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Conserved domains on  [gi|37523586|ref|NP_926963|]
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serine/threonine kinase [Gloeobacter violaceus PCC 7421]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PKc_like super family cl21453
Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the ...
13-185 9.45e-36

Protein Kinases, catalytic domain; The protein kinase superfamily is mainly composed of the catalytic domains of serine/threonine-specific and tyrosine-specific protein kinases. It also includes RIO kinases, which are atypical serine protein kinases, aminoglycoside phosphotransferases, and choline kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to hydroxyl groups in specific substrates such as serine, threonine, or tyrosine residues of proteins.


The actual alignment was detected with superfamily member cd14014:

Pssm-ID: 304357 [Multi-domain]  Cd Length: 260  Bit Score: 130.01  E-value: 9.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFGEGALWQDFKLFEREAETLQSLSHSRIPRQRDAFWWEqpeGNYFcL 92
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDD---GRPY-I 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  93 IQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQspPVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSAPEK 172
Cdd:cd14014  78 VMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRA--GIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGL 155
                       170
                ....*....|....*
gi 37523586 173 TMT--VVGTYrLYAP 185
Cdd:cd14014 156 TQTgsVLGTP-AYMA 169
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
13-185 9.45e-36

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


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 130.01  E-value: 9.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFGEGALWQDFKLFEREAETLQSLSHSRIPRQRDAFWWEqpeGNYFcL 92
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDD---GRPY-I 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  93 IQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQspPVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSAPEK 172
Cdd:cd14014  78 VMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRA--GIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGL 155
                       170
                ....*....|....*
gi 37523586 173 TMT--VVGTYrLYAP 185
Cdd:cd14014 156 TQTgsVLGTP-AYMA 169
PRK14879 PRK14879
serine/threonine protein kinase; Provisional
90-162 1.04e-07

serine/threonine protein kinase; Provisional


Pssm-ID: 237847  Cd Length: 211  Bit Score: 50.29  E-value: 1.04e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37523586   90 FCLIQDFIPGQSLEASVRNLGPlpeaEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWgEDGRIYLIDFG 162
Cdd:PRK14879  74 FIIVMEYIEGEPLKDLINSNGM----EELELSREIGRLVGKLHSAG--IIHGDLTTSNMIL-SGGKIYLIDFG 139
RIO1 pfam01163
RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria ...
59-168 4.22e-06

RIO1 family; This is a family of atypical serine kinases which are found in archaea, bacteria and eukaryotes. Activity of Rio1 is vital in Saccharomyces cerevisiae for the processing of ribosomal RNA, as well as for proper cell cycle progression and chromosome maintenance. The structure of RIO1 has been determined.


Pssm-ID: 279503  Cd Length: 186  Bit Score: 44.92  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586    59 EREAETLQSLS--HSRIPRQRDAfwweqpegNYFCLIQDFIPGQSLEAS-VRNLGPLPEAevRTIAAEVLEILI--YLHR 133
Cdd:pfam01163  54 EKEFRNLKRLYeaGVPVPKPIDL--------NRHVLVMEFIGKDGVPAPrLKDVELPEEA--REIYDEIIREMRrlYQEA 123
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 37523586   134 QsppVIHRDLTPANLIWGEDGrIYLIDFGavQAVS 168
Cdd:pfam01163 124 G---LVHGDLSEYNILVHDDK-PVIIDVP--QAVE 152
arch_bud32 TIGR03724
Kae1-associated kinase Bud32; Members of this protein family are the Bud32 protein associated ...
138-162 1.69e-05

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


Pssm-ID: 274749  Cd Length: 199  Bit Score: 43.35  E-value: 1.69e-05
                          10        20
                  ....*....|....*....|....*
gi 37523586   138 VIHRDLTPANLIWGEDgRIYLIDFG 162
Cdd:TIGR03724 111 IVHGDLTTSNIIVRDD-KVYLIDFG 134
CotS COG0510
Thiamine kinase and related kinases [Coenzyme transport and metabolism];
123-161 1.28e-04

Thiamine kinase and related kinases [Coenzyme transport and metabolism];


Pssm-ID: 223584  Cd Length: 269  Bit Score: 41.23  E-value: 1.28e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 37523586 123 EVLEILIYLHRQSPP-------VIHRDLTPANLIWGEDGRIYLIDF 161
Cdd:COG0510 133 LLRKKLKELRRALEEvpkddlvPCHNDLNPGNLLLTDKGGLFLIDW 178
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
13-185 1.31e-29

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 113.39  E-value: 1.31e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586     13 YRPVRLL--GANGTrqTWLAAEEKTGQTVTLKALYFGEgaLWQDFKLFEREAETLQSLSHSRIPRQRDAFWweqpEGNYF 90
Cdd:smart00220   1 YEILEKLgeGSFGK--VYLARDKKTGKLVAIKVIKKKK--IKKDRERILREIKILKKLKHPNIVRLYDVFE----DEDKL 72
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586     91 CLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSAP 170
Cdd:smart00220  73 YLVMEYCEGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENILLDEDGHVKLADFGLARQLDPG 150
                          170
                   ....*....|....*..
gi 37523586    171 EKTMTVVGT--YRlyAP 185
Cdd:smart00220 151 EKLTTFVGTpeYM--AP 165
Pkinase pfam00069
Protein kinase domain;
13-194 7.06e-27

Protein kinase domain;


Pssm-ID: 278497 [Multi-domain]  Cd Length: 254  Bit Score: 105.75  E-value: 7.06e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586    13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFgEGALWQDFKLFEREAETLQSLSHSRIPRQRDAFwwEQPegNYFCL 92
Cdd:pfam00069   1 YEVLEKLGSGSFGTVYKAKHRDTGKIVAVKKIKK-EKIKKKKDKNVLREIKILKKLNHPNIVRLYDVF--EDK--DHLYL 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586    93 IQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSAPEK 172
Cdd:pfam00069  76 VLEYVEGGSLFDLLSEKGAFSEREAKFIMKQILEGLEYLHSNG--IVHRDLKPENILIDEDGNLKITDFGLAKQLSSGSK 153
                         170       180
                  ....*....|....*....|...
gi 37523586   173 TMTVVGTYRLYAPGAVRG-PHGP 194
Cdd:pfam00069 154 LTTFVGTPWYMAPEVLRGnPYGP 176
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
13-185 2.57e-22

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 94.04  E-value: 2.57e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTgqtVTLKALYFGEGALWQDFKLFEREAETLQSLSH-SRIPRQRDAFWWEqpegNYFC 91
Cdd:COG0515   2 YRILRKLGEGSFGEVYLARDRKL---VALKVLAKKLESKSKEVERFLREIQILASLNHpPNIVKLYDFFQDE----GSLY 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  92 LIQDFIPGQSLEASVRNLG---PLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDG-RIYLIDFGAVQAV 167
Cdd:COG0515  75 LVMEYVDGGSLEDLLKKIGrkgPLSESEALFILAQILSALEYLHSKG--IIHRDIKPENILLDRDGrVVKLIDFGLAKLL 152
                       170       180
                ....*....|....*....|....*
gi 37523586 168 SA-------PEKTMTVVGTYRLYAP 185
Cdd:COG0515 153 PDpgstssiPALPSTSVGTPGYMAP 177
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
29-196 7.86e-11

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 60.60  E-value: 7.86e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586   29 LAAEEKTGQTVTLKALYFGEGALWQDFKLFEREAETLQSLSHSRIPRQRDAFwweQPEGN-YFCLiqDFIPGQSLEASVR 107
Cdd:PTZ00263  36 IAKHKGTGEYYAIKCLKKREILKMKQVQHVAQEKSILMELSHPFIVNMMCSF---QDENRvYFLL--EFVVGGELFTHLR 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  108 NLGPLPEAEVRTIAAEVLEILIYLHrqSPPVIHRDLTPANLIWGEDGRIYLIDFGAVQAVsaPEKTMTVVGTYRLYAPGA 187
Cdd:PTZ00263 111 KAGRFPNDVAKFYHAELVLAFEYLH--SKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKV--PDRTFTLCGTPEYLAPEV 186
                        170
                 ....*....|
gi 37523586  188 VRGP-HGPCV 196
Cdd:PTZ00263 187 IQSKgHGKAV 196
TOMM_kin_cyc TIGR03903
TOMM system kinase/cyclase fusion protein; This model represents proteins of 1350 in length, ...
35-190 3.08e-08

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 [Multi-domain]  Cd Length: 1266  Bit Score: 53.31  E-value: 3.08e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586     35 TGQTVTLKALYFGEGALWQDFKLFEREAETLQSLSHSRIPRQRDAfwWEQPEGNYFCLIQdFIPGQSLEASVRNLGPLPE 114
Cdd:TIGR03903    2 TGHEVAIKLLRTDAPEEEHQRARFRRETALCARLYHPNIVALLDS--GEAPPGLLFAVFE-YVPGRTLREVLAADGALPA 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586    115 AEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDG---RIYLIDFG------AVQAVSAPEKTMT--VVGTYRLY 183
Cdd:TIGR03903   79 GETGRLMLQVLDALACAHNQG--IVHRDLKPQNIMVSQTGvrpHAKVLDFGigtllpGVRDADVATLTRTteVLGTPTYC 156

                   ....*..
gi 37523586    184 APGAVRG 190
Cdd:TIGR03903  157 APEQLRG 163
 
Name Accession Description Interval E-value
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
13-185 9.45e-36

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


Pssm-ID: 270916 [Multi-domain]  Cd Length: 260  Bit Score: 130.01  E-value: 9.45e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFGEGALWQDFKLFEREAETLQSLSHSRIPRQRDAFWWEqpeGNYFcL 92
Cdd:cd14014   2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFLREARALARLSHPNIVRVYDVGEDD---GRPY-I 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  93 IQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQspPVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSAPEK 172
Cdd:cd14014  78 VMEYVEGGSLADLLRERGPLPPREALRILAQIADALAAAHRA--GIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGL 155
                       170
                ....*....|....*
gi 37523586 173 TMT--VVGTYrLYAP 185
Cdd:cd14014 156 TQTgsVLGTP-AYMA 169
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
13-190 6.32e-27

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


Pssm-ID: 270783 [Multi-domain]  Cd Length: 258  Bit Score: 106.07  E-value: 6.32e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFGEGALWQDFKLfEREAETLQSLSHSRIPRQRDAFWweqpEGNYFCL 92
Cdd:cd06606   2 WKKGELLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEAL-EREIRILSSLKHPNIVRYLGTER----TENTLNI 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  93 IQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFGA---VQAVSA 169
Cdd:cd06606  77 FLEYVPGGSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNG--IVHRDIKGANILVDSDGVVKLADFGCakrLAEIAT 154
                       170       180
                ....*....|....*....|.
gi 37523586 170 PEKTMTVVGTYRLYAPGAVRG 190
Cdd:cd06606 155 GEGTKSLRGTPYWMAPEVIRG 175
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
20-185 3.26e-26

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


Pssm-ID: 270622 [Multi-domain]  Cd Length: 215  Bit Score: 103.12  E-value: 3.26e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  20 GANGTrqTWLAAEEKTGQTVTLKALYFGEgaLWQDFKLFEREAETLQSLSHSRIPRQRDAFwweqPEGNYFCLIQDFIPG 99
Cdd:cd00180   4 GSFGK--VYKARDKETGKKVAVKVIPKEK--LKKLLEELLREIEILKKLNHPNIVKLYDVF----ETENFLYLVMEYCEG 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586 100 QSLEASVRNL-GPLPEAEVRTIAAEVLEILIYLHRQspPVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSAPEKTMTVVG 178
Cdd:cd00180  76 GSLKDLLKENkGPLSEEEALSILRQLLSALEYLHSN--GIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLLKTTG 153

                ....*..
gi 37523586 179 TYRLYAP 185
Cdd:cd00180 154 GTTPPYY 160
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
20-198 4.20e-20

Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily include Schizosaccharomyces pombe Cdc7, Saccharomyces cerevisiae Cdc15, Arabidopsis thaliana mitogen-activated protein kinase kinase kinase (MAPKKK) epsilon, and related proteins. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Cdc7 is essential for cell division by playing a key role in the initiation of septum formation and cytokinesis. Budding yeast Cdc15 functions to coordinate mitotic exit with cytokinesis. Arabidopsis MAPKKK epsilon is required for pollen development in the plasma membrane. The Cdc7-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270797 [Multi-domain]  Cd Length: 254  Bit Score: 86.12  E-value: 4.20e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  20 GANGTrqTWLAAEEKTGQTVTLKALYFgEGALWQDFKLFEREAETLQSLSHSRIPRQRDAFwweqPEGNYFCLIQDFIPG 99
Cdd:cd06627  11 GAFGS--VYKGLNLNTGEFVAIKQISL-EKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSV----KTKDSLYIILEYVEN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586 100 QSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFG-AVQAVSAPEKTMTVVG 178
Cdd:cd06627  84 GSLASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQG--VIHRDIKGANILTTKDGLVKLADFGvATKLNEVEKDENSVVG 161
                       170       180
                ....*....|....*....|
gi 37523586 179 TYRLYAPGAVRGpHGPCVRS 198
Cdd:cd06627 162 TPYWMAPEVIEM-SGVTTAS 180
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
13-185 1.00e-19

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


Pssm-ID: 270905 [Multi-domain]  Cd Length: 252  Bit Score: 84.88  E-value: 1.00e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFGEgALWQDFKLFEREAETLQSLSHSRIPRQRDAFwwEQPegNYFCL 92
Cdd:cd14003   2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSK-LKEEIEEKIKREIEIMKLLNHPNIIKLYEVI--ETE--NKIYL 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  93 IQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSAPEK 172
Cdd:cd14003  77 VMEYASGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNG--IVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSL 154
                       170
                ....*....|...
gi 37523586 173 TMTVVGTYrLYAP 185
Cdd:cd14003 155 LKTFCGTP-AYAA 166
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
65-196 1.23e-19

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


Pssm-ID: 270693 [Multi-domain]  Cd Length: 250  Bit Score: 84.88  E-value: 1.23e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  65 LQSLSHSRIPRQRDAFwweQPEgNYFCLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLT 144
Cdd:cd05123  47 LERVNHPFIVKLHYAF---QTE-EKLYLVLDYVPGGELFSHLSKEGRFPEERARFYAAEIVLALEYLHSLG--IIYRDLK 120
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 37523586 145 PANLIWGEDGRIYLIDFG-AVQAVSAPEKTMTVVGTYRLYAPGAVRG-PHGPCV 196
Cdd:cd05123 121 PENILLDSDGHIKLTDFGlAKELSSDGDRTYTFCGTPEYLAPEVLLGkGYGKAV 174
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
28-196 1.15e-18

Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Aurora kinases are key regulators of mitosis and are essential for the accurate and equal division of genomic material from parent to daughter cells. Yeast contains only one Aurora kinase while most higher eukaryotes have two. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). Aurora-A regulates cell cycle events from the late S-phase through the M-phase including centrosome maturation, mitotic entry, centrosome separation, spindle assembly, chromosome alignment, cytokinesis, and mitotic exit. Aurora-A activation depends on its autophosphorylation and binding to the microtubule-associated protein TPX2. Aurora-B is most active at the transition during metaphase to the end of mitosis. It is critical for accurate chromosomal segregation, cytokinesis, protein localization to the centrosome and kinetochore, correct microtubule-kinetochore attachments, and regulation of the mitotic checkpoint. Aurora-C is mainly expressed in meiotically dividing cells; it was originally discovered in mice as a testis-specific STK called Aie1. Both Aurora-B and -C are chromosomal passenger proteins that can form complexes with INCENP and survivin, and they may have redundant cellular functions. The Aurora subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270909 [Multi-domain]  Cd Length: 253  Bit Score: 81.75  E-value: 1.15e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  28 WLAAEEKTGQTVTLKALYFgegALWQDFKL---FEREAETLQSLSHSRIPRQRDAFWWEQpegnYFCLIQDFIPGQSLEA 104
Cdd:cd14007  17 YLAREKKSGFIVALKVISK---SQLQKSGLehqLRREIEIQSHLRHPNILRLYGYFEDKK----RIYLILEYAPNGELYK 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586 105 SVRNLGPLPEAEVRTIAAEVLEILIYLHrqSPPVIHRDLTPANLIWGEDGRIYLIDFG-AVQAVSapEKTMTVVGTYRLY 183
Cdd:cd14007  90 ELKKQKRFDEKEAAKYIYQLALALDYLH--SKNIIHRDIKPENILLGSNGELKLADFGwSVHAPS--NRRKTFCGTLDYL 165
                       170
                ....*....|....
gi 37523586 184 APGAVRG-PHGPCV 196
Cdd:cd14007 166 PPEMVEGkEYDYKV 179
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
12-194 2.79e-18

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


Pssm-ID: 270692 [Multi-domain]  Cd Length: 254  Bit Score: 80.71  E-value: 2.79e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  12 CYRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFGEGalwQDFKLFEREAETLQSLSHSRIPRQRDAFWweqpEGNYFC 91
Cdd:cd05122   1 LFEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESK---EKKESILNEIAILKKCKHPNIVKYYGSYL----KKDELW 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  92 LIQDFIPGQSLEASVRNL-GPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSAP 170
Cdd:cd05122  74 IVMEFCSGGSLKDLLKNTnKTLTEQQIAYVCKEVLKGLEYLHSHG--IIHRDIKAANILLTSDGEVKLIDFGLSAQLSDG 151
                       170       180
                ....*....|....*....|....*.
gi 37523586 171 EKTMTVVGT-YRLyAPGAVRG-PHGP 194
Cdd:cd05122 152 KTRNTFVGTpYWM-APEVIQGkPYGF 176
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
13-164 2.88e-18

Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes cyclin G-Associated Kinase (GAK), Drosophila melanogaster Numb-Associated Kinase (NAK)-like proteins, and similar protein kinases. GAK plays regulatory roles in clathrin-mediated membrane trafficking, the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses. NAK plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. The GAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270887 [Multi-domain]  Cd Length: 272  Bit Score: 80.84  E-value: 2.88e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFGEgalWQDFKLFEREAETLQSLS-HSRIPRQRDAFWWEQPEGNYFC 91
Cdd:cd13985   2 YQVTKQLGEGGFSYVYLAHDVNTGRRYALKRMYFND---EEQLRVAIKEIEIMKRLCgHPNIVQYYDSAILSSEGRKEVL 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 37523586  92 LIQDFIPGQ---SLEASVRNlgPLPEAEVRTIAAEVLEILIYLHRQSPPVIHRDLTPANLIWGEDGRIYLIDFGAV 164
Cdd:cd13985  79 LLMEYCPGSlvdILEKSPPS--PLSEEEVLRIFYQICQAVGHLHSQSPPIIHRDIKIENILFSNTGRFKLCDFGSA 152
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
35-189 6.44e-18

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


Pssm-ID: 270904 [Multi-domain]  Cd Length: 253  Bit Score: 79.60  E-value: 6.44e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  35 TGQTVTLKalyF--GEGALWQDFKLFEREAETLQSLSHSRIPRQRDAFWWEQPegnyFCLIQDFIPG---QSLEASvrnl 109
Cdd:cd14002  25 TGQVVALK---FipKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKE----FVVVTEYAQGelfQILEDD---- 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586 110 GPLPEAEVRTIAAEVLEILIYLHrqSPPVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSAPEKTMTVV-GTyRLY-APGA 187
Cdd:cd14002  94 GTLPEEEVRSIAKQLVSALHYLH--SNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLTSIkGT-PLYmAPEL 170

                ..
gi 37523586 188 VR 189
Cdd:cd14002 171 VQ 172
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
13-190 1.02e-17

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


Pssm-ID: 270795 [Multi-domain]  Cd Length: 260  Bit Score: 79.32  E-value: 1.02e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFG--EGALWQDFKLFEREAETLQSLSHSRIPRqrdaFWWEQPEGNYF 90
Cdd:cd06625   2 WKQGKLLGQGAFGQVYLCYDADTGRELAVKQVEIDpiNTEASKEVKALECEIQLLKNLQHERIVQ----YYGCLQDEKSL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  91 CLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFGA---VQAV 167
Cdd:cd06625  78 SIFMEYMPGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNM--IVHRDIKGANILRDSNGNVKLGDFGAskrLQTI 155
                       170       180
                ....*....|....*....|...
gi 37523586 168 SAPEKTMTVVGTYRLYAPGAVRG 190
Cdd:cd06625 156 CSSTGMKSVTGTPYWMSPEVING 178
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
60-162 5.28e-17

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270892 [Multi-domain]  Cd Length: 279  Bit Score: 77.36  E-value: 5.28e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  60 REAETLQSLSHSRIPRQRDAFwweQPEGNYFCLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSPPVI 139
Cdd:cd13990  53 REYEIHKSLDHPRIVKLYDVF---EIDTDSFCTVLEYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKPPII 129
                        90       100
                ....*....|....*....|....*.
gi 37523586 140 HRDLTPANLIWGED---GRIYLIDFG 162
Cdd:cd13990 130 HYDLKPGNILLHSGnvsGEIKITDFG 155
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
13-190 1.99e-16

Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Rad53 and Cds1 are the checkpoint kinase 2 (Chk2) homologs found in budding and fission yeast, respectively. They play a central role in the cell's response to DNA lesions to prevent genome rearrangements and maintain genome integrity. They are phosphorylated in response to DNA damage and incomplete replication, and are essential for checkpoint control. They help promote DNA repair by stalling the cell cycle prior to mitosis in the presence of DNA damage. The Rad53/Cds1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271000 [Multi-domain]  Cd Length: 265  Bit Score: 75.59  E-value: 1.99e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFGEGALWQ-DFKLFEREAETLQSLSHSRIPRQRDafWWEQPEgnYFC 91
Cdd:cd14098   2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKVAGNDkNLQLFQREINILKSLEHPGIVRLID--WYEDDQ--HIY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  92 LIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPAN-LIWGEDGRIYLI-DFGAVQAVSA 169
Cdd:cd14098  78 LVMEYVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMG--ITHRDLKPENiLITQDDPVIVKIsDFGLAKVIHT 155
                       170       180
                ....*....|....*....|.
gi 37523586 170 PEKTMTVVGTYRLYAPGAVRG 190
Cdd:cd14098 156 GTFLVTFCGTMAYLAPEILMS 176
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
53-185 2.88e-16

Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNKs comprise a subfamily of STKs with an unusual placement of a catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. They are also involved in cell signaling, survival, proliferation, and organ development. WNKs are activated by hyperosmotic or low-chloride hypotonic stress and they function upstream of SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. There are four vertebrate WNKs which show varying expression patterns. WNK1 and WNK2 are widely expressed while WNK3 and WNK4 show a more restricted expression pattern. Because mutations in human WNK1 and WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension (due to increased sodium reabsorption) and hyperkalemia (due to impaired renal potassium secretion), there are more studies conducted on these two proteins, compared to WNK2 and WNK3. The WNK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 74.95  E-value: 2.88e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  53 QDFKLFEREAETLQSLSHSRIPRQRDAfwWEQPEGNYFCLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLH 132
Cdd:cd13983  42 AERQRFKQEIEILKSLKHPNIIKFYDS--WESKSKKEVIFITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLH 119
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 37523586 133 RQSPPVIHRDLTPANL-IWGEDGRIYLIDFGaVQAVSAPEKTMTVVGTYRLYAP 185
Cdd:cd13983 120 TRDPPIIHRDLKCDNIfINGNTGEVKIGDLG-LATLLRQSFAKSVIGTPEFMAP 172
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
87-190 4.96e-16

Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include Saccharomyces cerevisiae Rim15, Schizosaccharomyces pombe cek1, and similar fungal proteins. They contain a central catalytic domain, which contains an insert relative to MAST kinases. In addition, Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. Rim15 (or Rim15p) functions as a regulator of meiosis. It acts as a downstream effector of PKA and regulates entry into stationary phase (G0). Thus, it plays a crucial role in regulating yeast proliferation, differentiation, and aging. Cek1 may facilitate progression of mitotic anaphase. The Rim15-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270762 [Multi-domain]  Cd Length: 263  Bit Score: 74.44  E-value: 4.96e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  87 GNYFCLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFGAVQA 166
Cdd:cd05611  69 KDYLYLVMEYLNGGDCASLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRG--IIHRDIKPENLLIDQTGHLKLTDFGLSRN 146
                        90       100
                ....*....|....*....|....
gi 37523586 167 VSAPEKTMTVVGTYRLYAPGAVRG 190
Cdd:cd05611 147 GLEKRHNKKFVGTPDYLAPETILG 170
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
29-179 7.65e-16

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


Pssm-ID: 270687 [Multi-domain]  Cd Length: 258  Bit Score: 74.05  E-value: 7.65e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  29 LAAEEKTGQTVTLKALYfGEGALWQDFKLFEREAETLQSLSHSRIPRQRDAFwwEqpEGNYFCLIQDFIPGQSL-EASVR 107
Cdd:cd05117  18 LAVHKKTGEEYAVKIID-KKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVF--E--DDKNLYLVMELCTGGELfDRIVK 92
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37523586 108 NlGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIW---GEDGRIYLIDFGAVQAVSAPEKTMTVVGT 179
Cdd:cd05117  93 K-GSFSEREAAKIMKQILSAVAYLHSQG--IVHRDLKPENILLaskDPDSPIKIIDFGLAKIFEEGEKLKTVCGT 164
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
60-172 1.54e-15

Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDK1 carries an N-terminal catalytic domain and a C-terminal pleckstrin homology (PH) domain that binds phosphoinositides. It phosphorylates the activation loop of AGC kinases that are regulated by PI3K such as PKB, SGK, and PKC, among others, and is crucial for their activation. Thus, it contributes in regulating many processes including metabolism, growth, proliferation, and survival. PDK1 also has the ability to autophosphorylate and is constitutively active in mammalian cells. It is essential for normal embryo development and is important in regulating cell volume. The PDK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270733 [Multi-domain]  Cd Length: 278  Bit Score: 73.40  E-value: 1.54e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  60 REAETLQSLSHSRIPRqrdAFWWEQPEGN-YFCLiqDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppV 138
Cdd:cd05581  50 IEKEVLSRLAHPGIVK---LYYTFQDESKlYFVL--EYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKG--I 122
                        90       100       110
                ....*....|....*....|....*....|....
gi 37523586 139 IHRDLTPANLIWGEDGRIYLIDFGAVQAVSAPEK 172
Cdd:cd05581 123 IHRDLKPENILLDEDMHIKITDFGTAKVLGPDSS 156
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
60-185 1.60e-15

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


Pssm-ID: 270724 [Multi-domain]  Cd Length: 262  Bit Score: 73.03  E-value: 1.60e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  60 REAETLQSLSHSRIPRQRDAFWWEQpegnYFCLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVI 139
Cdd:cd05572  42 SEKEILEECNSPFIVKLYRTFKDKK----YLYMLMEYCLGGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRG--II 115
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 37523586 140 HRDLTPANLIWGEDGRIYLIDFGAVQAVSAPEKTMTVVGTYRLYAP 185
Cdd:cd05572 116 YRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRKTWTFCGTPEYVAP 161
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
36-185 2.46e-15

Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed mainly of MAP3Ks and similar proteins, including TGF-beta Activated Kinase-1 (TAK1, also called MAP3K7), MAP3K12, MAP3K13, Mixed lineage kinase (MLK), MLK-Like mitogen-activated protein Triple Kinase (MLTK), and Raf (Rapidly Accelerated Fibrosarcoma) kinases. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Also included in this subfamily is the pseudokinase Kinase Suppressor of Ras (KSR), which is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway.


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 72.19  E-value: 2.46e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  36 GQTVTLKALYFGEGALWQdFKLFEREAETLQSLSHSRIPRQRDAFwweqPEGNYFCLIQDFIPGQSLEASVRN-LGPLPE 114
Cdd:cd13999  16 GTDVAIKKLKVEDDNDEL-LKEFRREVSILSKLRHPNIVQFIGAC----LSPPPLCIVTEYMPGGSLYDLLHKkKIPLSW 90
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37523586 115 AEVRTIAAEVLEILIYLHrqSPPVIHRDLTPANLIWGEDGRIYLIDFG-AVQAVSAPEKTMTVVGTYRLYAP 185
Cdd:cd13999  91 SLRLKIALDIARGMNYLH--SPPIIHRDLKSLNILLDENFTVKIADFGlSRIKNSTTEKMTGVVGTPRWMAP 160
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
19-188 4.78e-15

Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of the subfamily include SLK, STK10 (also called LOK for Lymphocyte-Oriented Kinase), SmSLK (Schistosoma mansoni SLK), and related proteins. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It also plays a role in mediating actin reorganization. STK10 is responsible in regulating the CD28 responsive element in T cells, as well as leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. SmSLK is capable of activating the MAPK Jun N-terminal kinase (JNK) pathway in human embryonic kidney cells as well as in Xenopus oocytes. It may participate in regulating MAPK cascades during host-parasite interactions. The SLK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132942 [Multi-domain]  Cd Length: 280  Bit Score: 72.08  E-value: 4.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  19 LGANGTRQTWLAAEEKTGQTVTLKALYFGEGALWQDFKLferEAETLQSLSHSRIPRQRDAFWWEqpeGNYFCLIQdFIP 98
Cdd:cd06611  13 LGDGAFGKVYKAQHKETGLFAAAKIIQIESEEELEDFMV---EIDILSECKHPNIVGLYEAYFYE---NKLWILIE-FCD 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  99 GQSLEASVRNLG-PLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFGavqaVSAP-----EK 172
Cdd:cd06611  86 GGALDSIMLELErGLTEPQIRYVCRQMLEALNFLHSHK--VIHRDLKAGNILLTLDGDVKLADFG----VSAKnkstlQK 159
                       170
                ....*....|....*.
gi 37523586 173 TMTVVGTYRLYAPGAV 188
Cdd:cd06611 160 RDTFIGTPYWMAPEVV 175
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
13-193 5.01e-15

Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PLKs play important roles in cell cycle progression and in DNA damage responses. They regulate mitotic entry, mitotic exit, and cytokinesis. In general PLKs contain an N-terminal catalytic kinase domain and a C-terminal regulatory polo box domain (PBD), which is comprised by two bipartite polo-box motifs (or polo boxes) and is involved in protein interactions. PLKs derive their names from homology to polo, a kinase first identified in Drosophila. There are five mammalian PLKs (PLK1-5) from distinct genes. There is good evidence that PLK1 may function as an oncogene while PLK2-5 have tumor suppressive properties. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. PLK2 functions in G1 progression, S-phase arrest, and centriole duplication. PLK3 regulates angiogenesis and responses to DNA damage. PLK4 is required for late mitotic progression, cell survival, and embryonic development. PLK5 was first identified as a pseudogene containing a stop codon within the kinase domain, however, both murine and human genes encode expressed proteins. PLK5 functions in cell cycle arrest.


Pssm-ID: 271001 [Multi-domain]  Cd Length: 258  Bit Score: 71.82  E-value: 5.01e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLK----ALYFGEGALwqdfKLFEREAETLQSLSHSRIPRQRDAFwweQPEGN 88
Cdd:cd14099   3 YRRGKFLGKGGFAKCYEVTDMSTGKVYAGKvvpkSSLTKPKQR----EKLKSEIKIHRSLKHPNIVKFHDCF---EDEEN 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  89 YFcLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFG-AVQAV 167
Cdd:cd14099  76 VY-ILLELCSNGSLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNR--IIHRDLKLGNLFLDENMNVKIGDFGlAARLE 152
                       170       180
                ....*....|....*....|....*.
gi 37523586 168 SAPEKTMTVVGTYRLYAPGAVRGPHG 193
Cdd:cd14099 153 YDGERKKTLCGTPNYIAPEVLEKKKG 178
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
61-188 7.30e-15

Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase or LOK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK10/LOK is also called polo-like kinase kinase 1 in Xenopus (xPlkk1). It is highly expressed in lymphocytes and is responsible in regulating leukocyte function associated antigen (LFA-1)-mediated lymphocyte adhesion. It plays a role in regulating the CD28 responsive element in T cells, and may also function as a regulator of polo-like kinase 1 (Plk1), a protein which is overexpressed in multiple tumor types. The STK10 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132975 [Multi-domain]  Cd Length: 292  Bit Score: 71.99  E-value: 7.30e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  61 EAETLQSLSHSRIPRQRDAFWWEqpeGNYFCLIQdFIPGQSLEASVRNLGP-LPEAEVRTIAAEVLEILIYLHrqSPPVI 139
Cdd:cd06644  59 EIEILATCNHPYIVKLLGAFYWD---GKLWIMIE-FCPGGAVDAIMLELDRgLTEPQIQVICRQMLEALQYLH--SMKII 132
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 37523586 140 HRDLTPANLIWGEDGRIYLIDFG-AVQAVSAPEKTMTVVGTYRLYAPGAV 188
Cdd:cd06644 133 HRDLKAGNVLLTLDGDIKLADFGvSAKNVKTLQRRDSFIGTPYWMAPEVV 182
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
55-185 1.15e-14

Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent Protein Kinase Kinase, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Both LKB1 and CaMKKs can phosphorylate and activate AMP-activated protein kinase (AMPK). LKB1, also called STK11, serves as a master upstream kinase that activates AMPK and most AMPK-like kinases. LKB1 and AMPK are part of an energy-sensing pathway that links cell energy to metabolism and cell growth. They play critical roles in the establishment and maintenance of cell polarity, cell proliferation, cytoskeletal organization, as well as T-cell metabolism, including T-cell development, homeostasis, and effector function. CaMKKs are upstream kinases of the CaM kinase cascade that phosphorylate and activate CaMKI and CamKIV. They may also phosphorylate other substrates including PKB and AMPK. Vertebrates contain two CaMKKs, CaMKK1 (or alpha) and CaMKK2 (or beta). CaMKK1 is involved in the regulation of glucose uptake in skeletal muscles. CaMKK2 is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. The LKB1/CaMKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270910 [Multi-domain]  Cd Length: 267  Bit Score: 70.66  E-value: 1.15e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  55 FKLFEREAETLQSLSHSRIPRQRDAFwwEQPEGNYFCLIQDFIPGQSLEA--SVRNLGPLPEAEVRTIAAEVLEILIYLH 132
Cdd:cd14008  48 LDDVRREIAIMKKLDHPNIVRLYEVI--DDPESDKLYLVLEYCEGGPVMEldSGDRVPPLPEETARKYFRDLVLGLEYLH 125
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 37523586 133 RQSppVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSAPEKTMT-VVGTYRLYAP 185
Cdd:cd14008 126 ENG--IVHRDIKPENLLLTADGTVKISDFGVSEMFEDGNDTLQkTAGTPAFLAP 177
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
88-196 1.86e-14

Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAST kinases, MAST-like (MASTL) kinases (also called greatwall kinase or Gwl), and fungal kinases with similarity to Saccharomyces cerevisiae Rim15 and Schizosaccharomyces pombe cek1. MAST kinases contain an N-terminal domain of unknown function, a central catalytic domain, and a C-terminal PDZ domain that mediates protein-protein interactions. MASTL kinases carry only a catalytic domain which contains a long insert relative to other kinases. The fungal kinases in this subfamily harbor other domains in addition to a central catalytic domain, which like in MASTL, also contains an insert relative to MAST kinases. Rim15 contains a C-terminal signal receiver (REC) domain while cek1 contains an N-terminal PAS domain. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MASTL/Gwl is involved in the regulation of mitotic entry, mRNA stabilization, and DNA checkpoint recovery. The fungal proteins Rim15 and cek1 are involved in the regulation of meiosis and mitosis, respectively. The MAST-like kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270731 [Multi-domain]  Cd Length: 272  Bit Score: 70.32  E-value: 1.86e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  88 NYFCLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFG----- 162
Cdd:cd05579  66 KNLYLVMEYLPGGDLYSLLENVGALDEDVARIYIAEIVLALEYLHSHG--IIHRDLKPDNILIDANGHLKLTDFGlskvg 143
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 37523586 163 -----------AVQAVSAPEKTMTVVGTYRLYAPGAVRG-PHGPCV 196
Cdd:cd05579 144 lvrrqiklsiqKKSNGAPEKEDRRIVGTPDYLAPEILLGqGHGKTV 189
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
13-185 3.01e-14

Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The CMGC family consists of Cyclin-Dependent protein Kinases (CDKs), Mitogen-activated protein kinases (MAPKs) such as Extracellular signal-regulated kinase (ERKs), c-Jun N-terminal kinases (JNKs), and p38, and other kinases. CDKs belong to a large subfamily of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. MAPKs serve as important mediators of cellular responses to extracellular signals. They control critical cellular functions including differentiation, proliferation, migration, and apoptosis. They are also implicated in the pathogenesis of many diseases including multiple types of cancer, stroke, diabetes, and chronic inflammation. Other members of the CMGC family include casein kinase 2 (CK2), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK), Glycogen Synthase Kinase 3 (GSK3), among many others. The CMGC family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270688 [Multi-domain]  Cd Length: 249  Bit Score: 69.19  E-value: 3.01e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKAL----YFGEGALwqdfklfeREAETLQSL----SHSRIPRQRDAFWWeq 84
Cdd:cd05118   1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKIkndfRHPKAAL--------REIKLLKHLndveGHPNIVKLLDVFEH-- 70
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  85 PEGNYFCLIQDFIpGQSLEASVRNLG-PLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPAN-LIWGEDGRIYLIDFG 162
Cdd:cd05118  71 RGGNHLCLVFELM-GMNLYELIKDYPrGLPLDLIKSYLYQLLQALDFLHSNG--IIHRDLKPENiLINLELGQLKLADFG 147
                       170       180
                ....*....|....*....|....
gi 37523586 163 AvqAVSAPEKTMTV-VGTYRLYAP 185
Cdd:cd05118 148 L--ARSFTSPPYTPyVATRWYRAP 169
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
61-188 3.64e-14

Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SLK promotes apoptosis through apoptosis signal-regulating kinase 1 (ASK1) and the mitogen-activated protein kinase (MAPK) p38. It acts as a MAPK kinase kinase by phosphorylating ASK1, resulting in the phosphorylation of p38. SLK also plays a role in mediating actin reorganization. It is part of a microtubule-associated complex that is targeted at adhesion sites, and is required in focal adhesion turnover and in regulating cell migration. The SLK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 69.67  E-value: 3.64e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  61 EAETLQSLSHSRIPRQRDAFWWEQpegNYFCLIQdFIPGQSLEASVRNLG-PLPEAEVRTIAAEVLEILIYLHRQSppVI 139
Cdd:cd06643  52 EIDILASCDHPNIVKLLDAFYYEN---NLWILIE-FCAGGAVDAVMLELErPLTEPQIRVVCKQTLEALVYLHENK--II 125
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 37523586 140 HRDLTPANLIWGEDGRIYLIDFG-AVQAVSAPEKTMTVVGTYRLYAPGAV 188
Cdd:cd06643 126 HRDLKAGNILFTLDGDIKLADFGvSAKNTRTLQRRDSFIGTPYWMAPEVV 175
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
17-194 5.17e-14

Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of plant MAPK kinase kinases (MAPKKKs) including Arabidopsis thaliana MEKK1 and MAPKKK3. Arabidopsis thaliana MEKK1 activates MPK4, a MAPK that regulates systemic acquired resistance. MEKK1 also participates in the regulation of temperature-sensitive and tissue-specific cell death. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The plant MEKK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270802 [Multi-domain]  Cd Length: 259  Bit Score: 68.97  E-value: 5.17e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  17 RLLGANGTRQTWLAAEEKTGQTVTLKALYFG-EGALWQD-FKLFEREAETLQSLSHSRIPRQRDAfwweQPEGNYFCLIQ 94
Cdd:cd06632   6 QLLGSGSFGSVYEGFNGDTGDFFAVKEVSLVdDDKKSREsVKQLEQEIALLSKLRHPNIVQYYGT----EREEDNLYIFL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  95 DFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSAPEKTM 174
Cdd:cd06632  82 EYVPGGSIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRN--TVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAK 159
                       170       180
                ....*....|....*....|
gi 37523586 175 TVVGTYRLYAPGAVRGPHGP 194
Cdd:cd06632 160 SFKGSPYWMAPEVIMQKNSG 179
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
13-175 1.12e-13

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK7 plays essential roles in the cell cycle and in transcription. It associates with cyclin H and MAT1 and acts as a CDK-Activating Kinase (CAK) by phosphorylating and activating cell cycle CDKs (CDK1/2/4/6). In the brain, it activates CDK5. CDK7 is also a component of the general transcription factor TFIIH, which phosphorylates the C-terminal domain (CTD) of RNA polymerase II when it is bound with unphosphorylated DNA, as present in the pre-initiation complex. Following phosphorylation, the CTD dissociates from the DNA which allows transcription initiation. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. The CDK7 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 68.37  E-value: 1.12e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGaNGTRQT-WLAAEEKTGQTVTLKALYFGEGALWQD---FKLFeREAETLQSLSHSRIPRQRDAFwweqPEGN 88
Cdd:cd07841   2 YEKGKKLG-EGTYAVvYKARDKETGRIVAIKKIKLGERKEAKDginFTAL-REIKLLQELKHPNIIGLLDVF----GHKS 75
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  89 YFCLIQDFIPGqSLEASVRN-LGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFGAVQAV 167
Cdd:cd07841  76 NINLVFEFMET-DLEKVIKDkSIVLTPADIKSYMLMTLRGLEYLHSNW--ILHRDLKPNNLLIASDGVLKLADFGLARSF 152

                ....*...
gi 37523586 168 SAPEKTMT 175
Cdd:cd07841 153 GSPNRKMT 160
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
34-189 1.22e-13

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


Pssm-ID: 270822 [Multi-domain]  Cd Length: 277  Bit Score: 68.27  E-value: 1.22e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  34 KTGQTVTLKALYFGEGAlwQDFKLFEREAETLQSLSHSRIPRQRDaFWWEQPEGNYFCLIQDFIPGqsleASVRNL---G 110
Cdd:cd06917  24 KTGRVVALKVLNLDTDD--DDVSDIQKEVALLSQLKLGQPKNIIK-YYGSYLKGPSLWIIMDYCEG----GSIRTLmraG 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586 111 PLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFG-AVQAVSAPEKTMTVVGTYRLYAPGAVR 189
Cdd:cd06917  97 PIAERYIAVIMREVLVALKFIHKDG--IIHRDIKAANILVTNTGNVKLCDFGvAASLNQNSSKRSTFVGTPYWMAPEVIT 174
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
34-179 1.60e-13

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


Pssm-ID: 132954 [Multi-domain]  Cd Length: 264  Bit Score: 67.62  E-value: 1.60e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  34 KTGQTVTLKALYFGEGALWQdfKLFEREAETLQSLSHSRIPRQRDAFwweqPEGNYFCLIQDFIPGQSLEASVRNLGPLP 113
Cdd:cd06623  24 PTGKIYALKKIHVDGDEEFR--KQLLRELKTLRSCESPYVVKCYGAF----YKEGEISIVLEYMDGGSLADLLKKVGKIP 97
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 37523586 114 EAEVRTIAAEVLEILIYLHRQSPpVIHRDLTPANLIWGEDGRIYLIDFGAVQAVS-APEKTMTVVGT 179
Cdd:cd06623  98 EPVLAYIARQILKGLDYLHTKRH-IIHRDIKPSNLLINSKGEVKIADFGISKVLEnTLDQCNTFVGT 163
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
13-185 1.62e-13

Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKs belong to a large family of STKs that are regulated by their cognate cyclins. Together, they are involved in the control of cell-cycle progression, transcription, and neuronal function. CDKs are partly regulated by their subcellular localization, which defines substrate phosphorylation and the resulting specific function. CDK1, CDK2, CDK4, and CDK6 have well-defined functions in the cell cycle, such as the regulation of the early G1 phase by CDK4 or CDK6, the G1/S phase transition by CDK2, or the entry of mitosis by CDK1. They also exhibit overlapping cyclin specificity and functions in certain conditions. Knockout mice with a single CDK deleted remain viable with specific phenotypes, showing that some CDKs can compensate for each other. For example, CDK4 can compensate for the loss of CDK6, however, double knockout mice with both CDK4 and CDK6 deleted die in utero. CDK8 and CDK9 are mainly involved in transcription while CDK5 is implicated in neuronal function. CDK7 plays essential roles in both the cell cycle as a CDK-Activating Kinase (CAK) and in transcription as a component of the general transcription factor TFIIH. The CDK-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270823 [Multi-domain]  Cd Length: 282  Bit Score: 67.89  E-value: 1.62e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGaNGTRQT-WLAAEEKTGQTVTLKAL---YFGEG----ALwqdfklfeREAETLQSLSHSRIPRQRDAFwweq 84
Cdd:cd07829   1 YEKLEKLG-EGTYGVvYKAKDKKTGEIVALKKIrldNEEEGipstAL--------REISLLKELKHPNIVKLLDVI---- 67
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  85 PEGNYFCLIQDFIPgQSLEASVRNL-GPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFGA 163
Cdd:cd07829  68 HTENKLYLVFEYCD-QDLKKYLDKRpGPLPPNLIKSIMYQLLRGLAYCHSHR--ILHRDLKPQNLLINRDGVLKLADFGL 144
                       170       180
                ....*....|....*....|....*
gi 37523586 164 VQAVSAPEKTMT-VVGT--YRlyAP 185
Cdd:cd07829 145 ARAFGIPLRTYThEVVTlwYR--AP 167
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
30-162 1.67e-13

Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CCRK was previously called p42. It is a Cyclin-Dependent Kinase (CDK)-Activating Kinase (CAK) which is essential for the activation of CDK2. It is indispensable for cell growth and has been implicated in the progression of glioblastoma multiforme. In the heart, a splice variant of CCRK with a different C-terminal half is expressed; this variant promotes cardiac cell growth and survival and is significantly down-regulated during the development of heart failure. The CCRK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270826 [Multi-domain]  Cd Length: 287  Bit Score: 67.74  E-value: 1.67e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  30 AAEEKTGQTVTLKALY-------FGEGALwqdfklfeREAETLQSL-SHSRIPRQRDAFwweqPEGNYFCLIQDFIPGqS 101
Cdd:cd07832  19 AKDRETGETVALKKVAlrkleggIPNQAL--------REIKALQACqGHPYVVKLRDVF----PHGTGFVLVFEYMLS-S 85
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 37523586 102 LEASVRNL-GPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFG 162
Cdd:cd07832  86 LSEVLRDEeRPLTEAQVKRYMRMLLKGVAYMHANR--IMHRDLKPANLLISSTGVLKIADFG 145
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
53-162 2.88e-13

Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. YSK4 is a putative MAPKKK, whose mammalian gene has been isolated. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The YSK4 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 67.08  E-value: 2.88e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  53 QDFKLFEREAETLQSLSHSRIPRqrdaFWWEQPEGNYFCLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLH 132
Cdd:cd06631  45 KEYEKLQEEVDLLKTLKHVNIVG----YLGTCLEDNVVSIFMEFVPGGSIASILARFGALEEPVFCRYTKQILEGVAYLH 120
                        90       100       110
                ....*....|....*....|....*....|
gi 37523586 133 RQSppVIHRDLTPANLIWGEDGRIYLIDFG 162
Cdd:cd06631 121 NNN--VIHRDIKGNNIMLMPNGVIKLIDFG 148
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
16-185 3.53e-13

Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the cAMP-dependent protein kinases, PKA and PRKX, and similar proteins. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. PRKX is also reulated by the R subunit and is is present in many tissues including fetal and adult brain, kidney, and lung. It is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PKA-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270732 [Multi-domain]  Cd Length: 290  Bit Score: 66.83  E-value: 3.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  16 VRLLGANGTRQTWLAAEEKTGQTVTLKALyfgegALWQDFKLFE-----REAETLQSLSHSRIPRQRDAFwweQPEGNYF 90
Cdd:cd05580   6 LKTLGTGSFGRVRLVKHKDSGKYYALKIL-----KKAKIIKLKQvehvlNEKRILSEVRHPFIVNLLGSF---QDDRNLY 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  91 cLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFGAVQAVsaP 170
Cdd:cd05580  78 -MVMEYVPGGELFSLLRRSGRFPNDVAKFYAAEVVLALEYLHSLD--IVYRDLKPENLLLDSDGHIKITDFGFAKRV--K 152
                       170
                ....*....|....*
gi 37523586 171 EKTMTVVGTYRLYAP 185
Cdd:cd05580 153 DRTYTLCGTPEYLAP 167
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
13-161 3.56e-13

Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phototropins are blue-light receptors that control responses such as phototropism, stromatal opening, and chloroplast movement in order to optimize the photosynthetic efficiency of plants. They are light-activated STKs that contain an N-terminal photosensory domain and a C-terminal catalytic domain. The N-terminal domain contains two LOV (Light, Oxygen or Voltage) domains that binds FMN. Photoexcitation of the LOV domains results in autophosphorylation at multiple sites and activation of the catalytic domain. In addition to plant phototropins, included in this subfamily are predominantly uncharacterized fungal STKs whose catalytic domains resemble the phototropin kinase domain. One protein from Neurospora crassa is called nrc-2, which plays a role in growth and development by controlling entry into the conidiation program. The phototropin-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270726 [Multi-domain]  Cd Length: 316  Bit Score: 67.26  E-value: 3.56e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFGEGALWQDFKLFEREAETLQSLSHSRIPrqrdAFWWEQPEGNYFCL 92
Cdd:cd05574   3 FKKIKLLGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRNKVKRVLTEREILATLDHPFLP----TLYASFQTSTHLCF 78
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 37523586  93 IQDFIPGQSLEA--SVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDF 161
Cdd:cd05574  79 VMDYCPGGELFRllQKQPGKRLPEEVARFYAAEVLLALEYLHLLG--FVYRDLKPENILLHESGHIMLTDF 147
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
19-190 3.84e-13

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. PAK deregulation is associated with tumor development. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). Group II PAKs contain a PBD and a catalytic domain, but lack other motifs found in group I PAKs. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. Group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX; no such binding has been demonstrated for group II PAKs. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270789 [Multi-domain]  Cd Length: 255  Bit Score: 66.47  E-value: 3.84e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  19 LGANGTRQTWLAAEEKTGQTVTLKALYFGEgalwQDFKLFEREAETLQSLSHSRIPRQRDAFWweqpEGNYFCLIQDFIP 98
Cdd:cd06614   8 IGEGASGEVYKATDRATGKEVAIKKMRLRK----QNKELIINEILIMKECKHPNIVDYYDSYL----VGDELWVVMEYMD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  99 GQSLEASVR-NLGPLPEAEVRTIAAEVLEILIYLHRQspPVIHRDLTPANLIWGEDGRIYLIDFG-AVQAVSAPEKTMTV 176
Cdd:cd06614  80 GGSLTDIITqNPVRMNESQIAYVCREVLQGLEYLHSQ--NVIHRDIKSDNILLSKDGSVKLADFGfAAQLTKEKSKRNSV 157
                       170
                ....*....|....
gi 37523586 177 VGTYRLYAPGAVRG 190
Cdd:cd06614 158 VGTPYWMAPEVIKR 171
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
17-188 7.49e-13

Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein Kinase Kinase Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include the MAPKKKs Schizosaccharomyces pombe Byr2, Saccharomyces cerevisiae and Cryptococcus neoformans Ste11, and related proteins. They contain an N-terminal SAM (sterile alpha-motif) domain, which mediates protein-protein interaction, and a C-terminal catalytic domain. MAPKKKs phosphorylate and activate MAPK kinases, which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. Fission yeast Byr2 is regulated by Ras1. It responds to pheromone signaling and controls mating through the MAPK pathway. Budding yeast Ste11 functions in MAPK cascades that regulate mating, high osmolarity glycerol, and filamentous growth responses. The Byr2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 65.63  E-value: 7.49e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  17 RLLGANGTRQTWLAAEEKTGQTVTLKALYFGEGALWQD------FKLFEREAETLQSLSHSRIPRQRDAfwweQPEGNYF 90
Cdd:cd06628   6 ALIGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENKdrkksmLDALQREIALLRELQHENIVQYLGS----SSDANHL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  91 CLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSAp 170
Cdd:cd06628  82 NIFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRG--IIHRDIKGANILVDNKGGIKISDFGISKKLEA- 158
                       170
                ....*....|....*...
gi 37523586 171 EKTMTVVGTYRLYAPGAV 188
Cdd:cd06628 159 NSLSTKNNGARPSLQGSV 176
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
13-190 3.36e-12

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


Pssm-ID: 270819 [Multi-domain]  Cd Length: 264  Bit Score: 63.89  E-value: 3.36e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFGEGA--LWQDFKLFEREAETLQSLSHSRIPRQRDAFwwEQPEGNYF 90
Cdd:cd06653   4 WRLGKLLGRGAFGEVYLCYDADTGRELAVKQVPFDPDSqeTSKEVNALECEIQLLKNLRHDRIVQYYGCL--RDPEEKKL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  91 CLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHrqSPPVIHRDLTPANLIWGEDGRIYLIDFGA---VQAV 167
Cdd:cd06653  82 SIFVEYMPGGSVKDQLKAYGALTENVTRRYTRQILQGVSYLH--SNMIVHRDIKGANILRDSAGNVKLGDFGAskrIQTI 159
                       170       180
                ....*....|....*....|....
gi 37523586 168 SAPEKTM-TVVGTYRLYAPGAVRG 190
Cdd:cd06653 160 CMSGTGIkSVTGTPYWMSPEVISG 183
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
20-196 3.61e-12

Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group I PAKs, also called conventional PAKs, include PAK1, PAK2, and PAK3. Group I PAKs contain a PBD (p21-binding domain) overlapping with an AID (autoinhibitory domain), a C-terminal catalytic domain, SH3 binding sites and a non-classical SH3 binding site for PIX (PAK-interacting exchange factor). They interact with the SH3 domain containing proteins Nck, Grb2 and PIX. Binding of group I PAKs to activated GTPases leads to conformational changes that destabilize the AID, allowing autophosphorylation and full activation of the kinase domain. Known group I PAK substrates include MLCK, Bad, Raf, MEK1, LIMK, Merlin, Vimentin, Myc, Stat5a, and Aurora A, among others. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs are implicated in the regulation of many cellular processes including growth factor receptor-mediated proliferation, cell polarity, cell motility, cell death and survival, and actin cytoskeleton organization. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270814 [Multi-domain]  Cd Length: 261  Bit Score: 63.79  E-value: 3.61e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  20 GANGTrqTWLAAEEKTGQTVTLKALYFGEgalwQDFK-LFEREAETLQSLSHSRIPRQRDAFWweqpEGNYFCLIQDFIP 98
Cdd:cd06647  18 GASGT--VYTAIDVATGQEVAIKQMNLQQ----QPKKeLIINEILVMRENKNPNIVNYLDSYL----VGDELWVVMEYLA 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  99 GQSLEASVRNLGpLPEAEVRTIAAEVLEILIYLHrqSPPVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSaPE--KTMTV 176
Cdd:cd06647  88 GGSLTDVVTETC-MDEGQIAAVCRECLQALEFLH--SNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQIT-PEqsKRSTM 163
                       170       180
                ....*....|....*....|.
gi 37523586 177 VGTYRLYAPGAV-RGPHGPCV 196
Cdd:cd06647 164 VGTPYWMAPEVVtRKAYGPKV 184
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
13-185 3.76e-12

Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this group include human PRKX (X chromosome-encoded protein kinase), Drosophila DC2, and similar proteins. PRKX is present in many tissues including fetal and adult brain, kidney, and lung. The PRKX gene is located in the Xp22.3 subregion and has a homolog called PRKY on the Y chromosome. An abnormal interchange between PRKX aand PRKY leads to the sex reversal disorder of XX males and XY females. PRKX is implicated in granulocyte/macrophage lineage differentiation, renal cell epithelial migration, and tubular morphogenesis in the developing kidney. The PRKX-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270763 [Multi-domain]  Cd Length: 292  Bit Score: 63.99  E-value: 3.76e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFGEGALWQDFKLFEREAETLQSLSHSRIPRqrdaFWWEQPEGNYFCL 92
Cdd:cd05612   3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHNEKRVLKEVSHPFIIR----LFWTEHDQRFLYM 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  93 IQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHrqSPPVIHRDLTPANLIWGEDGRIYLIDFGAVQAVSapEK 172
Cdd:cd05612  79 LMEYVPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLH--SKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLR--DR 154
                       170
                ....*....|...
gi 37523586 173 TMTVVGTYRLYAP 185
Cdd:cd05612 155 TWTLCGTPEYLAP 167
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
13-190 4.00e-12

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 63.91  E-value: 4.00e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYFGEGAL--WQDFKLFEREAETLQSLSHSRIPRQRDAFwwEQPEGNYF 90
Cdd:cd06652   4 WRLGKLLGQGAFGRVYLCYDADTGRELAVKQVQFDPESPetSKEVNALECEIQLLKNLLHERIVQYYGCL--RDPQERTL 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  91 CLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHrqSPPVIHRDLTPANLIWGEDGRIYLIDFGAVQAVS-- 168
Cdd:cd06652  82 SIFMEYMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLH--SNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQti 159
                       170       180
                ....*....|....*....|....
gi 37523586 169 --APEKTMTVVGTYRLYAPGAVRG 190
Cdd:cd06652 160 clSGTGMKSVTGTPYWMSPEVISG 183
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
14-192 4.45e-12

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MAPKKs are dual-specificity PKs that phosphorylate their downstream targets, MAPKs, at specific threonine and tyrosine residues. The MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The pathways involve a triple kinase core cascade comprising the MAPK, which is phosphorylated and activated by a MAPK kinase (MAPKK or MKK or MAP2K), which itself is phosphorylated and activated by a MAPKK kinase (MAPKKK or MKKK or MAP3K). There are three MAPK subfamilies: extracellular signal-regulated kinase (ERK), c-Jun N-terminal kinase (JNK), and p38. In mammalian cells, there are seven MAPKKs (named MKK1-7) and 20 MAPKKKs. Each MAPK subfamily can be activated by at least two cognate MAPKKs and by multiple MAPKKKs. The MAPKK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 63.52  E-value: 4.45e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  14 RPVRLLGANGTRQTWLAAEEKTGQTVTLKALYfgegaLWQDFKLFEREAETLQSLSHSRIPRQRDAFWWEQPEGNYFcLI 93
Cdd:cd06605   4 EYLGELGEGNGGVVSKVRHRPSGQIMAVKVIR-----LEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDIS-IC 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  94 QDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSPpVIHRDLTPANLIWGEDGRIYLIDFGaVQAVSAPEKT 173
Cdd:cd06605  78 MEYMDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHEKHK-IIHRDVKPSNILVNSRGQVKLCDFG-VSGQLVDSLA 155
                       170
                ....*....|....*....
gi 37523586 174 MTVVGTYRLYAPGAVRGPH 192
Cdd:cd06605 156 KTFVGTRSYMAPERISGGK 174
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
13-185 5.99e-12

Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of yeast Kin1, Kin2, and similar proteins. Fission yeast Kin1 is a membrane-associated kinase that is involved in regulating cell surface cohesiveness during interphase. It also plays a role during mitosis, linking actomyosin ring assembly with septum synthesis and membrane closure to ensure separation of daughter cells. Budding yeast Kin1 and Kin2 act downstream of the Rab-GTPase Sec4 and are associated with the exocytic apparatus; they play roles in the secretory pathway. The Kin1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270979 [Multi-domain]  Cd Length: 267  Bit Score: 63.24  E-value: 5.99e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  13 YRPVRLLGANGTRQTWLAAEEKTGQTVTLKALYF-------------GEGALWQDFKLFeREAETLQSLSHSRIPRQRDA 79
Cdd:cd14077   3 WEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIPRasnaglkkerekrLEKEISRDIRTI-REAALSSLLNHPHICRLRDF 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  80 FWweqpEGNYFCLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLI 159
Cdd:cd14077  82 LR----TPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNS--IVHRDLKIENILISKSGNIKII 155
                       170       180
                ....*....|....*....|....*.
gi 37523586 160 DFGAVQAVSAPEKTMTVVGTYRLYAP 185
Cdd:cd14077 156 DFGLSNLYDPRRLLRTFCGSLYFAAP 181
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
34-185 1.41e-11

Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes MAP4K3, MAP4K1, MAP4K2, MAP4K5, and related proteins. Vertebrate members contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K1, also called haematopoietic progenitor kinase 1 (HPK1), is a hematopoietic-specific STK involved in many cellular signaling cascades including MAPK, antigen receptor, apoptosis, growth factor, and cytokine signaling. It participates in the regulation of T cell receptor signaling and T cell-mediated immune responses. MAP4K2 was referred to as germinal center (GC) kinase because of its preferred location in GC B cells. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. It is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). The MAP4K3-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 61.94  E-value: 1.41e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  34 KTGQTVTLKALYFGEGalwQDFKLFEREAETLQSLSHSRIPRQRDAFWWeqpeGNYFCLIQDFIPGQSLEASVRNLGPLP 113
Cdd:cd06613  23 ATGELAAVKVIKLEPG---DDFEIIQQEISMLKECRHPNIVAYFGSYLR----RDKLWIVMEYCGGGSLQDIYQVTGPLS 95
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 37523586 114 EAEVRTIAAEVLEILIYLHRQSppVIHRDLTPANLIWGEDGRIYLIDFG-AVQAVSAPEKTMTVVGTYRLYAP 185
Cdd:cd06613  96 ELQIAYVCRETLKGLAYLHSTG--KIHRDIKGANILLTEDGDVKLADFGvSAQLTATIAKRKSFIGTPYWMAP 166
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
19-162 1.51e-11

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP kinases serve as essential sensors of cellular stress. They are involved in regulating NF-kappaB and MAPK signaling, and are implicated in mediating cellular processes such as apoptosis, necroptosis, differentiation, and survival. RIP kinases contain a homologous N-terminal kinase domain and varying C-terminal domains. Higher vertebrates contain multiple RIP kinases, with mammals harboring at least five members. RIP1 and RIP2 harbor C-terminal domains from the Death domain (DD) superfamily while RIP4 contains ankyrin (ANK) repeats. RIP3 contain a RIP homotypic interaction motif (RHIM) that facilitates binding to RIP1. RIP1 and RIP3 are important in apoptosis and necroptosis, while RIP2 and RIP4 play roles in keratinocyte differentiation and inflammatory immune responses. The RIP subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270880 [Multi-domain]  Cd Length: 263  Bit Score: 62.09  E-value: 1.51e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  19 LGANGTRQTWLAAEEKTGQTVTLKALYFGEGALWQDFKLFeREAETLQSLSHSRIPRQRDAFWWEQPEGnyfcLIQDFIP 98
Cdd:cd13978   1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALL-KEAEKMERARHSYVLPLLGVCVERRSLG----LVMEYME 75
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 37523586  99 GQSLEASV-RNLGPLPEAEVRTIAAEVLEILIYLHRQSPPVIHRDLTPANLIWGEDGRIYLIDFG 162
Cdd:cd13978  76 NGSLKSLLeREIQDVPWSLRFRIIHEIALGMNFLHNMDPPLLHHDLKPENILLDNHFHVKISDFG 140
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
59-190 1.55e-11

Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This family is composed of MLCKs and related MLCK-like kinase domains from giant STKs such as titin, obscurin, SPEG, Unc-89, Trio, kalirin, and Twitchin. Also included in this family are Death-Associated Protein Kinases (DAPKs) and Death-associated protein kinase-Related Apoptosis-inducing protein Kinase (DRAKs). MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. Titin, obscurin, Twitchin, and SPEG are muscle proteins involved in the contractile apparatus. The giant STKs are multidomain proteins containing immunoglobulin (Ig), fibronectin type III (FN3), SH3, RhoGEF, PH and kinase domains. Titin, obscurin, Twitchin, and SPEG contain many Ig domain repeats at the N-terminus, while Trio and Kalirin contain spectrin-like repeats. The MLCK-like family is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270908 [Multi-domain]  Cd Length: 247  Bit Score: 61.90  E-value: 1.55e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 37523586  59 EREAETLQSLSHSRIPRQRDAFwwEQPegNYFCLIQDFIPGQSLEASVRNLGPLPEAEVRTIAAEVLEILIYLHRQSppV 138
Cdd:cd14006  37 LREISILNQLQHPRIIQLHEAY--ESP--TELVLILELCSGGELLDRLAERGSLSEEEVRTYMRQLLEGLQYLHNHH--I 110
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 37523586 139 IHRDLTPANLIW--GEDGRIYLIDFGAVQAVSAPEKTMTVVGTYRLYAPGAVRG 190