGltATNMTVGTAAYAAPEQLMGLELDGRADQYSLAATAYHLLTGGPLFEN-SNPAVV---IGQHLNAPPPalgdsrPEL 247
Cdd:cd06606  155 GE--GTKSLRGTPYWMAPEVIRGEGYGRAADIWSLGCTVIEMATGKPPWSElGNPVAAlfkIGSSGEPPPI------PEH 226
                        250       260       270
                 ....*....|....*....|....*....|....
gi 118472741 248 APLDAA--LSRALAKNPDDRfATCTDFanaLEHP 279
Cdd:cd06606  227 LSEEAKdfLRKCLQRDPKKR-PTADEL---LQHP 256