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Conserved domains on  [gi|545477471|ref|NP_001269914|]
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tribbles homolog 1 isoform 2 [Homo sapiens]

Protein Classification

protein kinase family protein( domain architecture ID 229378)

protein kinase family protein may catalyze the transfer of the gamma-phosphoryl group from ATP to substrates such as serine/threonine and/or tyrosine residues on proteins, or may be a pseudokinase

CATH:  1.10.510.10
PubMed:  16244704
SCOP:  4003661

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 ...
1-172 6.69e-140

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 cd14023:

Pssm-ID: 473864 [Multi-domain]  Cd Length: 242  Bit Score: 390.56  E-value: 6.69e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKHGCP 80
Cdd:cd14023   71 MHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLESLEDTHIMKGEDDALSDKHGCP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd14023  151 AYVSPEILNTTGTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSER 230
                        170
                 ....*....|..
gi 545477471 161 LTAPEILLHPWF 172
Cdd:cd14023  231 LTAPEILLHPWF 242
 
Name Accession Description Interval E-value
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
1-172 6.69e-140

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 390.56  E-value: 6.69e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKHGCP 80
Cdd:cd14023   71 MHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLESLEDTHIMKGEDDALSDKHGCP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd14023  151 AYVSPEILNTTGTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSER 230
                        170
                 ....*....|..
gi 545477471 161 LTAPEILLHPWF 172
Cdd:cd14023  231 LTAPEILLHPWF 242
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
1-172 4.57e-40

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 136.89  E-value: 4.57e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471     1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteertqlrleslEDTHIM---------KGEDD 71
Cdd:smart00220  84 LFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD------------EDGHVKladfglarqLDPGE 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471    72 ALSDKHGCPAYVSPEILNTTGtYsGKAADVWSLGVMLYTLLVGRYPF-HDSDPSALFSKIRRGQFCIPEH---ISPKARC 147
Cdd:smart00220 152 KLTTFVGTPEYMAPEVLLGKG-Y-GKAVDIWSLGVILYELLTGKPPFpGDDQLLELFKKIGKPKPPFPPPewdISPEAKD 229
                          170       180
                   ....*....|....*....|....*
gi 545477471   148 LIRSLLRREPSERLTAPEILLHPWF 172
Cdd:smart00220 230 LIRKLLVKDPEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
2-172 6.85e-28

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 104.63  E-value: 6.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471    2 HSYVRSRKRLREEEAARLFKQIVSAVAHCHqsaivlgdlKLRKFVfsteertqlrlesledthimkgeddalsdkhGCPA 81
Cdd:pfam00069  86 FDLLSEKGAFSEREAKFIMKQILEGLESGS---------SLTTFV-------------------------------GTPW 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   82 YVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG---QFCIPEHISPKARCLIRSLLRREPS 158
Cdd:pfam00069 126 YMAPEVLGGNPY--GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQpyaFPELPSNLSEEAKDLLKKLLKKDPS 203
                         170
                  ....*....|....
gi 545477471  159 ERLTAPEILLHPWF 172
Cdd:pfam00069 204 KRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
2-160 8.66e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 89.30  E-value: 8.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   2 HSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEER---------TQLRLESLEDTHIMKGEdda 72
Cdd:COG0515   95 ADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRvklidfgiaRALGGATLTQTGTVVGT--- 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  73 lsdkhgcPAYVSPEILntTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF----CIPEHISPKARCL 148
Cdd:COG0515  172 -------PGYMAPEQA--RGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPpppsELRPDLPPALDAI 242
                        170
                 ....*....|..
gi 545477471 149 IRSLLRREPSER 160
Cdd:COG0515  243 VLRALAKDPEER 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
1-175 1.41e-18

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 81.79  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLrleslEDTHIMKGEDDALSDKHGCP 80
Cdd:PTZ00263 105 LFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKV-----TDFGFAKKVPDRTFTLCGTP 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGtySGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:PTZ00263 180 EYLAPEVIQSKG--HGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTDHTKR 257
                        170       180
                 ....*....|....*....|
gi 545477471 161 LTA-----PEILLHPWFESV 175
Cdd:PTZ00263 258 LGTlkggvADVKNHPYFHGA 277
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
4-121 3.61e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 46.71  E-value: 3.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLK-----LRK--------F----VFSTEERTQlrlesleDTHIM 66
Cdd:NF033483  97 YIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKpqnilITKdgrvkvtdFgiarALSSTTMTQ-------TNSVL 169
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 545477471  67 kgeddalsdkhGCPAYVSPEIlnTTGTYSGKAADVWSLGVMLYTLLVGRYPFH-DS 121
Cdd:NF033483 170 -----------GTVHYLSPEQ--ARGGTVDARSDIYSLGIVLYEMLTGRPPFDgDS 212
 
Name Accession Description Interval E-value
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
1-172 6.69e-140

Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB1 interacts directly with the mitogen activated protein kinase (MAPK) kinase MKK4, an activator of JNK. It regulates vascular smooth muscle cell proliferation and chemotaxis through the JNK signaling pathway. It is found to be down-regulated in human acute myeloid leukaemia (AML) and may play a role in the pathogenesis of the disease. It has also been identified as a potential biomarker for antibody-mediated allograft failure. TRB1 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB1 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270925 [Multi-domain]  Cd Length: 242  Bit Score: 390.56  E-value: 6.69e-140
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKHGCP 80
Cdd:cd14023   71 MHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQLRLESLEDTHIMKGEDDALSDKHGCP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd14023  151 AYVSPEILNTTGTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPDHVSPKARCLIRSLLRREPSER 230
                        170
                 ....*....|..
gi 545477471 161 LTAPEILLHPWF 172
Cdd:cd14023  231 LTAPEILLHPWF 242
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
1-172 4.87e-124

Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Tribbles Homolog (TRB) proteins interact with many proteins involved in signaling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, differentiation, and gene expression. TRB proteins bind to the middle kinase in mitogen activated protein kinase (MAPK) signaling cascades, MAPK kinases. They regulate the activity of MAPK kinases, and thus, affect MAPK signaling. In Drosophila, Tribbles regulates String, the ortholog of mammalian Cdc25, during morphogenesis. String is implicated in the progression of mitosis during embryonic development. Vertebrates contain three TRB proteins encoded by three separate genes: Tribbles-1 (TRB1 or TRIB1), Tribbles-2 (TRB2 or TRIB2), and Tribbles-3 (TRB3 or TRIB3). The TRB subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270878 [Multi-domain]  Cd Length: 242  Bit Score: 350.19  E-value: 4.87e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKHGCP 80
Cdd:cd13976   71 LHSYVRSRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLESLEDAVILEGEDDSLSDKHGCP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd13976  151 AYVSPEILNSGATYSGKAADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRSLLRREPSER 230
                        170
                 ....*....|..
gi 545477471 161 LTAPEILLHPWF 172
Cdd:cd13976  231 LTAEDILLHPWL 242
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
1-172 5.99e-112

Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB2 binds and negatively regulates the mitogen activated protein kinase (MAPK) kinases, MKK7 and MEK1, which are activators of the MAPKs, ERK and JNK. It controls the activation of inflammatory monocytes, which is essential in innate immune responses and the pathogenesis of inflammatory diseases such as atherosclerosis. TRB2 expression is down-regulated in human acute myeloid leukaemia (AML), which may lead to enhanced cell survival and pathogenesis of the disease. TRB2 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270924 [Multi-domain]  Cd Length: 242  Bit Score: 319.68  E-value: 5.99e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKHGCP 80
Cdd:cd14022   71 MHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDEERTRVKLESLEDAYILRGHDDSLSDKHGCP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd14022  151 AYVSPEILNTSGSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKIRRGQFNIPETLSPKAKCLIRSILRREPSER 230
                        170
                 ....*....|..
gi 545477471 161 LTAPEILLHPWF 172
Cdd:cd14022  231 LTSQEILDHPWF 242
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
1-171 1.45e-94

Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. TRB3 binds and regulates ATF4, p65/RelA, and PKB (or Akt). It negatively regulates ATF4-mediated gene expression including that of CHOP (C/EBP homologous protein) and HO-1, which are both involved in modulating apoptosis. It also inhibits insulin-mediated phosphorylation of PKB and is a possible determinant of insulin resistance and related disorders. In osteoarthritic chondrocytes where it inhibits insulin-like growth factor 1-mediated cell survival, TRB3 is overexpressed, resulting in increased cell death. TRB3 is one of three Tribbles Homolog (TRB) proteins present in vertebrates that are encoded by three separate genes. TRB proteins interact with many proteins involved in signalling pathways. They play scaffold-like regulatory functions and affect many cellular processes such as mitosis, apoptosis, and gene expression. The TRB3 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 275.60  E-value: 1.45e-94
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKHGCP 80
Cdd:cd14024   71 MHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVLVNLEDSCPLNGDDDSLTDKHGCP 150
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd14024  151 AYVGPEILSSRRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFAKIRRGAFSLPAWLSPGARCLVSCMLRRSPAER 230
                        170
                 ....*....|.
gi 545477471 161 LTAPEILLHPW 171
Cdd:cd14024  231 LKASEILLHPW 241
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
1-171 2.85e-54

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: 173.47  E-value: 2.85e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLR----------K---FVFSTEERTQLRLESLedthimk 67
Cdd:cd14003   86 LFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLEnilldkngnlKiidFGLSNEFRGGSLLKTF------- 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  68 geddalsdkHGCPAYVSPEILNTTGtYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARC 147
Cdd:cd14003  159 ---------CGTPAYAAPEVLLGRK-YDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARD 228
                        170       180
                 ....*....|....*....|....
gi 545477471 148 LIRSLLRREPSERLTAPEILLHPW 171
Cdd:cd14003  229 LIRRMLVVDPSKRITIEEILNHPW 252
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
7-171 8.40e-46

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: 151.86  E-value: 8.40e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEErtqlrleslEDTHIM---------KGEDDALSDKH 77
Cdd:cd05117   92 KKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKD---------PDSPIKiidfglakiFEEGEKLKTVC 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGtYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPE----HISPKARCLIRSLL 153
Cdd:cd05117  163 GTPYYVAPEVLKGKG-Y-GKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSpewkNVSEEAKDLIKRLL 240
                        170
                 ....*....|....*...
gi 545477471 154 RREPSERLTAPEILLHPW 171
Cdd:cd05117  241 VVDPKKRLTAAEALNHPW 258
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
4-167 8.67e-46

Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SHIK, also referred to as STK40 or LYK4, is a cytoplasmic and nuclear protein that is involved in the negative regulation of NF-kappaB- and p53-mediated transcription. It was identified as a protein related to SINK, a p65-interacting protein that inhibits p65 phosphorylation by the catalytic subunit of PKA, thereby inhibiting transcriptional competence of NF-kappaB. The SHIK 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: 270876 [Multi-domain]  Cd Length: 290  Bit Score: 152.95  E-value: 8.67e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKgEDDALSDKHGCPAYV 83
Cdd:cd13974  122 YVIREKRLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRKITITNFCLGKHLVS-EDDLLKDQRGSPAYI 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPE--HISPKARCLIRSLLRREPSERL 161
Cdd:cd13974  201 SPDVLSGK-PYLGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPEdgRVSENTVCLIRKLLVLNPQKRL 279

                 ....*.
gi 545477471 162 TAPEIL 167
Cdd:cd13974  280 TASEVL 285
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
4-172 2.94e-45

Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BRSK1, also called SAD-B or SAD1 (Synapses of Amphids Defective homolog 1), and BRSK2, also called SAD-A, are highly expressed in mammalian forebrain. They play important roles in establishing neuronal polarity. BRSK1/2 double knock-out mice die soon after birth, showing thin cerebral cortices due to disordered subplate layers and neurons that lack distinct axons and dendrites. BRSK1 regulates presynaptic neurotransmitter release. Its activity fluctuates during cell cysle progression and it acts as a regulator of centrosome duplication. BRSK2 is also abundant in pancreatic islets, where it is involved in the regulation of glucose-stimulated insulin secretion. The BRSK1/2 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: 270983 [Multi-domain]  Cd Length: 255  Bit Score: 150.48  E-value: 2.94e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRL-----ESLEdthimkGEDDALSDKHG 78
Cdd:cd14081   91 YLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLD--EKNNIKIadfgmASLQ------PEGSLLETSCG 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEILnTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPS 158
Cdd:cd14081  163 SPHYACPEVI-KGEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNPE 241
                        170
                 ....*....|....
gi 545477471 159 ERLTAPEILLHPWF 172
Cdd:cd14081  242 KRITIEEIKKHPWF 255
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
4-172 4.99e-44

Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. In response to decreased ATP levels, it enhances energy-producing processes and inhibits energy-consuming pathways. Once activated, AMPK phosphorylates a broad range of downstream targets, with effects in carbohydrate metabolism and uptake, lipid and fatty acid biosynthesis, carbon energy storage, and inflammation, among others. Defects in energy homeostasis underlie many human diseases including Type 2 diabetes, obesity, heart disease, and cancer. As a result, AMPK has emerged as a therapeutic target in the treatment of these diseases. The AMPK 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: 270981 [Multi-domain]  Cd Length: 256  Bit Score: 147.41  E-value: 4.99e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLEDTHIMKgEDDALSDKHGCPAYV 83
Cdd:cd14079   92 YIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLL--DSNMNVKIADFGLSNIMR-DGEFLKTSCGSPNYA 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLTA 163
Cdd:cd14079  169 APEVISGK-LYAGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSPGARDLIKRMLVVDPLKRITI 247

                 ....*....
gi 545477471 164 PEILLHPWF 172
Cdd:cd14079  248 PEIRQHPWF 256
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
1-172 4.57e-40

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 136.89  E-value: 4.57e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471     1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteertqlrleslEDTHIM---------KGEDD 71
Cdd:smart00220  84 LFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLD------------EDGHVKladfglarqLDPGE 151
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471    72 ALSDKHGCPAYVSPEILNTTGtYsGKAADVWSLGVMLYTLLVGRYPF-HDSDPSALFSKIRRGQFCIPEH---ISPKARC 147
Cdd:smart00220 152 KLTTFVGTPEYMAPEVLLGKG-Y-GKAVDIWSLGVILYELLTGKPPFpGDDQLLELFKKIGKPKPPFPPPewdISPEAKD 229
                          170       180
                   ....*....|....*....|....*
gi 545477471   148 LIRSLLRREPSERLTAPEILLHPWF 172
Cdd:smart00220 230 LIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
3-171 8.13e-39

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK3 is represented in this cd. The SnRK3 group contains members also known as CBL-interacting protein kinase, salt overly sensitive 2, SOS3-interacting proteins and protein kinase S. These kinases interact with calcium-binding proteins such as SOS3, SCaBPs, and CBL proteins, and are involved in responses to salt stress and in sugar and ABA signaling. The SnRKs belong to 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: 271133 [Multi-domain]  Cd Length: 256  Bit Score: 134.07  E-value: 8.13e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKHGCPAY 82
Cdd:cd14663   89 SKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSALSEQFRQDGLLHTTCGTPNY 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNTTGtYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLT 162
Cdd:cd14663  169 VAPEVLARRG-YDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILDPNPSTRIT 247

                 ....*....
gi 545477471 163 APEILLHPW 171
Cdd:cd14663  248 VEQIMASPW 256
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
1-172 1.53e-38

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: 133.45  E-value: 1.53e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteertqlrleslEDTHIMKGeDDALS------ 74
Cdd:cd14099   88 LMELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLD------------ENMNVKIG-DFGLAarleyd 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  75 -DKH----GCPAYVSPEILNTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEH--ISPKARC 147
Cdd:cd14099  155 gERKktlcGTPNYIAPEVLEKKKGHSFEV-DIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHlsISDEAKD 233
                        170       180
                 ....*....|....*....|....*
gi 545477471 148 LIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd14099  234 LIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
1-171 8.38e-38

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK1, also called ARK5 (AMPK-related protein kinase 5), regulates cell proliferation and displays tumor suppression through direct interaction and phosphorylation of p53. It is also involved in cell senescence and motility. High NUAK1 expression is associated with invasiveness of nonsmall cell lung cancer (NSCLC) and breast cancer cells. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. The NUAK 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: 270975 [Multi-domain]  Cd Length: 254  Bit Score: 131.36  E-value: 8.38e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVfsteertqlrlesLEDTHIMKGEDDALSDKH--- 77
Cdd:cd14073   88 LYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENIL-------------LDQNGNAKIADFGLSNLYskd 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 -------GCPAYVSPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISpKARCLIR 150
Cdd:cd14073  155 kllqtfcGSPLYASPEIVNGT-PYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPS-DASGLIR 232
                        170       180
                 ....*....|....*....|.
gi 545477471 151 SLLRREPSERLTAPEILLHPW 171
Cdd:cd14073  233 WMLTVNPKRRATIEDIANHWW 253
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
4-171 3.01e-37

Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MELK is a cell cycle dependent protein which functions in cytokinesis, cell cycle, apoptosis, cell proliferation, and mRNA processing. It is found upregulated in many types of cancer cells, playing an indispensable role in cancer cell survival. It makes an attractive target in the design of inhibitors for use in the treatment of a wide range of human cancer. The MELK 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: 270980 [Multi-domain]  Cd Length: 257  Bit Score: 129.81  E-value: 3.01e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLrlesledthI--------MKGEDDALSD 75
Cdd:cd14078   91 YIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKL---------IdfglcakpKGGMDHHLET 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  76 KHGCPAYVSPEILnTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRR 155
Cdd:cd14078  162 CCGSPAYAAPELI-QGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQV 240
                        170
                 ....*....|....*.
gi 545477471 156 EPSERLTAPEILLHPW 171
Cdd:cd14078  241 DPKKRITVKELLNHPW 256
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
8-172 1.45e-36

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: 128.44  E-value: 1.45e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLrleslED---THIMKGEDDALSDKHGCPAYVS 84
Cdd:cd14008  102 VPPLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKI-----SDfgvSEMFEDGNDTLQKTAGTPAFLA 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTT-GTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ--FCIPEHISPKARCLIRSLLRREPSERL 161
Cdd:cd14008  177 PELCDGDsKTYSGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNdeFPIPPELSPELKDLLRRMLEKDPEKRI 256
                        170
                 ....*....|.
gi 545477471 162 TAPEILLHPWF 172
Cdd:cd14008  257 TLKEIKEHPWV 267
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
1-172 2.69e-36

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: 127.25  E-value: 2.69e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteertqlrleslEDTHI--------MKGEDDA 72
Cdd:cd05123   80 LFSHLSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLD------------SDGHIkltdfglaKELSSDG 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  73 LSDKHGC--PAYVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIR 150
Cdd:cd05123  148 DRTYTFCgtPEYLAPEVLL--GKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLIS 225
                        170       180
                 ....*....|....*....|....*
gi 545477471 151 SLLRREPSERLT---APEILLHPWF 172
Cdd:cd05123  226 GLLQKDPTKRLGsggAEEIKAHPFF 250
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
4-172 3.46e-35

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


Pssm-ID: 270982 [Multi-domain]  Cd Length: 262  Bit Score: 124.60  E-value: 3.46e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLK-------------LRKFVFSTeertqlrlesledtHIMKGED 70
Cdd:cd14080   92 YIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKcenilldsnnnvkLSDFGFAR--------------LCPDDDG 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  71 DALSDKH-GCPAYVSPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIP---EHISPKAR 146
Cdd:cd14080  158 DVLSKTFcGSAAYAAPEILQGI-PYDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPssvKKLSPECK 236
                        170       180
                 ....*....|....*....|....*.
gi 545477471 147 CLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd14080  237 DLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
1-171 8.89e-35

Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNRK is a kinase highly expressed in testis and brain that is found inactive in cells that lack the LKB1 tumour suppressor protein kinase. The regulatory subunits STRAD and MO25 are required for LKB1 to activate SNRK. The SNRK mRNA is increased 3-fold when granule neurons are cultured in low potassium, and may thus play a role in the survival responses in these cells. In some vertebrates, a second SNRK gene (snrkb or snrk-1) has been sequenced and/or identified. Snrk-1 is expressed specifically in embryonic zebrafish vasculature; it plays an essential role in angioblast differentiation, maintenance, and migration. The SNRK 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: 270976 [Multi-domain]  Cd Length: 258  Bit Score: 123.68  E-value: 8.89e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYV-RSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTeertQLRLESLED----THIMKGEddALSD 75
Cdd:cd14074   89 MYDYImKHENGLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFFE----KQGLVKLTDfgfsNKFQPGE--KLET 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  76 KHGCPAYVSPEILnTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRR 155
Cdd:cd14074  163 SCGSLAYSAPEIL-LGDEYDAPAVDIWSLGVILYMLVCGQPPFQEANDSETLTMIMDCKYTVPAHVSPECKDLIRRMLIR 241
                        170
                 ....*....|....*.
gi 545477471 156 EPSERLTAPEILLHPW 171
Cdd:cd14074  242 DPKKRASLEEIENHPW 257
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
1-171 2.22e-34

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: 122.20  E-value: 2.22e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIV-------------LGDLKLRKFVFSTEERTQLRLESLedthimk 67
Cdd:cd14007   87 LYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIhrdikpenillgsNGELKLADFGWSVHAPSNRRKTFC------- 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  68 geddalsdkhGCPAYVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARC 147
Cdd:cd14007  160 ----------GTLDYLPPEMVE--GKEYDYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKD 227
                        170       180
                 ....*....|....*....|....
gi 545477471 148 LIRSLLRREPSERLTAPEILLHPW 171
Cdd:cd14007  228 LISKLLQKDPSKRLSLEQVLNHPW 251
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
5-174 6.68e-34

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK 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: 270994 [Multi-domain]  Cd Length: 311  Bit Score: 122.41  E-value: 6.68e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEErtqlrleslEDTHI---------MKGEDDALSD 75
Cdd:cd14092   90 IRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFTDED---------DDAEIkivdfgfarLKPENQPLKT 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  76 KHGCPAYVSPEILNTTGTYSG--KAADVWSLGVMLYTLLVGRYPFH----DSDPSALFSKIRRGQFCIP----EHISPKA 145
Cdd:cd14092  161 PCFTLPYAAPEVLKQALSTQGydESCDLWSLGVILYTMLSGQVPFQspsrNESAAEIMKRIKSGDFSFDgeewKNVSSEA 240
                        170       180
                 ....*....|....*....|....*....
gi 545477471 146 RCLIRSLLRREPSERLTAPEILLHPWFES 174
Cdd:cd14092  241 KSLIQGLLTVDPSKRLTMSELRNHPWLQG 269
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
3-172 5.76e-33

Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK4, also called TSSK5, is expressed in testis from haploid round spermatids to mature spermatozoa. It phosphorylates Cre-Responsive Element Binding protein (CREB), facilitating the binding of CREB to the specific cis cAMP responsive element (CRE), which is important in activating genes related to germ cell differentiation. Mutations in the human TSSK4 gene is associated with infertile Chinese men with impaired spermatogenesis. The TSSK4-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: 271064 [Multi-domain]  Cd Length: 259  Bit Score: 118.94  E-value: 5.76e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERtqLRLESL---EDTHIMKGEDDALSDKH-G 78
Cdd:cd14162   89 DYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNN--LKITDFgfaRGVMKTKDGKPKLSETYcG 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG-QFCIPEHISPKARCLIRSLLRREP 157
Cdd:cd14162  167 SYAYASPEILRGI-PYDPFLSDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRvVFPKNPTVSEECKDLILRMLSPVK 245
                        170
                 ....*....|....*
gi 545477471 158 sERLTAPEILLHPWF 172
Cdd:cd14162  246 -KRITIEEIKRDPWF 259
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
8-172 1.44e-32

Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LKB1, also called STK11, was first identified as a tumor suppressor responsible for Peutz-Jeghers syndrome, a disorder that leads to an increased risk of spontaneous epithelial cancer. It serves as a master upstream kinase that activates AMP-activated protein kinase (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. To be activated, LKB1 requires the adaptor proteins STe20-Related ADaptor (STRAD) and mouse protein 25 (MO25). The LKB1 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: 271021 [Multi-domain]  Cd Length: 255  Bit Score: 117.74  E-value: 1.44e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERtqLRLESL---EDTHiMKGEDDALSDKHGCPAYVS 84
Cdd:cd14119   91 DKRLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGT--LKISDFgvaEALD-LFAEDDTCTTSQGSPAFQP 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLTAP 164
Cdd:cd14119  168 PEIANGQDSFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQDLLRGMLEKDPEKRFTIE 247

                 ....*...
gi 545477471 165 EILLHPWF 172
Cdd:cd14119  248 QIRQHPWF 255
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
5-171 3.32e-32

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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 AMP-activated protein kinase (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 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: 271020 [Multi-domain]  Cd Length: 275  Bit Score: 117.46  E-value: 3.32e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLESLEDTHIMKGEDDALSDKHGCPAYVS 84
Cdd:cd14118  106 VPTDNPLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLG--DDGHVKIADFGVSNEFEGDDALLSSTAGTPAFMA 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTTGT-YSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEH--ISPKARCLIRSLLRREPSERL 161
Cdd:cd14118  184 PEALSESRKkFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFPDDpvVSEQLKDLILRMLDKNPSERI 263
                        170
                 ....*....|
gi 545477471 162 TAPEILLHPW 171
Cdd:cd14118  264 TLPEIKEHPW 273
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
1-171 6.73e-32

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 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: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 115.90  E-value: 6.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLrleslED----THIMKGEddALSDK 76
Cdd:cd14075   88 LYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKV-----GDfgfsTHAKRGE--TLNTF 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  77 HGCPAYVSPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRRE 156
Cdd:cd14075  161 CGSPPYAAPELFKDE-HYIGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGILQPV 239
                        170
                 ....*....|....*
gi 545477471 157 PSERLTAPEILLHPW 171
Cdd:cd14075  240 PSDRYSIDEIKNSEW 254
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
1-171 7.12e-32

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: 116.39  E-value: 7.12e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL---RLESLEDthimkgEDDALSDKH 77
Cdd:cd14077  100 LLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIidfGLSNLYD------PRRLLRTFC 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREP 157
Cdd:cd14077  174 GSLYFAAPELLQAQ-PYTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSSECKSLISRMLVVDP 252
                        170
                 ....*....|....
gi 545477471 158 SERLTAPEILLHPW 171
Cdd:cd14077  253 KKRATLEQVLNHPW 266
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
13-171 1.97e-31

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I gamma; 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. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. 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. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-gamma subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271068 [Multi-domain]  Cd Length: 285  Bit Score: 115.47  E-value: 1.97e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEER------TQLRLESLEDTHIMkgeddalSDKHGCPAYVSPE 86
Cdd:cd14166   99 EKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYLTPDEnskimiTDFGLSKMEQNGIM-------STACGTPGYVAPE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  87 ILnTTGTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG--QFCIP--EHISPKARCLIRSLLRREPSERLT 162
Cdd:cd14166  172 VL-AQKPYS-KAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGyyEFESPfwDDISESAKDFIRHLLEKNPSKRYT 249

                 ....*....
gi 545477471 163 APEILLHPW 171
Cdd:cd14166  250 CEKALSHPW 258
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
10-171 4.58e-31

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to 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: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 113.93  E-value: 4.58e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESL--EDTHIMKGEDDALSdkhGCPAYVSPEI 87
Cdd:cd14665   92 RFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKICDFgySKSSVLHSQPKSTV---GTPAYIAPEV 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  88 LnTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSK----IRRGQFCIPE--HISPKARCLIRSLLRREPSERL 161
Cdd:cd14665  169 L-LKKEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEPRNFRKtiqrILSVQYSIPDyvHISPECRHLISRIFVADPATRI 247
                        170
                 ....*....|
gi 545477471 162 TAPEILLHPW 171
Cdd:cd14665  248 TIPEIRNHEW 257
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
4-172 1.26e-30

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 and three PIM2 isoforms as a result of alternative translation initiation sites, while there is only one PIM3 protein. Compound knockout mice deficient of all three PIM kinases that survive the perinatal period show a profound reduction in body size, indicating that PIMs are important for body growth. The PIM 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: 270907 [Multi-domain]  Cd Length: 255  Bit Score: 112.72  E-value: 1.26e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEeRTQLRLESLEDTHIMKgeDDALSDKHGCPAYV 83
Cdd:cd14005   97 FITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINLR-TGEVKLIDFGCGALLK--DSVYTDFDGTRVYS 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEiLNTTGTYSGKAADVWSLGVMLYTLLVGRYPFHdSDpsalfSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLTA 163
Cdd:cd14005  174 PPE-WIRHGRYHGRPATVWSLGILLYDMLCGDIPFE-ND-----EQILRGNVLFRPRLSKECCDLISRCLQFDPSKRPSL 246

                 ....*....
gi 545477471 164 PEILLHPWF 172
Cdd:cd14005  247 EQILSHPWF 255
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
4-171 2.19e-30

Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kin4 is a central component of the spindle position checkpoint (SPOC), which monitors spindle position and regulates the mitotic exit network (MEN). Kin4 associates with spindle pole bodies in mother cells to inhibit MEN signaling and delay mitosis until the anaphase nucleus is properly positioned along the mother-bud axis. Kin4 activity is regulated by both the bud neck-associated kinase Elm1 and protein phosphatase 2A. The Kin4 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: 270978 [Multi-domain]  Cd Length: 270  Bit Score: 112.58  E-value: 2.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDThIMKGEDDALSDKHGCPAYV 83
Cdd:cd14076   96 YILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANT-FDHFNGDLMSTSCGSPCYA 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFhDSDPS--------ALFSKIRRGQFCIPEHISPKARCLIRSLLRR 155
Cdd:cd14076  175 APELVVSDSMYAGRKADIWSCGVILYAMLAGYLPF-DDDPHnpngdnvpRLYRYICNTPLIFPEYVTPKARDLLRRILVP 253
                        170
                 ....*....|....*.
gi 545477471 156 EPSERLTAPEILLHPW 171
Cdd:cd14076  254 NPRKRIRLSAIMRHAW 269
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
7-171 2.85e-30

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type II; 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. CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. In addition, CaMKII contains a C-terminal association domain that facilitates oligomerization. There are four CaMKII proteins (alpha, beta, gamma, delta) encoded by different genes; each gene undergoes alternative splicing to produce more than 30 isoforms. CaMKII-alpha and -beta are enriched in neurons while CaMKII-gamma and -delta are predominant in myocardium. 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. It is a major component of the postsynaptic density and is critical in regulating synaptic plasticity including long-term potentiation. It is critical in regulating ion channels and proteins involved in myocardial excitation-contraction and excitation-transcription coupling. Excessive CaMKII activity promotes processes that contribute to heart failure and arrhythmias. The CaMKII subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270988 [Multi-domain]  Cd Length: 292  Bit Score: 112.52  E-value: 2.85e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEER-TQLRLESLEDTHIMKGEDDALSDKHGCPAYVSP 85
Cdd:cd14086   93 AREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLASKSKgAAVKLADFGLAIEVQGDQQAWFGFAGTPGYLSP 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  86 EILNTTgTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIP----EHISPKARCLIRSLLRREPSERL 161
Cdd:cd14086  173 EVLRKD-PY-GKPVDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPspewDTVTPEAKDLINQMLTVNPAKRI 250
                        170
                 ....*....|
gi 545477471 162 TAPEILLHPW 171
Cdd:cd14086  251 TAAEALKHPW 260
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
1-171 3.00e-30

Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NUAK proteins are classified as AMP-activated protein kinase (AMPK)-related kinases, which like AMPK are activated by the major tumor suppressor LKB1. Vertebrates contain two NUAK proteins, called NUAK1 and NUAK2. NUAK2, also called SNARK (Sucrose, non-fermenting 1/AMP-activated protein kinase-related kinase), is involved in energy metabolism. It is activated by hyperosmotic stress, DNA damage, and nutrients such as glucose and glutamine. NUAK2-knockout mice develop obesity, altered serum lipid profiles, hyperinsulinaemia, hyperglycaemia, and impaired glucose tolerance. NUAK2 is implicated in regulating actin stress fiber assembly through its association with myosin phosphatase Rho-interacting protein (MRIP), which leads to an increase in myosin regulatory light chain (MLC) phosphorylation. It is also associated with tumor growth, migration, and oncogenicity of melanoma cells. The NUAK2 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: 271063 [Multi-domain]  Cd Length: 255  Bit Score: 111.58  E-value: 3.00e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLEDTHIMKGeDDALSDKHGCP 80
Cdd:cd14161   89 LYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILL--DANGNIKIADFGLSNLYNQ-DKFLQTYCGSP 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISpKARCLIRSLLRREPSER 160
Cdd:cd14161  166 LYASPEIVNGR-PYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPS-DACGLIRWLLMVNPERR 243
                        170
                 ....*....|.
gi 545477471 161 LTAPEILLHPW 171
Cdd:cd14161  244 ATLEDVASHWW 254
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
13-175 4.62e-30

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: 111.54  E-value: 4.62e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARL-FKQIVSAVAHCHQSAIVLGDLK-------------LRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKHG 78
Cdd:cd05579   91 DEDVARIyIAEIVLALEYLHSHGIIHRDLKpdnilidanghlkLTDFGLSKVGLVRRQIKLSIQKKSNGAPEKEDRRIVG 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPE--HISPKARCLIRSLLRRE 156
Cdd:cd05579  171 TPDYLAPEILLGQGH--GKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEdpEVSDEAKDLISKLLTPD 248
                        170       180
                 ....*....|....*....|..
gi 545477471 157 PSERL---TAPEILLHPWFESV 175
Cdd:cd05579  249 PEKRLgakGIEEIKNHPFFKGI 270
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
13-171 9.46e-30

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I; 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. In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. 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. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270985 [Multi-domain]  Cd Length: 259  Bit Score: 110.54  E-value: 9.46e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEErtqlrleslEDTHIM-------KGEDDA-LSDKHGCPAYVS 84
Cdd:cd14083  100 EKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLYYSPD---------EDSKIMisdfglsKMEDSGvMSTACGTPGYVA 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTTGtYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG--QFCIP--EHISPKARCLIRSLLRREPSER 160
Cdd:cd14083  171 PEVLAQKP-Y-GKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAeyEFDSPywDDISDSAKDFIRHLMEKDPNKR 248
                        170
                 ....*....|.
gi 545477471 161 LTAPEILLHPW 171
Cdd:cd14083  249 YTCEQALEHPW 259
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
1-172 2.41e-29

Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SIKs are part of a complex network that regulates Na,K-ATPase to maintain sodium homeostasis and blood pressure. Vertebrates contain three forms of SIKs (SIK1-3) from three distinct genes, which display tissue-specific effects. SIK1, also called SNF1LK, controls steroidogenic enzyme production in adrenocortical cells. In the brain, both SIK1 and SIK2 regulate energy metabolism. SIK2, also called QIK or SNF1LK2, is involved in the regulation of gluconeogenesis in the liver and lipogenesis in adipose tissues, where it phosphorylates the insulin receptor substrate-1. In the liver, SIK3 (also called QSK) regulates cholesterol and bile acid metabolism. In addition, SIK2 plays an important role in the initiation of mitosis and regulates the localization of C-Nap1, a centrosome linker protein. The SIK 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: 270973 [Multi-domain]  Cd Length: 253  Bit Score: 109.40  E-value: 2.41e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLEDTHIMKgEDDALSDKHGCP 80
Cdd:cd14071   86 IFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLL--DANMNIKIADFGFSNFFK-PGELLKTWCGSP 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd14071  163 PYAAPEVFEGK-EYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDPSKR 241
                        170
                 ....*....|..
gi 545477471 161 LTAPEILLHPWF 172
Cdd:cd14071  242 LTIEQIKKHKWM 253
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
3-172 3.06e-29

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: 109.61  E-value: 3.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLrEEEAARLF-KQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL----------RLESLEDTHIMKGEDD 71
Cdd:cd05581   90 EYIRKYGSL-DEKCTRFYtAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKItdfgtakvlgPDSSPESTKGDADSQI 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  72 ALSDKH-----GCPAYVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKAR 146
Cdd:cd05581  169 AYNQARaasfvGTAEYVSPELLN--EKPAGKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYEFPENFPPDAK 246
                        170       180       190
                 ....*....|....*....|....*....|..
gi 545477471 147 CLIRSLLRREPSERLTA------PEILLHPWF 172
Cdd:cd05581  247 DLIQKLLVLDPSKRLGVnenggyDELKAHPFF 278
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
13-171 3.26e-29

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I beta; 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. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. 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. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-beta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271071 [Multi-domain]  Cd Length: 277  Bit Score: 109.59  E-value: 3.26e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTeertqlrleSLEDTHIM-------KGEDD-ALSDKHGCPAYVS 84
Cdd:cd14169  100 EKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAT---------PFEDSKIMisdfglsKIEAQgMLSTACGTPGYVA 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTTgTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG--QFCIP--EHISPKARCLIRSLLRREPSER 160
Cdd:cd14169  171 PELLEQK-PY-GKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILKAeyEFDSPywDDISESAKDFIRHLLERDPEKR 248
                        170
                 ....*....|.
gi 545477471 161 LTAPEILLHPW 171
Cdd:cd14169  249 FTCEQALQHPW 259
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
5-171 5.50e-29

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called Doublecortin-like and CAM kinase-like); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL (or DCAMKL) proteins belong to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL proteins contain a C-terminal kinase domain with similarity to CAMKs. They are involved in the regulation of cAMP signaling. Vertebrates contain three DCKL proteins (DCKL1-3); DCKL1 and 2 also contain a serine, threonine, and proline rich domain (SP), while DCKL3 contains only a single DCX domain instead of tandem domains. The DCKL 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: 270997 [Multi-domain]  Cd Length: 258  Bit Score: 108.57  E-value: 5.50e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLEsLEDTHIMKGEDDALSDKHGCPAYVS 84
Cdd:cd14095   89 ITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVVEHEDGSKSLK-LADFGLATEVKEPLFTVCGTPTYVA 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTTGtYsGKAADVWSLGVMLYTLLVGRYPFH--DSDPSALFSKIRRGQFCIP----EHISPKARCLIRSLLRREPS 158
Cdd:cd14095  168 PEILAETG-Y-GLKVDIWAAGVITYILLCGFPPFRspDRDQEELFDLILAGEFEFLspywDNISDSAKDLISRMLVVDPE 245
                        170
                 ....*....|...
gi 545477471 159 ERLTAPEILLHPW 171
Cdd:cd14095  246 KRYSAGQVLDHPW 258
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
7-171 1.76e-28

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to 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: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 107.16  E-value: 1.76e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLR-----------LESLEDTHImkgeddalsd 75
Cdd:cd14662   89 NAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPAPRLKicdfgyskssvLHSQPKSTV---------- 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  76 khGCPAYVSPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSK----IRRGQFCIPE--HISPKARCLI 149
Cdd:cd14662  159 --GTPAYIAPEVLSRK-EYDGKVADVWSCGVTLYVMLVGAYPFEDPDDPKNFRKtiqrIMSVQYKIPDyvRVSQDCRHLL 235
                        170       180
                 ....*....|....*....|..
gi 545477471 150 RSLLRREPSERLTAPEILLHPW 171
Cdd:cd14662  236 SRIFVANPAKRITIPEIKNHPW 257
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
1-171 2.00e-28

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; 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. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK4, also called SAK or STK18, is structurally different from other PLKs in that it contains only one polo box that can form two adjacent polo boxes and a functional PDB by homodimerization. It is required for late mitotic progression, cell survival, and embryonic development. It localizes to centrosomes and is required for centriole duplication and chromosomal stability. Overexpression of PLK4 may be associated with colon tumors. The PLK4 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: 271088 [Multi-domain]  Cd Length: 256  Bit Score: 106.87  E-value: 2.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKR-LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEddalsdKH-- 77
Cdd:cd14186   88 MSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKMPHE------KHft 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 --GCPAYVSPEIlnTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRR 155
Cdd:cd14186  162 mcGTPNYISPEI--ATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRK 239
                        170
                 ....*....|....*.
gi 545477471 156 EPSERLTAPEILLHPW 171
Cdd:cd14186  240 NPADRLSLSSVLDHPF 255
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
8-172 2.72e-28

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK 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: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 107.33  E-value: 2.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERT--QLRLESLEDTHIMKGEDDALSDKHGCPAYVSP 85
Cdd:cd14091   88 QKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILYADESGDpeSLRICDFGFAKQLRAENGLLMTPCYTANFVAP 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  86 EILNTTGtYSgKAADVWSLGVMLYTLLVGRYPF----HDSdPSALFSKIRRGQFCIP----EHISPKARCLIRSLLRREP 157
Cdd:cd14091  168 EVLKKQG-YD-AACDIWSLGVLLYTMLAGYTPFasgpNDT-PEVILARIGSGKIDLSggnwDHVSDSAKDLVRKMLHVDP 244
                        170
                 ....*....|....*
gi 545477471 158 SERLTAPEILLHPWF 172
Cdd:cd14091  245 SQRPTAAQVLQHPWI 259
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
13-171 2.81e-28

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I alpha; 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. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. 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. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271069 [Multi-domain]  Cd Length: 263  Bit Score: 106.65  E-value: 2.81e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVF-STEERTQLRLESLEDTHImKGEDDALSDKHGCPAYVSPEILnTT 91
Cdd:cd14167  100 ERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLYySLDEDSKIMISDFGLSKI-EGSGSVMSTACGTPGYVAPEVL-AQ 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  92 GTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG--QFCIP--EHISPKARCLIRSLLRREPSERLTAPEIL 167
Cdd:cd14167  178 KPYS-KAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAeyEFDSPywDDISDSAKDFIQHLMEKDPEKRFTCEQAL 256

                 ....
gi 545477471 168 LHPW 171
Cdd:cd14167  257 QHPW 260
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
3-171 3.68e-28

Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Checkpoint Kinase 2 (Chk2) plays an important role in cellular responses to DNA double-strand breaks and related lesions. It is phosphorylated and activated by ATM kinase, resulting in its dissociation from sites of damage to phosphorylate downstream targets such as BRCA1, p53, cell cycle transcription factor E2F1, the promyelocytic leukemia protein (PML) involved in apoptosis, and CDC25 phosphatases, among others. Mutations in Chk2 is linked to a variety of cancers including familial breast cancer, myelodysplastic syndromes, prostate cancer, lung cancer, and osteosarcomas. Chk2 contains an N-terminal SQ/TQ cluster domain (SCD), a central forkhead-associated (FHA) domain, and a C-terminal catalytic kinase domain. The Chk2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270986 [Multi-domain]  Cd Length: 275  Bit Score: 106.71  E-value: 3.68e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFST-EERTQLRLESLEDTHIMkGEDDALSDKHGCPA 81
Cdd:cd14084  100 DRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSqEEECLIKITDFGLSKIL-GETSLMKTLCGTPT 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNTTGT--YSgKAADVWSLGVMLYTLLVGRYPF-HDSDPSALFSKIRRGQFC-IPEH---ISPKARCLIRSLLR 154
Cdd:cd14084  179 YLAPEVLRSFGTegYT-RAVDCWSLGVILFICLSGYPPFsEEYTQMSLKEQILSGKYTfIPKAwknVSEEAKDLVKKMLV 257
                        170
                 ....*....|....*..
gi 545477471 155 REPSERLTAPEILLHPW 171
Cdd:cd14084  258 VDPSRRPSIEEALEHPW 274
Pkinase pfam00069
Protein kinase domain;
2-172 6.85e-28

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 104.63  E-value: 6.85e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471    2 HSYVRSRKRLREEEAARLFKQIVSAVAHCHqsaivlgdlKLRKFVfsteertqlrlesledthimkgeddalsdkhGCPA 81
Cdd:pfam00069  86 FDLLSEKGAFSEREAKFIMKQILEGLESGS---------SLTTFV-------------------------------GTPW 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   82 YVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG---QFCIPEHISPKARCLIRSLLRREPS 158
Cdd:pfam00069 126 YMAPEVLGGNPY--GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQpyaFPELPSNLSEEAKDLLKKLLKKDPS 203
                         170
                  ....*....|....
gi 545477471  159 ERLTAPEILLHPWF 172
Cdd:pfam00069 204 KRLTATQALQHPWF 217
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
13-171 9.60e-28

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated 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 MAPK-activated protein kinases MK2, MK3, MK5 (also called PRAK for p38-regulated/activated protein kinase), and related proteins. These proteins contain a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. In addition, MK2 and MK3 contain an N-terminal proline-rich region that can bind to SH3 domains. MK2 and MK3 are bonafide substrates for the MAPK p38, while MK5 plays a functional role in the p38 MAPK pathway although their direct interaction has been difficult to detect. MK2 and MK3 are closely related and show, thus far, indistinguishable substrate specificity, while MK5 shows a distinct spectrum of substrates. MK2 and MK3 are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK 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: 270991 [Multi-domain]  Cd Length: 263  Bit Score: 105.45  E-value: 9.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFS-TEERTQLRLEsleDTHIMKGEDDALSDKHGC--PAYVSPEILN 89
Cdd:cd14089   99 EREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYSsKGPNAILKLT---DFGFAKETTTKKSLQTPCytPYYVAPEVLG 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  90 TTgTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALF----SKIRRGQFCIPE----HISPKARCLIRSLLRREPSERL 161
Cdd:cd14089  176 PE-KYD-KSCDMWSLGVIMYILLCGYPPFYSNHGLAISpgmkKRIRNGQYEFPNpewsNVSEEAKDLIRGLLKTDPSERL 253
                        170
                 ....*....|
gi 545477471 162 TAPEILLHPW 171
Cdd:cd14089  254 TIEEVMNHPW 263
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
6-172 1.57e-27

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; 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. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK3, also called Prk or Fnk (FGF-inducible kinase), regulates angiogenesis and responses to DNA damage. Activated PLK3 mediates Chk2 phosphorylation by ATM and the resulting checkpoint activation. PLK3 phosphorylates DNA polymerase delta and may be involved in DNA repair. It also inhibits Cdc25c, thereby regulating the onset of mitosis. The PLK3 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: 271091 [Multi-domain]  Cd Length: 255  Bit Score: 104.62  E-value: 1.57e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   6 RSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSP 85
Cdd:cd14189   93 KARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFIN--ENMELKVGDFGLAARLEPPEQRKKTICGTPNYLAP 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  86 EILNTTGtySGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLTAPE 165
Cdd:cd14189  171 EVLLRQG--HGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRLTLDQ 248

                 ....*..
gi 545477471 166 ILLHPWF 172
Cdd:cd14189  249 ILEHEFF 255
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
3-171 4.16e-27

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: 103.12  E-value: 4.16e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKhGCPAY 82
Cdd:cd14006   78 DRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPSPQIKIIDFGLARKLNPGEELKEIF-GTPEF 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF----CIPEHISPKARCLIRSLLRREPS 158
Cdd:cd14006  157 VAPEIVN--GEPVSLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVdfseEYFSSVSQEAKDFIRKLLVKEPR 234
                        170
                 ....*....|...
gi 545477471 159 ERLTAPEILLHPW 171
Cdd:cd14006  235 KRPTAQEALQHPW 247
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
7-175 1.75e-26

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-beta is the predominant PKB isoform expressed in insulin-responsive tissues. It plays a critical role in the regulation of glucose homeostasis. It is also implicated in muscle cell differentiation. Mice deficient in PKB-beta display normal growth weights but exhibit severe insulin resistance and diabetes, accompanied by lipoatrophy and B-cell failure. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain.The PKB-beta 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: 173686 [Multi-domain]  Cd Length: 323  Bit Score: 103.16  E-value: 1.75e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLREEEAARLF-KQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQ-----LRLESLEDTHIMKgeddalsDKHGCP 80
Cdd:cd05595   87 SRERVFTEDRARFYgAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKitdfgLCKEGITDGATMK-------TFCGTP 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd05595  160 EYLAPEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQR 237
                        170       180
                 ....*....|....*....|
gi 545477471 161 L-----TAPEILLHPWFESV 175
Cdd:cd05595  238 LgggpsDAKEVMEHRFFLSI 257
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
5-171 1.88e-26

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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 AMP-activated protein kinase (AMPK). CaMKK1, also called CaMKK alpha, is involved in the regulation of glucose uptake in skeletal muscles, independently of AMPK and PKB activation. It also play roles in learning and memory. Studies on CaMKK1 knockout mice reveal deficits in fear conditioning. The CaMKK1 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: 271102 [Multi-domain]  Cd Length: 284  Bit Score: 102.33  E-value: 1.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEerTQLRLESLEDTHIMKGEDDALSDKHGCPAYVS 84
Cdd:cd14200  115 VPSDKPFSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDD--GHVKIADFGVSNQFEGNDALLSSTAGTPAFMA 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTTG-TYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPE--HISPKARCLIRSLLRREPSERL 161
Cdd:cd14200  193 PETLSDSGqSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKIKNKPVEFPEepEISEELKDLILKMLDKNPETRI 272
                        170
                 ....*....|
gi 545477471 162 TAPEILLHPW 171
Cdd:cd14200  273 TVPEIKVHPW 282
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
4-172 8.94e-26

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). Each subunit has tissue-specific isoforms or splice variants. Vertebrates contain two isoforms of the gamma subunit (gamma 1 and gamma 2). The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG 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: 270995 [Multi-domain]  Cd Length: 272  Bit Score: 100.51  E-value: 8.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL-------RLEsledthimkgEDDALSDK 76
Cdd:cd14093   99 YLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKIsdfgfatRLD----------EGEKLREL 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  77 HGCPAYVSPEIL------NTTGtYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ--FCIPE--HISPKAR 146
Cdd:cd14093  169 CGTPGYLAPEVLkcsmydNAPG-Y-GKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKyeFGSPEwdDISDTAK 246
                        170       180
                 ....*....|....*....|....*.
gi 545477471 147 CLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd14093  247 DLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
4-171 1.10e-25

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK 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: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 99.90  E-value: 1.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSdkhGCPAYV 83
Cdd:cd14072   89 YLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLDTFC---GSPPYA 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLTA 163
Cdd:cd14072  166 APELFQGK-KYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNPSKRGTL 244

                 ....*...
gi 545477471 164 PEILLHPW 171
Cdd:cd14072  245 EQIMKDRW 252
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
1-171 1.14e-25

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK3 mRNA is up-regulated in fibroblasts after Ras-induced senescence, and its overexpression induces both autophagy and senescence in a fibroblast cell line. ULK3, through its kinase activity, positively regulates Gli proteins, mediators of the Sonic hedgehog (Shh) signaling pathway that is implicated in tissue homeostasis maintenance and neurogenesis. It is inhibited by binding to Suppressor of Fused (Sufu). The ULK3 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: 271023 [Multi-domain]  Cd Length: 252  Bit Score: 99.67  E-value: 1.14e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKhGCP 80
Cdd:cd14121   82 LSRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLADFGFAQHLKPNDEAHSLR-GSP 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILnTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ-FCIPE--HISPKARCLIRSLLRREP 157
Cdd:cd14121  161 LYMAPEMI-LKKKYDARV-DLWSVGVILYECLFGRAPFASRSFEELEEKIRSSKpIEIPTrpELSADCRDLLLRLLQRDP 238
                        170
                 ....*....|....
gi 545477471 158 SERLTAPEILLHPW 171
Cdd:cd14121  239 DRRISFEEFFAHPF 252
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
4-172 3.37e-25

Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PASK (or PASKIN) is a nutrient and energy sensor and thus, plays an important role in maintaining cellular energy homeostasis. It coordinates the utilization of glucose in response to metabolic demand. It contains an N-terminal PAS domain which directly interacts and inhibits a C-terminal catalytic kinase domain. The PAS domain serves as a sensory module for different environmental signals such as light, redox state, and various metabolites. Binding of ligands to the PAS domain causes structural changes which leads to kinase activation and the phosphorylation of substrates to trigger the appropriate cellular response. The PASK 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: 270906 [Multi-domain]  Cd Length: 256  Bit Score: 98.61  E-value: 3.37e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLrLESLEDTHIMKGEDDALSdkhGCPAYV 83
Cdd:cd14004   99 FIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKL-IDFGSAAYIKSGPFDTFV---GTIDYA 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDpsalfsKIRRGQFCIPEHISPKARCLIRSLLRREPSERLTA 163
Cdd:cd14004  175 APEVLRGN-PYGGKEQDIWALGVLLYTLVFKENPFYNIE------EILEADLRIPYAVSEDLIDLISRMLNRDVGDRPTI 247

                 ....*....
gi 545477471 164 PEILLHPWF 172
Cdd:cd14004  248 EELLTDPWL 256
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
5-171 3.60e-25

Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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 AMP-activated protein kinase (AMPK). CaMKK2, also called CaMKK beta, is one of the most versatile CaMKs. It is involved in regulating energy balance, glucose metabolism, adiposity, hematopoiesis, inflammation, and cancer. CaMKK2 contains unique N- and C-terminal domains and a central catalytic kinase domain that is followed by a regulatory domain that bears overlapping autoinhibitory and CaM-binding regions. It can be activated by signaling through G-coupled receptors, IP3 receptors, plasma membrane ion channels, and Toll-like receptors. Thus, CaMKK2 acts as a molecular hub that is capable of receiving and decoding signals from diverse pathways. The CaMKK2 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: 271101 [Multi-domain]  Cd Length: 286  Bit Score: 99.27  E-value: 3.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLESLEDTHIMKGEDDALSDKHGCPAYVS 84
Cdd:cd14199  117 VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVG--EDGHIKIADFGVSNEFEGSDALLTNTVGTPAFMA 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTT-GTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEH--ISPKARCLIRSLLRREPSERL 161
Cdd:cd14199  195 PETLSETrKIFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHSKIKTQPLEFPDQpdISDDLKDLLFRMLDKNPESRI 274
                        170
                 ....*....|
gi 545477471 162 TAPEILLHPW 171
Cdd:cd14199  275 SVPEIKLHPW 284
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
1-204 5.00e-25

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: 98.81  E-value: 5.00e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLrEEEAARLF-KQIVSAVAHCHQSAIVLGDLKLRkfvfsteertQLRLESleDTHImkgeddALSD---- 75
Cdd:cd05580   88 LFSLLRRSGRF-PNDVAKFYaAEVVLALEYLHSLDIVYRDLKPE----------NLLLDS--DGHI------KITDfgfa 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  76 KH---------GCPAYVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKAR 146
Cdd:cd05580  149 KRvkdrtytlcGTPEYLAPEIILSKGH--GKAVDWWALGILIYEMLAGYPPFFDENPMKIYEKILEGKIRFPSFFDPDAK 226
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 545477471 147 CLIRSLLRREPSERL-----TAPEILLHPWFESV----LEPGYIDSEigtsdqIVPEYQEDSDISSF 204
Cdd:cd05580  227 DLIKRLLVVDLTKRLgnlknGVEDIKNHPWFAGIdwdaLLQRKIPAP------YVPKVRGPGDTSNF 287
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
13-171 5.57e-25

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: 98.32  E-value: 5.57e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERtqlRLESLEDTHIMK--GEDDALSDKHGCPAYVSPEIL-- 88
Cdd:cd14098  100 EQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDP---VIVKISDFGLAKviHTGTFLVTFCGTMAYLAPEILms 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  89 ---NTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPE----HISPKARCLIRSLLRREPSERL 161
Cdd:cd14098  177 keqNLQGGYSNLV-DMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPPlvdfNISEEAIDFILRLLDVDPEKRM 255
                        170
                 ....*....|
gi 545477471 162 TAPEILLHPW 171
Cdd:cd14098  256 TAAQALDHPW 265
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
6-174 6.59e-25

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; 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. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK1 functions as a positive regulator of mitosis, meiosis, and cytokinesis. Its localization changes during mitotic progression; associating first with centrosomes in prophase, with kinetochores in prometaphase and metaphase, at the central spindle in anaphase, and in the midbody during telophase. It carries multiple functions throughout the cell cycle through interactions with differrent substrates at these specific subcellular locations. PLK1 is overexpressed in many human cancers and is associated with poor prognosis. The PLK1 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: 271089 [Multi-domain]  Cd Length: 265  Bit Score: 98.08  E-value: 6.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   6 RSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEdthiMKGEDDALSDKHGC--PAYV 83
Cdd:cd14187   99 KRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLA----TKVEYDGERKKTLCgtPNYI 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTGtySGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLTA 163
Cdd:cd14187  175 APEVLSKKG--HSFEVDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPTI 252
                        170
                 ....*....|.
gi 545477471 164 PEILLHPWFES 174
Cdd:cd14187  253 NELLNDEFFTS 263
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
13-171 1.14e-24

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type I delta; 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. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). In vertebrates, there are four CaMKI proteins encoded by different genes (alpha, beta, gamma, and delta), each producing at least one variant. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. 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. In addition, they may be involved in osteoclast differentiation and bone resorption. The CaMKI-delta subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271070 [Multi-domain]  Cd Length: 301  Bit Score: 98.20  E-value: 1.14e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFV-FSTEERTQLRLESLEDTHiMKGEDDALSDKHGCPAYVSPEILnTT 91
Cdd:cd14168  107 EKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLyFSQDEESKIMISDFGLSK-MEGKGDVMSTACGTPGYVAPEVL-AQ 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  92 GTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG--QFCIP--EHISPKARCLIRSLLRREPSERLTAPEIL 167
Cdd:cd14168  185 KPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAdyEFDSPywDDISDSAKDFIRNLMEKDPNKRYTCEQAL 263

                 ....
gi 545477471 168 LHPW 171
Cdd:cd14168  264 RHPW 267
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
10-172 1.32e-24

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs, also called STK17, were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. They may play a role in apoptotic signaling. The DRAK 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: 271008 [Multi-domain]  Cd Length: 268  Bit Score: 97.04  E-value: 1.32e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEErtqlrleSLEDTHIMK-------GEDDALSDKHGCPAY 82
Cdd:cd14106  104 CLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEF-------PLGDIKLCDfgisrviGEGEEIREILGTPDY 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNttgtYS--GKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEH----ISPKARCLIRSLLRRE 156
Cdd:cd14106  177 VAPEILS----YEpiSLATDMWSIGVLTYVLLTGHSPFGGDDKQETFLNISQCNLDFPEElfkdVSPLAIDFIKRLLVKD 252
                        170
                 ....*....|....*.
gi 545477471 157 PSERLTAPEILLHPWF 172
Cdd:cd14106  253 PEKRLTAKECLEHPWL 268
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
1-170 1.34e-24

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


Pssm-ID: 270855 [Multi-domain]  Cd Length: 258  Bit Score: 96.76  E-value: 1.34e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKR----LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKfVFSTEERTqLRLESLEDTHIMKGEDDALSDK 76
Cdd:cd08215   86 LAQKIKKQKKkgqpFPEEQILDWFVQICLALKYLHSRKILHRDLKTQN-IFLTKDGV-VKLGDFGISKVLESTTDLAKTV 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  77 HGCPAYVSPEILNTTGtYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC-IPEHISPKARCLIRSLLRR 155
Cdd:cd08215  164 VGTPYYLSPELCENKP-YNYKS-DIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQYSSELRDLVNSMLQK 241
                        170
                 ....*....|....*
gi 545477471 156 EPSERLTAPEILLHP 170
Cdd:cd08215  242 DPEKRPSANEILSSP 256
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
4-171 1.59e-24

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3). PIM3 can inhibit apoptosis and promote cell survival and protein translation, therefore, it can enhance the proliferation of normal and cancer cells. Mice deficient with PIM3 show minimal effects, suggesting that PIM3 msy not be essential. Since its expression is enhanced in several cancers, it may make a good molecular target for cancer drugs. The PIM3 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: 271004 [Multi-domain]  Cd Length: 253  Bit Score: 96.56  E-value: 1.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTeeRT-QLRLESLEDTHIMKgeDDALSDKHGCPAY 82
Cdd:cd14102   95 FITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDL--RTgELKLIDFGSGALLK--DTVYTDFDGTRVY 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDpsalfsKIRRGQFCIPEHISPKARCLIRSLLRREPSERLT 162
Cdd:cd14102  171 SPPEWIRYH-RYHGRSATVWSLGVLLYDMVCGDIPFEQDE------EILRGRLYFRRRVSPECQQLIKWCLSLRPSDRPT 243

                 ....*....
gi 545477471 163 APEILLHPW 171
Cdd:cd14102  244 LEQIFDHPW 252
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
1-172 2.16e-24

Catalytic domain of Fungal Halotolerance protein 4-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 HAL4, Saccharomyces cerevisiae Ptk2/Stk2, and similar fungal proteins. Proteins in this subfamily are involved in regulating ion transporters. In budding and fission yeast, HAL4 promotes potassium ion uptake, which increases cellular resistance to other cations such as sodium, lithium, and calcium ions. HAL4 stabilizes the major high-affinity K+ transporter Trk1 at the plasma membrane under low K+ conditions, which prevents endocytosis and vacuolar degradation. Budding yeast Ptk2 phosphorylates and regulates the plasma membrane H+ ATPase, Pma1. The HAL4-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: 270896 [Multi-domain]  Cd Length: 265  Bit Score: 96.61  E-value: 2.16e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLESLEDTHIMKGEDDALSDKH--- 77
Cdd:cd13994   85 LFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLD--EDGVLKLTDFGTAEVFGMPAEKESPMSagl 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 -GCPAYVSPEILnTTGTYSGKAADVWSLGVMLYTLLVGRYPF---HDSDPS-ALFSKIRRGQFCIPEHISP----KARCL 148
Cdd:cd13994  163 cGSEPYMAPEVF-TSGSYDGRAVDVWSCGIVLFALFTGRFPWrsaKKSDSAyKAYEKSGDFTNGPYEPIENllpsECRRL 241
                        170       180
                 ....*....|....*....|....
gi 545477471 149 IRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd13994  242 IYRMLHPDPEKRITIDEALNDPWV 265
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
13-204 2.98e-24

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K 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: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 97.48  E-value: 2.98e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHImkgEDDALSDKH-GCPAYVSPEILNTT 91
Cdd:cd05584   99 EDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKESI---HDGTVTHTFcGTIEYMAPEILTRS 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  92 GtySGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL-----TAPEI 166
Cdd:cd05584  176 G--HGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNVSSRLgsgpgDAEEI 253
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 545477471 167 LLHPWFESV---------LEPGYIdseigtsdqivPEYQEDSDISSF 204
Cdd:cd05584  254 KAHPFFRHInwddllakkVEPPFK-----------PLLQSEEDVSQF 289
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
1-172 3.23e-24

Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; 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. There are five mammalian PLKs (PLK1-5) from distinct genes. PLK2, also called Snk (serum-inducible kinase), functions in G1 progression, S-phase arrest, and centriole duplication. Its gene is responsive to both growth factors and cellular stress, is a transcriptional target of p53, and activates a G2-M checkpoint. The PLK2 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: 271090 [Multi-domain]  Cd Length: 255  Bit Score: 95.85  E-value: 3.23e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLESLEDTHIMKGEDDALSDKHGCP 80
Cdd:cd14188   88 MAHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFIN--ENMELKVGDFGLAARLEPLEHRRRTICGTP 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGtySGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd14188  166 NYLSPEVLNKQG--HGCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPEDR 243
                        170
                 ....*....|..
gi 545477471 161 LTAPEILLHPWF 172
Cdd:cd14188  244 PSLDEIIRHDFF 255
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
10-204 3.87e-24

Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear Dbf2-Related (NDR)-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 ROCK and ROCK-like proteins such as DMPK, MRCK, and CRIK, as well as NDR and NDR-like proteins such as LATS, CBK1 and Sid2p. ROCK and CRIK are effectors of the small GTPase Rho, while MRCK is an effector of the small GTPase Cdc42. NDR and NDR-like kinases contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Proteins in this subfamily are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. The ROCK/NDR-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: 270725 [Multi-domain]  Cd Length: 350  Bit Score: 97.36  E-value: 3.87e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIV-------------LGDLKLRKFVFSTE-ERTQLRLESLEDTHIMKGEDDALSD 75
Cdd:cd05573   97 VFPEETARFYIAELVLALDSLHKLGFIhrdikpdnilldaDGHIKLADFGLCTKmNKSGDRESYLNDSVNTLFQDNVLAR 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  76 KH-------------GCPAYVSPEILntTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ--FCIPEH 140
Cdd:cd05573  177 RRphkqrrvraysavGTPDYIAPEVL--RGTGYGPECDWWSLGVILYEMLYGFPPFYSDSLVETYSKIMNWKesLVFPDD 254
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545477471 141 --ISPKARCLIRSLLrREPSERLT-APEILLHPWFESvlepgyID--SEIGTSDQIVPEYQEDSDISSF 204
Cdd:cd05573  255 pdVSPEAIDLIRRLL-CDPEDRLGsAEEIKAHPFFKG------IDweNLRESPPPFVPELSSPTDTSNF 316
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
7-204 1.04e-23

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. There are three PKB isoforms from different genes, PKB-alpha (or Akt1), PKB-beta (or Akt2), and PKB-gamma (or Akt3). PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. It is activated downstream of phosphoinositide 3-kinase (PI3K) and plays important roles in diverse cellular functions including cell survival, growth, proliferation, angiogenesis, motility, and migration. PKB also has a central role in a variety of human cancers, having been implicated in tumor initiation, progression, and metastasis. The PKB 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 PI3K.


Pssm-ID: 270723 [Multi-domain]  Cd Length: 322  Bit Score: 95.89  E-value: 1.04e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLREEEAARLF-KQIVSAVAHCHQSAIVLGDLKLRkfvfsteertQLRLESleDTHImKGEDDALSDKH-------- 77
Cdd:cd05571   87 SRERVFSEDRTRFYgAEIVLALGYLHSQGIVYRDLKLE----------NLLLDK--DGHI-KITDFGLCKEEisygattk 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 ---GCPAYVSPEILNTTgTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLR 154
Cdd:cd05571  154 tfcGTPEYLAPEVLEDN-DY-GRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLK 231
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 545477471 155 REPSERL-----TAPEILLHPWFESVLEPGYIDSEIgtSDQIVPEYQEDSDISSF 204
Cdd:cd05571  232 KDPKKRLgggprDAKEIMEHPFFASINWDDLYQKKI--PPPFKPQVTSETDTRYF 284
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
3-171 1.80e-23

Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes yeast ATG1 and metazoan homologs including vertebrate ULK1-3. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. It is involved in nutrient sensing and signaling, the assembly of autophagy factors and the execution of autophagy. In metazoans, ATG1 homologs display additional functions. Unc-51 and ULKs have been implicated in neuronal and axonal development. The ATG1/ULK 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: 270911 [Multi-domain]  Cd Length: 251  Bit Score: 93.83  E-value: 1.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFST-EERTQLRL------ESLEDThimkGEDDALSd 75
Cdd:cd14009   81 QYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTsGDDPVLKIadfgfaRSLQPA----SMAETLC- 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  76 khGCPAYVSPEILNTTgTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG----QFCIPEHISPKARCLIRS 151
Cdd:cd14009  156 --GSPLYMAPEILQFQ-KYDAKA-DLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSdaviPFPIAAQLSPDCKDLLRR 231
                        170       180
                 ....*....|....*....|
gi 545477471 152 LLRREPSERLTAPEILLHPW 171
Cdd:cd14009  232 LLRRDPAERISFEEFFAHPF 251
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
4-171 1.83e-23

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 5 (MAPKAP5 or MK5) is also called PRAK (p38-regulated/activated protein kinase). It contains a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK5 is a ubiquitous protein that is implicated in neuronal morphogenesis, cell migration, and tumor angiogenesis. It interacts with PKA, which induces cytoplasmic translocation of MK5. Its substrates includes p53, ERK3/4, Hsp27, and cytosolic phospholipase A2 (cPLA2). The MAPKAPK 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: 271073 [Multi-domain]  Cd Length: 289  Bit Score: 94.45  E-value: 1.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVF--STEERTQlrleSLEDTHIMKGEDDALSDKHGCPA 81
Cdd:cd14171   99 RISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLkdNSEDAPI----KLCDFGFAKVDQGDLMTPQFTPY 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILN---------------TTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFS-----KIRRGQFCIPEH- 140
Cdd:cd14171  175 YVAPQVLEaqrrhrkersgiptsPTPYTYDKSCDMWSLGVIIYIMLCGYPPFYSEHPSRTITkdmkrKIMTGSYEFPEEe 254
                        170       180       190
                 ....*....|....*....|....*....|....
gi 545477471 141 ---ISPKARCLIRSLLRREPSERLTAPEILLHPW 171
Cdd:cd14171  255 wsqISEMAKDIVRKLLCVDPEERMTIEEVLHHPW 288
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
4-172 2.43e-23

Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK1 and TSSK2 are expressed specifically in meiotic and postmeiotic spermatogenic cells, respectively. TSSK2 is localized in the sperm neck, equatorial segment, and mid-piece of the sperm tail. Both TSSK1 and TSSK2 phosphorylate their common substrate TSKS (testis-specific-kinase-substrate). TSSK1/TSSK2 double knock-out mice are sterile without manifesting other defects, making these kinases viable targets for male contraception. The TSSK1/2-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: 271067 [Multi-domain]  Cd Length: 263  Bit Score: 93.69  E-value: 2.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL-------RLESLEDTHIMkgeddaLSDK 76
Cdd:cd14165   92 FIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLtdfgfskRCLRDENGRIV------LSKT 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  77 H-GCPAYVSPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALF--SKIRRGQFCIPEHISPKARCLIRSLL 153
Cdd:cd14165  166 FcGSAAYAAPEVLQGI-PYDPRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLkiQKEHRVRFPRSKNLTSECKDLIYRLL 244
                        170
                 ....*....|....*....
gi 545477471 154 RREPSERLTAPEILLHPWF 172
Cdd:cd14165  245 QPDVSQRLCIDEVLSHPWL 263
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
4-171 4.98e-23

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 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: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 92.73  E-value: 4.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEeRTQLRLESLEDTHIMKgeDDALSDKHGCPAYV 83
Cdd:cd14100   96 FITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDLN-TGELKLIDFGSGALLK--DTVYTDFDGTRVYS 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPF-HDSDpsalfskIRRGQFCIPEHISPKARCLIRSLLRREPSERLT 162
Cdd:cd14100  173 PPEWIRFH-RYHGRSAAVWSLGILLYDMVCGDIPFeHDEE-------IIRGQVFFRQRVSSECQHLIKWCLALRPSDRPS 244

                 ....*....
gi 545477471 163 APEILLHPW 171
Cdd:cd14100  245 FEDIQNHPW 253
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
8-171 6.89e-23

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK 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: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 92.57  E-value: 6.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEI 87
Cdd:cd14070   97 KKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGILGYSDPFSTQCGSPAYAAPEL 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  88 LNTTGTysGKAADVWSLGVMLYTLLVGRYPFhDSDP---SALFSKIRRGQFC-IPEHISPKARCLIRSLLRREPSERLTA 163
Cdd:cd14070  177 LARKKY--GPKVDVWSIGVNMYAMLTGTLPF-TVEPfslRALHQKMVDKEMNpLPTDLSPGAISFLRSLLEPDPLKRPNI 253

                 ....*...
gi 545477471 164 PEILLHPW 171
Cdd:cd14070  254 KQALANRW 261
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
13-172 7.74e-23

Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chk1 is implicated in many major checkpoints of the cell cycle, providing a link between upstream sensors and the cell cycle engine. It plays an important role in DNA damage response and maintaining genomic stability. Chk1 acts as an effector of the sensor kinase, ATR (ATM and Rad3-related), a member of the PI3K family, which is activated upon DNA replication stress. Chk1 delays mitotic entry in response to replication blocks by inhibiting cyclin dependent kinase (Cdk) activity. In addition, Chk1 contributes to the function of centrosome and spindle-based checkpoints, inhibits firing of origins of DNA replication (Ori), and represses transcription of cell cycle proteins including cyclin B and Cdk1. The Chk1 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: 270971 [Multi-domain]  Cd Length: 261  Bit Score: 92.39  E-value: 7.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLES--LEDTHIMKGEDDALSDKHGCPAYVSPEILNT 90
Cdd:cd14069   99 EDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLL--DENDNLKISDfgLATVFRYKGKERLLNKMCGTLPYVAPELLAK 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  91 TGtYSGKAADVWSLGVMLYTLLVGRYPFHD-SDPSALFS---KIRRGQFCIPEHISPKARCLIRSLLRREPSERLTAPEI 166
Cdd:cd14069  177 KK-YRAEPVDVWSCGIVLFAMLAGELPWDQpSDSCQEYSdwkENKKTYLTPWKKIDTAALSLLRKILTENPNKRITIEDI 255

                 ....*.
gi 545477471 167 LLHPWF 172
Cdd:cd14069  256 KKHPWY 261
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
5-194 8.86e-23

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 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: 271081 [Multi-domain]  Cd Length: 310  Bit Score: 93.18  E-value: 8.86e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTE-ERTQLRLESLEDTHIMKGEDDALSDKHGCPAYV 83
Cdd:cd14179   93 IKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFTDEsDNSEIKIIDFGFARLKPPDNQPLKTPCFTLHYA 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTGtYSgKAADVWSLGVMLYTLLVGRYPFHDSDPS-------ALFSKIRRGQFCIP----EHISPKARCLIRSL 152
Cdd:cd14179  173 APELLNYNG-YD-ESCDLWSLGVILYTMLSGQVPFQCHDKSltctsaeEIMKKIKQGDFSFEgeawKNVSQEAKDLIQGL 250
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 545477471 153 LRREPSERLTAPEILLHPWFESvlepgyiDSEIGTSDQIVPE 194
Cdd:cd14179  251 LTVDPNKRIKMSGLRYNEWLQD-------GSQLSSNPLMTPD 285
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
2-170 1.19e-22

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: 90.79  E-value: 1.19e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   2 HSYVRSR-KRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLESLEDTHIMKGEDDALSDKHGCP 80
Cdd:cd00180   79 KDLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLD--SDGTVKLADFGLAKDLDSDDSLLKTTGGTT 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGTYSGKAADVWSLGVMLYTLlvgrypfhdsdpsalfskirrgqfcipehisPKARCLIRSLLRREPSER 160
Cdd:cd00180  157 PPYYAPPELLGGRYYGPKVDIWSLGVILYEL-------------------------------EELKDLIRRMLQYDPKKR 205
                        170
                 ....*....|
gi 545477471 161 LTAPEILLHP 170
Cdd:cd00180  206 PSAKELLEHL 215
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
6-171 1.87e-22

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 3 (MAPKAP3 or MK3) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK3 is a bonafide substrate for the MAPK p38. It is closely related to MK2 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. MK3 activity is only significant when MK2 is absent. The MK3 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: 271074 [Multi-domain]  Cd Length: 267  Bit Score: 91.59  E-value: 1.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   6 RSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRleSLEDTHIMK--GEDDALSDKHGCPAYV 83
Cdd:cd14172   95 RGDQAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYTSKEKDAVL--KLTDFGFAKetTVQNALQTPCYTPYYV 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTgTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALF----SKIRRGQFCIPE----HISPKARCLIRSLLRR 155
Cdd:cd14172  173 APEVLGPE-KYD-KSCDMWSLGVIMYILLCGFPPFYSNTGQAISpgmkRRIRMGQYGFPNpewaEVSEEAKQLIRHLLKT 250
                        170
                 ....*....|....*.
gi 545477471 156 EPSERLTAPEILLHPW 171
Cdd:cd14172  251 DPTERMTITQFMNHPW 266
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
3-172 2.22e-22

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: 91.04  E-value: 2.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL-------RLESLEDTHIMKGeddalsd 75
Cdd:cd06606   88 SLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLadfgcakRLAEIATGEGTKS------- 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  76 KHGCPAYVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHD-SDPSALFSKIRRGQFC--IPEHISPKARCLIRSL 152
Cdd:cd06606  161 LRGTPYWMAPEVIRGEGY--GRAADIWSLGCTVIEMATGKPPWSElGNPVAALFKIGSSGEPppIPEHLSEEAKDFLRKC 238
                        170       180
                 ....*....|....*....|
gi 545477471 153 LRREPSERLTAPEILLHPWF 172
Cdd:cd06606  239 LQRDPKKRPTADELLQHPFL 258
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
11-172 3.09e-22

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 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: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 91.15  E-value: 3.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERT-QLRLESLEDTHIMKGEDDaLSDKHGCPAYVSPEILN 89
Cdd:cd14197  108 FKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESPLgDIKIVDFGLSRILKNSEE-LREIMGTPEYVAPEILS 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  90 TTGTYSgkAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIP----EHISPKARCLIRSLLRREPSERLTAPE 165
Cdd:cd14197  187 YEPIST--ATDMWSIGVLAYVMLTGISPFLGDDKQETFLNISQMNVSYSeeefEHLSESAIDFIKTLLIKKPENRATAED 264

                 ....*..
gi 545477471 166 ILLHPWF 172
Cdd:cd14197  265 CLKHPWL 271
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
4-171 3.17e-22

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are three PIM2 isoforms resulting from alternative translation initiation sites. PIM2 is highly expressed in leukemia and lymphomas and has been shown to promote the survival and proliferation of tumor cells. The PIM2 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: 271003 [Multi-domain]  Cd Length: 257  Bit Score: 90.68  E-value: 3.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEeRTQLRLESLEDTHIMKgeDDALSDKHGCPAYV 83
Cdd:cd14101   98 YITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLR-TGDIKLIDFGSGATLK--DSMYTDFDGTRVYS 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPF-HDSDpsalfskIRRGQFCIPEHISPKARCLIRSLLRREPSERLT 162
Cdd:cd14101  175 PPEWILYH-QYHALPATVWSLGILLYDMVCGDIPFeRDTD-------ILKAKPSFNKRVSNDCRSLIRSCLAYNPSDRPS 246

                 ....*....
gi 545477471 163 APEILLHPW 171
Cdd:cd14101  247 LEQILLHPW 255
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
1-204 4.68e-22

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: 90.96  E-value: 4.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLrleslEDTHIMKGEDDALSDKHGCP 80
Cdd:cd05612   88 LFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKL-----TDFGFAKKLRDRTWTLCGTP 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGtySGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd05612  163 EYLAPEVIQSKG--HNKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVDRTRR 240
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 545477471 161 L-----TAPEILLHPWFESV---------LEPgyidseigtsdQIVPEYQEDSDISSF 204
Cdd:cd05612  241 LgnmknGADDVKNHRWFKSVdwddvpqrkLKP-----------PIVPKVSHDGDTSNF 287
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
2-168 7.51e-22

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: 89.57  E-value: 7.51e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   2 HSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLR---LESLEDTHIMKGEDDALsdkhG 78
Cdd:cd14014   88 ADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTdfgIARALGDSGLTQTGSVL----G 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEILntTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPE----HISPKARCLIRSLLR 154
Cdd:cd14014  164 TPAYMAPEQA--RGGPVDPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSplnpDVPPALDAIILRALA 241
                        170
                 ....*....|....
gi 545477471 155 REPSERLTAPEILL 168
Cdd:cd14014  242 KDPEERPQSAAELL 255
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
13-171 9.22e-22

Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to Calcium/calmodulin-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 uncharacterized STKs with similarity to CaMKs, which are multifunctional calcium and calmodulin (CaM) stimulated STKs involved in cell cycle regulation. The CaMK family includes CaMKI, CaMKII, CaMKIV, and CaMK kinase (CaMKK). CaMKs contain an N-terminal catalytic domain followed by a regulatory domain that harbors a CaM binding site. This uncharacterized subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 89.70  E-value: 9.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTeeRTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTTg 92
Cdd:cd14088   98 ERDTSNVIRQVLEAVAYLHSLKIVHRNLKLENLVYYN--RLKNSKIVISDFHLAKLENGLIKEPCGTPEYLAPEVVGRQ- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  93 tYSGKAADVWSLGVMLYTLLVGRYPFHD--------SDPSALFSKIRRG--QFCIP--EHISPKARCLIRSLLRREPSER 160
Cdd:cd14088  175 -RYGRPVDCWAIGVIMYILLSGNPPFYDeaeeddyeNHDKNLFRKILAGdyEFDSPywDDISQAAKDLVTRLMEVEQDQR 253
                        170
                 ....*....|.
gi 545477471 161 LTAPEILLHPW 171
Cdd:cd14088  254 ITAEEAISHEW 264
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
13-204 9.35e-22

Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. There are four nPKC isoforms, delta, epsilon, eta, and theta. The nPKC-theta-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: 270744 [Multi-domain]  Cd Length: 320  Bit Score: 90.52  E-value: 9.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLF-KQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMkGEDDAlSDKHGCPAYVSPEILNtt 91
Cdd:cd05592   94 DEDRARFYgAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIY-GENKA-STFCGTPDYIAPEILK-- 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  92 GTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL-----TAPEI 166
Cdd:cd05592  170 GQKYNQSVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKRLgvpecPAGDI 249
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 545477471 167 LLHPWFESV----LEPGYIDSeigtsdQIVPEYQEDSDISSF 204
Cdd:cd05592  250 RDHPFFKTIdwdkLERREIDP------PFKPKVKSANDVSNF 285
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
7-175 1.14e-21

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-alpha is predominantly expressed in endothelial cells. It is critical for the regulation of angiogenesis and the maintenance of vascular integrity. It also plays a role in adipocyte differentiation. Mice deficient in PKB-alpha exhibit perinatal morbidity, growth retardation, reduction in body weight accompanied by reduced sizes of multiple organs, and enhanced apoptosis in some cell types. PKB-alpha activity has been reported to be frequently elevated in breast and prostate cancers. In some cancer cells, PKB-alpha may act as a suppressor of metastasis. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-alpha 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: 270746 [Multi-domain]  Cd Length: 356  Bit Score: 90.86  E-value: 1.14e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLREEEAARLF-KQIVSAVAHCH-QSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEddALSDKHGCPAYVS 84
Cdd:cd05594  117 SRERVFSEDRARFYgAEIVSALDYLHsEKNVVYRDLKLENLMLDKDGHIKITDFGLCKEGIKDGA--TMKTFCGTPEYLA 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL--- 161
Cdd:cd05594  195 PEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLSPEAKSLLSGLLKKDPKQRLggg 272
                        170
                 ....*....|....*.
gi 545477471 162 --TAPEILLHPWFESV 175
Cdd:cd05594  273 pdDAKEIMQHKFFAGI 288
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
13-171 1.21e-21

Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase Type IV; 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. CaMKs contain an N-terminal catalytic domain and a C-terminal regulatory domain that harbors a CaM binding site. CaMKIV is found predominantly in neurons and immune cells. It is activated by the binding of calcium/CaM and phosphorylation by CaMKK (alpha or beta). The CaMKK-CaMKIV cascade participates in regulating several transcription factors like CREB, MEF2, and retinoid orphan receptors. It also is implicated in T-cell development and signaling, cytokine secretion, and signaling through Toll-like receptors, and is thus, pivotal in immune response and inflammation. The CaMKIV subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270987 [Multi-domain]  Cd Length: 294  Bit Score: 89.88  E-value: 1.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTE-ERTQLRlesLEDTHIMKGEDDALSDKHGC--PAYVSPEILN 89
Cdd:cd14085   97 ERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATPaPDAPLK---IADFGLSKIVDQQVTMKTVCgtPGYCAPEILR 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  90 ttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSD-PSALFSKIRRGQ--FCIP--EHISPKARCLIRSLLRREPSERLTAP 164
Cdd:cd14085  174 --GCAYGPEVDMWSVGVITYILLCGFEPFYDERgDQYMFKRILNCDydFVSPwwDDVSLNAKDLVKKLIVLDPKKRLTTQ 251

                 ....*..
gi 545477471 165 EILLHPW 171
Cdd:cd14085  252 QALQHPW 258
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
3-173 1.21e-21

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk 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: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 89.70  E-value: 1.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQ------------LRLESlEDTHIMKGEd 70
Cdd:cd14174   89 AHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCESPDKVSpvkicdfdlgsgVKLNS-ACTPITTPE- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  71 daLSDKHGCPAYVSPEILNT---TGTYSGKAADVWSLGVMLYTLLVGRYPFHD---------------SDPSALFSKIRR 132
Cdd:cd14174  167 --LTTPCGSAEYMAPEVVEVftdEATFYDKRCDLWSLGVILYIMLSGYPPFVGhcgtdcgwdrgevcrVCQNKLFESIQE 244
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 545477471 133 GQFCIPE----HISPKARCLIRSLLRREPSERLTAPEILLHPWFE 173
Cdd:cd14174  245 GKYEFPDkdwsHISSEAKDLISKLLVRDAKERLSAAQVLQHPWVQ 289
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
14-171 2.05e-21

Catalytic domain of RCK1-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 fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-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: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 89.03  E-value: 2.05e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  14 EEAAR-LFKQIVSAVAHCHQSAIVLGDLKLRKFVFST----EERTQLRLESLEDTHIMKGE----------------DDA 72
Cdd:cd14096  105 EDLSRhVITQVASAVKYLHEIGVVHRDIKPENLLFEPipfiPSIVKLRKADDDETKVDEGEfipgvggggigivklaDFG 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  73 LS----DKH-----GCPAYVSPEILNTTgTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ--FCIP--E 139
Cdd:cd14096  185 LSkqvwDSNtktpcGTVGYTAPEVVKDE-RYS-KKVDMWALGCVLYTLLCGFPPFYDESIETLTEKISRGDytFLSPwwD 262
                        170       180       190
                 ....*....|....*....|....*....|..
gi 545477471 140 HISPKARCLIRSLLRREPSERLTAPEILLHPW 171
Cdd:cd14096  263 EISKSAKDLISHLLTVDPAKRYDIDEFLAHPW 294
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
3-173 2.50e-21

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: 88.44  E-value: 2.50e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL-------RLESLEDTHIMKGEddalsd 75
Cdd:cd05572   82 TILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLvdfgfakKLGSGRKTWTFCGT------ 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  76 khgcPAYVSPEILNTTGtYsGKAADVWSLGVMLYTLLVGRYPFH--DSDPSALFSKIRRGQFCI--PEHISPKARCLIRS 151
Cdd:cd05572  156 ----PEYVAPEIILNKG-Y-DFSVDYWSLGILLYELLTGRPPFGgdDEDPMKIYNIILKGIDKIefPKYIDKNAKNLIKQ 229
                        170       180
                 ....*....|....*....|....*..
gi 545477471 152 LLRREPSERL-----TAPEILLHPWFE 173
Cdd:cd05572  230 LLRRNPEERLgylkgGIRDIKKHKWFE 256
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
11-175 3.36e-21

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: 87.92  E-value: 3.36e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLES--LEDTHIMKGEDDALSdkhGCPAYVSPEIL 88
Cdd:cd05611   94 LPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLID--QTGHLKLTDfgLSRNGLEKRHNKKFV---GTPDYLAPETI 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  89 NttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIP----EHISPKARCLIRSLLRREPSERLTA- 163
Cdd:cd05611  169 L--GVGDDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPeevkEFCSPEAVDLINRLLCMDPAKRLGAn 246
                        170
                 ....*....|....
gi 545477471 164 --PEILLHPWFESV 175
Cdd:cd05611  247 gyQEIKSHPFFKSI 260
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
6-167 6.39e-21

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: 87.39  E-value: 6.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   6 RSRKRLREEEAARLFKQIVSAVAHCH--QSAIVLGDLKLRKFVFSTEERTQL-----------RLESLEDTHIMKGEdda 72
Cdd:cd13985   95 SPPSPLSEEEVLRIFYQICQAVGHLHsqSPPIIHRDIKIENILFSNTGRFKLcdfgsattehyPLERAEEVNIIEEE--- 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  73 lSDKHGCPAYVSPEILNTTGTYS-GKAADVWSLGVMLYTLLVGRYPFHDSDPsalfSKIRRGQFCIPEH--ISPKARCLI 149
Cdd:cd13985  172 -IQKNTTPMYRAPEMIDLYSKKPiGEKADIWALGCLLYKLCFFKLPFDESSK----LAIVAGKYSIPEQprYSPELHDLI 246
                        170
                 ....*....|....*...
gi 545477471 150 RSLLRREPSERLTAPEIL 167
Cdd:cd13985  247 RHMLTPDPAERPDIFQVI 264
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1-175 6.51e-21

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, in response to various stimuli such as growth factors, hormones, neurotransmitters, cellular stress, and pro-inflammatory cytokines. This triggers phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) in the C-terminal extension of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. MSKs are predominantly nuclear proteins. They are widely expressed in many tissues including heart, brain, lung, liver, kidney, and pancreas. There are two isoforms of MSK, called MSK1 and MSK2. The MSK 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: 270735 [Multi-domain]  Cd Length: 268  Bit Score: 87.45  E-value: 6.51e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSdKHGCP 80
Cdd:cd05583   86 LFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRAYS-FCGTI 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPF----HDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRRE 156
Cdd:cd05583  165 EYMAPEVVRGGSDGHDKAVDWWSLGVLTYELLTGASPFtvdgERNSQSEISKRILKSHPPIPKTFSAEAKDFILKLLEKD 244
                        170       180
                 ....*....|....*....|....
gi 545477471 157 PSERL-----TAPEILLHPWFESV 175
Cdd:cd05583  245 PKKRLgagprGAHEIKEHPFFKGL 268
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
2-160 8.66e-21

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 89.30  E-value: 8.66e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   2 HSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEER---------TQLRLESLEDTHIMKGEdda 72
Cdd:COG0515   95 ADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRvklidfgiaRALGGATLTQTGTVVGT--- 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  73 lsdkhgcPAYVSPEILntTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF----CIPEHISPKARCL 148
Cdd:COG0515  172 -------PGYMAPEQA--RGEPVDPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPpppsELRPDLPPALDAI 242
                        170
                 ....*....|..
gi 545477471 149 IRSLLRREPSER 160
Cdd:COG0515  243 VLRALAKDPEER 254
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
13-171 8.78e-21

Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CASK belongs to the MAGUK (membrane-associated guanylate kinase) protein family, which functions as multiple domain adaptor proteins and is characterized by the presence of a core of three domains: PDZ, SH3, and guanylate kinase (GuK). The enzymatically inactive GuK domain in MAGUK proteins mediates protein-protein interactions and associates intramolecularly with the SH3 domain. In addition, CASK contains a catalytic kinase and two L27 domains. It is highly expressed in the nervous system and plays roles in synaptic protein targeting, neural development, and regulation of gene expression. Binding partners include parkin (a Parkinson's disease molecule), neurexin (adhesion molecule), syndecans, calcium channel proteins, CINAP (nucleosome assembly protein), transcription factor Tbr-1, and the cytoplasmic adaptor proteins Mint1, Veli/mLIN-7/MALS, SAP97, caskin, and CIP98. Deletion or mutations in the CASK gene have been implicated in X-linked mental retardation. The CASK 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: 270996 [Multi-domain]  Cd Length: 300  Bit Score: 87.60  E-value: 8.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVF-STEERTQLRL------ESLEDTHIMKGeddalsDKHGCPAYVSP 85
Cdd:cd14094  108 EAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaSKENSAPVKLggfgvaIQLGESGLVAG------GRVGTPHFMAP 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  86 EILntTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDpSALFSKIRRGQFCIP----EHISPKARCLIRSLLRREPSERL 161
Cdd:cd14094  182 EVV--KREPYGKPVDVWGCGVILFILLSGCLPFYGTK-ERLFEGIIKGKYKMNprqwSHISESAKDLVRRMLMLDPAERI 258
                        170
                 ....*....|
gi 545477471 162 TAPEILLHPW 171
Cdd:cd14094  259 TVYEALNHPW 268
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
7-175 1.22e-20

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKB-gamma is predominantly expressed in neuronal tissues. Mice deficient in PKB-gamma show a reduction in brain weight due to the decreases in cell size and cell number. PKB-gamma has also been shown to be upregulated in estrogen-deficient breast cancer cells, androgen-independent prostate cancer cells, and primary ovarian tumors. It acts as a key mediator in the genesis of ovarian cancer. PKB contains an N-terminal pleckstrin homology (PH) domain and a C-terminal catalytic domain. The PKB-gamma 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: 270745 [Multi-domain]  Cd Length: 348  Bit Score: 87.83  E-value: 1.22e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLREEEAARLF-KQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLedthIMKGEDDALSDKHGC--PAYV 83
Cdd:cd05593  107 SRERVFSEDRTRFYgAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGL----CKEGITDAATMKTFCgtPEYL 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL-- 161
Cdd:cd05593  183 APEVLEDNDY--GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKSLLSGLLIKDPNKRLgg 260
                        170
                 ....*....|....*..
gi 545477471 162 ---TAPEILLHPWFESV 175
Cdd:cd05593  261 gpdDAKEIMRHSFFTGV 277
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
1-171 1.31e-20

Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PSKH1 is an autophosphorylating STK that is expressed ubiquitously and exhibits multiple intracellular localizations including the centrosome, Golgi apparatus, and splice factor compartments. It contains a catalytic kinase domain and an N-terminal SH4-like motif that is acylated to facilitate membrane attachment. PSKH1 plays a rile in the maintenance of the Golgi apparatus, an important organelle within the secretory pathway. It may also function as a novel splice factor and a regulator of prostate cancer cell growth. The PSKH1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270989 [Multi-domain]  Cd Length: 259  Bit Score: 86.43  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVF---STEER---TQLRLESLEDthimKGEDDALS 74
Cdd:cd14087   84 LFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpGPDSKimiTDFGLASTRK----KGPNCLMK 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  75 DKHGCPAYVSPEILnTTGTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCI-PEH---ISPKARCLIR 150
Cdd:cd14087  160 TTCGTPEYIAPEIL-LRKPYT-QSVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYsGEPwpsVSNLAKDFID 237
                        170       180
                 ....*....|....*....|.
gi 545477471 151 SLLRREPSERLTAPEILLHPW 171
Cdd:cd14087  238 RLLTVNPGERLSATQALKHPW 258
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
8-171 1.39e-20

Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK33 is highly expressed in the testis and is present in low levels in most tissues. It may be involved in spermatogenesis and organ ontogenesis. It interacts with and phosphorylates vimentin and may be involved in regulating intermediate filament cytoskeletal dynamics. Its role in promoting the cell viability of KRAS-dependent cancer cells is under debate; some studies have found STK33 to promote cancer cell viability, while other studies have found it to be non-essential. KRAS is the most commonly mutated human oncogene, thus, studies on the role of STK33 in KRAS mutant cancer cells are important. The STK33 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: 270999 [Multi-domain]  Cd Length: 266  Bit Score: 86.45  E-value: 1.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFST-----EERTQLRLESLE-DTHIMKGEDDALSDKHGCPA 81
Cdd:cd14097   94 KGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVKSsiidnNDKLNIKVTDFGlSVQKYGLGEDMLQETCGTPI 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNTTGtYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG--QF--CIPEHISPKARCLIRSLLRREP 157
Cdd:cd14097  174 YMAPEVISAHG-YS-QQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGdlTFtqSVWQSVSDAAKNVLQQLLKVDP 251
                        170
                 ....*....|....
gi 545477471 158 SERLTAPEILLHPW 171
Cdd:cd14097  252 AHRMTASELLDNPW 265
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
10-171 1.72e-20

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called Doublecortin-like and CAM kinase-like 3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL3 (or DCAMKL3) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. DCKL3 contains a single DCX domain (instead of a tandem) and a C-terminal kinase domain with similarity to CAMKs. It has been shown to interact with tubulin and JIP1/2. The DCKL3 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: 271087 [Multi-domain]  Cd Length: 258  Bit Score: 86.16  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLEsLEDTHIMKGEDDALSDKHGCPAYVSPEILN 89
Cdd:cd14185   94 KFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVQHNPDKSTTLK-LADFGLAKYVTGPIFTVCGTPTYVAPEILS 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  90 TTGTysGKAADVWSLGVMLYTLLVGRYPFH--DSDPSALFSKIRRG--QFCIP--EHISPKARCLIRSLLRREPSERLTA 163
Cdd:cd14185  173 EKGY--GLEVDMWAAGVILYILLCGFPPFRspERDQEELFQIIQLGhyEFLPPywDNISEAAKDLISRLLVVDPEKRYTA 250

                 ....*...
gi 545477471 164 PEILLHPW 171
Cdd:cd14185  251 KQVLQHPW 258
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
3-171 1.93e-20

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk 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: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 86.31  E-value: 1.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEER------------TQLRLESLEDTHIMKGEd 70
Cdd:cd14090   89 SHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILCESMDKvspvkicdfdlgSGIKLSSTSMTPVTTPE- 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  71 daLSDKHGCPAYVSPEILNT---TGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSA---------------LFSKIRR 132
Cdd:cd14090  168 --LLTPVGSAEYMAPEVVDAfvgEALSYDKRCDLWSLGVILYIMLCGYPPFYGRCGEDcgwdrgeacqdcqelLFHSIQE 245
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 545477471 133 GQFCIPE----HISPKARCLIRSLLRREPSERLTAPEILLHPW 171
Cdd:cd14090  246 GEYEFPEkewsHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
4-171 2.48e-20

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK 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: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 86.00  E-value: 2.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKlrkfvfstEERTQLrLESLEDTHIMKGEDDALSDK------- 76
Cdd:cd14105   98 FLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLK--------PENIML-LDKNVPIPRIKLIDFGLAHKiedgnef 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  77 ---HGCPAYVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPE----HISPKARCLI 149
Cdd:cd14105  169 kniFGTPEFVAPEIVNYEPL--GLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVNYDFDDeyfsNTSELAKDFI 246
                        170       180
                 ....*....|....*....|..
gi 545477471 150 RSLLRREPSERLTAPEILLHPW 171
Cdd:cd14105  247 RQLLVKDPRKRMTIQESLRHPW 268
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
13-170 4.21e-20

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: 85.15  E-value: 4.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLF-KQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEdTHIMKgEDDALSDKhGCPAYVSPEILNTT 91
Cdd:cd06632  100 EEPVIRLYtRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMA-KHVEA-FSFAKSFK-GSPYWMAPEVIMQK 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  92 GTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC--IPEHISPKARCLIRSLLRREPSERLTAPEILLH 169
Cdd:cd06632  177 NSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFKIGNSGELppIPDHLSPDAKDFIRLCLQRDPEDRPTASQLLEH 256

                 .
gi 545477471 170 P 170
Cdd:cd06632  257 P 257
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
1-175 6.89e-20

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. The PKA 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: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 85.15  E-value: 6.89e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLEDTHIMKGEDDALSdkhGCP 80
Cdd:cd14209   88 MFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLI--DQQGYIKVTDFGFAKRVKGRTWTLC---GTP 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGtYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd14209  163 EYLAPEIILSKG-Y-NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQVDLTKR 240
                        170       180
                 ....*....|....*....|
gi 545477471 161 L-----TAPEILLHPWFESV 175
Cdd:cd14209  241 FgnlknGVNDIKNHKWFATT 260
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
8-171 7.14e-20

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called Ribosomal protein S6 kinase alpha-2 or 90kDa ribosomal protein S6 kinase 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK3 is also called S6K-alpha-2, RPS6KA2, p90RSK2 or MAPK-activated protein kinase 1c (MAPKAPK-1c). RSK3 binds muscle A-kinase anchoring protein (mAKAP)-b directly and regulates concentric cardiac myocyte growth. The RSK3 gene, RPS6KA2, is a putative tumor suppressor gene in sporadic epithelial ovarian cancer and variations to the gene may be associated with rectal cancer risk. RSK3 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK3 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: 271080 [Multi-domain]  Cd Length: 293  Bit Score: 85.07  E-value: 7.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERT--QLRLESLEDTHIMKGEDDALSDKHGCPAYVSP 85
Cdd:cd14178   91 QKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILYMDESGNpeSIRICDFGFAKQLRAENGLLMTPCYTANFVAP 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  86 EILNTTGtYSGkAADVWSLGVMLYTLLVGRYPFH---DSDPSALFSKIRRGQFCIP----EHISPKARCLIRSLLRREPS 158
Cdd:cd14178  171 EVLKRQG-YDA-ACDIWSLGILLYTMLAGFTPFAngpDDTPEEILARIGSGKYALSggnwDSISDAAKDIVSKMLHVDPH 248
                        170
                 ....*....|...
gi 545477471 159 ERLTAPEILLHPW 171
Cdd:cd14178  249 QRLTAPQVLRHPW 261
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
6-170 9.91e-20

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Nek2 subfamily includes Aspergillus nidulans NIMA kinase, the founding member of the Nek family, which was identified in a screen for cell cycle mutants prevented from entering mitosis. NIMA is essential for mitotic entry and progression through mitosis, and its degradation is essential for mitotic exit. NIMA is involved in nuclear membrane fission. Vertebrate Nek2 is a cell cycle-regulated STK, localized in centrosomes and kinetochores, that regulates centrosome splitting at the G2/M phase. It also interacts with other mitotic kinases such as Polo-like kinase 1 and may play a role in spindle checkpoint. An increase in the expression of the human NEK2 gene is strongly associated with the progression of non-Hodgkin lymphoma. Nek2 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. It The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270857 [Multi-domain]  Cd Length: 265  Bit Score: 84.13  E-value: 9.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   6 RSRKRLREEEAARLFKQIVSAVAHCH-----QSAIVLGDLKLRKfVFsteertqlrlesLEDTHIMK----GEDDALSDK 76
Cdd:cd08217   97 KENQYIPEEFIWKIFTQLLLALYECHnrsvgGGKILHRDLKPAN-IF------------LDSDNNVKlgdfGLARVLSHD 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  77 H-------GCPAYVSPEILNTtGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF-CIPEHISPKARCL 148
Cdd:cd08217  164 SsfaktyvGTPYYMSPELLNE-QSYDEKS-DIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFpRIPSRYSSELNEV 241
                        170       180
                 ....*....|....*....|..
gi 545477471 149 IRSLLRREPSERLTAPEILLHP 170
Cdd:cd08217  242 IKSMLNVDPDKRPSVEELLQLP 263
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
8-171 9.96e-20

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called Ribosomal protein S6 kinase alpha-1 or 90kDa ribosomal protein S6 kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK1 is also called S6K-alpha-1, RPS6KA1, p90RSK1 or MAPK-activated protein kinase 1a (MAPKAPK-1a). It is a component of the insulin transduction pathway, regulating the function of IRS1. It also interacts with PKA and promotes its inactivation. RSK1 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK1 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: 271077 [Multi-domain]  Cd Length: 291  Bit Score: 84.69  E-value: 9.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTE--ERTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSP 85
Cdd:cd14175   89 QKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILYVDEsgNPESLRICDFGFAKQLRAENGLLMTPCYTANFVAP 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  86 EILNTTGTYSGkaADVWSLGVMLYTLLVGRYPFHD--SD-PSALFSKIRRGQFCIP----EHISPKARCLIRSLLRREPS 158
Cdd:cd14175  169 EVLKRQGYDEG--CDIWSLGILLYTMLAGYTPFANgpSDtPEEILTRIGSGKFTLSggnwNTVSDAAKDLVSKMLHVDPH 246
                        170
                 ....*....|...
gi 545477471 159 ERLTAPEILLHPW 171
Cdd:cd14175  247 QRLTAKQVLQHPW 259
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
6-177 1.16e-19

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK-activated protein kinase 2 (MAPKAP2 or MK2) contains an N-terminal proline-rich region that can bind to SH3 domains, a catalytic kinase domain followed by a C-terminal autoinhibitory region that contains nuclear localization (NLS) and nuclear export (NES) signals with a p38 MAPK docking motif that overlaps the NLS. MK2 is a bonafide substrate for the MAPK p38. It is closely related to MK3 and thus far, MK2/3 show indistinguishable substrate specificity. They are mainly involved in the regulation of gene expression and they participate in diverse cellular processes such as endocytosis, cytokine production, cytoskeletal reorganization, cell migration, cell cycle control and chromatin remodeling. They are implicated in inflammation and cance and their substrates include mRNA-AU-rich-element (ARE)-binding proteins (TTP and hnRNP A0), Hsp proteins (Hsp27 and Hsp25) and RSK, among others. MK2/3 are both expressed ubiquitously but MK2 is expressed at significantly higher levels. The MK2 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: 271072 [Multi-domain]  Cd Length: 303  Bit Score: 84.70  E-value: 1.16e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   6 RSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRleSLEDTHIMK--GEDDALSDKHGCPAYV 83
Cdd:cd14170   93 RGDQAFTEREASEIMKSIGEAIQYLHSINIAHRDVKPENLLYTSKRPNAIL--KLTDFGFAKetTSHNSLTTPCYTPYYV 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTgTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALF----SKIRRGQFCIP----EHISPKARCLIRSLLRR 155
Cdd:cd14170  171 APEVLGPE-KYD-KSCDMWSLGVIMYILLCGYPPFYSNHGLAISpgmkTRIRMGQYEFPnpewSEVSEEVKMLIRNLLKT 248
                        170       180
                 ....*....|....*....|..
gi 545477471 156 EPSERLTAPEILLHPWFESVLE 177
Cdd:cd14170  249 EPTQRMTITEFMNHPWIMQSTK 270
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
5-171 1.23e-19

Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK6, also called SSTK, is expressed at the head of elongated sperm. It can phosphorylate histones and associate with heat shock protens HSP90 and HSC70. Male mice deficient in TSSK6 are infertile, showing spermatogenic impairment including reduced sperm counts, impaired DNA condensation, abnormal morphology and decreased motility rates. The TSSK6-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: 271066 [Multi-domain]  Cd Length: 256  Bit Score: 83.76  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERtQLRLESLEDTHIMKGEDDALSDKHGCPAYVS 84
Cdd:cd14164   91 IQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSADDR-KIKIADFGFARFVEDYPELSTTFCGSRAYTP 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILntTGT-YSGKAADVWSLGVMLYTLLVGRYPFHDSdpsaLFSKIRRGQFCI--PEHISPKARC--LIRSLLRREPSE 159
Cdd:cd14164  170 PEVI--LGTpYDPKKYDVWSLGVVLYVMVTGTMPFDET----NVRRLRLQQRGVlyPSGVALEEPCraLIRTLLQFNPST 243
                        170
                 ....*....|..
gi 545477471 160 RLTAPEILLHPW 171
Cdd:cd14164  244 RPSIQQVAGNSW 255
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
14-175 1.48e-19

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, classical PKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. Novel PKCs are calcium-independent, but require DAG and PS for activity, while atypical PKCs only require PS. PKCs phosphorylate and modify the activities of a wide variety of cellular proteins including receptors, enzymes, cytoskeletal proteins, transcription factors, and other kinases. They play a central role in signal transduction pathways that regulate cell migration and polarity, proliferation, differentiation, and apoptosis. Also included in this subfamily are the PKC-like proteins, called PKNs. The PKC 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: 270722 [Multi-domain]  Cd Length: 318  Bit Score: 84.57  E-value: 1.48e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  14 EEAARLFK-QIVSAVAHCHQSAIVLGDLKLRKFVFSTEertqlrlesledTHI-----------MKGeDDALSDKHGCPA 81
Cdd:cd05570   95 EERARFYAaEICLALQFLHERGIIYRDLKLDNVLLDAE------------GHIkiadfgmckegIWG-GNTTSTFCGTPD 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL 161
Cdd:cd05570  162 YIAPEILR--EQDYGFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPARRL 239
                        170
                 ....*....|....*....
gi 545477471 162 -----TAPEILLHPWFESV 175
Cdd:cd05570  240 gcgpkGEADIKAHPFFRNI 258
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
5-171 1.91e-19

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 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: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 83.51  E-value: 1.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLEsLEDTHIMKGEDDALSDKHGCPAYVS 84
Cdd:cd14183   95 ITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVYEHQDGSKSLK-LGDFGLATVVDGPLYTVCGTPTYVA 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDS--DPSALFSKIRRGQFCIP----EHISPKARCLIRSLLRREPS 158
Cdd:cd14183  174 PEIIAETGY--GLKVDIWAAGVITYILLCGFPPFRGSgdDQEVLFDQILMGQVDFPspywDNVSDSAKELITMMLQVDVD 251
                        170
                 ....*....|...
gi 545477471 159 ERLTAPEILLHPW 171
Cdd:cd14183  252 QRYSALQVLEHPW 264
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
4-172 2.10e-19

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 2 subunit (PhKG2) is also referred to as the testis/liver gamma isoform. Mutations in its gene cause autosomal-recessive glycogenosis of the liver. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG2 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: 271083 [Multi-domain]  Cd Length: 279  Bit Score: 83.48  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLEDTHIMkGEDDALSDKHGCPAYV 83
Cdd:cd14181  106 YLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILL--DDQLHIKLSDFGFSCHL-EPGEKLRELCGTPGYL 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEIL----NTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG--QFCIPE--HISPKARCLIRSLLRR 155
Cdd:cd14181  183 APEILkcsmDETHPGYGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGryQFSSPEwdDRSSTVKDLISRLLVV 262
                        170
                 ....*....|....*..
gi 545477471 156 EPSERLTAPEILLHPWF 172
Cdd:cd14181  263 DPEIRLTAEQALQHPFF 279
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
10-171 2.62e-19

Catalytic domain of the Serine/Threonine kinase, Aurora-A 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. 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, which also localizes the kinase to spindle microtubules. Aurora-A is overexpressed in many cancer types such as prostate, ovarian, breast, bladder, gastric, and pancreatic. 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: 271018 [Multi-domain]  Cd Length: 258  Bit Score: 83.08  E-value: 2.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEerTQLRLESLE-DTHIMKGEDDALSdkhGCPAYVSPEIL 88
Cdd:cd14116  101 KFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSA--GELKIADFGwSVHAPSSRRTTLC---GTLDYLPPEMI 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  89 NttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLTAPEILL 168
Cdd:cd14116  176 E--GRMHDEKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLE 253

                 ...
gi 545477471 169 HPW 171
Cdd:cd14116  254 HPW 256
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
78-204 2.72e-19

Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CRIK (also called citron kinase) is an effector of the small GTPase Rho. It plays an important function during cytokinesis and affects its contractile process. CRIK-deficient mice show severe ataxia and epilepsy as a result of abnormal cytokinesis and massive apoptosis in neuronal precursors. A Down syndrome critical region protein TTC3 interacts with CRIK and inhibits CRIK-dependent neuronal differentiation and neurite extension. CRIK contains a catalytic domain, a central coiled-coil domain, and a C-terminal region containing a Rho-binding domain (RBD), a zinc finger, and a pleckstrin homology (PH) domain, in addition to other motifs. The CRIK 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: 270752 [Multi-domain]  Cd Length: 328  Bit Score: 83.90  E-value: 2.72e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEIL-----NTTGTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ--FCIPEH--ISPKARCL 148
Cdd:cd05601  165 GTPDYIAPEVLtsmngGSKGTY-GVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKkfLKFPEDpkVSESAVDL 243
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 545477471 149 IRSLLrREPSERLTAPEILLHPWFESVlepgYIDSEIGTSDQIVPEYQEDSDISSF 204
Cdd:cd05601  244 IKGLL-TDAKERLGYEGLCCHPFFSGI----DWNNLRQTVPPFVPTLTSDDDTSNF 294
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
6-172 3.99e-19

Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The pseudokinase domain may function as a regulatory domain or a protein interaction domain. The Unc-89 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: 271011 [Multi-domain]  Cd Length: 255  Bit Score: 82.17  E-value: 3.99e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   6 RSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEertQLRLESLEDTHimKGEDDALS-DKHGCPAYVS 84
Cdd:cd14109   91 PGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQDD---KLKLADFGQSR--RLLRGKLTtLIYGSPEFVS 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF----CIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd14109  166 PEIVNSYPV--TLATDMWSVGVLTYVLLGGISPFLGDNDRETLTNVRSGKWsfdsSPLGNISDDARDFIKKLLVYIPESR 243
                        170
                 ....*....|..
gi 545477471 161 LTAPEILLHPWF 172
Cdd:cd14109  244 LTVDEALNHPWF 255
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
8-171 4.79e-19

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called 90kDa ribosomal protein S6 kinase 3 or Ribosomal protein S6 kinase alpha-3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK2 is also called p90RSK3, RPS6KA3, S6K-alpha-3, or MAPK-activated protein kinase 1b (MAPKAPK-1b). RSK2 is expressed highly in the regions of the brain with high synaptic activity. It plays a role in the maintenance and consolidation of excitatory synapses. It is a specific modulator of phospholipase D in calcium-regulated exocytosis. Mutations in the RSK2 gene, RPS6KA3, cause Coffin-Lowry syndrome (CLS), a rare syndromic form of X-linked mental retardation characterized by growth and psychomotor retardation and skeletal abnormalities. RSK2 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK2 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: 271078 [Multi-domain]  Cd Length: 339  Bit Score: 83.53  E-value: 4.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERT--QLRLESLEDTHIMKGEDDALSDKHGCPAYVSP 85
Cdd:cd14176  107 QKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILYVDESGNpeSIRICDFGFAKQLRAENGLLMTPCYTANFVAP 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  86 EILNTTGtYSGkAADVWSLGVMLYTLLVGRYPFH---DSDPSALFSKIRRGQFCIP----EHISPKARCLIRSLLRREPS 158
Cdd:cd14176  187 EVLERQG-YDA-ACDIWSLGVLLYTMLTGYTPFAngpDDTPEEILARIGSGKFSLSggywNSVSDTAKDLVSKMLHVDPH 264
                        170
                 ....*....|...
gi 545477471 159 ERLTAPEILLHPW 171
Cdd:cd14176  265 QRLTAALVLRHPW 277
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1-175 5.08e-19

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 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: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 82.74  E-value: 5.08e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSdKHGCP 80
Cdd:cd05613   92 LFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFLLDENERAYS-FCGTI 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFH---DSDPSALFSK-IRRGQFCIPEHISPKARCLIRSLLRRE 156
Cdd:cd05613  171 EYMAPEIVRGGDSGHDKAVDWWSLGVLMYELLTGASPFTvdgEKNSQAEISRrILKSEPPYPQEMSALAKDIIQRLLMKD 250
                        170       180
                 ....*....|....*....|....
gi 545477471 157 PSERL-----TAPEILLHPWFESV 175
Cdd:cd05613  251 PKKRLgcgpnGADEIKKHPFFQKI 274
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
5-173 6.52e-19

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 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: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 82.61  E-value: 6.52e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTE-ERTQLRLESLEDTHIMKGEDDALSDKHGCPAYV 83
Cdd:cd14180   92 IKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADEsDGAVLKVIDFGFARLRPQGSRPLQTPCFTLQYA 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFH-------DSDPSALFSKIRRGQFCIP----EHISPKARCLIRSL 152
Cdd:cd14180  172 APELFSNQGY--DESCDLWSLGVILYTMLSGQVPFQskrgkmfHNHAADIMHKIKEGDFSLEgeawKGVSEEAKDLVRGL 249
                        170       180
                 ....*....|....*....|.
gi 545477471 153 LRREPSERLTAPEILLHPWFE 173
Cdd:cd14180  250 LTVDPAKRLKLSELRESDWLQ 270
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
10-172 6.61e-19

The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 and DRAK2 (also called STK17B). Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. DRAK2 has been implicated in inducing or enhancing apoptosis in beta cells, fibroblasts, and lymphoid cells, where it is highly expressed. It is involved in regulating many immune processes including the germinal center (GC) reaction, responses to thymus-dependent antigens, activated T cell survival, memory T cell responses. It may be involved in the development of autoimmunity. The DRAK2 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: 271100 [Multi-domain]  Cd Length: 270  Bit Score: 81.89  E-value: 6.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTeertqlrLESLEDTHIMK-------GEDDALSDKHGCPAY 82
Cdd:cd14198  106 MVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSS-------IYPLGDIKIVDfgmsrkiGHACELREIMGTPEY 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILN----TTGTysgkaaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEH----ISPKARCLIRSLLR 154
Cdd:cd14198  179 LAPEILNydpiTTAT------DMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVNVDYSEEtfssVSQLATDFIQKLLV 252
                        170
                 ....*....|....*...
gi 545477471 155 REPSERLTAPEILLHPWF 172
Cdd:cd14198  253 KNPEKRPTAEICLSHSWL 270
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
1-171 7.10e-19

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 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: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 81.99  E-value: 7.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLE---DTHIMKGEDdaLSDKH 77
Cdd:cd14194   95 LFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENIMLLDRNVPKPRIKIIDfglAHKIDFGNE--FKNIF 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPE----HISPKARCLIRSLL 153
Cdd:cd14194  173 GTPEFVAPEIVNYEPL--GLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDeyfsNTSALAKDFIRRLL 250
                        170
                 ....*....|....*...
gi 545477471 154 RREPSERLTAPEILLHPW 171
Cdd:cd14194  251 VKDPKKRMTIQDSLQHPW 268
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
4-204 8.12e-19

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-delta plays a role in cell cycle regulation and programmed cell death in many cell types. It slows down cell proliferation, inducing cell cycle arrest and enhancing cell differentiation. PKC-delta is also involved in the regulation of transcription as well as immune and inflammatory responses. It plays a central role in the genotoxic stress response that leads to DNA damaged-induced apoptosis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-delta 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: 173710 [Multi-domain]  Cd Length: 316  Bit Score: 82.68  E-value: 8.12e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMkGEDDAlSDKHGCPAYV 83
Cdd:cd05620   86 HIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVF-GDNRA-STFCGTPDYI 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL-T 162
Cdd:cd05620  164 APEILQ--GLKYTFSVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTRRLgV 241
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 545477471 163 APEILLHPWFESV----LEPGYIDSEIGtsdqivPEYQEDSDISSF 204
Cdd:cd05620  242 VGNIRGHPFFKTInwtaLEKRELDPPFK------PKVKSPSDYSNF 281
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
4-171 8.31e-19

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 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: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 81.93  E-value: 8.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLEsLEDTHIMKGEDDALSDKH--GCPA 81
Cdd:cd14196   98 FLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENIMLLDKNIPIPHIK-LIDFGLAHEIEDGVEFKNifGTPE 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPE----HISPKARCLIRSLLRREP 157
Cdd:cd14196  177 FVAPEIVNYEPL--GLEADMWSIGVITYILLSGASPFLGDTKQETLANITAVSYDFDEeffsHTSELAKDFIRKLLVKET 254
                        170
                 ....*....|....
gi 545477471 158 SERLTAPEILLHPW 171
Cdd:cd14196  255 RKRLTIQEALRHPW 268
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
3-171 8.61e-19

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk 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: 271075 [Multi-domain]  Cd Length: 288  Bit Score: 82.00  E-value: 8.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEER-TQLRLESLEDTHIMKGEDDA-------LS 74
Cdd:cd14173   89 SHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQvSPVKICDFDLGSGIKLNSDCspistpeLL 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  75 DKHGCPAYVSPEIL---NTTGTYSGKAADVWSLGVMLYTLLVGRYPF---HDSD------------PSALFSKIRRGQFC 136
Cdd:cd14173  169 TPCGSAEYMAPEVVeafNEEASIYDKRCDLWSLGVILYIMLSGYPPFvgrCGSDcgwdrgeacpacQNMLFESIQEGKYE 248
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 545477471 137 IPE----HISPKARCLIRSLLRREPSERLTAPEILLHPW 171
Cdd:cd14173  249 FPEkdwaHISCAAKDLISKLLVRDAKQRLSAAQVLQHPW 287
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
1-204 9.71e-19

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 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: 270765 [Multi-domain]  Cd Length: 332  Bit Score: 82.66  E-value: 9.71e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSdKHGCP 80
Cdd:cd05614   92 LFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEKERTYS-FCGTI 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGTYsGKAADVWSLGVMLYTLLVGRYPF----HDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRRE 156
Cdd:cd05614  171 EYMAPEIIRGKSGH-GKAVDWWSLGILMFELLTGASPFtlegEKNTQSEVSRRILKCDPPFPSFIGPVARDLLQKLLCKD 249
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 545477471 157 PSERL-----TAPEILLHPWFESVLEPGYIDSEIGTSDQivPEYQEDSDISSF 204
Cdd:cd05614  250 PKKRLgagpqGAQEIKEHPFFKGLDWEALALRKVNPPFR--PSIRSELDVGNF 300
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
9-170 1.05e-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: 81.14  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   9 KRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL------RLESLeDTHIMKgeddalSDKhGCPAY 82
Cdd:cd14002   94 GTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLcdfgfaRAMSC-NTLVLT------SIK-GTPLY 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEIL-----NTTgtysgkaADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREP 157
Cdd:cd14002  166 MAPELVqeqpyDHT-------ADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLLNKDP 238
                        170
                 ....*....|...
gi 545477471 158 SERLTAPEILLHP 170
Cdd:cd14002  239 SKRLSWPDLLEHP 251
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
22-175 1.40e-18

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-theta is selectively expressed in T-cells and plays an important and non-redundant role in several aspects of T-cell biology. Although T-cells also express other PKC isoforms, PKC-theta is unique in that upon antigen stimulation, it is translocated to the plasma membrane at the immunological synapse, where it mediates signals essential for T-cell activation. It is essential for TCR-induced proliferation, cytokine production, T-cell survival, and the differentiation and effector function of T-helper (Th) cells, particularly Th2 and Th17. PKC-theta is being developed as a therapeutic target for Th2-mediated allergic inflammation and Th17-mediated autoimmune diseases. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC 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: 270770 [Multi-domain]  Cd Length: 331  Bit Score: 81.89  E-value: 1.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  22 QIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKgeDDALSDKHGCPAYVSPEILntTGTYSGKAADV 101
Cdd:cd05619  114 EIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLG--DAKTSTFCGTPDYIAPEIL--LGQKYNTSVDW 189
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545477471 102 WSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLTAP-EILLHPWFESV 175
Cdd:cd05619  190 WSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKLFVREPERRLGVRgDIRQHPFFREI 264
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
1-175 1.41e-18

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 81.79  E-value: 1.41e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLrleslEDTHIMKGEDDALSDKHGCP 80
Cdd:PTZ00263 105 LFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKV-----TDFGFAKKVPDRTFTLCGTP 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTGtySGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:PTZ00263 180 EYLAPEVIQSKG--HGKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTDHTKR 257
                        170       180
                 ....*....|....*....|
gi 545477471 161 LTA-----PEILLHPWFESV 175
Cdd:PTZ00263 258 LGTlkggvADVKNHPYFHGA 277
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
14-175 1.51e-18

Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine/threonine kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. There are four mammalian MAST kinases, named MAST1-MAST4. MAST1 is also called syntrophin-associated STK (SAST) while MAST2 is also called MAST205. MAST kinases are cytoskeletal associated kinases of unknown function that are also expressed at neuromuscular junctions and postsynaptic densities. MAST1, MAST2, and MAST3 bind and phosphorylate the tumor suppressor PTEN, and may contribute to the regulation and stabilization of PTEN. MAST2 is involved in the regulation of the Fc-gamma receptor of the innate immune response in macrophages, and may also be involved in the regulation of the Na+/H+ exchanger NHE3. The MAST 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: 270760 [Multi-domain]  Cd Length: 280  Bit Score: 81.30  E-value: 1.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  14 EEAARL-FKQIVSAVAHCHQSAIV-------------LGDLKLRKFVFSTEERTQLRLESLEDtHIMKgEDDALSDKH-- 77
Cdd:cd05609   99 VDMARMyFAETVLALEYLHSYGIVhrdlkpdnllitsMGHIKLTDFGLSKIGLMSLTTNLYEG-HIEK-DTREFLDKQvc 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGtYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEH---ISPKARCLIRSLLR 154
Cdd:cd05609  177 GTPEYIAPEVILRQG-Y-GKPVDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEGddaLPDDAQDLITRLLQ 254
                        170       180
                 ....*....|....*....|....
gi 545477471 155 REPSERL---TAPEILLHPWFESV 175
Cdd:cd05609  255 QNPLERLgtgGAEEVKQHPFFQDL 278
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
4-172 1.55e-18

Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TSSK proteins are almost exclusively expressed postmeiotically in the testis and play important roles in spermatogenesis and/or spermiogenesis. There are five mammalian TSSK proteins which show differences in their localization and timing of expression. TSSK3 has been reported to be expressed in the interstitial Leydig cells of adult testis. Its mRNA levels is low at birth, increases at puberty, and remains high throughout adulthood. The TSSK3-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: 271065 [Multi-domain]  Cd Length: 257  Bit Score: 80.80  E-value: 1.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFsteERTQLRLESLEDTHIMKGEDDALSDKH-GCPAY 82
Cdd:cd14163   91 CVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL---QGFTLKLTDFGFAKQLPKGGRELSQTFcGSTAY 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGqFCIPEHISPKARC--LIRSLLRREPSER 160
Cdd:cd14163  168 AAPEVLQGV-PHDSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKG-VSLPGHLGVSRTCqdLLKRLLEPDMVLR 245
                        170
                 ....*....|..
gi 545477471 161 LTAPEILLHPWF 172
Cdd:cd14163  246 PSIEEVSWHPWL 257
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
4-170 1.79e-18

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii CNK2 has both cilliary and cell cycle functions. It influences flagellar length through promoting flagellar disassembly, and it regulates cell size, through influencing the size threshold at which cells commit to mitosis. This subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily includes CNK1, and -2. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270869 [Multi-domain]  Cd Length: 256  Bit Score: 80.51  E-value: 1.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRK-FVFSTEertQLRLESLEDTHIMKGedDALSDKHGCPAY 82
Cdd:cd08530   93 RKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANiLLSAGD---LVKIGDLGISKVLKK--NLAKTQIGTPLY 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNTTgTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC-IPEHISPKARCLIRSLLRREPSERL 161
Cdd:cd08530  168 AAPEVWKGR-PYDYKS-DIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFPpIPPVYSQDLQQIIRSLLQVNPKKRP 245

                 ....*....
gi 545477471 162 TAPEILLHP 170
Cdd:cd08530  246 SCDKLLQSP 254
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
82-175 2.15e-18

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: 81.13  E-value: 2.15e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNTTGtySGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEH--ISPKARCLIRSLLRREPSE 159
Cdd:cd05574  198 YIAPEVIKGDG--HGSAVDWWTLGILLYEMLYGTTPFKGSNRDETFSNILKKELTFPESppVSSEAKDLIRKLLVKDPSK 275
                         90       100
                 ....*....|....*....|
gi 545477471 160 RL----TAPEILLHPWFESV 175
Cdd:cd05574  276 RLgskrGASEIKRHPFFRGV 295
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
4-171 4.40e-18

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin 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: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 79.62  E-value: 4.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERT-QLRLESLEDTHIMKGEDDaLSDKHGCPAY 82
Cdd:cd14115   79 YLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIPVpRVKLIDLEDAVQISGHRH-VHHLLGNPEF 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEH----ISPKARCLIRSLLRREPS 158
Cdd:cd14115  158 AAPEVIQ--GTPVSLATDIWSIGVLTYVMLSGVSPFLDESKEETCINVCRVDFSFPDEyfgdVSQAARDFINVILQEDPR 235
                        170
                 ....*....|...
gi 545477471 159 ERLTAPEILLHPW 171
Cdd:cd14115  236 RRPTAATCLQHPW 248
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
10-172 5.85e-18

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-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: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 79.16  E-value: 5.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLE-DTHImkGEDDALSDKHGCPAYVSPEIL 88
Cdd:cd14114   96 KMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTTKRSNEVKLIDFGlATHL--DPKESVKVTTGTAEFAAPEIV 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  89 NttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPE----HISPKARCLIRSLLRREPSERLTAP 164
Cdd:cd14114  174 E--REPVGFYTDMWAVGVLSYVLLSGLSPFAGENDDETLRNVKSCDWNFDDsafsGISEEAKDFIRKLLLADPNKRMTIH 251

                 ....*...
gi 545477471 165 EILLHPWF 172
Cdd:cd14114  252 QALEHPWL 259
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
1-170 8.95e-18

Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Chlamydomonas reinhardtii FA2 was discovered in a genetic screen for deflagellation-defective mutants. It is essential for basal-body/centriole-associated microtubule severing, and plays a role in cell cycle progression. No cellular function has yet been ascribed to CNK4. The Chlamydomonas reinhardtii FA2-like subfamily belongs to the (NIMA)-related kinase (Nek) family, which includes seven different Chlamydomonas Neks (CNKs 1-6 and Fa2). This subfamily contains FA2 and CNK4. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 78.61  E-value: 8.95e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSR--KRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLESLEDTHIMKGEDDALSDKHG 78
Cdd:cd08529   86 LHSLIKSQrgRPLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLD--KGDNVKIGDLGVAKILSDTTNFAQTIVG 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEiLNTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC-IPEHISPKARCLIRSLLRREP 157
Cdd:cd08529  164 TPYYLSPE-LCEDKPYNEKS-DVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASYSQDLSQLIDSCLTKDY 241
                        170
                 ....*....|...
gi 545477471 158 SERLTAPEILLHP 170
Cdd:cd08529  242 RQRPDTTELLRNP 254
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
13-175 1.00e-17

N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), p90-RSKs, or p90S6Ks. The RSK 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: 270734 [Multi-domain]  Cd Length: 317  Bit Score: 79.37  E-value: 1.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteertqlrleslEDTHImKGEDDALSDKH-----------GCPA 81
Cdd:cd05582   96 EEDVKFYLAELALALDHLHSLGIIYRDLKPENILLD------------EDGHI-KLTDFGLSKESidhekkaysfcGTVE 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNTTGtySGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL 161
Cdd:cd05582  163 YMAPEVVNRRG--HTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANRL 240
                        170
                 ....*....|....*....
gi 545477471 162 TAP-----EILLHPWFESV 175
Cdd:cd05582  241 GAGpdgveEIKRHPFFATI 259
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
1-170 1.39e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek8 contains an N-terminal kinase catalytic domain and a C-terminal RCC1 (regulator of chromosome condensation) domain. A double point mutation in Nek8 causes cystic kidney disease in mice that genetically resembles human autosomal recessive polycystic kidney disease (ARPKD). Nek8 is also associated with a rare form of juvenile renal cystic disease, nephronophthisis type 9. It has been suggested that a defect in the ciliary localization of Nek8 contributes to the development of cysts manifested by these diseases. Nek8 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270859 [Multi-domain]  Cd Length: 256  Bit Score: 78.24  E-value: 1.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKR--LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFStEERTQLRLESLEDTHIMKGEDDALSdKHG 78
Cdd:cd08220   86 LFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLN-KKRTVVKIGDFGISKILSSKSKAYT-VVG 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC-IPEHISPKARCLIRSLLRREP 157
Cdd:cd08220  164 TPCYISPELCE--GKPYNQKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFApISDRYSEELRHLILSMLHLDP 241
                        170
                 ....*....|...
gi 545477471 158 SERLTAPEILLHP 170
Cdd:cd08220  242 NKRPTLSEIMAQP 254
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
9-172 2.12e-17

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: 77.63  E-value: 2.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   9 KRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL-------RLESLEDTHIMKGEddalsdkhgcPA 81
Cdd:cd05122   93 KTLTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLidfglsaQLSDGKTRNTFVGT----------PY 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC---IPEHISPKARCLIRSLLRREPS 158
Cdd:cd05122  163 WMAPEVIQ--GKPYGFKADIWSLGITAIEMAEGKPPYSELPPMKALFLIATNGPPglrNPKKWSKEFKDFLKKCLQKDPE 240
                        170
                 ....*....|....
gi 545477471 159 ERLTAPEILLHPWF 172
Cdd:cd05122  241 KRPTAEQLLKHPFI 254
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
4-198 2.33e-17

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-iota is directly implicated in carcinogenesis. It is critical to oncogenic signaling mediated by Ras and Bcr-Abl. The PKC-iota gene is the target of tumor-specific gene amplification in many human cancers, and has been identified as a human oncogene. In addition to its role in transformed growth, PKC-iota also promotes invasion, chemoresistance, and tumor cell survival. Expression profiling of PKC-iota is a prognostic marker of poor clinical outcome in several human cancers. PKC-iota also plays a role in establishing cell polarity, and has critical embryonic functions. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC 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: 270769 [Multi-domain]  Cd Length: 364  Bit Score: 78.92  E-value: 2.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGedDALSDKHGCPAYV 83
Cdd:cd05618  111 HMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPG--DTTSTFCGTPNYI 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPF----HDSDPSA-----LFSKIRRGQFCIPEHISPKARCLIRSLLR 154
Cdd:cd05618  189 APEILR--GEDYGFSVDWWALGVLMFEMMAGRSPFdivgSSDNPDQntedyLFQVILEKQIRIPRSLSVKAASVLKSFLN 266
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 545477471 155 REPSERLTA------PEILLHPWFESVlepgyiDSEIGTSDQIVPEYQED 198
Cdd:cd05618  267 KDPKERLGChpqtgfADIQGHPFFRNV------DWDLMEQKQVVPPFKPN 310
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
10-172 3.71e-17

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: 76.88  E-value: 3.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIV-------------LGDLKLRKFVFSTEertqlrlesledthiMKGEDDALSDK 76
Cdd:cd06627   95 KFPESLVAVYIYQVLEGLAYLHEQGVIhrdikganilttkDGLVKLADFGVATK---------------LNEVEKDENSV 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  77 HGCPAYVSPEILNTTGTYSgkAADVWSLGVMLYTLLVGRYPFHDSDP-SALFSKIRRGQFCIPEHISPKARCLIRSLLRR 155
Cdd:cd06627  160 VGTPYWMAPEVIEMSGVTT--ASDIWSVGCTVIELLTGNPPYYDLQPmAALFRIVQDDHPPLPENISPELRDFLLQCFQK 237
                        170
                 ....*....|....*..
gi 545477471 156 EPSERLTAPEILLHPWF 172
Cdd:cd06627  238 DPTLRPSAKELLKHPWL 254
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
10-171 4.23e-17

Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK4 is a MAPK kinase kinase that phosphorylates and activates the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. MEKK4 also plays roles in the re-polarization of the actin cytoskeleton in response to osmotic stress, in the proper closure of the neural tube, in cardiovascular development, and in immune responses. The MEKK4 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: 270796 [Multi-domain]  Cd Length: 265  Bit Score: 76.96  E-value: 4.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLF-KQIVSAVAHCHQSAIVLGDLK----------LRKFV-FSTEERTQLRlesleDTHIMKGEDDALSdkh 77
Cdd:cd06626   94 RILDEAVIRVYtLQLLEGLAYLHENGIVHRDIKpanifldsngLIKLGdFGSAVKLKNN-----TTTMAPGEVNSLV--- 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPE-ILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSD-PSALFSKIRRGQF-CIPEH--ISPKARCLIRSL 152
Cdd:cd06626  166 GTPAYMAPEvITGNKGEGHGRAADIWSLGCVVLEMATGKRPWSELDnEWAIMYHVGMGHKpPIPDSlqLSPEGKDFLSRC 245
                        170
                 ....*....|....*....
gi 545477471 153 LRREPSERLTAPEILLHPW 171
Cdd:cd06626  246 LESDPKKRPTASELLDHPF 264
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
11-171 6.81e-17

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK 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: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 76.11  E-value: 6.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL---------RLESLEDTHIMkgeddalsdkHGCPA 81
Cdd:cd14103   88 LTERDCILFMRQICEGVQYMHKQGILHLDLKPENILCVSRTGNQIkiidfglarKYDPDKKLKVL----------FGTPE 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNttgtYS--GKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC----IPEHISPKARCLIRSLLRR 155
Cdd:cd14103  158 FVAPEVVN----YEpiSYATDMWSVGVICYVLLSGLSPFMGDNDAETLANVTRAKWDfddeAFDDISDEAKDFISKLLVK 233
                        170
                 ....*....|....*.
gi 545477471 156 EPSERLTAPEILLHPW 171
Cdd:cd14103  234 DPRKRMSAAQCLQHPW 249
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
69-175 7.18e-17

Catalytic domain of Yeast Protein Kinase 1-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 fungal proteins with similarity to the AGC STKs, Saccharomyces cerevisiae YPK1 and Schizosaccharomyces pombe Gad8p. YPK1 is required for cell growth and acts as a downstream kinase in the sphingolipid-mediated signaling pathway of yeast. It also plays a role in efficient endocytosis and in the maintenance of cell wall integrity. Gad8p is a downstream target of Tor1p, the fission yeast homolog of mTOR. It plays a role in cell growth and sexual development. The YPK1-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: 270737 [Multi-domain]  Cd Length: 313  Bit Score: 77.23  E-value: 7.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  69 EDDALSDKHGCPAYVSPEILNTTGtYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCL 148
Cdd:cd05585  147 DDDKTNTFCGTPEYLAPELLLGHG-YT-KAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDL 224
                         90       100       110
                 ....*....|....*....|....*....|
gi 545477471 149 IRSLLRREPSERL---TAPEILLHPWFESV 175
Cdd:cd05585  225 LIGLLNRDPTKRLgynGAQEIKNHPFFDQI 254
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
13-171 8.14e-17

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 77.17  E-value: 8.14e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTeeRTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTT- 91
Cdd:PLN00034 167 EQFLADVARQILSGIAYLHRRHIVHRDIKPSNLLINS--AKNVKIADFGVSRILAQTMDPCNSSVGTIAYMSPERINTDl 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  92 --GTYSGKAADVWSLGVMLYTLLVGRYPF---HDSDPSALFSKIrrgqfCI------PEHISPKARCLIRSLLRREPSER 160
Cdd:PLN00034 245 nhGAYDGYAGDIWSLGVSILEFYLGRFPFgvgRQGDWASLMCAI-----CMsqppeaPATASREFRHFISCCLQREPAKR 319
                        170
                 ....*....|.
gi 545477471 161 LTAPEILLHPW 171
Cdd:PLN00034 320 WSAMQLLQHPF 330
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
8-204 1.67e-16

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC 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: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 76.31  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFK-QIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGedDALSDKHGCPAYVSPE 86
Cdd:cd05588   89 RQRRLPEEHARFYSaEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPG--DTTSTFCGTPNYIAPE 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  87 ILNttGTYSGKAADVWSLGVMLYTLLVGRYPF----HDSDPSA-----LFSKIRRGQFCIPEHISPKARCLIRSLLRREP 157
Cdd:cd05588  167 ILR--GEDYGFSVDWWALGVLMFEMLAGRSPFdivgSSDNPDQntedyLFQVILEKPIRIPRSLSVKAASVLKGFLNKNP 244
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 545477471 158 SERLTA------PEILLHPWFESvlepgyIDSEIGTSDQIVPEYQ----EDSDISSF 204
Cdd:cd05588  245 AERLGChpqtgfADIQSHPFFRT------IDWEQLEQKQVTPPYKprieSERDLENF 295
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
7-172 1.83e-16

Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily contains uncharacterized STKs with similarity to the human protein designated as Yank1 or STK32A. The Yank1 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: 270730 [Multi-domain]  Cd Length: 257  Bit Score: 74.99  E-value: 1.83e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLREEEAARLF-KQIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLeDTHIMKGEDDALSDKHGCPAYVSP 85
Cdd:cd05578   92 QQKVKFSEETVKFYiCEIVLALDYLHSKNIIHRDIKPDNILL--DEQGHVHITDF-NIATKLTDGTLATSTSGTKPYMAP 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  86 EILNTTGtySGKAADVWSLGVMLYTLLVGRYPF--HDSDPS----ALFSKIRRgqfCIPEHISPKARCLIRSLLRREPSE 159
Cdd:cd05578  169 EVFMRAG--YSFAVDWWSLGVTAYEMLRGKRPYeiHSRTSIeeirAKFETASV---LYPAGWSEEAIDLINKLLERDPQK 243
                        170
                 ....*....|....
gi 545477471 160 RLTAPEILL-HPWF 172
Cdd:cd05578  244 RLGDLSDLKnHPYF 257
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
5-170 2.01e-16

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 76.83  E-value: 2.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKR----LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKHGCP 80
Cdd:PTZ00283 130 IKSRAKtnrtFREHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMYAATVSDDVGRTFCGTP 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTgTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF-CIPEHISPKARCLIRSLLRREPSE 159
Cdd:PTZ00283 210 YYVAPEIWRRK-PYS-KKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYdPLPPSISPEMQEIVTALLSSDPKR 287
                        170
                 ....*....|.
gi 545477471 160 RLTAPEILLHP 170
Cdd:PTZ00283 288 RPSSSKLLNMP 298
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
11-171 2.16e-16

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: 75.17  E-value: 2.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLK----------LRKFV-FSTEERTQLRLESLEDTHIMKgeddalsDKHGC 79
Cdd:cd06631  100 LEEPVFCRYTKQILEGVAYLHNNNVIHRDIKgnnimlmpngVIKLIdFGCAKRLCINLSSGSQSQLLK-------SMRGT 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  80 PAYVSPEILNTTGtySGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQF-CIPEHISPKARCLIRSLLRRE 156
Cdd:cd06631  173 PYWMAPEVINETG--HGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIgsGRKPVpRLPDKFSPEARDFVHACLTRD 250
                        170
                 ....*....|....*
gi 545477471 157 PSERLTAPEILLHPW 171
Cdd:cd06631  251 QDERPSAEQLLKHPF 265
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
8-171 2.16e-16

C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called Ribosomal protein S6 kinase alpha-6 or 90kDa ribosomal protein S6 kinase 6); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSK4 is also called S6K-alpha-6, RPS6KA6, p90RSK6 or pp90RSK4. RSK4 is a substrate of ERK and is a modulator of p53-dependent proliferation arrest in human cells. Deletion of the RSK4 gene, RPS6KA6, frequently occurs in patients of X-linked deafness type 3, mental retardation and choroideremia. Studies of RSK4 in cancer cells and tissues suggest that it may be oncogenic or tumor suppressive depending on many factors. RSK4 is one of four RSK isoforms (RSK1-4) from distinct genes present in vertebrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. The RSK4 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: 271079 [Multi-domain]  Cd Length: 295  Bit Score: 75.44  E-value: 2.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERT--QLRLESLEDTHIMKGEDDALSDKHGCPAYVSP 85
Cdd:cd14177   92 QKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILYMDDSANadSIRICDFGFAKQLRGENGLLLTPCYTANFVAP 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  86 EILNTTGtYSGkAADVWSLGVMLYTLLVGRYPFH---DSDPSALFSKIRRGQFCIP----EHISPKARCLIRSLLRREPS 158
Cdd:cd14177  172 EVLMRQG-YDA-ACDIWSLGVLLYTMLAGYTPFAngpNDTPEEILLRIGSGKFSLSggnwDTVSDAAKDLLSHMLHVDPH 249
                        170
                 ....*....|...
gi 545477471 159 ERLTAPEILLHPW 171
Cdd:cd14177  250 QRYTAEQVLKHSW 262
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
5-171 3.25e-16

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 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: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 74.68  E-value: 3.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFStEERTQLRLESLEDTHIMKGEDDALSDKHGCPAYVS 84
Cdd:cd14184   90 ITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVC-EYPDGTKSLKLGDFGLATVVEGPLYTVCGTPTYVA 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSD--PSALFSKIRRGQFCIP----EHISPKARCLIRSLLRREPS 158
Cdd:cd14184  169 PEIIAETGY--GLKVDIWAAGVITYILLCGFPPFRSENnlQEDLFDQILLGKLEFPspywDNITDSAKELISHMLQVNVE 246
                        170
                 ....*....|...
gi 545477471 159 ERLTAPEILLHPW 171
Cdd:cd14184  247 ARYTAEQILSHPW 259
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
78-175 3.35e-16

Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR kinases regulate mitosis, cell growth, embryonic development, and neurological processes. They are also required for proper centrosome duplication. Higher eukaryotes contain two NDR isoforms, NDR1 and NDR2. This subfamily also contains fungal NDR-like kinases. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR 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: 270750 [Multi-domain]  Cd Length: 324  Bit Score: 75.34  E-value: 3.35e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGtYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIR--RGQFCIPE--HISPKARCLIRSLL 153
Cdd:cd05599  162 GTPDYIAPEVFLQKG-Y-GKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMnwRETLVFPPevPISPEAKDLIERLL 239
                         90       100
                 ....*....|....*....|....*
gi 545477471 154 rREPSERLTAP---EILLHPWFESV 175
Cdd:cd05599  240 -CDAEHRLGANgveEIKSHPFFKGV 263
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
20-170 3.38e-16

Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle 1 (also called TTK); Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TTK/Mps1 is a spindle checkpoint kinase that was first discovered due to its necessity in centrosome duplication in budding yeast. It was later found to function in the spindle assembly checkpoint, which monitors the proper attachment of chromosomes to the mitotic spindle. In yeast, substrates of Mps1 include the spindle pole body components Spc98p, Spc110p, and Spc42p. The TTK/Mps1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271033 [Multi-domain]  Cd Length: 271  Bit Score: 74.56  E-value: 3.38e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  20 FKQIVSAVAHCHQSAIVLGDLKLRKFVFsteerTQLRLEsLED-----------THIMKgeddalSDKHGCPAYVSPEIL 88
Cdd:cd14131  109 WKQMLEAVHTIHEEGIVHSDLKPANFLL-----VKGRLK-LIDfgiakaiqndtTSIVR------DSQVGTLNYMSPEAI 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  89 NTTGTYS--------GKAADVWSLGVMLYTLLVGRYPF-HDSDPSALFSKIRRGQFCI--PEHISPKARCLIRSLLRREP 157
Cdd:cd14131  177 KDTSASGegkpkskiGRPSDVWSLGCILYQMVYGKTPFqHITNPIAKLQAIIDPNHEIefPDIPNPDLIDVMKRCLQRDP 256
                        170
                 ....*....|...
gi 545477471 158 SERLTAPEILLHP 170
Cdd:cd14131  257 KKRPSIPELLNHP 269
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
3-171 3.82e-16

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 11; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek11 is involved, through direct phosphorylation, in regulating the degradation of Cdc25A (Cell Division Cycle 25 homolog A), which plays a role in cell cycle progression and in activating cyclin dependent kinases. Nek11 is activated by CHK1 (CHeckpoint Kinase 1) and may be involved in the G2/M checkpoint. Nek11 may also play a role in the S-phase checkpoint as well as in DNA replication and genotoxic stress responses. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270861 [Multi-domain]  Cd Length: 260  Bit Score: 74.38  E-value: 3.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKfVFSteERTQLRLESLEDTHIMKGEDDALSDKHGCPAY 82
Cdd:cd08222   95 EYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKN-IFL--KNNVIKVGDFGISRILMGTSDLATTFTGTPYY 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNTTGtYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF-CIPEHISPKARCLIRSLLRREPSERL 161
Cdd:cd08222  172 MSPEVLKHEG-YNSKS-DIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYSRMLNKDPALRP 249
                        170
                 ....*....|
gi 545477471 162 TAPEILLHPW 171
Cdd:cd08222  250 SAAEILKIPF 259
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
1-174 4.45e-16

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 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: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 74.27  E-value: 4.45e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLE--DTHIMKGEDDaLSDKHG 78
Cdd:cd14195   95 LFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENIMLLDKNVPNPRIKLIDfgIAHKIEAGNE-FKNIFG 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPE----HISPKARCLIRSLLR 154
Cdd:cd14195  174 TPEFVAPEIVNYEPL--GLEADMWSIGVITYILLSGASPFLGETKQETLTNISAVNYDFDEeyfsNTSELAKDFIRRLLV 251
                        170       180
                 ....*....|....*....|
gi 545477471 155 REPSERLTAPEILLHPWFES 174
Cdd:cd14195  252 KDPKKRMTIAQSLEHSWIKA 271
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
4-204 4.76e-16

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-eta is predominantly expressed in squamous epithelia, where it plays a crucial role in the signaling of cell-type specific differentiation. It is also expressed in pro-B cells and early-stage thymocytes, and acts as a key regulator in early B-cell development. PKC-eta increases glioblastoma multiforme (GBM) proliferation and resistance to radiation, and is being developed as a therapeutic target for the management of GBM. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-eta 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: 270742 [Multi-domain]  Cd Length: 323  Bit Score: 74.94  E-value: 4.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEddALSDKHGCPAYV 83
Cdd:cd05590   86 HIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEGIFNGK--TTSTFCGTPDYI 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTgtYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLTA 163
Cdd:cd05590  164 APEILQEM--LYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRLGS 241
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 545477471 164 ------PEILLHPWFESvlepgyIDSEIGTSDQIVPEY----QEDSDISSF 204
Cdd:cd05590  242 ltlggeEAILRHPFFKE------LDWEKLNRRQIEPPFrpriKSREDVSNF 286
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
10-196 5.18e-16

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PKC beta isoforms (I and II), generated by alternative splicing of a single gene, are preferentially activated by hyperglycemia-induced DAG (1,2-diacylglycerol) in retinal tissues. This is implicated in diabetic microangiopathy such as ischemia, neovascularization, and abnormal vasodilator function. PKC-beta also plays an important role in VEGF signaling. In addition, glucose regulates proliferation in retinal endothelial cells via PKC-betaI. PKC-beta is also being explored as a therapeutic target in cancer. It contributes to tumor formation and is involved in the tumor host mechanisms of inflammation and angiogenesis. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG, and in most cases, phosphatidylserine (PS) for activation. The cPKC-beta 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: 270767 [Multi-domain]  Cd Length: 323  Bit Score: 74.65  E-value: 5.18e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMkgedDALSDKHGC--PAYVSPEI 87
Cdd:cd05616   97 RFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKENIW----DGVTTKTFCgtPDYIAPEI 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  88 LnttgTYS--GKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL-TAP 164
Cdd:cd05616  173 I----AYQpyGKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRLgCGP 248
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 545477471 165 E----ILLHPWFEsvlepgYIDSEIGTSDQIVPEYQ 196
Cdd:cd05616  249 EgerdIKEHAFFR------YIDWEKLERKEIQPPYK 278
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
78-204 5.60e-16

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS was originally identified in Drosophila using a screen for genes whose inactivation led to overproliferation of cells. In tetrapods, there are two LATS isoforms, LATS1 and LATS2. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. LATS functions as a tumor suppressor and is implicated in cell cycle regulation. The LATS 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: 270749 [Multi-domain]  Cd Length: 333  Bit Score: 74.66  E-value: 5.60e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGtYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIR--RGQFCIPEH--ISPKARCLIRSLL 153
Cdd:cd05598  167 GTPNYIAPEVLLRTG-Y-TQLCDWWSVGVILYEMLVGQPPFLAQTPAETQLKVInwRTTLKIPHEanLSPEAKDLILRLC 244
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545477471 154 rREPSERL---TAPEILLHPWFESV-------LEPGYIdseigtsdqivPEYQEDSDISSF 204
Cdd:cd05598  245 -CDAEDRLgrnGADEIKAHPFFAGIdweklrkQKAPYI-----------PTIRHPTDTSNF 293
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
81-171 5.84e-16

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: 73.78  E-value: 5.84e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRR-GQFCIPE----HISPKARCLIRSLLRR 155
Cdd:cd06623  165 TYMSPERIQ--GESYSYAADIWSLGLTLLECALGKFPFLPPGQPSFFELMQAiCDGPPPSlpaeEFSPEFRDFISACLQK 242
                         90
                 ....*....|....*.
gi 545477471 156 EPSERLTAPEILLHPW 171
Cdd:cd06623  243 DPKKRPSAAELLQHPF 258
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
9-170 5.89e-16

Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. ULK2 is ubiquitously expressed and is essential in autophagy induction. ULK1 and ULK2 have unique and cell-type specific roles, but also display partially redundant roles in starvation-induced autophagy. They both display neuron-specific functions: ULK1 is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, and axon branching; ULK2 plays a role in axon development. The ULK1/2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271022 [Multi-domain]  Cd Length: 256  Bit Score: 73.94  E-value: 5.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   9 KRLREEEAARLF-KQIVSAVAHCHQSAIVLGDLKLRKFVFSTEER-----TQLRLEsLED---THIMKGEDDALSdKHGC 79
Cdd:cd14120   86 KGTLSEDTIRVFlQQIAAAMKALHSKGIVHRDLKPQNILLSHNSGrkpspNDIRLK-IADfgfARFLQDGMMAAT-LCGS 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  80 PAYVSPEILnTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSAL---FSKIRRGQFCIPEHISPKARCLIRSLLRRE 156
Cdd:cd14120  164 PMYMAPEVI-MSLQYDAKA-DLWSIGTIVYQCLTGKAPFQAQTPQELkafYEKNANLRPNIPSGTSPALKDLLLGLLKRN 241
                        170
                 ....*....|....
gi 545477471 157 PSERLTAPEILLHP 170
Cdd:cd14120  242 PKDRIDFEDFFSHP 255
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
2-172 1.04e-15

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: 73.16  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   2 HSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLK----LRKFV-------FSTEERTQlrlesledTHIMKGed 70
Cdd:cd06625   90 KDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKganiLRDSNgnvklgdFGASKRLQ--------TICSST-- 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  71 dALSDKHGCPAYVSPEILNTTGtYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFCIPEHISPKARCL 148
Cdd:cd06625  160 -GMKSVTGTPYWMSPEVINGEG-Y-GRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIatQPTNPQLPPHVSEDARDF 236
                        170       180
                 ....*....|....*....|....
gi 545477471 149 IRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd06625  237 LSLIFVRNKKQRPSAEELLSHSFV 260
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
4-173 1.40e-15

Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Phosphorylase kinase (PhK) catalyzes the phosphorylation of inactive phosphorylase b to form the active phosphorylase a. It coordinates hormonal, metabolic, and neuronal signals to initiate the breakdown of glycogen stores, which enables the maintenance of blood-glucose homeostasis during fasting, and is also used as a source of energy for muscle contraction. PhK is one of the largest and most complex protein kinases, composed of a heterotetramer containing four molecules each of four subunit types: one catalytic (gamma) and three regulatory (alpha, beta, and delta). The gamma 1 subunit (PhKG1) is also referred to as the muscle gamma isoform. The gamma subunit, when isolated, is constitutively active and does not require phosphorylation of the A-loop for activity. The regulatory subunits restrain this kinase activity until signals are received to relieve this inhibition. For example, the kinase is activated in response to hormonal stimulation, after autophosphorylation or phosphorylation by cAMP-dependent kinase of the alpha and beta subunits. The high-affinity binding of ADP to the beta subunit also stimulates kinase activity, whereas calcium relieves inhibition by binding to the delta (calmodulin) subunit. The PhKG1 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: 271084 [Multi-domain]  Cd Length: 276  Bit Score: 73.03  E-value: 1.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEdTHIMKGEDdaLSDKHGCPAYV 83
Cdd:cd14182  100 YLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFS-CQLDPGEK--LREVCGTPGYL 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTGTYS----GKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG--QFCIPE--HISPKARCLIRSLLRR 155
Cdd:cd14182  177 APEIIECSMDDNhpgyGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGnyQFGSPEwdDRSDTVKDLISRFLVV 256
                        170
                 ....*....|....*...
gi 545477471 156 EPSERLTAPEILLHPWFE 173
Cdd:cd14182  257 QPQKRYTAEEALAHPFFQ 274
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
4-173 2.64e-15

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK2 is ubiquitously expressed and is essential in autophagy induction. It displays partially redundant functions with ULK1 and is able to compensate for the loss of ULK1 in non-selective autophagy. It also displays neuron-specific functions and is important in axon development. The ULK2 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: 271103 [Multi-domain]  Cd Length: 271  Bit Score: 72.35  E-value: 2.64e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDKH------ 77
Cdd:cd14201   95 YLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKSSVSGIRIKIADFGFARYLQSNMmaatlc 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILnTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSAL---FSKIRRGQFCIPEHISPKARCLIRSLLR 154
Cdd:cd14201  175 GSPMYMAPEVI-MSQHYDAKA-DLWSIGTVIYQCLVGKPPFQANSPQDLrmfYEKNKNLQPSIPRETSPYLADLLLGLLQ 252
                        170
                 ....*....|....*....
gi 545477471 155 REPSERLTAPEILLHPWFE 173
Cdd:cd14201  253 RNQKDRMDFEAFFSHPFLE 271
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
3-204 3.29e-15

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 72.71  E-value: 3.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLrleslEDTHIMKGEDDALSDKHGCPAY 82
Cdd:PTZ00426 120 TFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKM-----TDFGFAKVVDTRTYTLCGTPEY 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNTTGtySGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL- 161
Cdd:PTZ00426 195 IAPEILLNVG--HGKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLSHDLTKRYg 272
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 545477471 162 ----TAPEILLHPWFESVLEPGYIDSEIGTSDQivPEYQEDSDISSF 204
Cdd:PTZ00426 273 nlkkGAQNVKEHPWFGNIDWVSLLHKNVEVPYK--PKYKNVFDSSNF 317
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
10-204 4.37e-15

Catalytic domain of Suppressor of loss of cAMP-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. This subfamily is composed of Schizosaccharomyces pombe Sck1 and similar fungal proteins. Sck1 plays a role in trehalase activation triggered by glucose and a nitrogen source. Trehalase catalyzes the cleavage of the disaccharide trehalose to glucose. Trehalose, as a carbohydrate reserve and stress metabolite, plays an important role in the response of yeast to environmental changes. The Sck1-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: 270738 [Multi-domain]  Cd Length: 330  Bit Score: 72.22  E-value: 4.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHImkgEDDALSDKH-GCPAYVSPEIL 88
Cdd:cd05586   92 RFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKADL---TDNKTTNTFcGTTEYLAPEVL 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  89 NTTGTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEH-ISPKARCLIRSLLRREPSERLTA---- 163
Cdd:cd05586  169 LDEKGY-TKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKDvLSDEGRSFVKGLLNRNPKHRLGAhdda 247
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 545477471 164 PEILLHPWFESvlepgyIDSEIGTSDQIVPEY----QEDSDISSF 204
Cdd:cd05586  248 VELKEHPFFAD------IDWDLLSKKKITPPFkpivDSDTDVSNF 286
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
11-172 4.82e-15

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK1 (or MYLK1) phosphorylates myosin regulatory light chain and controls the contraction of smooth muscles. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module which results in the expression of telokin in phasic smooth muscles, leading to Ca2+ desensitization by cyclic nucleotides of smooth muscle force. MLCK1 is also responsible for myosin regulatory light chain phosphorylation in nonmuscle cells and may play a role in regulating myosin II ATPase activity. The MLCK1 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: 271093 [Multi-domain]  Cd Length: 259  Bit Score: 71.57  E-value: 4.82e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLEsleDTHIMKGEDDALSDK--HGCPAYVSPEIL 88
Cdd:cd14191   97 LTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTGTKIKLI---DFGLARRLENAGSLKvlFGTPEFVAPEVI 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  89 NTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEH----ISPKARCLIRSLLRREPSERLTAP 164
Cdd:cd14191  174 NYEPI--GYATDMWSIGVICYILVSGLSPFMGDNDNETLANVTSATWDFDDEafdeISDDAKDFISNLLKKDMKARLTCT 251

                 ....*...
gi 545477471 165 EILLHPWF 172
Cdd:cd14191  252 QCLQHPWL 259
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
4-173 4.96e-15

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. ULK1 is required for efficient amino acid starvation-induced autophagy and mitochondrial clearance. It associates with three autophagy-related proteins (Atg13, FIP200 amd Atg101) to form the ULK1 complex. All fours proteins are essential for autophagosome formation. ULK1 is regulated by both mammalian target-of rapamycin complex 1 (mTORC1) and AMP-activated protein kinase (AMPK). mTORC1 negatively regulates the ULK1 complex in a nutrient-dependent manner while AMPK stimulates autophagy by inhibiting mTORC1. ULK1 also plays neuron-specific roles and is involved in non-clathrin-coated endocytosis in growth cones, filopodia extension, neurite extension, and axon branching. The ULK1 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: 271104 [Multi-domain]  Cd Length: 267  Bit Score: 71.58  E-value: 4.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFS-------TEERTQLRLESLEDTHIMKGEDDAlSDK 76
Cdd:cd14202   91 YLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksNPNNIRIKIADFGFARYLQNNMMA-ATL 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  77 HGCPAYVSPEILnTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSAL---FSKIRRGQFCIPEHISPKARCLIRSLL 153
Cdd:cd14202  170 CGSPMYMAPEVI-MSQHYDAKA-DLWSIGTIIYQCLTGKAPFQASSPQDLrlfYEKNKSLSPNIPRETSSHLRQLLLGLL 247
                        170       180
                 ....*....|....*....|
gi 545477471 154 RREPSERLTAPEILLHPWFE 173
Cdd:cd14202  248 QRNQKDRMDFDEFFHHPFLD 267
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
8-171 5.53e-15

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD 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: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 71.29  E-value: 5.53e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFST-EERTQLRLESLEDTHIMkGEDDALSDKHGCPAYVSPE 86
Cdd:cd14082   97 KGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASaEPFPQVKLCDFGFARII-GEKSFRRSVVGTPAYLAPE 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  87 ILNTTGtYSgKAADVWSLGVMLYTLLVGRYPFH-DSDPSalfSKIRRGQFCIP----EHISPKARCLIRSLLRREPSERL 161
Cdd:cd14082  176 VLRNKG-YN-RSLDMWSVGVIIYVSLSGTFPFNeDEDIN---DQIQNAAFMYPpnpwKEISPDAIDLINNLLQVKMRKRY 250
                        170
                 ....*....|
gi 545477471 162 TAPEILLHPW 171
Cdd:cd14082  251 SVDKSLSHPW 260
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
14-171 5.79e-15

Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ULK4 is a functionally uncharacterized kinase that shows similarity to ATG1/ULKs. The ATG1/ULK complex is conserved from yeast to humans and it plays a critical role in the initiation of autophagy, the intracellular system that leads to the lysosomal degradation of cellular components and their recycling into basic metabolic units. The ULK4 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: 270912 [Multi-domain]  Cd Length: 269  Bit Score: 71.17  E-value: 5.79e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  14 EEAARLF-KQIVSAVAHCHQSAIVLGDLKLRKFV-----------FSTEERTQLRLESLEDTHIMKGEDDALSDKH---G 78
Cdd:cd14010   93 ESSVRKFgRDLVRGLHYIHSKGIIYCDLKPSNILldgngtlklsdFGLARREGEILKELFGQFSDEGNVNKVSKKQakrG 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEILnTTGTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQfciPEHISPKARC--------LIR 150
Cdd:cd14010  173 TPYYMAPELF-QGGVHS-FASDLWALGCVLYEMFTGKPPFVAESFTELVEKILNED---PPPPPPKVSSkpspdfksLLK 247
                        170       180
                 ....*....|....*....|..
gi 545477471 151 SLLRREPSERLTAPEILLHP-W 171
Cdd:cd14010  248 GLLEKDPAKRLSWDELVKHPfW 269
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1-171 6.55e-15

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek4 is highly abundant in the testis. Its specific function is unknown. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. Nek4 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 70.93  E-value: 6.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRK--RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKfVFSTEERTqLRLESLEDTHIMKGEDDALSDKHG 78
Cdd:cd08223   87 LYTRLKEQKgvLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQN-IFLTKSNI-IKVGDLGIARVLESSSDMATTLIG 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEiLNTTGTYSGKaADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF-CIPEHISPKARCLIRSLLRREP 157
Cdd:cd08223  165 TPYYMSPE-LFSNKPYNHK-SDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELIKAMLHQDP 242
                        170
                 ....*....|....
gi 545477471 158 SERLTAPEILLHPW 171
Cdd:cd08223  243 EKRPSVKRILRQPY 256
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
10-171 7.33e-15

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 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: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 70.71  E-value: 7.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDaLSDKHGCPAYVSPEILN 89
Cdd:cd14193   98 NLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSREANQVKIIDFGLARRYKPREK-LRVNFGTPEFLAPEVVN 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  90 TTgtYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEH----ISPKARCLIRSLLRREPSERLTAPE 165
Cdd:cd14193  177 YE--FVSFPTDMWSLGVIAYMLLSGLSPFLGEDDNETLNNILACQWDFEDEefadISEEAKDFISKLLIKEKSWRMSASE 254

                 ....*.
gi 545477471 166 ILLHPW 171
Cdd:cd14193  255 ALKHPW 260
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
15-169 8.18e-15

Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GCN2 (or EIF2AK4) is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. Its kinase domain is activated via conformational changes as a result of the binding of uncharged tRNA to the HisRS-like domain. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. The GCN2 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: 270948 [Multi-domain]  Cd Length: 278  Bit Score: 70.86  E-value: 8.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  15 EAARLFKQIVSAVAHCHQSAIV-------------LGDLKLRKFVFSTEERTQLRLESLEDTHI---MKGEDDALSDKHG 78
Cdd:cd14046  105 RLWRLFRQILEGLAYIHSQGIIhrdlkpvnifldsNGNVKIGDFGLATSNKLNVELATQDINKStsaALGSSGDLTGNVG 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEIL-NTTGTYSGKaADVWSLGVMLYTLLvgrYPFHDSDPSALFSKIRRG-------QFCIPEHisPKARCLIR 150
Cdd:cd14046  185 TALYVAPEVQsGTKSTYNEK-VDMYSLGIIFFEMC---YPFSTGMERVQILTALRSvsiefppDFDDNKH--SKQAKLIR 258
                        170
                 ....*....|....*....
gi 545477471 151 SLLRREPSERLTAPEILLH 169
Cdd:cd14046  259 WLLNHDPAKRPSAQELLKS 277
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
8-196 8.54e-15

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-zeta plays a critical role in activating the glucose transport response. It is activated by glucose, insulin, and exercise through diverse pathways. PKC-zeta also plays a central role in maintaining cell polarity in yeast and mammalian cells. In addition, it affects actin remodeling in muscle cells. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. aPKCs only require phosphatidylserine (PS) for activation. The aPKC-zeta 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: 270768 [Multi-domain]  Cd Length: 357  Bit Score: 71.59  E-value: 8.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFK-QIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGedDALSDKHGCPAYVSPE 86
Cdd:cd05617  109 RQRKLPEEHARFYAaEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPG--DTTSTFCGTPNYIAPE 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  87 ILNttGTYSGKAADVWSLGVMLYTLLVGRYPFH--DSDPSA-----LFSKIRRGQFCIPEHISPKARCLIRSLLRREPSE 159
Cdd:cd05617  187 ILR--GEEYGFSVDWWALGVLMFEMMAGRSPFDiiTDNPDMntedyLFQVILEKPIRIPRFLSVKASHVLKGFLNKDPKE 264
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 545477471 160 RLTA------PEILLHPWFESvlepgyIDSEIGTSDQIVPEYQ 196
Cdd:cd05617  265 RLGCqpqtgfSDIKSHTFFRS------IDWDLLEKKQVTPPFK 301
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
78-204 1.22e-14

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK2 was the first identified target of activated RhoA, and was found to play a role in stress fiber and focal adhesion formation. It is prominently expressed in the brain, heart, and skeletal muscles. It is implicated in vascular and neurological disorders, such as hypertension and vasospasm of the coronary and cerebral arteries. ROCK2 is also activated by caspase-2 cleavage, resulting in thrombin-induced microparticle generation in response to cell activation. Mice deficient in ROCK2 show intrauterine growth retardation and embryonic lethality because of placental dysfunction. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK2 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: 270771 [Multi-domain]  Cd Length: 379  Bit Score: 71.18  E-value: 1.22e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGT--YSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFCIPE--HISPKARCLIRS 151
Cdd:cd05621  214 GTPDYISPEVLKSQGGdgYYGRECDWWSVGVFLFEMLVGDTPFYADSLVGTYSKImdHKNSLNFPDdvEISKHAKNLICA 293
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 545477471 152 LL--RREPSERLTAPEILLHPWFESvlEPGYIDSEIGTSDQIVPEYQEDSDISSF 204
Cdd:cd05621  294 FLtdREVRLGRNGVEEIKQHPFFRN--DQWNWDNIRETAAPVVPELSSDIDTSNF 346
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
5-172 1.33e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek9, also called Nercc1, is primarily a cytoplasmic protein but can also localize in the nucleus. It is involved in modulating chromosome alignment and splitting during mitosis. It interacts with the gamma-tubulin ring complex and the Ran GTPase, and is implicated in microtubule organization. Nek9 associates with FACT (FAcilitates Chromatin Transcription) and modulates interphase progression. It also interacts with Nek6, and Nek7, during mitosis, resulting in their activation. Nek9 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270860 [Multi-domain]  Cd Length: 256  Bit Score: 70.15  E-value: 1.33e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLK-LRKFVfsteerTQLRLESLEDTHIMK---GEDDALSDKHGCP 80
Cdd:cd08221   92 QQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKtLNIFL------TKADLVKLGDFGISKvldSESSMAESIVGTP 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTgTYSGKaADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC-IPEHISPKARCLIRSLLRREPSE 159
Cdd:cd08221  166 YYMSPELVQGV-KYNFK-SDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEdIDEQYSEEIIQLVHDCLHQDPED 243
                        170
                 ....*....|...
gi 545477471 160 RLTAPEILLHPWF 172
Cdd:cd08221  244 RPTAEELLERPLL 256
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
20-167 1.72e-14

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek3 is primarily localized in the cytoplasm and shows no cell cycle-dependent changes in its activity. It is present in the axons of neurons and affects morphogenesis and polarity through its regulation of microtubule acetylation. Nek3 modulates the signaling of the prolactin receptor through its activation of Vav2 and contributes to prolactin-mediated motility of breast cancer cells. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173759 [Multi-domain]  Cd Length: 255  Bit Score: 69.62  E-value: 1.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  20 FKQIVSAVAHCHQSAIVLGDLKlRKFVFSTEErTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTTgTYSGKAa 99
Cdd:cd08219  106 FVQMCLGVQHIHEKRVLHRDIK-SKNIFLTQN-GKVKLGDFGSARLLTSPGAYACTYVGTPYYVPPEIWENM-PYNNKS- 181
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545477471 100 DVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC-IPEHISPKARCLIRSLLRREPSERLTAPEIL 167
Cdd:cd08219  182 DIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKpLPSHYSYELRSLIKQMFKRNPRSRPSATTIL 250
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
2-182 2.05e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK6 is widely expressed in many tissues and is expressed as multiple splice variants with different domain architectures. It is post-translationally palmitoylated and localized in the membrane. GRK6 plays important roles in the regulation of dopamine, M3 muscarinic, opioid, and chemokine receptor signaling. It also plays maladaptive roles in addiction and Parkinson's disease. GRK6-deficient mice exhibit altered dopamine receptor regulation, decreased lymphocyte chemotaxis, and increased acute inflammation and neutrophil chemotaxis. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK6 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: 270779 [Multi-domain]  Cd Length: 285  Bit Score: 70.05  E-value: 2.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   2 HSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLE-DTHImkGEDDALSDKHGCP 80
Cdd:cd05630   90 HIYHMGQAGFPEARAVFYAAEICCGLEDLHRERIVYRDLKPENILL--DDHGHIRISDLGlAVHV--PEGQTIKGRVGTV 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEIL-NTTGTYSgkaADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRR----GQFCIPEHISPKARCLIRSLLRR 155
Cdd:cd05630  166 GYMAPEVVkNERYTFS---PDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERlvkeVPEEYSEKFSPQARSLCSMLLCK 242
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 545477471 156 EPSERL-----TAPEILLHPWFESV----LEPGYID 182
Cdd:cd05630  243 DPAERLgcrggGAREVKEHPLFKKLnfkrLGAGMLE 278
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
6-172 2.23e-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: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   6 RSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFsTEERTQLRL-----ESLEDTHIMkgeddalsDKHGCP 80
Cdd:cd05118   93 DYPRGLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILI-NLELGQLKLadfglARSFTSPPY--------TPYVAT 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 -AYVSPEILNTTGTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRR--GqfcipehiSPKARCLIRSLLRREP 157
Cdd:cd05118  164 rWYRAPEVLLGAKPY-GSSIDIWSLGCILAELLTGRPLFPGDSEVDQLAKIVRllG--------TPEALDLLSKMLKYDP 234
                        170
                 ....*....|....*
gi 545477471 158 SERLTAPEILLHPWF 172
Cdd:cd05118  235 AKRITASQALAHPYF 249
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
22-175 2.27e-14

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. GRKs play important roles in the cardiovascular, immune, respiratory, skeletal, and nervous systems. They contain a central catalytic domain, flanked by N- and C-terminal extensions. The N-terminus contains an RGS (regulator of G protein signaling) homology (RH) domain and several motifs. The C-terminus diverges among different groups of GRKs. There are seven types of GRKs, named GRK1 to GRK7, which are subdivided into three main groups: visual (GRK1/7); beta-adrenergic receptor kinases (GRK2/3); and GRK4-like (GRK4/5/6). Expression of GRK2/3/5/6 is widespread while GRK1/4/7 show a limited tissue distribution. The substrate spectrum of the widely expressed GRKs partially overlaps. The GRK 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: 270729 [Multi-domain]  Cd Length: 278  Bit Score: 69.86  E-value: 2.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  22 QIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLEDTHIMKGEDdALSDKHGCPAYVSPEILNTTGTYSgKAADV 101
Cdd:cd05577  103 EIICGLEHLHNRFIVYRDLKPENILL--DDHGHVRISDLGLAVEFKGGK-KIKGRVGTHGYMAPEVLQKEVAYD-FSVDW 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471 102 WSLGVMLYTLLVGRYPFHDS----DPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL-----TAPEILLHPWF 172
Cdd:cd05577  179 FALGCMLYEMIAGRSPFRQRkekvDKEELKRRTLEMAVEYPDSFSPEARSLCEGLLQKDPERRLgcrggSADEVKEHPFF 258

                 ...
gi 545477471 173 ESV 175
Cdd:cd05577  259 RSL 261
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
8-175 3.23e-14

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGKs are activated by insulin and growth factors via phosphoinositide 3-kinase and PDK1. They activate ion channels, ion carriers, and the Na-K-ATPase, as well as regulate the activity of enzymes and transcription factors. SGKs play important roles in transport, hormone release, neuroexcitability, cell proliferation, and apoptosis. There are three isoforms of SGK, named SGK1, SGK2, and SGK3 (also called cytokine-independent survival kinase CISK). The SGK 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: 270727 [Multi-domain]  Cd Length: 323  Bit Score: 69.65  E-value: 3.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFK-QIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLrleslEDTHIMKgEDDALSDKH----GCPAY 82
Cdd:cd05575   89 RERHFPEPRARFYAaEIASALGYLHSLNIIYRDLKPENILLDSQGHVVL-----TDFGLCK-EGIEPSDTTstfcGTPEY 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNTTgTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLT 162
Cdd:cd05575  163 LAPEVLRKQ-PY-DRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKRLG 240
                        170
                 ....*....|....*..
gi 545477471 163 AP----EILLHPWFESV 175
Cdd:cd05575  241 SGndflEIKNHSFFRPI 257
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
1-167 5.02e-14

Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related kinase 6 and 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 and Nek7 are the shortest Neks, consisting only of the catalytic domain and a very short N-terminal extension. They show distinct expression patterns and both appear to be downstream substrates of Nek9. They are required for mitotic spindle formation and cytokinesis. They may also be regulators of the p70 ribosomal S6 kinase. Nek6/7 is part of a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 68.45  E-value: 5.02e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAA-RLFKQIVSAVAHCHQSAIVLGDLKLRKfVFSTEErTQLRLESLEDTHIMKGEDDALSDKHGC 79
Cdd:cd08224   90 LIKHFKKQKRLIPERTIwKYFVQLCSALEHMHSKRIMHRDIKPAN-VFITAN-GVVKLGDLGLGRFFSSKTTAAHSLVGT 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  80 PAYVSPEILNTTGtYSGKaADVWSLGVMLYTLLVGRYPFHDSDPS--ALFSKIRRGQFC-IP-EHISPKARCLIRSLLRR 155
Cdd:cd08224  168 PYYMSPERIREQG-YDFK-SDIWSLGCLLYEMAALQSPFYGEKMNlySLCKKIEKCEYPpLPaDLYSQELRDLVAACIQP 245
                        170
                 ....*....|..
gi 545477471 156 EPSERLTAPEIL 167
Cdd:cd08224  246 DPEKRPDISYVL 257
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
13-172 5.77e-14

Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin 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: 271009 [Multi-domain]  Cd Length: 257  Bit Score: 68.38  E-value: 5.77e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSdKHGCPAYVSPEILNTTG 92
Cdd:cd14107   97 EAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMVSPTREDIKICDFGFAQEITPSEHQFS-KYGSPEFVAPEIVHQEP 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  93 TysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ--FCIPE--HISPKARCLIRSLLRREPSERLTAPEILL 168
Cdd:cd14107  176 V--SAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVvsWDTPEitHLSEDAKDFIKRVLQPDPEKRPSASECLS 253

                 ....
gi 545477471 169 HPWF 172
Cdd:cd14107  254 HEWF 257
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
6-166 6.48e-14

Catalytic domain of Numb-Associated Kinase (NAK)-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 Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It 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. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-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: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 68.46  E-value: 6.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   6 RSRKRLREEEAARLFKQIVSAVAHCH--QSAIVLGDLKL--------RKFVF----STEERTQLRLESLEDTHImkgEDD 71
Cdd:cd14037  100 RLQTGLTESEILKIFCDVCEAVAAMHylKPPLIHRDLKVenvlisdsGNYKLcdfgSATTKILPPQTKQGVTYV---EED 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  72 ALsdKHGCPAYVSPEILNTtgtYSGKA----ADVWSLGVMLYTLLVGRYPFHDSDPSAlfskIRRGQFCIPEH--ISPKA 145
Cdd:cd14037  177 IK--KYTTLQYRAPEMIDL---YRGKPitekSDIWALGCLLYKLCFYTTPFEESGQLA----ILNGNFTFPDNsrYSKRL 247
                        170       180
                 ....*....|....*....|.
gi 545477471 146 RCLIRSLLRREPSERltaPEI 166
Cdd:cd14037  248 HKLIRYMLEEDPEKR---PNI 265
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
78-204 7.62e-14

Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The DMPK-like subfamily is composed of DMPK and DMPK-related cell division control protein 42 (Cdc42) binding kinase (MRCK). DMPK is expressed in skeletal and cardiac muscles, and in central nervous tissues. The functional role of DMPK is not fully understood. It may play a role in the signal transduction and homeostasis of calcium. The DMPK gene is implicated in myotonic dystrophy 1 (DM1), an inherited multisystemic disorder with symptoms that include muscle hyperexcitability, progressive muscle weakness and wasting, cataract development, testicular atrophy, and cardiac conduction defects. The genetic basis for DM1 is the mutational expansion of a CTG repeat in the 3'-UTR of DMPK. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. Three isoforms of MRCK are known, named alpha, beta and gamma. MRCKgamma is expressed in heart and skeletal muscles, unlike MRCKalpha and MRCKbeta, which are expressed ubiquitously. The DMPK-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: 270748 [Multi-domain]  Cd Length: 331  Bit Score: 68.91  E-value: 7.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNT----TGTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFCIPEH---ISPKARCL 148
Cdd:cd05597  165 GTPDYISPEILQAmedgKGRY-GPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnHKEHFSFPDDeddVSEEAKDL 243
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545477471 149 IRSLLRRePSERL---TAPEILLHPWFESV-------LEPGYIdseigtsdqivPEYQEDSDISSF 204
Cdd:cd05597  244 IRRLICS-RERRLgqnGIDDFKKHPFFEGIdwdnirdSTPPYI-----------PEVTSPTDTSNF 297
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
4-161 8.57e-14

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha 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: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 68.87  E-value: 8.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEddALSDKHGCPAYV 83
Cdd:cd05615  101 HIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEHMVEGV--TTRTFCGTPDYI 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILnttgTYS--GKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL 161
Cdd:cd05615  179 APEII----AYQpyGRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLMTKHPAKRL 254
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
78-204 9.58e-14

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK 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: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 68.56  E-value: 9.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTG--TYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ----FCIPEHISPKARCLIRS 151
Cdd:cd05596  188 GTPDYISPEVLKSQGgdGVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHKnslqFPDDVEISKDAKSLICA 267
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 545477471 152 LLrREPSERLTA---PEILLHPWFESvlEPGYIDSEIGTSDQIVPEYQEDSDISSF 204
Cdd:cd05596  268 FL-TDREVRLGRngiEEIKAHPFFKN--DQWTWDNIRETVPPVVPELSSDIDTSNF 320
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
18-172 1.57e-13

Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRE1, also called Endoplasmic reticulum (ER)-to-nucleus signaling protein (or ERN), is an ER-localized type I transmembrane protein with kinase and endoribonuclease domains in the cytoplasmic side. It acts as an ER stress sensor and is the oldest and most conserved component of the unfolded protein response (UPR) in eukaryotes. The UPR is activated when protein misfolding is detected in the ER in order to decrease the synthesis of new proteins and increase the capacity of the ER to cope with the stress. During ER stress, IRE1 dimerizes and forms oligomers, allowing the kinase domain to undergo trans-autophosphorylation. This leads to a conformational change that stimulates its endoribonuclease activity and results in the cleavage of its mRNA substrate, HAC1 in yeast and XBP1 in metazoans, promoting a splicing event that enables translation into a transcription factor which activates the UPR. Mammals contain two IRE1 proteins, IRE1alpha (or ERN1) and IRE1beta (or ERN2). The Ire1 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: 270884 [Multi-domain]  Cd Length: 269  Bit Score: 67.30  E-value: 1.57e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  18 RLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERT-QLRLEsLEDTHIMKGEDDALSDKH------GCPAYVSPEILN- 89
Cdd:cd13982  103 RLLRQIASGLAHLHSLNIVHRDLKPQNILISTPNAHgNVRAM-ISDFGLCKKLDVGRSSFSrrsgvaGTSGWIAPEMLSg 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  90 TTGTYSGKAADVWSLG-VMLYTLLVGRYPFHDSdpsalFSK---IRRGQFCIPE-----HISPKARCLIRSLLRREPSER 160
Cdd:cd13982  182 STKRRQTRAVDIFSLGcVFYYVLSGGSHPFGDK-----LEReanILKGKYSLDKllslgEHGPEAQDLIERMIDFDPEKR 256
                        170
                 ....*....|..
gi 545477471 161 LTAPEILLHPWF 172
Cdd:cd13982  257 PSAEEVLNHPFF 268
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
1-180 1.72e-13

Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; 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. Vertebrates contain at least 2 Aurora kinases (A and B); mammals contains a third Aurora kinase gene (C). This subfamily includes Aurora-B and Aurora-C. Aurora-B is most active at the transition during metaphase to the end of mitosis. It associates with centromeres, relocates to the midzone of the central spindle, and concentrates at the midbody during cell division. 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. INCENP participates in the activation of Aurora-B in a two-step process: first by binding to form an intermediate state of activation and the phosphorylation of its C-terminal TSS motif to generate the fully active kinase. The Aurora-B 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: 271019 [Multi-domain]  Cd Length: 270  Bit Score: 67.20  E-value: 1.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTeeRTQLRLESLE-DTHImkgedDALSDKHGC 79
Cdd:cd14117   93 LYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGY--KGELKIADFGwSVHA-----PSLRRRTMC 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  80 PA--YVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREP 157
Cdd:cd14117  166 GTldYLPPEMIE--GRTHDEKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRYHP 243
                        170       180
                 ....*....|....*....|....*..
gi 545477471 158 SERLTAPEILLHPWFES----VLEPGY 180
Cdd:cd14117  244 SERLPLKGVMEHPWVKAnsrrVLPPVY 270
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1-166 1.74e-13

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek6 is required for the transition from metaphase to anaphase. It also plays important roles in mitotic spindle formation and cytokinesis. Activated by Nek9 during mitosis, Nek6 phosphorylates Eg5, a kinesin that is important for spindle bipolarity. Nek6 localizes to spindle microtubules during metaphase and anaphase, and to the midbody during cytokinesis. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 67.36  E-value: 1.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAA-RLFKQIVSAVAHCHQSAIVLGDLK-LRKFVFSTEErtqLRLESLEDTHIMKGEDDALSDKHG 78
Cdd:cd08228   92 MIKYFKKQKRLIPERTVwKYFVQLCSAVEHMHSRRVMHRDIKpANVFITATGV---VKLGDLGLGRFFSSKTTAAHSLVG 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEILNTTGtYSGKAaDVWSLGVMLYTLLVGRYPFHdSDPSALFSKIRRGQFC----IP-EHISPKARCLIRSLL 153
Cdd:cd08228  169 TPYYMSPERIHENG-YNFKS-DIWSLGCLLYEMAALQSPFY-GDKMNLFSLCQKIEQCdyppLPtEHYSEKLRELVSMCI 245
                        170
                 ....*....|...
gi 545477471 154 RREPSERltaPEI 166
Cdd:cd08228  246 YPDPDQR---PDI 255
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
18-168 1.99e-13

Catalytic domain of Fungal Pat1-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 Pat1 (also called Ran1), Saccharomyces cerevisiae VHS1 and KSP1, and similar fungal STKs. Pat1 blocks Mei2, an RNA-binding protein which is indispensable in the initiation of meiosis. Pat1 is inactivated and Mei2 activated, which initiates meiosis, under nutrient-deprived conditions through a signaling cascade involving Ste11. Meiosis induced by Pat1 inactivation may show different characteristics than normal meiosis including aberrant positioning of centromeres. VHS1 was identified in a screen for suppressors of cell cycle arrest at the G1/S transition, while KSP1 may be involved in regulating PRP20, which is required for mRNA export and maintenance of nuclear structure. The Pat1-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: 270895 [Multi-domain]  Cd Length: 267  Bit Score: 66.99  E-value: 1.99e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  18 RLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEErTQLRLES--LEDTHIMKGEDDALSDKhgcpaYVSPEILNTTGT-- 93
Cdd:cd13993  111 NVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDE-GTVKLCDfgLATTEKISMDFGVGSEF-----YMAPECFDEVGRsl 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  94 --YSGKAADVWSLGVMLYTLLVGRYPF---HDSDPSALFSKIRRGQFCipEHISPKAR---CLIRSLLRREPSERLTAPE 165
Cdd:cd13993  185 kgYPCAAGDIWSLGIILLNLTFGRNPWkiaSESDPIFYDYYLNSPNLF--DVILPMSDdfyNLLRQIFTVNPNNRILLPE 262

                 ...
gi 545477471 166 ILL 168
Cdd:cd13993  263 LQL 265
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
31-175 2.16e-13

Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKN has a C-terminal catalytic domain that is highly homologous to PKCs. Its unique N-terminal regulatory region contains antiparallel coiled-coil (ACC) domains. In mammals, there are three PKN isoforms from different genes (designated PKN-alpha, beta, and gamma), which show different enzymatic properties, tissue distribution, and varied functions. PKN can be activated by the small GTPase Rho, and by fatty acids such as arachidonic and linoleic acids. It is involved in many biological processes including cytokeletal regulation, cell adhesion, vesicle transport, glucose transport, regulation of meiotic maturation and embryonic cell cycles, signaling to the nucleus, and tumorigenesis. The PKN 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: 270741 [Multi-domain]  Cd Length: 326  Bit Score: 67.33  E-value: 2.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  31 HQSAIVLGDLKLRKFVFSTEERTQLrleslEDTHIMK---GEDDALSDKHGCPAYVSPEILnTTGTYSgKAADVWSLGVM 107
Cdd:cd05589  118 HEHKIVYRDLKLDNLLLDTEGYVKI-----ADFGLCKegmGFGDRTSTFCGTPEFLAPEVL-TDTSYT-RAVDWWGLGVL 190
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545477471 108 LYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL-----TAPEILLHPWFESV 175
Cdd:cd05589  191 IYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAISIMRRLLRKNPERRLgaserDAEDVKKQPFFRNI 263
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
6-167 2.76e-13

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


Pssm-ID: 270898 [Multi-domain]  Cd Length: 273  Bit Score: 66.55  E-value: 2.76e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   6 RSRKRLREEEAARLFKQIVSAVAHCHQSAIV-------------------LGDLKLRKFVFSTEErtqlrlESLEDTHIM 66
Cdd:cd13996   99 NSSSKNDRKLALELFKQILKGVSYIHSKGIVhrdlkpsnifldnddlqvkIGDFGLATSIGNQKR------ELNNLNNNN 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  67 KGEDDALSDKHGCPAYVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSdpSALFSKIRRGQFciPEHIS---P 143
Cdd:cd13996  173 NGNTSNNSVGIGTPLYASPEQLD--GENYNEKADIYSLGIILFEMLHPFKTAMER--STILTDLRNGIL--PESFKakhP 246
                        170       180
                 ....*....|....*....|....
gi 545477471 144 KARCLIRSLLRREPSERLTAPEIL 167
Cdd:cd13996  247 KEADLIQSLLSKNPEERPSAEQLL 270
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
13-172 3.28e-13

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Neks are involved in the regulation of downstream processes following the activation of Cdc2, and many of their functions are cell cycle-related. They play critical roles in microtubule dynamics during ciliogenesis and mitosis. The specific function of Nek5 is unknown. Nek5 is one in a family of 11 different Neks (Nek1-11). The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173765 [Multi-domain]  Cd Length: 257  Bit Score: 66.13  E-value: 3.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERtqlrLESLEDTHIMKGEDDALSDKHGC---PAYVSPEILN 89
Cdd:cd08225  100 EDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGM----VAKLGDFGIARQLNDSMELAYTCvgtPYYLSPEICQ 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  90 TTgTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC-IPEHISPKARCLIRSLLRREPSERLTAPEILL 168
Cdd:cd08225  176 NR-PYNNKT-DIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFApISPNFSRDLRSLISQLFKVSPRDRPSITSILK 253

                 ....
gi 545477471 169 HPWF 172
Cdd:cd08225  254 RPFL 257
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
5-167 3.68e-13

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK 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: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 66.38  E-value: 3.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCH--QSAIVLGDLKLRKFVFSTEERTQL------RLESLEDTHIMKGEDDALSD- 75
Cdd:cd14036   99 VEAPGPFSPDTVLKIFYQTCRAVQHMHkqSPPIIHRDLKIENLLIGNQGQIKLcdfgsaTTEAHYPDYSWSAQKRSLVEd 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  76 ---KHGCPAYVSPEILNTTGTYS-GKAADVWSLGVMLYTLLVGRYPFHDSdpsalfSKIR--RGQFCIPEHiSPKARC-- 147
Cdd:cd14036  179 eitRNTTPMYRTPEMIDLYSNYPiGEKQDIWALGCILYLLCFRKHPFEDG------AKLRiiNAKYTIPPN-DTQYTVfh 251
                        170       180
                 ....*....|....*....|.
gi 545477471 148 -LIRSLLRREPSERLTAPEIL 167
Cdd:cd14036  252 dLIRSTLKVNPEERLSITEIV 272
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
14-204 3.84e-13

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK1 is preferentially expressed in the liver, lung, spleen, testes, and kidney. It mediates signaling from Rho to the actin cytoskeleton. It is implicated in the development of cardiac fibrosis, cardiomyocyte apoptosis, and hyperglycemia. Mice deficient with ROCK1 display eyelids open at birth (EOB) and omphalocele phenotypes due to the disorganization of actin filaments in the eyelids and the umbilical ring. ROCK contains an N-terminal extension, a catalytic kinase domain, and a C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain, and is activated via interaction with Rho GTPases. The ROCK1 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: 270772 [Multi-domain]  Cd Length: 405  Bit Score: 66.95  E-value: 3.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  14 EEAARLFK-QIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLEDTHIMKGEDDALSDKH-GCPAYVSPEILNTT 91
Cdd:cd05622  171 EKWARFYTaEVVLALDAIHSMGFIHRDVKPDNMLL--DKSGHLKLADFGTCMKMNKEGMVRCDTAvGTPDYISPEVLKSQ 248
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  92 GT--YSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFCIPE--HISPKARCLIRSLL--RREPSERLTA 163
Cdd:cd05622  249 GGdgYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKImnHKNSLTFPDdnDISKEAKNLICAFLtdREVRLGRNGV 328
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 545477471 164 PEILLHPWFESvlEPGYIDSEIGTSDQIVPEYQEDSDISSF 204
Cdd:cd05622  329 EEIKRHLFFKN--DQWAWETLRDTVAPVVPDLSSDIDTSNF 367
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
13-181 6.94e-13

Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek1 is associated with centrosomes throughout the cell cycle. It is involved in the formation of primary cilium and in the maintenance of centrosomes. It cycles through the nucleus and may be capable of relaying signals between the cilium and the nucleus. Nek1 is implicated in the development of polycystic kidney disease, which is characterized by benign polycystic tumors formed by abnormal overgrowth of renal epithelial cells. It appears also to be involved in DNA damage response, and may be important for both correct DNA damage checkpoint activation and DNA repair. Nek1 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270858 [Multi-domain]  Cd Length: 256  Bit Score: 65.22  E-value: 6.94e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKfVFSTEERTqLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNTTg 92
Cdd:cd08218  100 EDQILDWFVQLCLALKHVHDRKILHRDIKSQN-IFLTKDGI-IKLGDFGIARVLNSTVELARTCIGTPYYLSPEICENK- 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  93 TYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF-CIPEHISPKARCLIRSLLRREPSERltapeillhPW 171
Cdd:cd08218  177 PYNNKS-DIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYpPVPSRYSYDLRSLVSQLFKRNPRDR---------PS 246
                        170
                 ....*....|
gi 545477471 172 FESVLEPGYI 181
Cdd:cd08218  247 INSILEKPFI 256
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
73-171 7.61e-13

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG 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: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 65.23  E-value: 7.61e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  73 LSDKHGCPAYVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF---CIPEHISPKARCLI 149
Cdd:cd14111  157 LGRRTGTLEYMAPEMVK--GEPVGPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFdafKLYPNVSQSASLFL 234
                         90       100
                 ....*....|....*....|..
gi 545477471 150 RSLLRREPSERLTAPEILLHPW 171
Cdd:cd14111  235 KKVLSSYPWSRPTTKDCFAHAW 256
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
6-172 8.30e-13

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 66.19  E-value: 8.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   6 RSRKRL--REEEAARLFKQIVSAVAHCHQSAIVLGDLK-------------LRKFVFSTEERTQLRLesledthimkged 70
Cdd:PTZ00267 159 RLKEHLpfQEYEVGLLFYQIVLALDEVHSRKMMHRDLKsaniflmptgiikLGDFGFSKQYSDSVSL------------- 225
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  71 DALSDKHGCPAYVSPEILNTTgTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF-CIPEHISPKARCLI 149
Cdd:PTZ00267 226 DVASSFCGTPYYLAPELWERK-RYS-KKADMWSLGVILYELLTLHRPFKGPSQREIMQQVLYGKYdPFPCPVSSGMKALL 303
                        170       180
                 ....*....|....*....|...
gi 545477471 150 RSLLRREPSERLTAPEiLLHPWF 172
Cdd:PTZ00267 304 DPLLSKNPALRPTTQQ-LLHTEF 325
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
11-172 8.68e-13

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 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: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 65.33  E-value: 8.68e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDaLSDKHGCPAYVSPEILNT 90
Cdd:cd14190   99 LTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGHQVKIIDFGLARRYNPREK-LKVNFGTPEFLSPEVVNY 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  91 TgtYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPE----HISPKARCLIRSLLRREPSERLTAPEI 166
Cdd:cd14190  178 D--QVSFPTDMWSMGVITYMLLSGLSPFLGDDDTETLNNVLMGNWYFDEetfeHVSDEAKDFVSNLIIKERSARMSATQC 255

                 ....*.
gi 545477471 167 LLHPWF 172
Cdd:cd14190  256 LKHPWL 261
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
1-175 1.10e-12

Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-epsilon has been shown to behave as an oncoprotein. Its overexpression contributes to neoplastic transformation depending on the cell type. It contributes to oncogenesis by inducing disordered cell growth and inhibiting cell death. It also plays a role in tumor invasion and metastasis. PKC-epsilon has also been found to confer cardioprotection against ischemia and reperfusion-mediated damage. Other cellular functions include the regulation of gene expression, cell adhesion, and cell motility. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. nPKCs are calcium-independent, but require DAG (1,2-diacylglycerol) and phosphatidylserine (PS) for activity. The nPKC-epsilon 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: 270743 [Multi-domain]  Cd Length: 321  Bit Score: 65.21  E-value: 1.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRlrEEEAARLF-KQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEddALSDKHGC 79
Cdd:cd05591   84 MFQIQRARKF--DEPRARFYaAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKEGILNGK--TTTTFCGT 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  80 PAYVSPEILNTTgTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSE 159
Cdd:cd05591  160 PDYIAPEILQEL-EY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAK 237
                        170       180
                 ....*....|....*....|...
gi 545477471 160 RL-------TAPEILLHPWFESV 175
Cdd:cd05591  238 RLgcvasqgGEDAIRQHPFFREI 260
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
4-172 2.10e-12

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio 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: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 64.23  E-value: 2.10e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVF-STEERTQLRLESLEDThIMKGEDDALSDKHGCPAY 82
Cdd:cd14113   93 YVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVdQSLSKPTIKLADFGDA-VQLNTTYYIHQLLGSPEF 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILntTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEH----ISPKARCLIRSLLRREPS 158
Cdd:cd14113  172 AAPEII--LGNPVSLTSDLWSIGVLTYVLLSGVSPFLDESVEETCLNICRLDFSFPDDyfkgVSQKAKDFVCFLLQMDPA 249
                        170
                 ....*....|....
gi 545477471 159 ERLTAPEILLHPWF 172
Cdd:cd14113  250 KRPSAALCLQEQWL 263
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
8-171 2.30e-12

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin 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: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 63.78  E-value: 2.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLESLEDTHIMKGEDDALSDKhgCPAYV---S 84
Cdd:cd14110   93 RNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIIT--EKNLLKIVDLGNAQPFNQGKVLMTDK--KGDYVetmA 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILntTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF----CIPeHISPKARCLIRSLLRREPSER 160
Cdd:cd14110  169 PELL--EGQGAGPQTDIWAIGVTAFIMLSADYPVSSDLNWERDRNIRKGKVqlsrCYA-GLSGGAVNFLKSTLCAKPWGR 245
                        170
                 ....*....|.
gi 545477471 161 LTAPEILLHPW 171
Cdd:cd14110  246 PTASECLQNPW 256
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
5-172 3.46e-12

Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RPK118 contains an N-terminal Phox homology (PX) domain, a Microtubule Interacting and Trafficking (MIT) domain, and a kinase domain containing a long uncharacterized insert. Also included in the family is human RPK60 (or ribosomal protein S6 kinase-like 1), which also contains MIT and kinase domains but lacks a PX domain. RPK118 binds sphingosine kinase, a key enzyme in the synthesis of sphingosine 1-phosphate (SPP), a lipid messenger involved in many cellular events. RPK118 may be involved in transmitting SPP-mediated signaling. RPK118 also binds the antioxidant peroxiredoxin-3. RPK118 may be involved in the transport of PRDX3 from the cytoplasm to its site of function in the mitochondria. The RPK118-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: 270728 [Multi-domain]  Cd Length: 265  Bit Score: 63.33  E-value: 3.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL----RLESLEDThimkGEDDALSDkhgcp 80
Cdd:cd05576  104 AASRFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLtyfsRWSEVEDS----CDSDAIEN----- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPE---ILNTTgtysgKAADVWSLGVMLYTLLVGRyPFHDSDPSALFskiRRGQFCIPEHISPKARCLIRSLLRREP 157
Cdd:cd05576  175 MYCAPEvggISEET-----EACDWWSLGALLFELLTGK-ALVECHPAGIN---THTTLNIPEWVSEEARSLLQQLLQFNP 245
                        170       180
                 ....*....|....*....|
gi 545477471 158 SERLTA-----PEILLHPWF 172
Cdd:cd05576  246 TERLGAgvagvEDIKSHPFF 265
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
78-175 4.15e-12

Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group is composed of fungal NDR-like proteins including Saccharomyces cerevisiae CBK1 (or CBK1p), Schizosaccharomyces pombe Orb6 (or Orb6p), Ustilago maydis Ukc1 (or Ukc1p), and Neurospora crassa Cot1. Like NDR kinase, group members contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. CBK1 is an essential component in the RAM (regulation of Ace2p activity and cellular morphogenesis) network. CBK1 and Orb6 play similar roles in coordinating cell morphology with cell cycle progression. Ukc1 is involved in morphogenesis, pathogenicity, and pigment formation. Cot1 plays a role in polar tip extension.The fungal NDR 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: 270778 [Multi-domain]  Cd Length: 377  Bit Score: 64.10  E-value: 4.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIR--RGQFCIPE--HISPKARCLIRSLL 153
Cdd:cd05629  210 GTPDYIAPEIFLQQGY--GQECDWWSLGAIMFECLIGWPPFCSENSHETYRKIInwRETLYFPDdiHLSVEAEDLIRRLI 287
                         90       100
                 ....*....|....*....|....*
gi 545477471 154 rREPSERL---TAPEILLHPWFESV 175
Cdd:cd05629  288 -TNAENRLgrgGAHEIKSHPFFRGV 311
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
10-178 5.46e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 63.99  E-value: 5.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   10 RLREEEAARLFKQIVSAVAHCHQ-------SAIVLGDLKLRKFVFSTEER----TQLRLESLEDTHIMKGEDDALSDK-- 76
Cdd:PTZ00266  114 KIEEHAIVDITRQLLHALAYCHNlkdgpngERVLHRDLKPQNIFLSTGIRhigkITAQANNLNGRPIAKIGDFGLSKNig 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   77 -----HGC---PAYVSPEIL-NTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDP-SALFSKIRRGQFCIPEHISPKAR 146
Cdd:PTZ00266  194 iesmaHSCvgtPYYWSPELLlHETKSYDDKS-DMWALGCIIYELCSGKTPFHKANNfSQLISELKRGPDLPIKGKSKELN 272
                         170       180       190
                  ....*....|....*....|....*....|..
gi 545477471  147 CLIRSLLRREPSERLTAPEILLHPWFESVLEP 178
Cdd:PTZ00266  273 ILIKNLLNLSAKERPSALQCLGYQIIKNVGPP 304
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
78-174 5.73e-12

Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; 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 the MAPKKs Polymyxin B resistance protein 2 (PBS2) from Saccharomyces cerevisiae, Wis1 from Schizosaccharomyces pombe, and related proteins. PBS2 and Wis1 are components of stress-activated MAPK cascades in budding and fission yeast, respectively. PBS2 is the specific activator of the MAPK Hog1, which plays a central role in the response of budding yeast to stress including exposure to arsenite and hyperosmotic environments. Wis1 phosphorylates and activates the MAPK Sty1 (also called Spc1 or Phh1), which stimulates a transcriptional response to a wide range of cellular insults through the bZip transcription factors Atf1, Pcr1, and Pap1. The PBS2 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132953 [Multi-domain]  Cd Length: 286  Bit Score: 62.94  E-value: 5.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEIL-----NTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRrgQFC------IPEHISPKAR 146
Cdd:cd06622  163 GCQSYMAPERIksggpNQNPTYTVQS-DVWSLGLSILEMALGRYPYPPETYANIFAQLS--AIVdgdpptLPSGYSDDAQ 239
                         90       100
                 ....*....|....*....|....*...
gi 545477471 147 CLIRSLLRREPSERLTAPEILLHPWFES 174
Cdd:cd06622  240 DFVAKCLNKIPNRRPTYAQLLEHPWLVK 267
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
1-172 6.06e-12

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: 63.12  E-value: 6.06e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKR-LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLESLEDTHIMKGEDDAL-SDKHG 78
Cdd:cd07832   86 LSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLIS--STGVLKIADFGLARLFSEEDPRLySHQVA 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEILNTTGTYsGKAADVWSLGVMLYTLLVGRYPFH-DSDPSALFSKIRR------------------GQFCIPE 139
Cdd:cd07832  164 TRWYRAPELLYGSRKY-DEGVDLWAVGCIFAELLNGSPLFPgENDIEQLAIVLRTlgtpnektwpeltslpdyNKITFPE 242
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 545477471 140 H-----------ISPKARCLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd07832  243 SkgirleeifpdCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
8-172 8.30e-12

Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG 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: 271010 [Multi-domain]  Cd Length: 255  Bit Score: 62.23  E-value: 8.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKgEDDALSDKHGCPAYVSPEI 87
Cdd:cd14108   91 RPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKTDQVRICDFGNAQELT-PNEPQYCKYGTPEFVAPEI 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  88 LNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEH----ISPKARCLIRSLLRREpSERLTA 163
Cdd:cd14108  170 VNQSPV--SKVTDIWPVGVIAYLCLTGISPFVGENDRTTLMNIRNYNVAFEESmfkdLCREAKGFIIKVLVSD-RLRPDA 246

                 ....*....
gi 545477471 164 PEILLHPWF 172
Cdd:cd14108  247 EETLEHPWF 255
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
22-175 8.83e-12

Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The beta-ARK group is composed of GRK2, GRK3, and similar proteins. GRK2 and GRK3 are both widely expressed in many tissues, although GRK2 is present at higher levels. They contain an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRK2 (also called beta-ARK or beta-ARK1) is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The beta-ARK 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: 270757 [Multi-domain]  Cd Length: 279  Bit Score: 62.46  E-value: 8.83e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  22 QIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLE-DTHIMKGEDDALSDKHGcpaYVSPEILNTTGTYSgKAAD 100
Cdd:cd05606  106 EVILGLEHMHNRFIVYRDLKPANILL--DEHGHVRISDLGlACDFSKKKPHASVGTHG---YMAPEVLQKGVAYD-SSAD 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471 101 VWSLGVMLYTLLVGRYPF--------HDSDPSALFSKIRrgqfcIPEHISPKARCLIRSLLRREPSERL-----TAPEIL 167
Cdd:cd05606  180 WFSLGCMLYKLLKGHSPFrqhktkdkHEIDRMTLTMNVE-----LPDSFSPELKSLLEGLLQRDVSKRLgclgrGATEVK 254

                 ....*...
gi 545477471 168 LHPWFESV 175
Cdd:cd05606  255 EHPFFKGV 262
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
8-172 1.12e-11

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


Pssm-ID: 132943 [Multi-domain]  Cd Length: 256  Bit Score: 61.90  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIV-------------LGDLKLRKFVFSTEertqlrlesLEDTHIMKGEddals 74
Cdd:cd06612   93 NKTLTEEEIAAILYQTLKGLEYLHSNKKIhrdikagnillneEGQAKLADFGVSGQ---------LTDTMAKRNT----- 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  75 dKHGCPAYVSPEILNTTGtYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPS-ALFSKIRR--GQFCIPEHISPKARCLIRS 151
Cdd:cd06612  159 -VIGTPFWMAPEVIQEIG-YNNKA-DIWSLGITAIEMAEGKPPYSDIHPMrAIFMIPNKppPTLSDPEKWSPEFNDFVKK 235
                        170       180
                 ....*....|....*....|.
gi 545477471 152 LLRREPSERLTAPEILLHPWF 172
Cdd:cd06612  236 CLVKDPEERPSAIQLLQHPFI 256
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
78-175 1.61e-11

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL 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: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 62.20  E-value: 1.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGtySGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIP---EHISPKARCLIRSLLR 154
Cdd:cd05610  219 GTPDYLAPELLLGKP--HGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLT 296
                         90       100
                 ....*....|....*....|.
gi 545477471 155 REPSERLTAPEILLHPWFESV 175
Cdd:cd05610  297 MDPTKRAGLKELKQHPLFHGV 317
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
10-172 1.66e-11

Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Group II PAKs, also called non-conventional PAKs, include PAK4, PAK5, and PAK6. Group II PAKs contain PBD (p21-binding domain) and catalytic domains, but lack other motifs found in group I PAKs, such as an AID (autoinhibitory domain) and SH3 binding sites. Since group II PAKs do not contain an obvious AID, they may be regulated differently from group I PAKs. While group I PAKs interact with the SH3 containing proteins Nck, Grb2 and PIX, no such binding has been demonstrated for group II PAKs. Some known substrates of group II PAKs are also substrates of group I PAKs such as Raf, BAD, LIMK and GEFH1. Unique group II substrates include MARK/Par-1 and PDZ-RhoGEF. Group II PAKs play important roles in filopodia formation, neuron extension, cytoskeletal organization, and cell survival. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. 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: 270815 [Multi-domain]  Cd Length: 261  Bit Score: 61.69  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL--------------RLESLEdthimkgeddalsd 75
Cdd:cd06648   99 RMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLsdfgfcaqvskevpRRKSLV-------------- 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  76 khGCPAYVSPEILNTTgTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ---FCIPEHISPKARCLIRSL 152
Cdd:cd06648  165 --GTPYWMAPEVISRL-PY-GTEVDIWSLGIMVIEMVDGEPPYFNEPPLQAMKRIRDNEppkLKNLHKVSPRLRSFLDRM 240
                        170       180
                 ....*....|....*....|
gi 545477471 153 LRREPSERLTAPEILLHPWF 172
Cdd:cd06648  241 LVRDPAQRATAAELLNHPFL 260
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
7-172 1.78e-11

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK6 may play a role in stress responses through its activation by the mitogen-activated protein kinase (MAPK) p38 and MAPK kinase 6 (MKK6) pathway. PAK6 is highly expressed in the brain. It is not required for viability, but together with PAK5, it is required for normal levels of locomotion and activity, and for learning and memory. Increased expression of PAK6 is found in primary and metastatic prostate cancer. PAK6 may play a role in the regulation of motility. PAK6 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. 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: 270821 [Multi-domain]  Cd Length: 297  Bit Score: 61.93  E-value: 1.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLrleslED----THIMKgedDALSDKH--GCP 80
Cdd:cd06659  110 SQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVKL-----SDfgfcAQISK---DVPKRKSlvGTP 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEILNTTgTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG---QFCIPEHISPKARCLIRSLLRREP 157
Cdd:cd06659  182 YWMAPEVISRC-PY-GTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMKRLRDSpppKLKNSHKASPVLRDFLERMLVRDP 259
                        170
                 ....*....|....*
gi 545477471 158 SERLTAPEILLHPWF 172
Cdd:cd06659  260 QERATAQELLDHPFL 274
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
8-175 2.01e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK3 (also called cytokine-independent survival kinase or CISK) is expressed in most tissues and is most abundant in the embryo and adult heart and spleen. It was originally discovered in a screen for antiapoptotic genes. It phosphorylates and inhibits the proapoptotic proteins, Bad and FKHRL1. SGK3 also regulates many transporters, ion channels, and receptors. It plays a critical role in hair follicle morphogenesis and hair cycling. The SGK3 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: 270755 [Multi-domain]  Cd Length: 326  Bit Score: 61.90  E-value: 2.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLF-KQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTqlrleSLEDTHIMKgEDDALSDKH----GCPAY 82
Cdd:cd05604   90 RERSFPEPRARFYaAEIASALGYLHSINIVYRDLKPENILLDSQGHI-----VLTDFGLCK-EGISNSDTTttfcGTPEY 163
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNTTgTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLT 162
Cdd:cd05604  164 LAPEVIRKQ-PYD-NTVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLRLG 241
                        170
                 ....*....|....*..
gi 545477471 163 AP----EILLHPWFESV 175
Cdd:cd05604  242 AKedflEIKNHPFFESI 258
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
4-198 2.41e-11

Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK1 is ubiquitously expressed and is under transcriptional control of numerous stimuli including cell stress (cell shrinkage), serum, hormones (gluco- and mineralocorticoids), gonadotropins, growth factors, interleukin-6, and other cytokines. It plays roles in sodium retention and potassium elimination in the kidney, nutrient transport, salt sensitivity, memory consolidation, and cardiac repolarization. A common SGK1 variant is associated with increased blood pressure and body weight. SGK1 may also contribute to tumor growth, neurodegeneration, fibrosing disease, and ischemia. The SGK1 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: 270753 [Multi-domain]  Cd Length: 339  Bit Score: 61.57  E-value: 2.41e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFK-QIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMkgEDDALSDKHGCPAY 82
Cdd:cd05602   97 YHLQRERCFLEPRARFYAaEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKENIE--PNGTTSTFCGTPEY 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNTTgTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLT 162
Cdd:cd05602  175 LAPEVLHKQ-PYD-RTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDRTKRLG 252
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 545477471 163 AP----EILLHPWFESV---------LEPGYIDSEIGTSD--QIVPEYQED 198
Cdd:cd05602  253 AKddftEIKNHIFFSPInwddlinkkITPPFNPNVSGPNDlrHFDPEFTDE 303
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
4-169 2.45e-11

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 3 or PKR-like Endoplasmic Reticulum Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PERK (or EIF2AK3) is a type-I ER transmembrane protein containing a luminal domain bound with the chaperone BiP under unstressed conditions and a cytoplasmic catalytic kinase domain. In response to the accumulation of misfolded or unfolded proteins in the ER, PERK is activated through the release of BiP, allowing it to dimerize and autophosphorylate. It functions as the central regulator of translational control during the Unfolded Protein Response (UPR) pathway. In addition to the eIF-2 alpha subunit, PERK also phosphorylates Nrf2, a leucine zipper transcription factor which regulates cellular redox status and promotes cell survival during the UPR. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PERK 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: 270950 [Multi-domain]  Cd Length: 281  Bit Score: 61.43  E-value: 2.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEE---AARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESL------EDTHIMKGEDDALS 74
Cdd:cd14048  105 WMNRRCTMESRElfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLvtamdqGEPEQTVLTPMPAY 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  75 DKH----GCPAYVSPEILNTTgTYSGKaADVWSLGVMLYTLLvgrYPFH-DSDPSALFSKIRRGQF-CIPEHISPKARCL 148
Cdd:cd14048  185 AKHtgqvGTRLYMSPEQIHGN-QYSEK-VDIFALGLILFELI---YSFStQMERIRTLTDVRKLKFpALFTNKYPEERDM 259
                        170       180
                 ....*....|....*....|.
gi 545477471 149 IRSLLRREPSERLTAPEILLH 169
Cdd:cd14048  260 VQQMLSPSPSERPEAHEVIEH 280
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
8-206 2.71e-11

Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SGK2 shows a more restricted distribution than SGK1 and is most abundantly expressed in epithelial tissues including kidney, liver, pancreas, and the choroid plexus of the brain. In vitro cellular assays show that SGK2 can stimulate the activity of ion channels, the glutamate transporter EEAT4, and the glutamate receptors, GluR6 and GLUR1. The SGK2 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: 270754 [Multi-domain]  Cd Length: 321  Bit Score: 61.52  E-value: 2.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFK-QIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLR-----LESLEdthimkgEDDALSDKHGCPA 81
Cdd:cd05603   89 RERCFLEPRARFYAaEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTdfglcKEGME-------PEETTSTFCGTPE 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNTTgTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL 161
Cdd:cd05603  162 YLAPEVLRKE-PYD-RTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRRRL 239
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471 162 TAP----EILLHPWFESV---------LEPGYIDSEIGTSD--QIVPEYQEDSDISSFFC 206
Cdd:cd05603  240 GAKadflEIKNHVFFSPInwddlyhkrITPPYNPNVAGPADlrHFDPEFTQEAVPHSVGR 299
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
4-172 2.97e-11

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: 60.82  E-value: 2.97e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQ-----------SAIVL---GDLKLRKFVFSTEertqlrlesLEDThimKGE 69
Cdd:cd06605   89 ILKEVGRIPERILGKIAVAVVKGLIYLHEkhkiihrdvkpSNILVnsrGQVKLCDFGVSGQ---------LVDS---LAK 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  70 DDAlsdkhGCPAYVSPEILNTTGtYSGKAaDVWSLGVMLYTLLVGRYPF---HDSDPSALFSKIRrgqfCI--------P 138
Cdd:cd06605  157 TFV-----GTRSYMAPERISGGK-YTVKS-DIWSLGLSLVELATGRFPYpppNAKPSMMIFELLS----YIvdepppllP 225
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 545477471 139 EHI-SPKARCLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd06605  226 SGKfSPDFQDFVSQCLQKDPTERPSYKELMEHPFI 260
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
13-182 3.21e-11

Catalytic domain of G protein-coupled Receptor Kinase 4-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 GRK4-like group include GRK4, GRK5, GRK6, and similar GRKs. They contain an N-terminal RGS homology (RH) domain and a catalytic domain, but lack a G protein betagamma-subunit binding domain. They are localized to the plasma membrane through post-translational lipid modification or direct binding to PIP2. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4-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: 270756 [Multi-domain]  Cd Length: 285  Bit Score: 60.83  E-value: 3.21e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFK-QIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLE-DTHIMKGEddALSDKHGCPAYVSPEIL-N 89
Cdd:cd05605  100 EEERAVFYAaEITCGLEHLHSERIVYRDLKPENILL--DDHGHVRISDLGlAVEIPEGE--TIRGRVGTVGYMAPEVVkN 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  90 TTGTYSgkaADVWSLGVMLYTLLVGRYPFHdsdpsALFSKIRR---------GQFCIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd05605  176 ERYTFS---PDWWGLGCLIYEMIEGQAPFR-----ARKEKVKReevdrrvkeDQEEYSEKFSEEAKSICSQLLQKDPKTR 247
                        170       180       190
                 ....*....|....*....|....*....|.
gi 545477471 161 L-----TAPEILLHPWFESV----LEPGYID 182
Cdd:cd05605  248 LgcrgeGAEDVKSHPFFKSInfkrLEAGLLE 278
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
7-181 3.27e-11

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK5 is mainly expressed in the brain. It is not required for viability, but together with PAK6, it is required for normal levels of locomotion and activity, and for learning and memory. PAK5 cooperates with Inca (induced in neural crest by AP2) in the regulation of cell adhesion and cytoskeletal organization in the embryo and in neural crest cells during craniofacial development. PAK5 may also play a role in controlling the signaling of Raf-1, an effector of Ras, at the mitochondria. PAK5 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. 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: 132989 [Multi-domain]  Cd Length: 292  Bit Score: 61.21  E-value: 3.27e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERtqLRLESLEDTHIMKGEDDALSDKHGCPAYVSPE 86
Cdd:cd06658  111 THTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGR--IKLSDFGFCAQVSKEVPKRKSLVGTPYWMAPE 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  87 ILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG---QFCIPEHISPKARCLIRSLLRREPSERLTA 163
Cdd:cd06658  189 VISRLPY--GTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMRRIRDNlppRVKDSHKVSSVLRGFLDLMLVREPSQRATA 266
                        170
                 ....*....|....*...
gi 545477471 164 PEILLHPWFESVLEPGYI 181
Cdd:cd06658  267 QELLQHPFLKLAGPPSCI 284
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
13-171 3.29e-11

Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-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 Saccharomyces cerevisiae Bck1 and Schizosaccharomyces pombe Mkh1, and related proteins. Budding yeast Bck1 is part of the cell integrity MAPK pathway, which is activated by stresses and aggressions to the cell wall. The MAPKKK Bck1, MAPKKs Mkk1 and Mkk2, and the MAPK Slt2 make up the cascade that is important in the maintenance of cell wall homeostasis. Fission yeast Mkh1 is involved in MAPK cascades regulating cell morphology, cell wall integrity, salt resistance, and filamentous growth in response to stress. 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 Bck1 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: 270799 [Multi-domain]  Cd Length: 270  Bit Score: 60.86  E-value: 3.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLF-KQIVSAVAHCHQSAIVLGDLKlrkfvfstEERTQLRLE---SLEDTHIMKGEDDALSDK-----HGCPAYV 83
Cdd:cd06629  106 EEDLVRFFtRQILDGLAYLHSKGILHRDLK--------ADNILVDLEgicKISDFGISKKSDDIYGNNgatsmQGSVFWM 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTGT-YSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFCIPE--HISPKARCLIRSLLRREPS 158
Cdd:cd06629  178 APEVIHSQGQgYSAKV-DIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLgnKRSAPPVPEdvNLSPEALDFLNACFAIDPR 256
                        170
                 ....*....|...
gi 545477471 159 ERLTAPEILLHPW 171
Cdd:cd06629  257 DRPTAAELLSHPF 269
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
78-172 4.06e-11

Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and Ste20-related proline alanine-rich kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SPAK is also referred to as STK39 or PASK (proline-alanine-rich STE20-related kinase). OSR1 and SPAK regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. They are also implicated in cytoskeletal rearrangement, cell differentiation, transformation and proliferation. OSR1 and SPAK contain a conserved C-terminal (CCT) domain, which recognizes a unique motif ([RK]FX[VI]) present in their activating kinases (WNK1/WNK4) and their substrates. The OSR1 and SPAK 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: 270787 [Multi-domain]  Cd Length: 267  Bit Score: 60.45  E-value: 4.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF-CIPEHISPKA-----RCLIRS 151
Cdd:cd06610  168 GTPCWMAPEVMEQVRGYDFKA-DIWSFGITAIELATGAAPYSKYPPMKVLMLTLQNDPpSLETGADYKKysksfRKMISL 246
                         90       100
                 ....*....|....*....|.
gi 545477471 152 LLRREPSERLTAPEILLHPWF 172
Cdd:cd06610  247 CLQKDPSKRPTAEELLKHKFF 267
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
9-181 4.22e-11

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: 60.53  E-value: 4.22e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   9 KRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEerTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEIL 88
Cdd:cd06611   98 RGLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLD--GDVKLADFGVSAKNKSTLQKRDTFIGTPYWMAPEVV 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  89 NTTgTYSGKA----ADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ---FCIPEHISPKARCLIRSLLRREPSERL 161
Cdd:cd06611  176 ACE-TFKDNPydykADIWSLGITLIELAQMEPPHHELNPMRVLLKILKSEpptLDQPSKWSSSFNDFLKSCLVKDPDDRP 254
                        170       180
                 ....*....|....*....|
gi 545477471 162 TAPEILLHPWFESVLEPGYI 181
Cdd:cd06611  255 TAAELLKHPFVSDQSDNKAI 274
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
11-175 4.47e-11

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: 60.43  E-value: 4.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRL--ESLEDTHIMKGEDDALsdkhGCPAYVSPEIL 88
Cdd:cd06643  100 LTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADfgVSAKNTRTLQRRDSFI----GTPYWMAPEVV 175
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  89 NTTGT----YSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ---FCIPEHISPKARCLIRSLLRREPSERL 161
Cdd:cd06643  176 MCETSkdrpYDYKA-DVWSLGVTLIEMAQIEPPHHELNPMRVLLKIAKSEpptLAQPSRWSPEFKDFLRKCLEKNVDARW 254
                        170
                 ....*....|....
gi 545477471 162 TAPEILLHPWFESV 175
Cdd:cd06643  255 TTSQLLQHPFVSVL 268
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
10-204 4.66e-11

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta 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. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 61.18  E-value: 4.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEerTQLRLESLEDThiMKGEDDAL---SDKHGCPAYVSPE 86
Cdd:cd05624  169 KLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMN--GHIRLADFGSC--LKMNDDGTvqsSVAVGTPDYISPE 244
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  87 ILNTT----GTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI----RRGQFciPEHI---SPKARCLIRSLL-R 154
Cdd:cd05624  245 ILQAMedgmGKY-GPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnheERFQF--PSHVtdvSEEAKDLIQRLIcS 321
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471 155 REpsERLTA---PEILLHPWFESV-------LEPGYIdseigtsdqivPEYQEDSDISSF 204
Cdd:cd05624  322 RE--RRLGQngiEDFKKHAFFEGLnwenirnLEAPYI-----------PDVSSPSDTSNF 368
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
78-171 7.32e-11

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 7; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK7 is a dual-specificity PK that phosphorylates and activates its downstream target, c-Jun N-terminal kinase (JNK), on specific threonine and tyrosine residues. Although MKK7 is capable of dual phosphorylation, it prefers to phosphorylate the threonine residue of JNK. Thus, optimal activation of JNK requires both MKK4 and MKK7. MKK7 is primarily activated by cytokines. MKK7 is essential for liver formation during embryogenesis. It plays roles in G2/M cell cycle arrest and cell growth. In addition, it is involved in the control of programmed cell death, which is crucial in oncogenesis, cancer chemoresistance, and antagonism to TNFalpha-induced killing, through its inhibition by Gadd45beta and the subsequent suppression of the JNK cascade. The MKK7 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: 270791 [Multi-domain]  Cd Length: 295  Bit Score: 60.08  E-value: 7.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEIL--NTTGTYSGKAaDVWSLGVMLYTLLVGRYPFH--DSDPSALfSKIRRGQF-CIP--EHISPKARCLIR 150
Cdd:cd06618  176 GCAAYMAPERIdpPDNPKYDIRA-DVWSLGISLVELATGQFPYRncKTEFEVL-TKILNEEPpSLPpnEGFSPDFCSFVD 253
                         90       100
                 ....*....|....*....|.
gi 545477471 151 SLLRREPSERLTAPEILLHPW 171
Cdd:cd06618  254 LCLTKDHRYRPKYRELLQHPF 274
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
11-175 7.70e-11

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: 60.05  E-value: 7.70e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEerTQLRLE----SLEDTHIMKGEDDALsdkhGCPAYVSPE 86
Cdd:cd06644  107 LTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLD--GDIKLAdfgvSAKNVKTLQRRDSFI----GTPYWMAPE 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  87 IL---NTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ---FCIPEHISPKARCLIRSLLRREPSER 160
Cdd:cd06644  181 VVmceTMKDTPYDYKADIWSLGITLIEMAQIEPPHHELNPMRVLLKIAKSEpptLSQPSKWSMEFRDFLKTALDKHPETR 260
                        170
                 ....*....|....*
gi 545477471 161 LTAPEILLHPWFESV 175
Cdd:cd06644  261 PSAAQLLEHPFVSSV 275
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
20-172 7.84e-11

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 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: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 59.54  E-value: 7.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  20 FKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRL-----ESLEDTHIMKGeddalsDKHGCPAYVSPEILnTTGTY 94
Cdd:cd14019  107 LRNLFKALKHVHSFGIIHRDVKPGNFLYNRETGKGVLVdfglaQREEDRPEQRA------PRAGTRGFRAPEVL-FKCPH 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  95 SGKAADVWSLGVMLYTLLVGRYPF----HDSDPSALFSKIrRGqfcipehiSPKARCLIRSLLRREPSERLTAPEILLHP 170
Cdd:cd14019  180 QTTAIDIWSAGVILLSILSGRFPFffssDDIDALAEIATI-FG--------SDEAYDLLDKLLELDPSKRITAEEALKHP 250

                 ..
gi 545477471 171 WF 172
Cdd:cd14019  251 FF 252
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
78-172 8.68e-11

Catalytic domain of the Protein Serine/Threonine Kinase, 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. MEKK1 is a MAPK kinase kinase (MAPKKK or MKKK) that phosphorylates and activates activates the ERK1/2 and c-Jun N-terminal kinase (JNK) pathways by activating their respective MAPKKs, MEK1/2 and MKK4/MKK7, respectively. MEKK1 is important in regulating cell survival and apoptosis. MEKK1 also plays a role in cell migration, tissue maintenance and homeostasis, and wound healing. The 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: 270800 [Multi-domain]  Cd Length: 268  Bit Score: 59.75  E-value: 8.68e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPS---ALFSKIRRGQFC--IPEHISPKARCLIRSL 152
Cdd:cd06630  170 GTIAFMAPEVLR--GEQYGRSCDVWSVGCVIIEMATAKPPWNAEKISnhlALIFKIASATTPppIPEHLSPGLRDVTLRC 247
                         90       100
                 ....*....|....*....|
gi 545477471 153 LRREPSERLTAPEILLHPWF 172
Cdd:cd06630  248 LELQPEDRPPARELLKHPVF 267
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
7-177 1.06e-10

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin 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: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 59.49  E-value: 1.06e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKgEDDALSDKHGCPAYVSPE 86
Cdd:cd14104   90 ARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRGSYIKIIEFGQSRQLK-PGDKFRLQYTSAEFYAPE 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  87 ILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPE----HISPKARCLIRSLLRREPSERLT 162
Cdd:cd14104  169 VHQHESV--STATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEYAFDDeafkNISIEALDFVDRLLVKERKSRMT 246
                        170
                 ....*....|....*
gi 545477471 163 APEILLHPWFESVLE 177
Cdd:cd14104  247 AQEALNHPWLKQGME 261
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
11-172 1.17e-10

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 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: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 59.21  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDaLSDKHGCPAYVSPEILNT 90
Cdd:cd14192   99 LTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTGNQIKIIDFGLARRYKPREK-LKVNFGTPEFLAPEVVNY 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  91 TgtYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIP----EHISPKARCLIRSLLRREPSERLTAPEI 166
Cdd:cd14192  178 D--FVSFPTDMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKWDFDaeafENLSEEAKDFISRLLVKEKSCRMSATQC 255

                 ....*.
gi 545477471 167 LLHPWF 172
Cdd:cd14192  256 LKHEWL 261
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
11-175 1.24e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK1 (also called rhodopsin kinase) belongs to the visual group of GRKs and is expressed in retinal cells. It phosphorylates rhodopsin in rod cells, which leads to termination of the phototransduction cascade. Mutations in GRK1 are associated to a recessively inherited form of stationary nightblindness called Oguchi disease. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK1 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: 270759 [Multi-domain]  Cd Length: 288  Bit Score: 59.51  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEerTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILNt 90
Cdd:cd05608  102 FQEPRACFYTAQIISGLEHLHQRRIIYRDLKPENVLLDDD--GNVRISDLGLAVELKDGQTKTKGYAGTPGFMAPELLL- 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  91 tGTYSGKAADVWSLGVMLYTLLVGRYPF----HDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERL----- 161
Cdd:cd05608  179 -GEEYDYSVDYFTLGVTLYEMIAARGPFrargEKVENKELKQRILNDSVTYSEKFSPASKSICEALLAKDPEKRLgfrdg 257
                        170
                 ....*....|....
gi 545477471 162 TAPEILLHPWFESV 175
Cdd:cd05608  258 NCDGLRTHPFFRDI 271
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
10-170 1.86e-10

Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity kinase Myt1, the protein tyrosine kinase Wee1, and similar proteins. These proteins are cell cycle checkpoint kinases that are involved in the regulation of cyclin-dependent kinase CDK1, the master engine for mitosis. CDK1 is kept inactivated through phosphorylation of N-terminal thr (T14 by Myt1) and tyr (Y15 by Myt1 and Wee1) residues. Mitosis progression is ensured through activation of CDK1 by dephoshorylation and inactivation of Myt1/Wee1. The Wee1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270899 [Multi-domain]  Cd Length: 252  Bit Score: 58.55  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL-------RLESledthimkgeddALSDKHGCPAY 82
Cdd:cd13997   99 KLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIgdfglatRLET------------SGDVEEGDSRY 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNTTGTYSgKAADVWSLGVMLYTlLVGRYPFHDSDPSALfsKIRRGQFCIPEH--ISPKARCLIRSLLRREPSER 160
Cdd:cd13997  167 LAPELLNENYTHL-PKADIFSLGVTVYE-AATGEPLPRNGQQWQ--QLRQGKLPLPPGlvLSQELTRLLKVMLDPDPTRR 242
                        170
                 ....*....|
gi 545477471 161 LTAPEILLHP 170
Cdd:cd13997  243 PTADQLLAHD 252
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
2-175 1.93e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK4 has a limited tissue distribution. It is mainly found in the testis, but is also present in the cerebellum and kidney. It is expressed as multiple splice variants with different domain architectures and is post-translationally palmitoylated and localized in the membrane. GRK4 polymorphisms are associated with hypertension and salt sensitivity, as they cause hyperphosphorylation, desensitization, and internalization of the dopamine 1 (D1) receptor while increasing the expression of the angiotensin II type 1 receptor. GRK4 plays a crucial role in the D1 receptor regulation of sodium excretion and blood pressure. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK4 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: 173720 [Multi-domain]  Cd Length: 285  Bit Score: 58.85  E-value: 1.93e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   2 HSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLE-DTHIMKGEddALSDKHGCP 80
Cdd:cd05631   90 HIYNMGNPGFDEQRAIFYAAELCCGLEDLQRERIVYRDLKPENILL--DDRGHIRISDLGlAVQIPEGE--TVRGRVGTV 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVSPEIL-NTTGTYSgkaADVWSLGVMLYTLLVGRYPFHDSDPSA----LFSKIRRGQFCIPEHISPKARCLIRSLLRR 155
Cdd:cd05631  166 GYMAPEVInNEKYTFS---PDWWGLGCLIYEMIQGQSPFRKRKERVkreeVDRRVKEDQEEYSEKFSEDAKSICRMLLTK 242
                        170       180
                 ....*....|....*....|....*
gi 545477471 156 EPSERL-----TAPEILLHPWFESV 175
Cdd:cd05631  243 NPKERLgcrgnGAAGVKQHPIFKNI 267
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
7-181 7.00e-10

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK4 regulates cell morphology and cytoskeletal organization. It is essential for embryonic viability and proper neural development. Mice lacking PAK4 die due to defects in the fetal heart. In addition, their spinal cord motor neurons showed failure to differentiate and migrate. PAK4 also plays a role in cell survival and tumorigenesis. It is overexpressed in many primary tumors including colon, esophageal, and mammary tumors. PAK4 has also been implicated in viral and bacterial infection pathways. PAK4 belongs to the group II PAKs, which contain a PBD (p21-binding domain) and a C-terminal catalytic domain, but do not harbor an AID (autoinhibitory domain) or SH3 binding sites. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132988 [Multi-domain]  Cd Length: 292  Bit Score: 57.34  E-value: 7.00e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERtqLRLESLEDTHIMKGEDDALSDKHGCPAYVSPE 86
Cdd:cd06657  109 THTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGR--VKLSDFGFCAQVSKEVPRRKSLVGTPYWMAPE 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  87 ILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG---QFCIPEHISPKARCLIRSLLRREPSERLTA 163
Cdd:cd06657  187 LISRLPY--GPEVDIWSLGIMVIEMVDGEPPYFNEPPLKAMKMIRDNlppKLKNLHKVSPSLKGFLDRLLVRDPAQRATA 264
                        170
                 ....*....|....*...
gi 545477471 164 PEILLHPWFESVLEPGYI 181
Cdd:cd06657  265 AELLKHPFLAKAGPPSCI 282
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
78-175 7.25e-10

Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS1 functions as a tumor suppressor and is implicated in cell cycle regulation. Inactivation of LATS1 in mice results in the development of various tumors, including sarcomas and ovarian cancer. Promoter methylation, loss of heterozygosity, and missense mutations targeting the LATS1 gene have also been found in human sarcomas and ovarian cancers. In addition, decreased expression of LATS1 is associated with an aggressive phenotype and poor prognosis. LATS1 induces G2 arrest and promotes cytokinesis. It may be a component of the mitotic exit network in higher eukaryotes. The LATS1 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: 270775 [Multi-domain]  Cd Length: 382  Bit Score: 57.36  E-value: 7.25e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGtYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ--FCIPEH--ISPKARCLIRSLL 153
Cdd:cd05625  210 GTPNYIAPEVLLRTG-YT-QLCDWWSVGVILFEMLVGQPPFLAQTPLETQMKVINWQtsLHIPPQakLSPEASDLIIKLC 287
                         90       100
                 ....*....|....*....|....*
gi 545477471 154 rREPSERL---TAPEILLHPWFESV 175
Cdd:cd05625  288 -RGPEDRLgknGADEIKAHPFFKTI 311
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
11-169 8.33e-10

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. 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. The MAP3K8 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: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 56.56  E-value: 8.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERT----QLRLESLEDTHIMKgeddalsDKHGCPAYVSPE 86
Cdd:cd13995   93 MREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVFMSTKAVlvdfGLSVQMTEDVYVPK-------DLRGTEIYMSPE 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  87 ILNTTGtYSGKAaDVWSLGVMLYTLLVG------RYPfHDSDPSALFSKIRRGQFC--IPEHISPKARCLIRSLLRREPS 158
Cdd:cd13995  166 VILCRG-HNTKA-DIYSLGATIIHMQTGsppwvrRYP-RSAYPSYLYIIHKQAPPLedIAQDCSPAMRELLEAALERNPN 242
                        170
                 ....*....|.
gi 545477471 159 ERLTAPEILLH 169
Cdd:cd13995  243 HRSSAAELLKH 253
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
15-169 8.72e-10

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Protein Kinase regulated by RNA; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKR (or EIF2AK2) contains an N-terminal double-stranded RNA (dsRNA) binding domain and a C-terminal catalytic kinase domain. It is activated by dsRNA, which is produced as a replication intermediate in virally infected cells. It plays a key role in mediating innate immune responses to viral infection. PKR is also directly activated by PACT (protein activator of PKR) and heparin, and is inhibited by viral proteins and RNAs. PKR also regulates transcription and signal transduction in diseased cells, playing roles in tumorigenesis and neurodegenerative diseases. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The PKR 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: 270949 [Multi-domain]  Cd Length: 267  Bit Score: 56.73  E-value: 8.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  15 EAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLESLEDTHIMKGeDDALSDKHGCPAYVSPEILNTTgTY 94
Cdd:cd14047  118 LALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLV--DTGKVKIGDFGLVTSLKN-DGKRTKSKGTLSYMSPEQISSQ-DY 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  95 sGKAADVWSLGVMLYTLLvgrYPFHDS-DPSALFSKIRRG----QFCIPEHISPKarcLIRSLLRREPSERLTAPEILLH 169
Cdd:cd14047  194 -GKEVDIYALGLILFELL---HVCDSAfEKSKFWTDLRNGilpdIFDKRYKIEKT---IIKKMLSKKPEDRPNASEILRT 266
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
6-172 9.13e-10

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. This subfamily is composed of CDKL1-5 and similar proteins. Some CDKLs, like CDKL1 and CDKL3, may be implicated in transformation and others, like CDKL3 and CDKL5, are associated with mental retardation when impaired. CDKL2 plays a role in learning and memory. 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 CDKL 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: 270827 [Multi-domain]  Cd Length: 288  Bit Score: 56.94  E-value: 9.13e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   6 RSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGD-------------LKLRKFVFSTeertQLRlesledthimKGEDDA 72
Cdd:cd07833   92 ASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDikpenilvsesgvLKLCDFGFAR----ALT----------ARPASP 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  73 LSDKHGCPAYVSPEILNTTGTYsGKAADVWSLGVMLYTLLVGRYPF-HDSD---------------PS--ALFSK---IR 131
Cdd:cd07833  158 LTDYVATRWYRAPELLVGDTNY-GKPVDVWAIGCIMAELLDGEPLFpGDSDidqlyliqkclgplpPShqELFSSnprFA 236
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 545477471 132 RGQFCIPEHI-----------SPKARCLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd07833  237 GVAFPEPSQPeslerrypgkvSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
2-182 9.48e-10

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK5 is widely expressed in many tissues. It associates with the membrane though an N-terminal PIP2 binding domain and also binds phospholipids via its C-terminus. GRK5 deficiency is associated with early Alzheimer's disease in humans and mouse models. GRK5 also plays a crucial role in the pathogenesis of sporadic Parkinson's disease. It participates in the regulation and desensitization of PDGFRbeta, a receptor tyrosine kinase involved in a variety of downstream cellular effects including cell growth, chemotaxis, apoptosis, and angiogenesis. GRK5 also regulates Toll-like receptor 4, which is involved in innate and adaptive immunity. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK5 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: 270780 [Multi-domain]  Cd Length: 313  Bit Score: 56.90  E-value: 9.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   2 HSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLeDTHIMKGEDDALSDKHGCPA 81
Cdd:cd05632   92 HIYNMGNPGFEEERALFYAAEILCGLEDLHRENTVYRDLKPENILL--DDYGHIRISDL-GLAVKIPEGESIRGRVGTVG 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNTTgtYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPK----ARCLIRSLLRREP 157
Cdd:cd05632  169 YMAPEVLNNQ--RYTLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREEVDRRVLETEEVYSAKfseeAKSICKMLLTKDP 246
                        170       180       190
                 ....*....|....*....|....*....|....
gi 545477471 158 SERL-----TAPEILLHPWFESV----LEPGYID 182
Cdd:cd05632  247 KQRLgcqeeGAGEVKRHPFFRNMnfkrLEAGMLD 280
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
13-171 9.69e-10

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: 56.77  E-value: 9.69e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLF-KQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLR----LESLEDTHIMKGEDDALSDKHGCPAYVSPEI 87
Cdd:cd06628  104 EESLVRNFvRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISdfgiSKKLEANSLSTKNNGARPSLQGSVFWMAPEV 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  88 LNTTgTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDP-SALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLTAPEI 166
Cdd:cd06628  184 VKQT-SYTRKA-DIWSLGCLVVEMLTGTHPFPDCTQmQAIFKIGENASPTIPSNISSEARDFLEKTFEIDHNKRPTADEL 261

                 ....*
gi 545477471 167 LLHPW 171
Cdd:cd06628  262 LKHPF 266
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
1-171 1.13e-09

Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SBK1, also called BSK146, is predominantly expressed in the brain. Its expression is increased in the developing brain during the late embryonic stage, coinciding with dramatic neuronal proliferation, migration, and maturation. SBK1 may play an important role in regulating brain development. The SBK1 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: 270889 [Multi-domain]  Cd Length: 259  Bit Score: 56.18  E-value: 1.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLEsledthimkgeDDALSDKHGCP 80
Cdd:cd13987   78 LFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDCRRVKLC-----------DFGLTRRVGST 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 A--------YVSPEILNTT---GTYSGKAADVWSLGVMLYTLLVGRYPF----HDSDPSALFSKIRRGQFCIP----EHI 141
Cdd:cd13987  147 VkrvsgtipYTAPEVCEAKkneGFVVDPSIDVWAFGVLLFCCLTGNFPWekadSDDQFYEEFVRWQKRKNTAVpsqwRRF 226
                        170       180       190
                 ....*....|....*....|....*....|...
gi 545477471 142 SPKARCLIRSLLRREPSERLTAPEI---LLHPW 171
Cdd:cd13987  227 TPKALRMFKKLLAPEPERRCSIKEVfkyLGDRW 259
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
3-171 1.47e-09

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein 89; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The nematode Unc-89 gene, through alternative promoter use and splicing, encodes at least six major isoforms (Unc-89A to Unc-89F) of giant muscle proteins that are homologs for the vetebrate obscurin. In flies, five isoforms of Unc-89 have been detected: four in the muscles of adult flies (two in the indirect flight muscle and two in other muscles) and another isoform in the larva. Unc-89 in nematodes is required for normal muscle cell architecture. In flies, it is necessary for the development of a symmetrical sarcomere in the flight muscles. Unc-89 proteins contain several adhesion and signaling domains including multiple copies of the immunoglobulin (Ig) domain, as well as fibronectin type III (FN3), SH3, RhoGEF, and PH domains. The nematode Unc-89 isoforms D, C, D, and F contain two kinase domain with B and F having two complete kinase domains while the first repeat of C and D are partial domains. Homology modeling suggests that the first kinase repeat of Unc-89 may be catalytically inactive, a pseudokinase, while the second kinase repeat may be active. The Unc-89 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: 271014 [Multi-domain]  Cd Length: 259  Bit Score: 56.00  E-value: 1.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGEDDALSDkhGCPAY 82
Cdd:cd14112   88 TRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQVKLVDFGRAQKVSKLGKVPVD--GDTDW 165
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNTTgTYSGKAADVWSLGVMLYTLLVGRYPFH-----DSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREP 157
Cdd:cd14112  166 ASPEFHNPE-TPITVQSDIWGLGVLTFCLLSGFHPFTseyddEEETKENVIFVKCRPNLIFVEATQEALRFATWALKKSP 244
                        170
                 ....*....|....
gi 545477471 158 SERLTAPEILLHPW 171
Cdd:cd14112  245 TRRMRTDEALEHRW 258
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
1-175 1.53e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK3, also called beta-adrenergic receptor kinase 2 (beta-ARK2), is widely expressed in many tissues. It is involved in modulating the cholinergic response of airway smooth muscles, and also plays a role in dopamine receptor regulation. GRK3-deficient mice show a lack of olfactory receptor desensitization and altered regulation of the M2 muscarinic airway. GRK3 promoter polymorphisms may also be associated with bipolar disorder. GRK3 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK3 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: 270781 [Multi-domain]  Cd Length: 346  Bit Score: 56.61  E-value: 1.53e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLE-DTHIMKGEDDALSDKHGc 79
Cdd:cd05633   95 LHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILL--DEHGHVRISDLGlACDFSKKKPHASVGTHG- 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  80 paYVSPEILNTtGTYSGKAADVWSLGVMLYTLLVGRYPF--------HDSDPSALFSKIRrgqfcIPEHISPKARCLIRS 151
Cdd:cd05633  172 --YMAPEVLQK-GTAYDSSADWFSLGCMLFKLLRGHSPFrqhktkdkHEIDRMTLTVNVE-----LPDSFSPELKSLLEG 243
                        170       180
                 ....*....|....*....|....*....
gi 545477471 152 LLRREPSERL-----TAPEILLHPWFESV 175
Cdd:cd05633  244 LLQRDVSKRLgchgrGAQEVKEHSFFKGI 272
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
10-171 2.06e-09

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


Pssm-ID: 270786 [Multi-domain]  Cd Length: 274  Bit Score: 55.71  E-value: 2.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQ---------SAIVL----GDLKLRKFVFSTE-ERTQLRLesleDTHImkgeddalsd 75
Cdd:cd06609   94 PLDETYIAFILREVLLGLEYLHSegkihrdikAANILlseeGDVKLADFGVSGQlTSTMSKR----NTFV---------- 159
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  76 khGCPAYVSPEILNTTGtYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPsalfskiRRGQFCIPEH---------ISPKAR 146
Cdd:cd06609  160 --GTPFWMAPEVIKQSG-YDEKA-DIWSLGITAIELAKGEPPLSDLHP-------MRVLFLIPKNnppslegnkFSKPFK 228
                        170       180
                 ....*....|....*....|....*
gi 545477471 147 CLIRSLLRREPSERLTAPEILLHPW 171
Cdd:cd06609  229 DFVELCLNKDPKERPSAKELLKHKF 253
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
10-167 2.17e-09

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. No function has yet been ascribed to Nek10. The gene encoding Nek10 is a putative causative gene for breast cancer; it is located within a breast cancer susceptibility loci on chromosome 3p24. Nek10 is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270867 [Multi-domain]  Cd Length: 270  Bit Score: 55.59  E-value: 2.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCH-QSAIVLGDLKLRKFVFSTEERTQLRLESLEDthiMKGEDDA-LSDKHGCPAYVSPEI 87
Cdd:cd08528  109 HFTEDRIWNIFVQMVLALRYLHkEKQIVHRDLKPNNIMLGEDDKVTITDFGLAK---QKGPESSkMTSVVGTILYSCPEI 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  88 LNTTgTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF-CIPEHI-SPKARCLIRSLLRREPSERltaPE 165
Cdd:cd08528  186 VQNE-PY-GEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYePLPEGMySDDITFVIRSCLTPDPEAR---PD 260

                 ..
gi 545477471 166 IL 167
Cdd:cd08528  261 IV 262
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
22-170 2.40e-09

Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or General Control Non-derepressible-2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the overall downregulation of protein synthesis. eIF-2 phosphorylation is induced in response to cellular stresses including virus infection, heat shock, nutrient deficiency, and the accummulation of unfolded proteins, among others. There are four distinct kinases that phosphorylate eIF-2 and control protein synthesis under different stress conditions: GCN2, protein kinase regulated by RNA (PKR), heme-regulated inhibitor kinase (HRI), and PKR-like endoplasmic reticulum kinase (PERK). GCN2 is activated by amino acid or serum starvation and UV irradiation. It induces GCN4, a transcriptional activator of amino acid biosynthetic genes, leading to increased production of amino acids under amino acid-deficient conditions. In serum-starved cells, GCN2 activation induces translation of the stress-responsive transcription factor ATF4, while under UV stress, GCN2 triggers transcriptional rescue via NF-kappaB signaling. GCN2 contains an N-terminal RWD, a degenerate kinase-like (repeat 1), the catalytic kinase (repeat 2), a histidyl-tRNA synthetase (HisRS)-like, and a C-terminal ribosome-binding and dimerization (RB/DD) domains. The degenerate pseudokinase domain of GCN2 may function as a regulatory domain. The GCN2 subfamily is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270914 [Multi-domain]  Cd Length: 254  Bit Score: 55.44  E-value: 2.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  22 QIVSAVAHCHQSAIVLGDLKL-RKFVFSTEERTQLRLEsleDTHIMKGEDDALS----DKHGCPAYVSPEILNTTGTYsG 96
Cdd:cd14012  112 QLLEALEYLHRNGVVHKSLHAgNVLLDRDAGTGIVKLT---DYSLGKTLLDMCSrgslDEFKQTYWLPPELAQGSKSP-T 187
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545477471  97 KAADVWSLGVMLYTLLVGRYPFHDSDPSALFSkirrgqfcIPEHISPKARCLIRSLLRREPSERLTAPEILLHP 170
Cdd:cd14012  188 RKTDVWDLGLLFLQMLFGLDVLEKYTSPNPVL--------VSLDLSASLQDFLSKCLSLDPKKRPTALELLPHE 253
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
4-172 2.52e-09

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 55.25  E-value: 2.52e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFsTEERTQLR-----LESLEDThimKGEDDALSDkhg 78
Cdd:PHA03390  99 LLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLY-DRAKDRIYlcdygLCKIIGT---PSCYDGTLD--- 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 cpaYVSPE-ILNTTGTYSgkaADVWSLGVMLYTLLVGRYPFHDS-----DPSALFSKIRRgQFCIPEHISPKARCLIRSL 152
Cdd:PHA03390 172 ---YFSPEkIKGHNYDVS---FDWWAVGVLTYELLTGKHPFKEDedeelDLESLLKRQQK-KLPFIKNVSKNANDFVQSM 244
                        170       180
                 ....*....|....*....|.
gi 545477471 153 LRREPSERLTA-PEILLHPWF 172
Cdd:PHA03390 245 LKYNINYRLTNyNEIIKHPFL 265
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
11-173 2.80e-09

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK2 plays a role in pro-apoptotic signaling. It is cleaved and activated by caspases leading to morphological changes during apoptosis. PAK2 is also activated in response to a variety of stresses including DNA damage, hyperosmolarity, serum starvation, and contact inhibition, and may play a role in coordinating the stress response. PAK2 also contributes to cancer cell invasion through a mechanism distinct from that of PAK1. It belongs to the group I PAKs, which 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). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132986 [Multi-domain]  Cd Length: 296  Bit Score: 55.50  E-value: 2.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEerTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILnT 90
Cdd:cd06655  112 MDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMD--GSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVV-T 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  91 TGTYsGKAADVWSLGVMLYTLLVGRYPFHDSDP-SALFSKIRRG--QFCIPEHISPKARCLIRSLLRREPSERLTAPEIL 167
Cdd:cd06655  189 RKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGtpELQNPEKLSPIFRDFLNRCLEMDVEKRGSAKELL 267

                 ....*.
gi 545477471 168 LHPWFE 173
Cdd:cd06655  268 QHPFLK 273
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
82-172 3.68e-09

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: 55.18  E-value: 3.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNTTGTYSgKAADVWSLGVMLYTLLVGRYPFH-DSDPSALF-----------------SKIRRGQFCIPEH--- 140
Cdd:cd07829  164 YRAPEILLGSKHYS-TAVDIWSVGCIFAELITGKPLFPgDSEIDQLFkifqilgtpteeswpgvTKLPDYKPTFPKWpkn 242
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 545477471 141 --------ISPKARCLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd07829  243 dlekvlprLDPEGIDLLSKMLQYNPAKRISAKEALKHPYF 282
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
82-170 4.12e-09

Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily are mitogen-activated protein kinase (MAPK) kinase kinases (MAPKKKs or MKKKs) and include ASK1, ASK2, and MAPKKK15. ASK1 (also called MAPKKK5) functions in the c-Jun N-terminal kinase (JNK) and p38 MAPK signaling pathways by directly activating their respective MAPKKs, MKK4/MKK7 and MKK3/MKK6. It plays important roles in cytokine and stress responses, as well as in reactive oxygen species-mediated cellular responses. ASK1 is implicated in various diseases mediated by oxidative stress including inschemic heart disease, hypertension, vessel injury, brain ischemia, Fanconi anemia, asthma, and pulmonary edema, among others. ASK2 (also called MAPKKK6) functions only in a heteromeric complex with ASK1, and can activate ASK1 by direct phosphorylation. The function of MAPKKK15 is still unknown. The ASK 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: 270794 [Multi-domain]  Cd Length: 268  Bit Score: 54.72  E-value: 4.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFHD-SDPSALFSKIrrGQFC----IPEHISPKARCLIRSLLRRE 156
Cdd:cd06624  175 YMAPEVIDKGQRGYGPPADIWSLGCTIIEMATGKPPFIElGEPQAAMFKV--GMFKihpeIPESLSEEAKSFILRCFEPD 252
                         90
                 ....*....|....
gi 545477471 157 PSERLTAPEILLHP 170
Cdd:cd06624  253 PDKRATASDLLQDP 266
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
7-172 4.51e-09

Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like protein kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. This subfamily is composed of the dual-specificity DYRKs and YAK1, as well as the S/T kinases (STKs), HIPKs. DYRKs and YAK1 autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. Proteins in this subfamily play important roles in cell proliferation, differentiation, survival, growth, and development. The DYRK-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: 271035 [Multi-domain]  Cd Length: 262  Bit Score: 54.58  E-value: 4.51e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLReeeaaRLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRL----ESLEDThimkgedDALSDKHGCPAY 82
Cdd:cd14133  100 SLPRIR-----KIAQQILEALVFLHSLGLIHCDLKPENILLASYSRCQIKIidfgSSCFLT-------QRLYSYIQSRYY 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILntTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISPKARC-------LIRSLLRR 155
Cdd:cd14133  168 RAPEVI--LGLPYDEKIDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMLDQGKAddelfvdFLKKLLEI 245
                        170
                 ....*....|....*..
gi 545477471 156 EPSERLTAPEILLHPWF 172
Cdd:cd14133  246 DPKERPTASQALSHPWL 262
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
11-171 5.85e-09

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: 54.26  E-value: 5.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLK----LRKFV-------FSTEERTQlrlesledTHIMKGEddALSDKHGC 79
Cdd:cd06653  103 LTENVTRRYTRQILQGVSYLHSNMIVHRDIKganiLRDSAgnvklgdFGASKRIQ--------TICMSGT--GIKSVTGT 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  80 PAYVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFCIPEHISPKARCLIRSLLRREp 157
Cdd:cd06653  173 PYWMSPEVISGEGY--GRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIatQPTKPQLPDGVSDACRDFLRQIFVEE- 249
                        170
                 ....*....|....
gi 545477471 158 SERLTAPEILLHPW 171
Cdd:cd06653  250 KRRPTAEFLLRHPF 263
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
10-204 6.46e-09

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha 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. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 54.64  E-value: 6.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLR-----LESLEDTHIMKgeddalSDKHGCPAYVS 84
Cdd:cd05623  169 RLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLAdfgscLKLMEDGTVQS------SVAVGTPDYIS 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTT----GTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFCIPEH---ISPKARCLIRSLL-R 154
Cdd:cd05623  243 PEILQAMedgkGKY-GPECDWWSLGVCMYEMLYGETPFYAESLVETYGKImnHKERFQFPTQvtdVSENAKDLIRRLIcS 321
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 545477471 155 REpsERLTAPEI---LLHPWFESVlepgYIDSEIGTSDQIVPEYQEDSDISSF 204
Cdd:cd05623  322 RE--HRLGQNGIedfKNHPFFVGI----DWDNIRNCEAPYIPEVSSPTDTSNF 368
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
11-191 6.83e-09

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK 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: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 54.34  E-value: 6.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQlrlesLEDTHIMKGEDDALSDKH---GCPAYVSPEI 87
Cdd:cd06637  108 LKEEWIAYICREILRGLSHLHQHKVIHRDIKGQNVLLTENAEVK-----LVDFGVSAQLDRTVGRRNtfiGTPYWMAPEV 182
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  88 L----NTTGTYSGKaADVWSLGVMLYTLLVGRYPFHDSDPsalfskiRRGQFCIPEHISP---------KARCLIRSLLR 154
Cdd:cd06637  183 IacdeNPDATYDFK-SDLWSLGITAIEMAEGAPPLCDMHP-------MRALFLIPRNPAPrlkskkwskKFQSFIESCLV 254
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 545477471 155 REPSERLTAPEILLHPWFESvlEPGYIDSEIGTSDQI 191
Cdd:cd06637  255 KNHSQRPSTEQLMKHPFIRD--QPNERQVRIQLKDHI 289
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
11-171 7.63e-09

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: 54.02  E-value: 7.63e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL----RLESLEDTHIMKgeddalSDKHGCPAYVSPE 86
Cdd:cd06917   98 IAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLcdfgVAASLNQNSSKR------STFVGTPYWMAPE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  87 ILNTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSalfskirRGQFCIP---------EHISPKARCLIRSLLRREP 157
Cdd:cd06917  172 VITEGKYYDTKA-DIWSLGITTYEMATGNPPYSDVDAL-------RAVMLIPkskpprlegNGYSPLLKEFVAACLDEEP 243
                        170
                 ....*....|....
gi 545477471 158 SERLTAPEILLHPW 171
Cdd:cd06917  244 KDRLSADELLKSKW 257
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
1-175 8.54e-09

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 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: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 54.28  E-value: 8.54e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLE-DTHIMKGEDDALSDKHGc 79
Cdd:cd14223   90 LHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILL--DEFGHVRISDLGlACDFSKKKPHASVGTHG- 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  80 paYVSPEILNTTGTYSgKAADVWSLGVMLYTLLVGRYPF--------HDSDPSALFSKIRrgqfcIPEHISPKARCLIRS 151
Cdd:cd14223  167 --YMAPEVLQKGVAYD-SSADWFSLGCMLFKLLRGHSPFrqhktkdkHEIDRMTLTMAVE-----LPDSFSPELRSLLEG 238
                        170       180
                 ....*....|....*....|....*....
gi 545477471 152 LLRREPSERL-----TAPEILLHPWFESV 175
Cdd:cd14223  239 LLQRDVNRRLgcmgrGAQEVKEEPFFRGL 267
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
4-171 9.10e-09

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: 53.86  E-value: 9.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHC--HQSAIVLGDLKLRKFVF-STEERTQLRLESLEDTHIMKGEDDAL------S 74
Cdd:cd13990   95 YLKQHKSIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLhSGNVSGEIKITDFGLSKIMDDESYNSdgmeltS 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  75 DKHGCPAYVSPEILNTTGTY---SGKAaDVWSLGVMLYTLLVGRYPF-HDSDPSA-LFSKI----RRGQFCIPEHISPKA 145
Cdd:cd13990  175 QGAGTYWYLPPECFVVGKTPpkiSSKV-DVWSVGVIFYQMLYGRKPFgHNQSQEAiLEENTilkaTEVEFPSKPVVSSEA 253
                        170       180
                 ....*....|....*....|....*.
gi 545477471 146 RCLIRSLLRREPSERLTAPEILLHPW 171
Cdd:cd13990  254 KDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
11-171 1.13e-08

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MEKK3 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. MEKK3 plays an essential role in embryonic angiogenesis and early heart development. In addition, MEKK3 is involved in interleukin-1 receptor and Toll-like receptor 4 signaling. It is also a specific regulator of the proinflammatory cytokines IL-6 and GM-CSF in some immune cells. MEKK3 also regulates calcineurin, which plays a critical role in T cell activation, apoptosis, skeletal myocyte differentiation, and cardiac hypertrophy. The MEKK3 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: 270817 [Multi-domain]  Cd Length: 271  Bit Score: 53.55  E-value: 1.13e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL-------RLESLedthIMKGEddALSDKHGCPAYV 83
Cdd:cd06651  108 LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLgdfgaskRLQTI----CMSGT--GIRSVTGTPYWM 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFCIPEHISPKARCLIRSLLrREPSERL 161
Cdd:cd06651  182 SPEVISGEGY--GRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIatQPTNPQLPSHISEHARDFLGCIF-VEARHRP 258
                        170
                 ....*....|
gi 545477471 162 TAPEILLHPW 171
Cdd:cd06651  259 SAEELLRHPF 268
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
1-163 1.33e-08

Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PINK1 contains an N-terminal mitochondrial targeting sequence, a catalytic domain, and a C-terminal regulatory region. It plays an important role in maintaining mitochondrial homeostasis. It protects cells against oxidative stress-induced apoptosis by phosphorylating the chaperone TNFR-associated protein 1 (TRAP1), also called Hsp75. Phosphorylated TRAP1 prevents cytochrome c release and peroxide-induced apoptosis. PINK1 interacts with Omi/HtrA2, a serine protease, and Parkin, an E3 ubiquitin ligase, in different pathways to promote mitochondrial health. The parkin gene is the most commonly mutated gene in autosomal recessive familial parkinsonism. Mutations within the catalytic domain of PINK1 are also associated with Parkinson's disease. The PINK1 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: 270920 [Multi-domain]  Cd Length: 313  Bit Score: 53.65  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEeAARLFKQIVSAVAHCHQSAIVLGDLKLRKFV--FSTEERTQLRLESL-----EDTHIMK---GED 70
Cdd:cd14018  126 LRQYLWVNTPSYRL-ARVMILQLLEGVDHLVRHGIAHRDLKSDNILleLDFDGCPWLVIADFgcclaDDSIGLQlpfSSW 204
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  71 DAlsDKHGCPAYVSPEILNTTG------TYSgkAADVWSLGVMLYTLLVGRYPFHD-SDPSALFSKIRRGQF-CIPEHIS 142
Cdd:cd14018  205 YV--DRGGNACLMAPEVSTAVPgpgvviNYS--KADAWAVGAIAYEIFGLSNPFYGlGDTMLESRSYQESQLpALPSAVP 280
                        170       180
                 ....*....|....*....|.
gi 545477471 143 PKARCLIRSLLRREPSERLTA 163
Cdd:cd14018  281 PDVRQVVKDLLQRDPNKRVSA 301
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
1-134 1.45e-08

Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR is a scaffold protein that functions downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases, but there is some debate in this designation as a few groups have reported detecting kinase catalytic activity for KSRs, specifically KSR1. Vertebrates contain two KSR proteins, KSR1 and KSR2. The KSR subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270965 [Multi-domain]  Cd Length: 271  Bit Score: 53.12  E-value: 1.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRK-RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKlRKFVFSTEER---TQLRLESLEDTHIMKGEDDALSDK 76
Cdd:cd14063   83 LYSLIHERKeKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLK-SKNIFLENGRvviTDFGLFSLSGLLQPGRREDTLVIP 161
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545477471  77 HGCPAYVSPEILN--TTGTYSG------KAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ 134
Cdd:cd14063  162 NGWLCYLAPEIIRalSPDLDFEeslpftKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGK 227
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
78-173 1.65e-08

Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase Kinases 3 and 6; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK3 and MKK6 are dual-specificity PKs that phosphorylate and activate their downstream target, p38 MAPK, on specific threonine and tyrosine residues. MKK3/6 play roles in the regulation of cell cycle progression, cytokine- and stress-induced apoptosis, oncogenic transformation, and adult tissue regeneration. In addition, MKK6 plays a critical role in osteoclast survival in inflammatory disease while MKK3 is associated with tumor invasion, progression, and poor patient survival in glioma. The MKK3/6 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: 173729 [Multi-domain]  Cd Length: 283  Bit Score: 53.20  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGTYSGK--AADVWSLGVMLYTLLVGRYPF--------------HDSDPSalfskirrgqfcIP-EH 140
Cdd:cd06617  165 GCKPYMAPERINPELNQKGYdvKSDVWSLGITMIELATGRFPYdswktpfqqlkqvvEEPSPQ------------LPaEK 232
                         90       100       110
                 ....*....|....*....|....*....|...
gi 545477471 141 ISPKARCLIRSLLRREPSERLTAPEILLHPWFE 173
Cdd:cd06617  233 FSPEFQDFVNKCLKKNYKERPNYPELLQHPFFE 265
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
6-168 2.22e-08

Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mos (or c-Mos) is a germ-cell specific kinase that plays roles in both the release of primary arrest and the induction of secondary arrest in oocytes. It is expressed towards the end of meiosis I and is quickly degraded upon fertilization. It is a component of the cytostatic factor (CSF), which is responsible for metaphase II arrest. In addition, Mos activates a phoshorylation cascade that leads to the activation of the p34 subunit of MPF (mitosis-promoting factor or maturation promoting factor), a cyclin-dependent kinase that is responsible for the release of primary arrest in meiosis I. The Mos 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: 270881 [Multi-domain]  Cd Length: 265  Bit Score: 52.77  E-value: 2.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   6 RSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQL-------RLESLEDThimkgeDDALSDKHG 78
Cdd:cd13979   95 EGSEPLPLAHRILISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLcdfgcsvKLGEGNEV------GTPRSHIGG 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISP-----KARCLIRSLL 153
Cdd:cd13979  169 TYTYRAPELLK--GERVTPKADIYSFGITLWQMLTRELPYAGLRQHVLYAVVAKDLRPDLSGLEDsefgqRLRSLISRCW 246
                        170
                 ....*....|....*
gi 545477471 154 RREPSERLTAPEILL 168
Cdd:cd13979  247 SAQPAERPNADESLL 261
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
78-175 3.38e-08

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 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: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 52.37  E-value: 3.38e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIR--RGQFCIPEH--ISPKARCLIrslL 153
Cdd:cd05627  199 GTPDYIAPEVFMQTGY--NKLCDWWSLGVIMYEMLIGYPPFCSETPQETYRKVMnwKETLVFPPEvpISEKAKDLI---L 273
                         90       100
                 ....*....|....*....|....*..
gi 545477471 154 R--REPSERL---TAPEILLHPWFESV 175
Cdd:cd05627  274 RfcTDAENRIgsnGVEEIKSHPFFEGV 300
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
22-182 4.27e-08

Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK7 (also called iodopsin kinase) belongs to the visual group of GRKs. It is primarily found in the retina and plays a role in the regulation of opsin light receptors. GRK7 is located in retinal cone outer segments and plays an important role in regulating photoresponse of the cones. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors, which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. The GRK7 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: 270758 [Multi-domain]  Cd Length: 286  Bit Score: 51.83  E-value: 4.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  22 QIVSAVAHCHQSAIVLGDLKLRKFVFstEERTQLRLESLEDTHIMKgEDDALSDKHGCPAYVSPEILnTTGTYSgKAADV 101
Cdd:cd05607  112 QITCGILHLHSLKIVYRDMKPENVLL--DDNGNCRLSDLGLAVEVK-EGKPITQRAGTNGYMAPEIL-KEESYS-YPVDW 186
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471 102 WSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF---CIPEH--ISPKARCLIRSLLRREPSERLTAPEIL----LHPWF 172
Cdd:cd05607  187 FAMGCSIYEMVAGRTPFRDHKEKVSKEELKRRTLedeVKFEHqnFTEEAKDICRLFLAKKPENRLGSRTNDddprKHEFF 266
                        170
                 ....*....|....
gi 545477471 173 ESV----LEPGYID 182
Cdd:cd05607  267 KSInfprLEAGLID 280
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
7-173 6.48e-08

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: 51.06  E-value: 6.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   7 SRKRLREEEAARLFKQIVSAVAHCHQ---------SAIVL----GDLKLRKFVFSTeertQLRLESLEDTHIMkgeddal 73
Cdd:cd06614   90 NPVRMNESQIAYVCREVLQGLEYLHSqnvihrdikSDNILlskdGSVKLADFGFAA----QLTKEKSKRNSVV------- 158
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  74 sdkhGCPAYVSPEILntTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDP-SALFSKIRRG--QFCIPEHISPKARCLIR 150
Cdd:cd06614  159 ----GTPYWMAPEVI--KRKDYGPKVDIWSLGIMCIEMAEGEPPYLEEPPlRALFLITTKGipPLKNPEKWSPEFKDFLN 232
                        170       180
                 ....*....|....*....|...
gi 545477471 151 SLLRREPSERLTAPEILLHPWFE 173
Cdd:cd06614  233 KCLVKDPEKRPSAEELLQHPFLK 255
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
9-178 7.28e-08

Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase (also called MAPK12); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38gamma/MAPK12 is predominantly expressed in skeletal muscle. Unlike p38alpha and p38beta, p38gamma is insensitive to pyridinylimidazoles. It displays an antagonizing function compared to p38alpha. p38gamma inhibits, while p38alpha stimulates, c-Jun phosphorylation and AP-1 mediated transcription. p38gamma also plays a role in the signaling between Ras and the estrogen receptor and has been implicated to increase cell invasion and breast cancer progression. In Xenopus, p38gamma is critical in the meiotic maturation of oocytes. p38 kinases are MAPKs, serving as important mediators of cellular responses to extracellular signals. They are activated by the MAPK kinases MKK3 and MKK6, which in turn are activated by upstream MAPK kinase kinases including TAK1, ASK1, and MLK3, in response to cellular stresses or inflammatory cytokines. The p38gamma 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: 143385 [Multi-domain]  Cd Length: 343  Bit Score: 51.49  E-value: 7.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   9 KRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFvfSTEERTQLRLEsleDTHIMKGEDDALSDKHGCPAYVSPEIL 88
Cdd:cd07880  113 EKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNL--AVNEDCELKIL---DFGLARQTDSEMTGYVVTRWYRAPEVI 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  89 NTTGTYSgKAADVWSLGVMLYTLLVGRYPFHDSD--------------PSALFS----------------KIRRGQF-CI 137
Cdd:cd07880  188 LNWMHYT-QTVDIWSVGCIMAEMLTGKPLFKGHDhldqlmeimkvtgtPSKEFVqklqsedaknyvkklpRFRKKDFrSL 266
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 545477471 138 PEHISPKARCLIRSLLRREPSERLTAPEILLHPWFESVLEP 178
Cdd:cd07880  267 LPNANPLAVNVLEKMLVLDAESRITAAEALAHPYFEEFHDP 307
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
10-169 1.31e-07

Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK16 is associated with many names including Myristylated and Palmitylated Serine/threonine Kinase 1 (MPSK1), Kinase related to cerevisiae and thaliana (Krct), and Protein Kinase expressed in day 12 fetal liver (PKL12). It is widely expressed in mammals with highest levels found in liver, testis, and kidney. It is localized in the Golgi but is translocated to the nucleus upon disorganization of the Golgi. STK16 is constitutively active and is capable of phosphorylating itself and other substrates. It may be involved in regulating stromal-epithelial interactions during mammary gland ductal morphogenesis. It may also function as a transcriptional co-activator of type-C natriuretic peptide and VEGF. The STK16 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: 270888 [Multi-domain]  Cd Length: 282  Bit Score: 50.37  E-value: 1.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIV---LGDLKLRKFVFSTEER---------TQLRLEsLEDTHIMKGEDDALSDkH 77
Cdd:cd13986  102 FFPEDRILHIFLGICRGLKAMHEPELVpyaHRDIKPGNVLLSEDDEpilmdlgsmNPARIE-IEGRREALALQDWAAE-H 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNT-TGTYSGKAADVWSLGVMLYTLLVGRYPF----HDSDPSALfsKIRRGQFCIPEH--ISPKARCLIR 150
Cdd:cd13986  180 CTMPYRAPELFDVkSHCTIDEKTDIWSLGCTLYALMYGESPFerifQKGDSLAL--AVLSGNYSFPDNsrYSEELHQLVK 257
                        170
                 ....*....|....*....
gi 545477471 151 SLLRREPSERLTAPEILLH 169
Cdd:cd13986  258 SMLVVNPAERPSIDDLLSR 276
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
11-171 1.40e-07

N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinase Kinase 4 and 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. MAP4K4 is also called Nck Interacting kinase (NIK). It facilitates the activation of the MAPKs, extracellular signal-regulated kinase (ERK) 1, ERK2, and c-Jun N-terminal kinase (JNK), by phosphorylating and activating MEKK1. MAP4K4 plays a role in tumor necrosis factor (TNF) alpha-induced insulin resistance. MAP4K4 silencing in skeletal muscle cells from type II diabetic patients restores insulin-mediated glucose uptake. MAP4K4, through JNK, also plays a broad role in cell motility, which impacts inflammation, homeostasis, as well as the invasion and spread of cancer. MAP4K4 is found to be highly expressed in most tumor cell lines relative to normal tissue. MAP4K6 (also called MINK for Misshapen/NIKs-related kinase) is activated after Ras induction and mediates activation of p38 MAPK. MAP4K6 plays a role in cell cycle arrest, cytoskeleton organization, cell adhesion, and cell motility. The MAP4K4/6 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: 270806 [Multi-domain]  Cd Length: 282  Bit Score: 50.39  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLEsleDTHIMKGEDDALSDKH---GCPAYVSPEI 87
Cdd:cd06636  118 LKEDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLT--ENAEVKLV---DFGVSAQLDRTVGRRNtfiGTPYWMAPEV 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  88 L----NTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPsalfskiRRGQFCIPEHISPKAR--------------CLI 149
Cdd:cd06636  193 IacdeNPDATYDYRS-DIWSLGITAIEMAEGAPPLCDMHP-------MRALFLIPRNPPPKLKskkwskkfidfiegCLV 264
                        170       180
                 ....*....|....*....|..
gi 545477471 150 RSLLRREPSERLtapeiLLHPW 171
Cdd:cd06636  265 KNYLSRPSTEQL-----LKHPF 281
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
1-172 1.69e-07

Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MOK, also called Renal tumor antigen 1 (RAGE-1), is widely expressed and is enriched in testis, kidney, lung, and brain. It is expressed in approximately 50% of renal cell carcinomas (RCC) and is a potential target for immunotherapy. MOK is stabilized by its association with the HSP90 molecular chaperone. It is induced by the transcription factor Cdx2 and may be involved in regulating intestinal epithelial development and differentiation. The MOK 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: 270825 [Multi-domain]  Cd Length: 282  Bit Score: 50.35  E-value: 1.69e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKR-LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEErtqLRLESLedthimkGEDDALSDKHGC 79
Cdd:cd07831   86 LYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDDI---LKLADF-------GSCRGIYSKPPY 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  80 PAYVS------PEILNTTGTYSGKAaDVWSLGVMLYTLLVGRYPF------------HD---SDPSALFSKIRRG----- 133
Cdd:cd07831  156 TEYIStrwyraPECLLTDGYYGPKM-DIWAVGCVFFEILSLFPLFpgtneldqiakiHDvlgTPDAEVLKKFRKSrhmny 234
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 545477471 134 QF----------CIPeHISPKARCLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd07831  235 NFpskkgtglrkLLP-NASAEGLDLLKKLLAYDPDERITAKQALRHPYF 282
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
10-170 1.83e-07

Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. Myt1 is a cytoplasmic cell cycle checkpoint kinase that can keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of N-terminal thr (T14) and tyr (Y15) residues, leading to the delay of meiosis I entry. Meiotic progression is ensured by a two-step inhibition and downregulation of Myt1 by CDK1/XRINGO and p90Rsk during oocyte maturation. In addition, Myt1 targets cyclin B1/B2 and is essential for Golgi and ER assembly during telophase. In Drosophila, Myt1 may be a downstream target of Notch during eye development. The Myt1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270952 [Multi-domain]  Cd Length: 249  Bit Score: 50.00  E-value: 1.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEdthIMKGEDDALSDKHGCPAYVSPEILN 89
Cdd:cd14050   96 SLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLV---VELDKEDIHDAQEGDPRYMAPELLQ 172
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  90 ttGTYsGKAADVWSLGVmlyTLLVGRYPFHDSDPSALFSKIRRGQfcIPEH----ISPKARCLIRSLLRREPSERLTAPE 165
Cdd:cd14050  173 --GSF-TKAADIFSLGI---TILELACNLELPSGGDGWHQLRQGY--LPEEftagLSPELRSIIKLMMDPDPERRPTAED 244

                 ....*
gi 545477471 166 ILLHP 170
Cdd:cd14050  245 LLALP 249
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
11-173 1.85e-07

Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine/threonine kinases (STKs), p21-activated kinase (PAK) 3, catalytic (c) domain. STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. PAKs from higher eukaryotes are classified into two groups (I and II), according to their biochemical and structural features. PAK3 belongs to group I. 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). PAK3 is highly expressed in the brain. It is implicated in neuronal plasticity, synapse formation, dendritic spine morphogenesis, cell cycle progression, neuronal migration, and apoptosis. Inactivating mutations in the PAK3 gene cause X-linked non-syndromic mental retardation, the severity of which depends on the site of the mutation.


Pssm-ID: 132987 [Multi-domain]  Cd Length: 297  Bit Score: 50.11  E-value: 1.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEerTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILnT 90
Cdd:cd06656  112 MDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMD--GSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVV-T 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  91 TGTYsGKAADVWSLGVMLYTLLVGRYPFHDSDP-SALFSKIRRG--QFCIPEHISPKARCLIRSLLRREPSERLTAPEIL 167
Cdd:cd06656  189 RKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGtpELQNPERLSAVFRDFLNRCLEMDVDRRGSAKELL 267

                 ....*.
gi 545477471 168 LHPWFE 173
Cdd:cd06656  268 QHPFLK 273
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
5-169 1.92e-07

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: 50.04  E-value: 1.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLK----LRKFV-------FSTEERTQlrlesledTHIMKGEddAL 73
Cdd:cd06652   97 LKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKganiLRDSVgnvklgdFGASKRLQ--------TICLSGT--GM 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  74 SDKHGCPAYVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFCIPEHISPKARCLIRS 151
Cdd:cd06652  167 KSVTGTPYWMSPEVISGEGY--GRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIatQPTNPQLPAHVSDHCRDFLKR 244
                        170
                 ....*....|....*...
gi 545477471 152 LLrREPSERLTAPEILLH 169
Cdd:cd06652  245 IF-VEAKLRPSADELLRH 261
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
78-175 1.94e-07

Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LATS2 is an essential mitotic regulator responsible for coordinating accurate cytokinesis completion and governing the stabilization of other mitotic regulators. It is also critical in the maintenance of proper chromosome number, genomic stability, mitotic fidelity, and the integrity of centrosome duplication. Downregulation of LATS2 is associated with poor prognosis in acute lymphoblastic leukemia and breast cancer. The LATS2 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: 173715 [Multi-domain]  Cd Length: 381  Bit Score: 50.40  E-value: 1.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGtYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFCIPEHI--SPKARCLIRSLL 153
Cdd:cd05626  210 GTPNYIAPEVLLRKG-YT-QLCDWWSVGVILFEMLVGQPPFLAPTPTETQLKVinWENTLHIPPQVklSPEAVDLITKLC 287
                         90       100
                 ....*....|....*....|....*
gi 545477471 154 rREPSERL---TAPEILLHPWFESV 175
Cdd:cd05626  288 -CSAEERLgrnGADDIKAHPFFSEV 311
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
1-160 2.00e-07

Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase 7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Nek7 is required for mitotic spindle formation and cytokinesis. It is enriched in the centrosome and is critical for microtubule nucleation. Nek7 is activated by Nek9 during mitosis, and may regulate the p70 ribosomal S6 kinase. It is one in a family of 11 different Neks (Nek1-11) that are involved in cell cycle control. The Nek family is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 50.03  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAA-RLFKQIVSAVAHCHQSAIVLGDLKLRKfVFSTEERTqLRLESLEDTHIMKGEDDALSDKHGC 79
Cdd:cd08229  114 MIKHFKKQKRLIPEKTVwKYFVQLCSALEHMHSRRVMHRDIKPAN-VFITATGV-VKLGDLGLGRFFSSKTTAAHSLVGT 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  80 PAYVSPEILNTTGtYSGKAaDVWSLGVMLYTLLVGRYPFHdSDPSALFSKIRRGQFC----IP-EHISPKARCLIRSLLR 154
Cdd:cd08229  192 PYYMSPERIHENG-YNFKS-DIWSLGCLLYEMAALQSPFY-GDKMNLYSLCKKIEQCdyppLPsDHYSEELRQLVNMCIN 268

                 ....*.
gi 545477471 155 REPSER 160
Cdd:cd08229  269 PDPEKR 274
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
11-173 2.09e-07

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: 49.93  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEerTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILnT 90
Cdd:cd06647  100 MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMD--GSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVV-T 176
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  91 TGTYsGKAADVWSLGVMLYTLLVGRYPFHDSDP-SALFSKIRRG--QFCIPEHISPKARCLIRSLLRREPSERLTAPEIL 167
Cdd:cd06647  177 RKAY-GPKVDIWSLGIMAIEMVEGEPPYLNENPlRALYLIATNGtpELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELL 255

                 ....*.
gi 545477471 168 LHPWFE 173
Cdd:cd06647  256 QHPFLK 261
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
78-167 2.28e-07

Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLKs act as mitogen-activated protein kinase kinase kinases (MAP3Ks, MKKKs, MAPKKKs), which 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. Mammals have four MLKs (MLK1-4), mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK 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: 270963 [Multi-domain]  Cd Length: 258  Bit Score: 49.70  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILnTTGTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIP---EHISPKARcLIRSLLR 154
Cdd:cd14061  163 GTYAWMAPEVI-KSSTFS-KASDVWSYGVLLWELLTGEVPYKGIDGLAVAYGVAVNKLTLPipsTCPEPFAQ-LMKDCWQ 239
                         90
                 ....*....|...
gi 545477471 155 REPSERLTAPEIL 167
Cdd:cd14061  240 PDPHDRPSFADIL 252
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
78-201 2.65e-07

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR1 (also called STK38) plays a role in proper centrosome duplication. It is highly expressed in thymus, muscle, lung and spleen. It is not an essential protein because mice deficient of NDR1 remain viable and fertile. However, these mice develop T-cell lymphomas and appear to be hypersenstive to carcinogenic treatment. NDR1 appears to also act as a tumor suppressor. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR1 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: 270777 [Multi-domain]  Cd Length: 376  Bit Score: 50.04  E-value: 2.65e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTGTysGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIR--RGQFCIPEH--ISPKARCLIRSLL 153
Cdd:cd05628  198 GTPDYIAPEVFMQTGY--NKLCDWWSLGVIMYEMLIGYPPFCSETPQETYKKVMnwKETLIFPPEvpISEKAKDLILRFC 275
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545477471 154 rREPSERLTAP---EILLHPWFESV------LEPGYIDSEIGTSDQiVPEYQE--DSDI 201
Cdd:cd05628  276 -CEWEHRIGAPgveEIKTNPFFEGVdwehirERPAAIPIEIKSIDD-TSNFDEfpDSDI 332
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
11-204 3.73e-07

Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This group contains fungal kinases including Schizosaccharomyces pombe Sid2p and Saccharomyces cerevisiae Dbf2p. Group members show similarity to NDR kinases in that they contain an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Sid2p plays a crucial role in the septum initiation network (SIN) and in the initiation of cytokinesis. Dbf2p is important in regulating the mitotic exit network (MEN) and in cytokinesis. The Sid2p-like group 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: 270751 [Multi-domain]  Cd Length: 386  Bit Score: 49.65  E-value: 3.73e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIV-------------LGDLKLRKFVFSTE-------ERTQLRLESLEDT------- 63
Cdd:cd05600  108 LSEEHARFYIAEMFAAISSLHQLGYIhrdlkpenflidsSGHIKLTDFGLASGtlspkkiESMKIRLEEVKNTaflelta 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  64 ----HIMKGEDDALSDKH----GCPAYVSPEILNTTGtYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQF 135
Cdd:cd05600  188 kerrNIYRAMRKEDQNYAnsvvGSPDYMAPEVLRGEG-YD-LTVDYWSLGCILFECLVGFPPFSGSTPNETWANLYHWKK 265
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471 136 CI-------PEH---ISPKARCLIRSLLrREPSERLTAPE-ILLHPWFEsvlepgYIDSEI---GTSDQIVPEYQEDSDI 201
Cdd:cd05600  266 TLqrpvytdPDLefnLSDEAWDLITKLI-TDPQDRLQSPEqIKNHPFFK------NIDWDRlreGSKPPFIPELESEIDT 338

                 ...
gi 545477471 202 SSF 204
Cdd:cd05600  339 SYF 341
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
9-171 6.62e-07

N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class III myosins are motor proteins with an N-terminal kinase catalytic domain and a C-terminal actin-binding motor domain. Class III myosins are present in the photoreceptors of invertebrates and vertebrates and in the auditory hair cells of mammals. The kinase domain of myosin III can phosphorylate several cytoskeletal proteins, conventional myosin regulatory light chains, and can autophosphorylate the C-terminal motor domain. Myosin III may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. It may also function as a cargo carrier during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The Drosophila class III myosin, called NinaC (Neither inactivation nor afterpotential protein C), is critical in normal adaptation and termination of photoresponse. Vertebrates contain two isoforms of class III myosin, IIIA and IIIB. This subfamily also includes mammalian NIK-like embryo-specific kinase (NESK), Traf2- and Nck-interacting kinase (TNIK), and mitogen-activated protein kinase (MAPK) kinase kinase kinase 4/6. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The class III myosin-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: 270785 [Multi-domain]  Cd Length: 275  Bit Score: 48.45  E-value: 6.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   9 KRLREEEAARLFKQIVSAVAHCHQSAI---------VL----GDLKLRKFVFSTE-ERTQLRleslEDTHImkgeddals 74
Cdd:cd06608  108 KRLKEEWIAYILRETLRGLAYLHENKVihrdikgqnILlteeAEVKLVDFGVSAQlDSTLGR----RNTFI--------- 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  75 dkhGCPAYVSPEIL----NTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPS-ALFsKIRRG---QFCIPEHISPKAR 146
Cdd:cd06608  175 ---GTPYWMAPEVIacdqQPDASYDARC-DVWSLGITAIELADGKPPLCDMHPMrALF-KIPRNpppTLKSPEKWSKEFN 249
                        170       180
                 ....*....|....*....|....*
gi 545477471 147 CLIRSLLRREPSERLTAPEILLHPW 171
Cdd:cd06608  250 DFISECLIKNYEQRPFTEELLEHPF 274
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
78-172 7.29e-07

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: 48.38  E-value: 7.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEIlnttgtYSGK---AADVWSLGVMLYTLLVGRYPFHD-SDPSALFSKIRRGQFciPEHIS----PKARCLI 149
Cdd:cd13983  165 GTPEFMAPEM------YEEHydeKVDIYAFGMCLLEMATGEYPYSEcTNAAQIYKKVTSGIK--PESLSkvkdPELKDFI 236
                         90       100
                 ....*....|....*....|...
gi 545477471 150 RSLLRRePSERLTAPEILLHPWF 172
Cdd:cd13983  237 EKCLKP-PDERPSARELLEHPFF 258
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
21-169 8.09e-07

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase Kinases 12 and 13; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K12 is also called MAPK upstream kinase (MUK), dual leucine zipper-bearing kinase (DLK) or leucine-zipper protein kinase (ZPK). It is involved in the c-Jun N-terminal kinase (JNK) pathway that directly regulates axonal regulation through the phosphorylation of microtubule-associated protein 1B (MAP1B). It also regulates the differentiation of many cell types including adipocytes and may play a role in adipogenesis. MAP3K13, also called leucine zipper-bearing kinase (LZK), directly phosphorylates and activates MKK7, which in turn activates the JNK pathway. It also activates NF-kB through IKK activation and this activity is enhanced by antioxidant protein-1 (AOP-1). MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAP2Ks (MAPKKs or MKKs), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K12/13 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: 270961 [Multi-domain]  Cd Length: 237  Bit Score: 47.87  E-value: 8.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  21 KQIVSAVAHCHQSAIVLGDLKLRKFVFSTEertqlrlesledtHIMK----GEDDALSDKH------GCPAYVSPEILNT 90
Cdd:cd14059   88 KQIASGMNYLHLHKIIHRDLKSPNVLVTYN-------------DVLKisdfGTSKELSEKStkmsfaGTVAWMAPEVIRN 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  91 TGTySGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG--QFCIPEHISPKARCLIRSLLRREPSERLTAPEILL 168
Cdd:cd14059  155 EPC-SEKV-DIWSFGVVLWELLTGEIPYKDVDSSAIIWGVGSNslQLPVPSTCPDGFKLLMKQCWNSKPRNRPSFRQILM 232

                 .
gi 545477471 169 H 169
Cdd:cd14059  233 H 233
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
11-169 1.42e-06

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST3 phosphorylates the STK NDR and may play a role in cell cycle progression and cell morphology. It may also regulate paxillin and consequently, cell migration. MST3 is present in human placenta, where it plays an essential role in the oxidative stress-induced apoptosis of trophoblasts in normal spontaneous delivery. Dysregulation of trophoblast apoptosis may result in pregnancy complications such as preeclampsia and intrauterine growth retardation. The MST3 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: 270809 [Multi-domain]  Cd Length: 277  Bit Score: 47.37  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLE------SLEDTHIMKgeddalSDKHGCPAYVS 84
Cdd:cd06641   98 LDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLS--EHGEVKLAdfgvagQLTDTQIKR------N*FVGTPFWMA 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  85 PEILNTTGtYSGKAaDVWSLGVMLYTLLVGRYPFHDSDP-SALFSKIRRGQFCIPEHISPKARCLIRSLLRREPSERLTA 163
Cdd:cd06641  170 PEVIKQSA-YDSKA-DIWSLGITAIELARGEPPHSELHPmKVLFLIPKNNPPTLEGNYSKPLKEFVEACLNKEPSFRPTA 247

                 ....*.
gi 545477471 164 PEILLH 169
Cdd:cd06641  248 KELLKH 253
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
13-169 2.00e-06

Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MST4 is sometimes referred to as MASK (MST3 and SOK1-related kinase). It plays a role in mitogen-activated protein kinase (MAPK) signaling during cytoskeletal rearrangement, morphogenesis, and apoptosis. It influences cell growth and transformation by modulating the extracellular signal-regulated kinase (ERK) pathway. MST4 may also play a role in tumor formation and progression. It localizes in the Golgi apparatus by interacting with the Golgi matrix protein GM130 and may play a role in cell migration. The MST4 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: 132971 [Multi-domain]  Cd Length: 277  Bit Score: 46.97  E-value: 2.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLE------SLEDTHIMKgeddalSDKHGCPAYVSPE 86
Cdd:cd06640  100 EFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLS--EQGDVKLAdfgvagQLTDTQIKR------NTFVGTPFWMAPE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  87 ILNTTGtYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPsalfskiRRGQFCIPEHISPKA--------RCLIRSLLRREPS 158
Cdd:cd06640  172 VIQQSA-YDSKA-DIWSLGITAIELAKGEPPNSDMHP-------MRVLFLIPKNNPPTLvgdfskpfKEFIDACLNKDPS 242
                        170
                 ....*....|.
gi 545477471 159 ERLTAPEILLH 169
Cdd:cd06640  243 FRPTAKELLKH 253
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
97-167 2.25e-06

Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein 15; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Vps15 is a large protein consisting of an N-terminal kinase domain, a C-terminal WD-repeat containing domain, and an intermediate bridge domain that contain HEAT repeats. The kinase domain is necessary for the signaling functions of Vps15. Human Vps15 was previously called p150. It associates and regulates Vps34, also called Class III phosphoinositide 3-kinase (PI3K), which catalyzes the phosphorylation of D-myo-phosphatidylinositol (PtdIns). Vps34 is the only PI3K present in yeast. It plays an important role in the regulation of protein and vesicular trafficking and sorting, autophagy, trimeric G-protein signaling, and phagocytosis. The Vps15 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 PI3K.


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 46.86  E-value: 2.25e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 545477471  97 KAADVWSLG-VMLYTLLVGRYPFhdsDPSALFSkIRRGQFCIPEHIS----PKARCLIRSLLRREPSERLTAPEIL 167
Cdd:cd13980  195 PAMDIFSLGcVIAELFTEGRPLF---DLSQLLA-YRKGEFSPEQVLEkiedPNIRELILHMIQRDPSKRLSAEDYL 266
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
78-182 2.27e-06

Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; 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 the MAPKKs Byr1 from Schizosaccharomyces pombe, FUZ7 from Ustilago maydis, and related proteins. Byr1 phosphorylates its downstream target, the MAPK Spk1, and is regulated by the MAPKK kinase Byr2. The Spk1 cascade is pheromone-responsive and is essential for sporulation and sexual differentiation in fission yeast. FUZ7 phosphorylates and activates its target, the MAPK Crk1, which is required in mating and virulence in U. maydis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. The Byr-1 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: 270792 [Multi-domain]  Cd Length: 286  Bit Score: 47.05  E-value: 2.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTtGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIPEHI----SPK--------- 144
Cdd:cd06620  165 GTSTYMSPERIQG-GKYSVKS-DVWSLGLSIIELALGEFPFAGSNDDDDGYNGPMGILDLLQRIvnepPPRlpkdrifpk 242
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 545477471 145 -ARCLIRSLLRREPSERLTAPEILLHPWFESVLEPGYID 182
Cdd:cd06620  243 dLRDFVDRCLLKDPRERPSPQLLLDHDPFIQAVRASDVD 281
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
11-173 2.49e-06

Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PAK1 is important in the regulation of many cellular processes including cytoskeletal dynamics, cell motility, growth, and proliferation. Although PAK1 has been regarded mainly as a cytosolic protein, recent reports indicate that PAK1 also exists in significant amounts in the nucleus, where it is involved in transcription modulation and in cell cycle regulatory events. PAK1 is also involved in transformation and tumorigenesis. Its overexpression, hyperactivation and increased nuclear accumulation is correlated to breast cancer invasiveness and progression. Nuclear accumulation is also linked to tamoxifen resistance in breast cancer cells. PAK1 belongs to the group I PAKs, which 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). PAKs are Rho family GTPase-regulated kinases that serve as important mediators in the function of Cdc42 (cell division cycle 42) and Rac. The PAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270820 [Multi-domain]  Cd Length: 296  Bit Score: 47.03  E-value: 2.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEerTQLRLESLEDTHIMKGEDDALSDKHGCPAYVSPEILnT 90
Cdd:cd06654  113 MDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMD--GSVKLTDFGFCAQITPEQSKRSTMVGTPYWMAPEVV-T 189
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  91 TGTYsGKAADVWSLGVMLYTLLVGRYPFHDSDP-SALFSKIRRG--QFCIPEHISPKARCLIRSLLRREPSERLTAPEIL 167
Cdd:cd06654  190 RKAY-GPKVDIWSLGIMAIEMIEGEPPYLNENPlRALYLIATNGtpELQNPEKLSAIFRDFLNRCLEMDVEKRGSAKELL 268

                 ....*.
gi 545477471 168 LHPWFE 173
Cdd:cd06654  269 QHQFLK 274
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
4-121 3.61e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 46.71  E-value: 3.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLK-----LRK--------F----VFSTEERTQlrlesleDTHIM 66
Cdd:NF033483  97 YIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKpqnilITKdgrvkvtdFgiarALSSTTMTQ-------TNSVL 169
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 545477471  67 kgeddalsdkhGCPAYVSPEIlnTTGTYSGKAADVWSLGVMLYTLLVGRYPFH-DS 121
Cdd:NF033483 170 -----------GTVHYLSPEQ--ARGGTVDARSDIYSLGIVLYEMLTGRPPFDgDS 212
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
10-193 3.77e-06

Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also called ERK4) and 6 (also called ERK3); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK4 (also called ERK4 or p63MAPK) and MAPK6 (also called ERK3 or p97MAPK) are atypical MAPKs that are not regulated by MAPK kinases. MAPK6 is expressed ubiquitously with highest amounts in brain and skeletal muscle. It may be involved in the control of cell differentiation by negatively regulating cell cycle progression in certain conditions. It may also play a role in glucose-induced insulin secretion. MAPK6 and MAPK4 cooperate to regulate the activity of MAPK-activated protein kinase 5 (MK5), leading to its relocation to the cytoplasm and exclusion from the nucleus. The MAPK6/MK5 and MAPK4/MK5 pathways may play critical roles in embryonic and post-natal development. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK4/6 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: 143359 [Multi-domain]  Cd Length: 342  Bit Score: 46.31  E-value: 3.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTqLRLESLEDTHIM------KGEddaLSDKHGCPAYV 83
Cdd:cd07854  110 PLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTEDLV-LKIGDFGLARIVdphyshKGY---LSEGLVTKWYR 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTGTYSgKAADVWSLGVMLYTLLVGRYPF-------------------HDSDPSALFSKIR---RGQFCIPEH- 140
Cdd:cd07854  186 SPRLLLSPNNYT-KAIDMWAAGCIFAEMLTGKPLFagaheleqmqlilesvpvvREEDRNELLNVIPsfvRNDGGEPRRp 264
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 545477471 141 -------ISPKARCLIRSLLRREPSERLTAPEILLHPWF--------ESV-LEPGYIDSEIgtsDQIVP 193
Cdd:cd07854  265 lrdllpgVNPEALDFLEQILTFNPMDRLTAEEALMHPYMscyscpfdEPVsLHPFHIEDEL---DDILL 330
PTK_Ryk cd05043
Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase ...
22-133 4.41e-06

Pseudokinase domain of Ryk (Receptor related to tyrosine kinase); Ryk is a receptor tyr kinase (RTK) containing an extracellular region with two leucine-rich motifs, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. The extracellular region of Ryk shows homology to the N-terminal domain of Wnt inhibitory factor-1 (WIF) and serves as the ligand (Wnt) binding domain of Ryk. Ryk is expressed in many different tissues both during development and in adults, suggesting a widespread function. It acts as a chemorepulsive axon guidance receptor of Wnt glycoproteins and is responsible for the establishment of axon tracts during the development of the central nervous system. In addition, studies in mice reveal that Ryk is essential in skeletal, craniofacial, and cardiac development. Thus, it appears Ryk is involved in signal transduction despite its lack of kinase activity. Ryk may function as an accessory protein that modulates the signals coming from catalytically active partner RTKs such as the Eph receptors. The Ryk subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270639 [Multi-domain]  Cd Length: 279  Bit Score: 45.91  E-value: 4.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  22 QIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEdTHIMKGEDDALSDKHGCP-AYVSPEILNTTgTYSgKAAD 100
Cdd:cd05043  124 QIACGMSYLHRRGVIHKDIAARNCVIDDELQVKITDNALS-RDLFPMDYHCLGDNENRPiKWMSLESLVNK-EYS-SASD 200
                         90       100       110
                 ....*....|....*....|....*....|....
gi 545477471 101 VWSLGVMLYTLL-VGRYPFHDSDPSALFSKIRRG 133
Cdd:cd05043  201 VWSFGVLLWELMtLGQTPYVEIDPFEMAAYLKDG 234
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
11-174 4.67e-06

Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This subfamily is composed of the catalytically inactive kinases with similarity to yeast Scy1. It includes four mammalian proteins called SCY1-like protein 1 (SCYL1), SCYL2, SCYL3, as well as Testis-EXpressed protein 14 (TEX14). SCYL1 binds to and co-localizes with the membrane trafficking coatomer I (COPI) complex, and regulates COPI-mediated vesicle trafficking. Null mutations in the SCYL1 gene are responsible for the pathology in mdf (muscle-deficient) mice which display progressive motor neuropathy. SCYL2, also called coated vesicle-associated kinase of 104 kDa (CVAK104), is involved in the trafficking of clathrin-coated vesicles. It also binds the HIV-1 accessory protein Vpu and acts as a regulatory factor that promotes the dephosphorylation of Vpu, facilitating the restriction of HIV-1 release. SCYL3, also called ezrin-binding protein PACE-1, may be involved in regulating cell adhesion and migration. TEX14 is required for spermatogenesis and male fertility. It localizes to kinetochores (KT) during mitosis and is a target of the mitotic kinase PLK1. It regulates the maturation of the outer KT and the KT-microtubule attachment. The SCY1-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270913 [Multi-domain]  Cd Length: 287  Bit Score: 46.16  E-value: 4.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSA-----------IVL---GDLKLRKFVF--STEERTQLRLESLEDthimkgEDDALS 74
Cdd:cd14011  111 LYDVEIKYGLLQISEALSFLHNDVklvhgnicpesVVInsnGEWKLAGFDFciSSEQATDQFPYFREY------DPNLPP 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  75 DKHGCPAYVSPE-ILNTTgtySGKAADVWSLGVMLYTLLVGRYPFHDSD-----PSALFSKIRRGQFCIPEHISPKARCL 148
Cdd:cd14011  185 LAQPNLNYLAPEyILSKT---CDPASDMFSLGVLIYAIYNKGKPLFDCVnnllsYKKNSNQLRQLSLSLLEKVPEELRDH 261
                        170       180
                 ....*....|....*....|....*.
gi 545477471 149 IRSLLRREPSERLTAPEILLHPWFES 174
Cdd:cd14011  262 VKTLLNVTPEVRPDAEQLSKIPFFDD 287
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
63-162 5.91e-06

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: 45.52  E-value: 5.91e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  63 THIMKGEDDALSDkHGCPAYVSPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSAL-FSKIRRGQ------F 135
Cdd:cd13978  148 SISANRRRGTENL-GGTPIYMAPEAFDDFNKKPTSKSDVYSFAIVIWAVLTRKEPFENAINPLLiMQIVSKGDrpslddI 226
                         90       100       110
                 ....*....|....*....|....*....|
gi 545477471 136 CIPEHIsPKARCLIRSLLR---REPSERLT 162
Cdd:cd13978  227 GRLKQI-ENVQELISLMIRcwdGNPDARPT 255
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
21-172 5.94e-06

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (S/T) as well as tyrosine residues on protein substrates. CLKs are involved in the phosphorylation and regulation of serine/arginine-rich (SR) proteins, which play a crucial role in pre-mRNA splicing by directing splice site selection. SR proteins are phosphorylated first by SR protein kinases (SRPKs) at the N-terminus, which leads to its assembly into nuclear speckles where splicing factors are stored. CLKs phosphorylate the C-terminal part of SR proteins, causing the nuclear speckles to dissolve and splicing factors to be recruited at sites of active transcription. Based on a conserved "EHLAMMERILG" signature motif which may be crucial for substrate specificity, CLKs are also referred to as LAMMER kinases. CLKs autophosphorylate at tyrosine residues and phosphorylate their substrates exclusively on S/T residues. In Drosophila, the CLK homolog DOA (Darkener of apricot) is essential for embryogenesis and its mutation leads to defects in sexual differentiation, eye formation, and neuronal development. In fission yeast, the CLK homolog Lkh1 is a negative regulator of filamentous growth and asexual flocculation, and is also involved in oxidative stress response. Vertebrates contain mutliple CLK proteins and mammals have four (CLK1-4). The CLK 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: 271036 [Multi-domain]  Cd Length: 332  Bit Score: 45.63  E-value: 5.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  21 KQIVSAVAHCHQSAIVLGDLKL----------RKFVFSTEERTQLRLES------------LEDTHimkgEDDALSDKHg 78
Cdd:cd14134  122 KQLLEAVAFLHDLKLTHTDLKPenillvdsdyVKVYNPKKKRQIRVPKStdiklidfgsatFDDEY----HSSIVSTRH- 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 cpaYVSPE-ILNTTGTYSgkaADVWSLGVMLYTLLVGR--YPFHD-------------SDPSALFSKIRRGQ-------- 134
Cdd:cd14134  197 ---YRAPEvILGLGWSYP---CDVWSIGCILVELYTGEllFQTHDnlehlammerilgPLPKRMIRRAKKGAkyfyfyhg 270
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545477471 135 ---------------------FCIPEHISPKARC---LIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd14134  271 rldwpegsssgrsikrvckplKRLMLLVDPEHRLlfdLIRKMLEYDPSKRITAKEALKHPFF 332
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
22-172 8.23e-06

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK2 is regulated by cyclin E or cyclin A. Upon activation by cyclin E, it phosphorylates the retinoblastoma (pRb) protein which activates E2F mediated transcription and allows cells to move into S phase. The CDK2/cyclin A complex plays a role in regulating DNA replication. CDK2, together with CDK4, also regulates embryonic cell proliferation. Despite these important roles, mice deleted for the cdk2 gene are viable and normal except for being sterile. This may be due to compensation provided by CDK1 (also called Cdc2), which can also bind cyclin E and drive the G1 to S phase transition. CDK3 is regulated by cyclin C and it phosphorylates pRB specifically during the G0/G1 transition. This phosphorylation is required for cells to exit G0 efficiently and enter the G1 phase. 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 CDK2/3 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: 270844 [Multi-domain]  Cd Length: 284  Bit Score: 45.19  E-value: 8.23e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  22 QIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLrlesledthimkgEDDALSDKHGCPA-----------YVSPEILNT 90
Cdd:cd07860  108 QLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKL-------------ADFGLARAFGVPVrtythevvtlwYRAPEILLG 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  91 TGTYSgKAADVWSLGVMLYTLLVGRYPF-HDSDPSALFSKIRR----------GQFCIPEH------------------I 141
Cdd:cd07860  175 CKYYS-TAVDIWSLGCIFAEMVTRRALFpGDSEIDQLFRIFRTlgtpdevvwpGVTSMPDYkpsfpkwarqdfskvvppL 253
                        170       180       190
                 ....*....|....*....|....*....|.
gi 545477471 142 SPKARCLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd07860  254 DEDGRDLLSQMLHYDPNKRISAKAALAHPFF 284
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
11-169 1.00e-05

Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. STK25 is also called Ste20/oxidant stress response kinase 1 (SOK1) or yeast Sps1/Ste20-related kinase 1 (YSK1). It is localized in the Golgi apparatus through its interaction with the Golgi matrix protein GM130. It may be involved in the regulation of cell migration and polarization. STK25 binds and phosphorylates CCM3 (cerebral cavernous malformation 3), also called PCD10 (programmed cell death 10), and may play a role in apoptosis. Human STK25 is a candidate gene responsible for pseudopseudohypoparathyroidism (PPHP), a disease that shares features with the Albright hereditary osteodystrophy (AHO) phenotype. The STK25 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: 270810 [Multi-domain]  Cd Length: 277  Bit Score: 45.05  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLR----LESLEDTHIMKgeddalSDKHGCPAYVSPE 86
Cdd:cd06642   98 LEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLAdfgvAGQLTDTQIKR------NTFVGTPFWMAPE 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  87 ILNTTGtYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPsalfskiRRGQFCIPEHISPKA--------RCLIRSLLRREPS 158
Cdd:cd06642  172 VIKQSA-YDFKA-DIWSLGITAIELAKGEPPNSDLHP-------MRVLFLIPKNSPPTLegqhskpfKEFVEACLNKDPR 242
                        170
                 ....*....|.
gi 545477471 159 ERLTAPEILLH 169
Cdd:cd06642  243 FRPTAKELLKH 253
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
22-117 1.41e-05

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK1 is one of two vertebrate LRRKs which show complementary expression in the brain. It can form heterodimers with LRRK2, and may influence the age of onset of LRRK2-associated Parkinson's disease. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. The LRRK1 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: 270969 [Multi-domain]  Cd Length: 276  Bit Score: 44.57  E-value: 1.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  22 QIVSAVAHCHQSAIVLGDLKLRK-FVFSTEERTQLRLEsLEDTHIMKG--EDDALSDKhGCPAYVSPEIlnTTGTYSGKA 98
Cdd:cd14067  122 QIAAGLAYLHKKNIIFCDLKSDNiLVWSLDVQEHINIK-LSDYGISRQsfHEGALGVE-GTPGYQAPEI--RPRIVYDEK 197
                         90
                 ....*....|....*....
gi 545477471  99 ADVWSLGVMLYTLLVGRYP 117
Cdd:cd14067  198 VDMFSYGMVLYELLSGQRP 216
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
13-171 1.60e-05

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK12 is also called Cdc2-related protein kinase 7 (CRK7) or Cdc2-related kinase arginine/serine-rich (CrkRS). It is a unique CDK that contains an RS domain, which is predominantly found in splicing factors. CDK12 is widely expressed in tissues. It interacts with cyclins L1 and L2, and plays roles in regulating transcription and alternative splicing. 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 CDK12 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: 270847 [Multi-domain]  Cd Length: 302  Bit Score: 44.41  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  13 EEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTeeRTQLRLESLEDTHIMKGEDDAL-SDKHGCPAYVSPEILNTT 91
Cdd:cd07864  115 EDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNN--KGQIKLADFGLARLYNSEESRPyTNKVITLWYRPPELLLGE 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  92 GTYsGKAADVWSLGVMLYTLLVGR--------------------------YP-------FHDSDPSALFSKIRRGQFcip 138
Cdd:cd07864  193 ERY-GPAIDVWSCGCILGELFTKKpifqanqelaqlelisrlcgspcpavWPdviklpyFNTMKPKKQYRRRLREEF--- 268
                        170       180       190
                 ....*....|....*....|....*....|...
gi 545477471 139 EHISPKARCLIRSLLRREPSERLTAPEILLHPW 171
Cdd:cd07864  269 SFIPTPALDLLDHMLTLDPSKRCTAEQALNSPW 301
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
84-167 1.64e-05

Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class of kinases can not be predicted. Possible dual-specificity Ser/Thr/Tyr kinase.


Pssm-ID: 214568 [Multi-domain]  Cd Length: 258  Bit Score: 44.08  E-value: 1.64e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471    84 SPEILNTtGTYSgKAADVWSLGVMLY---TLlvGRYPFHDSDPSALFSKIRRGQF-CIPEHISPKARCLIRSLLRREPSE 159
Cdd:smart00221 172 APESLKE-GKFT-SKSDVWSFGVLLWeifTL--GEEPYPGMSNAEVLEYLKKGYRlPKPPNCPPELYKLMLQCWAEDPED 247

                   ....*...
gi 545477471   160 RLTAPEIL 167
Cdd:smart00221 248 RPTFSELV 255
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
4-172 1.65e-05

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; 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 TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 44.28  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQ--SAIVLGDLKLRKFVFSTEERT-QLRLESLEDTHIMKGED-------DAL 73
Cdd:cd14041  101 YLKQHKLMSEKEARSIIMQIVNALKYLNEikPPIIHYDLKPGNILLVNGTACgEIKITDFGLSKIMDDDSynsvdgmELT 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  74 SDKHGCPAYVSPE--ILNTTGTYSGKAADVWSLGVMLYTLLVGRYPF-HDSDPSALFS-----KIRRGQFCIPEHISPKA 145
Cdd:cd14041  181 SQGAGTYWYLPPEcfVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFgHNQSQQDILQentilKATEVQFPPKPVVTPEA 260
                        170       180
                 ....*....|....*....|....*..
gi 545477471 146 RCLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd14041  261 KAFIRRCLAYRKEDRIDVQQLACDPYL 287
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
84-167 1.80e-05

Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 44.06  E-value: 1.80e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471    84 SPEILNTtGTYSgKAADVWSLGVMLY---TLlvGRYPFHDSDPSALFSKIRRGQFC-IPEHISPKARCLIRSLLRREPSE 159
Cdd:smart00219 171 APESLKE-GKFT-SKSDVWSFGVLLWeifTL--GEQPYPGMSNEEVLEYLKNGYRLpQPPNCPPELYDLMLQCWAEDPED 246

                   ....*...
gi 545477471   160 RLTAPEIL 167
Cdd:smart00219 247 RPTFSELV 254
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
82-202 1.88e-05

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. Typical MAPK pathways involve a triple kinase core cascade comprising of the MAPK, which is phosphorylated and activated by a MAPK kinase (MAP2K or MKK), which itself is phosphorylated and activated by a MAPK kinase kinase (MAP3K or MKKK). Each cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. There are three typical MAPK subfamilies: Extracellular signal-Regulated Kinase (ERK), c-Jun N-terminal Kinase (JNK), and p38. Some MAPKs are atypical in that they are not regulated by MAP2Ks. These include MAPK4, MAPK6, NLK, and ERK7. The MAPK 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: 270828 [Multi-domain]  Cd Length: 329  Bit Score: 44.44  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNTTGTYSgKAADVWSLGVMLYTLLVGR--YPFHD-----------------------SDPSA------LFSKI 130
Cdd:cd07834  171 YRAPELLLSSKKYT-KAIDIWSVGCIFAELLTRKplFPGRDyidqlnlivevlgtpseedlkfiSSEKArnylksLPKKP 249
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 545477471 131 RRGQFCIPEHISPKARCLIRSLLRREPSERLTAPEILLHPWFESVLEPgyIDSEIGTSDQIVPEYqEDSDIS 202
Cdd:cd07834  250 KKPLSEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYLAQLHDP--EDEPVAKPPFDFPFF-DDEELT 318
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
78-171 1.98e-05

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 5; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK5 (also called MEK5) is a dual-specificity PK that phosphorylates its downstream target, extracellular signal-regulated kinase 5 (ERK5), on specific threonine and tyrosine residues. MKK5 is activated by MEKK2 and MEKK3 in response to mitogenic and stress stimuli. The ERK5 cascade promotes cell proliferation, differentiation, neuronal survival, and neuroprotection. This cascade plays an essential role in heart development. Mice deficient in either ERK5 or MKK5 die around embryonic day 10 due to cardiovascular defects including underdevelopment of the myocardium. In addition, MKK5 is associated with metastasis and unfavorable prognosis in prostate cancer. The MKK5 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: 132950 [Multi-domain]  Cd Length: 279  Bit Score: 44.10  E-value: 1.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEilNTTGTYSGKAADVWSLGVMLYTLLVGRYPFH-------------------DSDPSALfskiRRGQFcip 138
Cdd:cd06619  155 GTNAYMAPE--RISGEQYGIHSDVWSLGISFMELALGRFPYPqiqknqgslmplqllqcivDEDPPVL----PVGQF--- 225
                         90       100       110
                 ....*....|....*....|....*....|...
gi 545477471 139 ehiSPKARCLIRSLLRREPSERLTAPEILLHPW 171
Cdd:cd06619  226 ---SEKFVHFITQCMRKQPKERPAPENLMDHPF 255
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
78-138 1.98e-05

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK1 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K9. MAP3Ks 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. Little is known about the specific function of MLK1. It is capable of activating the c-Jun N-terminal kinase pathway. Mice lacking both MLK1 and MLK2 are viable, fertile, and have normal life spans. There could be redundancy in the function of MLKs. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK1 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: 271047 [Multi-domain]  Cd Length: 270  Bit Score: 44.26  E-value: 1.98e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545477471  78 GCPAYVSPEILNTTgTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIP 138
Cdd:cd14145  175 GTYAWMAPEVIRSS-MFS-KGSDVWSYGVLLWELLTGEVPFRGIDGLAVAYGVAMNKLSLP 233
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
82-172 1.99e-05

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 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: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 44.03  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPE-ILNTTgTYSGkAADVWSLGVMLYTLLVGRYPFH-DSD-------------PSA-------------LFSKIRRG 133
Cdd:cd14137  172 YRAPElIFGAT-DYTT-AIDIWSAGCVLAELLLGQPLFPgESSvdqlveiikvlgtPTReqikamnpnytefKFPQIKPH 249
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 545477471 134 QF--CIPEHISPKARCLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd14137  250 PWekVFPKRTPPDAIDLLSKILVYNPSKRLTALEALAHPFF 290
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
78-118 3.05e-05

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase Kinase 4; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MKK4 is a dual-specificity PK that phosphorylates and activates the downstream targets, c-Jun N-terminal kinase (JNK) and p38 MAPK, on specific threonine and tyrosine residues. JNK and p38 are collectively known as stress-activated MAPKs, as they are activated in response to a variety of environmental stresses and pro-inflammatory cytokines. Their activation is associated with the induction of cell death. Mice deficient in MKK4 die during embryogenesis and display anemia, severe liver hemorrhage, and abnormal hepatogenesis. MKK4 may also play roles in the immune system and in cardiac hypertrophy. It plays a major role in cancer as a tumor and metastasis suppressor. Under certain conditions, MKK4 is pro-oncogenic. The MKK4 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: 270790 [Multi-domain]  Cd Length: 291  Bit Score: 43.51  E-value: 3.05e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 545477471  78 GCPAYVSPEILNTTGTYSGK--AADVWSLGVMLYTLLVGRYPF 118
Cdd:cd06616  171 GCRPYMAPERIDPSASRDGYdvRSDVWSLGITLYEVATGKFPY 213
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
78-172 3.07e-05

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 and MEK2 are MAPK kinases (MAPKKs or MKKs), and are dual-specificity PKs that phosphorylate and activate the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1/2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. This cascade has also been implicated in synaptic plasticity, migration, morphological determination, and stress response immunological reactions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1/2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK 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: 132946 [Multi-domain]  Cd Length: 308  Bit Score: 43.58  E-value: 3.07e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILntTGTYSGKAADVWSLGVMLYTLLVGRYP--------------------------------FHDSDPS- 124
Cdd:cd06615  160 GTRSYMSPERL--QGTHYTVQSDIWSLGLSLVEMAIGRYPipppdakeleamfgrpvsegeakeshrpvsghPPDSPRPm 237
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545477471 125 ALFS-----------KIRRGQFcipehiSPKARCLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd06615  238 AIFElldyivnepppKLPSGAF------SDEFQDFVDKCLKKNPKERADLKELTKHPFI 290
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
11-141 3.15e-05

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The IKK complex functions as a master regulator of Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. It is composed of two kinases, IKKalpha and IKKbeta, and the regulatory subunit IKKgamma or NEMO (NF-kB Essential MOdulator). IKKs facilitate the release of NF-kB dimers from an inactive state, allowing them to migrate to the nucleus where they regulate gene transcription. There are two IKK pathways that regulate NF-kB signaling, called the classical (involving IKKbeta and NEMO) and non-canonical (involving IKKalpha) pathways. The classical pathway regulates the majority of genes activated by NF-kB. The IKK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270891 [Multi-domain]  Cd Length: 289  Bit Score: 43.59  E-value: 3.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEE-RTQLRLESLedthimkGEDDALSDKHGCPA------YV 83
Cdd:cd13989   99 LKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLQQGGgRVIYKLIDL-------GYAKELDQGSLCTSfvgtlqYL 171
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 545477471  84 SPEILNTTgTYSgKAADVWSLGVMLYTLLVGRYPF-HDSDPSALFSKIRRGQfciPEHI 141
Cdd:cd13989  172 APELFESK-KYT-CTVDYWSFGTLAFECITGYRPFlPNWQPVQWHGKVKQKK---PEHI 225
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
4-172 3.93e-05

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A splice variant of TLK1, called TLK1B, is expressed in the presence of double strand breaks (DSBs). It lacks the N-terminal part of TLK1, but is expected to phosphorylate the same substrates. TLK1/1B interacts with Rad9, which is critical in DNA damage-activated checkpoint response, and plays a role in the repair of linearized DNA with incompatible ends. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. The TLK1 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: 270942 [Multi-domain]  Cd Length: 299  Bit Score: 43.12  E-value: 3.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQ--SAIVLGDLKLRKFVFSTEERT-QLRLESLEDTHIMKGED------DALS 74
Cdd:cd14040  101 YLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTACgEIKITDFGLSKIMDDDSygvdgmDLTS 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  75 DKHGCPAYVSPE--ILNTTGTYSGKAADVWSLGVMLYTLLVGRYPF-HDSDPSALFS-----KIRRGQFCIPEHISPKAR 146
Cdd:cd14040  181 QGAGTYWYLPPEcfVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQentilKATEVQFPVKPVVSNEAK 260
                        170       180
                 ....*....|....*....|....*.
gi 545477471 147 CLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd14040  261 AFIRRCLAYRKEDRFDVHQLASDPYL 286
PK_MviN-like cd13973
Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain ...
10-138 4.27e-05

Pseudokinase domain of the peptidoglycan biosynthetic protein MviN; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. This family is composed of the mycobacterial protein MviN and similar proteins. MviN is an integral membrane protein that is essential for growth and is required for cell wall integrity and peptidogylcan (PG) biosynthesis. It comprises of 14 predicted transmembrane (TM) helices at the N-terminus, followed by an intracellular pseudokinase domain linked through a single TM helix to a carbohydrate binding extracellular domain. Phosphorylation of the MviN pseudokinase domain by the PG-sensitive serine/threonine protein kinase PknB recruits a forkhead associated (FHA) domain protein FhaA, which modulates local PG synthesis at cell poles and the septum. The MviN pseudokinase forms a canonical receptor kinase dimer.


Pssm-ID: 270875 [Multi-domain]  Cd Length: 236  Bit Score: 43.09  E-value: 4.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  10 RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRlesledthimkgeddalsdkhgcpayvSPEILN 89
Cdd:cd13973   96 PLDPEAAARAVAELAEALAAAHRAGLALGIDHPDRVRISSDGRVVLA---------------------------FPAVLA 148
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 545477471  90 TTGTysgkAADVWSLGVMLYTLLVGRYPfHDSDPSALFSKIRRGQFCIP 138
Cdd:cd13973  149 ALSP----ATDVRALGALLYALLTGRWP-LPEGGAALAAAPADAAEPVP 192
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
11-172 4.29e-05

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL2, also called p56 KKIAMRE, is expressed in testis, kidney, lung, and brain. It functions mainly in mature neurons and plays an important role in learning and memory. Inactivation of CDKL3, also called NKIAMRE (NKIATRE in rat), by translocation is associated with mild mental retardation. It has been reported that CDKL3 is lost in leukemic cells having a chromosome arm 5q deletion, and may contribute to the transformed phenotype. 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 CDKL2/3 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: 270836 [Multi-domain]  Cd Length: 286  Bit Score: 43.18  E-value: 4.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDThiMKGEDDALSDKHGCPAYVSPEILNT 90
Cdd:cd07846   97 LDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFART--LAAPGEVYTDYVATRWYRAPELLVG 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  91 TGTYsGKAADVWSLGVMLYTLLVGRYPF-HDSDPSALFSKIRRGQFCIPEH----------------------------- 140
Cdd:cd07846  175 DTKY-GKAVDVWAVGCLVTEMLTGEPLFpGDSDIDQLYHIIKCLGNLIPRHqelfqknplfagvrlpevkeveplerryp 253
                        170       180       190
                 ....*....|....*....|....*....|...
gi 545477471 141 -ISPKARCLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd07846  254 kLSGVVIDLAKKCLHIDPDKRPSCSELLHHEFF 286
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
78-177 6.19e-05

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK2 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK) and is also called MAP3K10. MAP3Ks 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. MLK2 is abundant in brain, skeletal muscle, and testis. It functions upstream of the MAPK, c-Jun N-terminal kinase. It binds hippocalcin, a calcium-sensor protein that protects neurons against calcium-induced cell death. Both MLK2 and hippocalcin may be associated with the pathogenesis of Parkinson's disease. MLK2 also binds to normal huntingtin (Htt), which is important in neuronal transcription, development, and survival. MLK2 does not bind to the polyglutamine-expanded Htt, which is implicated in the pathogeneis of Huntington's disease, leading to neuronal toxicity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation. The MLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271050 [Multi-domain]  Cd Length: 258  Bit Score: 42.67  E-value: 6.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTTgTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIP-EHISPKA-RCLIRSLLRR 155
Cdd:cd14148  163 GTYAWMAPEVIRLS-LFS-KSSDVWSFGVLLWELLTGEVPYREIDALAVAYGVAMNKLTLPiPSTCPEPfARLLEECWDP 240
                         90       100
                 ....*....|....*....|..
gi 545477471 156 EPSERltapeillhPWFESVLE 177
Cdd:cd14148  241 DPHGR---------PDFGSILK 253
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
78-146 6.24e-05

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 2; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK2 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK2, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK2, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. The MEK subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 132980 [Multi-domain]  Cd Length: 331  Bit Score: 42.73  E-value: 6.24e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545477471  78 GCPAYVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDP---SALFSK-IRRGQFCIPEHISPKAR 146
Cdd:cd06649  164 GTRSYMSPERLQ--GTHYSVQSDIWSMGLSLVELAIGRYPIPPPDAkelEAIFGRpVVDGEEGEPHSISPRPR 234
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
5-166 6.30e-05

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK 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: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 42.50  E-value: 6.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   5 VRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLrlesLED-THIMKGEDDALSDK------- 76
Cdd:cd13991   89 IKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLSSDGSDAF----LCDfGHAECLDPDGLGKSlftgdyi 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  77 HGCPAYVSPEILntTGTYSGKAADVWSLGVMLYTLLVGRYPfhdsdpsalFSKIRRGQFC------------IPEHISPK 144
Cdd:cd13991  165 PGTETHMAPEVV--LGKPCDAKVDVWSSCCMMLHMLNGCHP---------WTQYYSGPLClkianeppplreIPPSCAPL 233
                        170       180
                 ....*....|....*....|..
gi 545477471 145 ARCLIRSLLRREPSERLTAPEI 166
Cdd:cd13991  234 TAQAIQAGLRKEPVHRASAAEL 255
PTKc_Aatyk1 cd05087
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs ...
18-168 6.49e-05

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk1 (or simply Aatyk) is also called lemur tyrosine kinase 1 (Lmtk1). It is a cytoplasmic (or nonreceptor) kinase containing a long C-terminal region. The expression of Aatyk1 is upregulated during growth arrest and apoptosis in myeloid cells. Aatyk1 has been implicated in neural differentiation, and is a regulator of the Na-K-2Cl cotransporter, a membrane protein involved in cell proliferation and survival, epithelial transport, and blood pressure control. The Aatyk1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270670 [Multi-domain]  Cd Length: 271  Bit Score: 42.67  E-value: 6.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  18 RLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLedTHIMKGEDDAL-SDKHGCP-AYVSPEIL-----NT 90
Cdd:cd05087  106 RMACEVACGLLHLHRNNFVHSDLALRNCLLTADLTVKIGDYGL--SHCKYKEDYFVtADQLWVPlRWIAPELVdevhgNL 183
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  91 TGTYSGKAADVWSLGVMLYTLL-VGRYPF-HDSDPSALFSKIRRGQFCIPEhisPKarcLIRSLLRR----------EPS 158
Cdd:cd05087  184 LVVDQTKQSNVWSLGVTIWELFeLGNQPYrHYSDRQVLTYTVREQQLKLPK---PQ---LKLSLAERwyevmqfcwlQPE 257
                        170
                 ....*....|
gi 545477471 159 ERLTAPEILL 168
Cdd:cd05087  258 QRPTAEEVHL 267
STKc_KSR1 cd14152
Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the ...
1-134 6.60e-05

Catalytic domain of the Serine/Threonine Kinase, Kinase Suppressor of Ras 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KSR1 functions as a transducer of TNFalpha-stimulated C-Raf activation of ERK1/2 and NF-kB. Detected activity of KSR1 is cell type specific and context dependent. It is inactive in normal colon epithelial cells and becomes activated at the onset of inflammatory bowel disease (IBD). Similarly, KSR1 activity is undetectable prior to stimulation by EGF or ceramide in COS-7 or YAMC cells, respectively. KSR proteins are widely regarded as pseudokinases, however, this matter is up for debate as catalytic activity has been detected for KSR1 in some systems. The KSR1 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: 271054 [Multi-domain]  Cd Length: 279  Bit Score: 42.65  E-value: 6.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRK-RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKlRKFVFSTEER---TQLRLESLEDTHIMKGEDDALSDK 76
Cdd:cd14152   83 LYSFVRDPKtSLDINKTRQIAQEIIKGMGYLHAKGIVHKDLK-SKNVFYDNGKvviTDFGLFGISGVVQEGRRENELKLP 161
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 545477471  77 HGCPAYVSPEILNTTGTYSG-------KAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQ 134
Cdd:cd14152  162 HDWLCYLAPEIVREMTPGKDedclpfsKAADVYAFGTIWYELQARDWPLKNQPAEALIWQIGSGE 226
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
21-166 6.66e-05

Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs lack a critical aspartate involved in ATP binding and does not exhibit kinase activity. It functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 42.38  E-value: 6.66e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  21 KQIVSAVAHCHQSAIVL-GDLKLRKFVfsTEERTQLRLESLEDTHIMKGEDDALSDKHGCPA---YVSPEIL--NTTGTY 94
Cdd:cd13992  104 KDIVKGMNYLHSSSIGYhGRLKSSNCL--VDSRWVVKLTDFGLRNLLEEQTNHQLDEDAQHKkllWTAPELLrgSLLEVR 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  95 SGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFC--IPEHISPKARC------LIRSLLRREPSERLTAPEI 166
Cdd:cd13992  182 GTQKGDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGNKpfRPELAVLLDEFpprlvlLVKQCWAENPEKRPSFKQI 261
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
82-178 6.78e-05

Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ERK5 (also called Big MAPK1 (BMK1) or MAPK7) has a unique C-terminal extension, making it approximately twice as big as other MAPKs. This extension contains transcriptional activation capability which is inhibited by the N-terminal half. ERK5 is activated in response to growth factors and stress by a cascade that leads to its phosphorylation by the MAP2K MEK5, which in turn is regulated by the MAP3Ks MEKK2 and MEKK3. Activated ERK5 phosphorylates its targets including myocyte enhancer factor 2 (MEF2), Sap1a, c-Myc, and RSK. It plays a role in EGF-induced cell proliferation during the G1/S phase transition. Studies on knockout mice revealed that ERK5 is essential for cardiovascular development and plays an important role in angiogenesis. It is also critical for neural differentiation and survival. The ERK5 pathway has been implicated in the pathogenesis of many diseases including cancer, cardiac hypertrophy, and atherosclerosis. MAPKs are important mediators of cellular responses to extracellular signals. The ERK5 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: 270842 [Multi-domain]  Cd Length: 336  Bit Score: 42.74  E-value: 6.78e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNTTGTYSgKAADVWSLGVMLYTLLV------GRYPFHD---------SDPSALFSKIR--RGQFCI---PEH- 140
Cdd:cd07855  179 YRAPELMLSLPEYT-QAIDMWSVGCIFAEMLGrrqlfpGKNYVHQlqliltvlgTPSQAVINAIGadRVRRYIqnlPNKq 257
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 545477471 141 ------ISPKARC----LIRSLLRREPSERLTAPEILLHPWFESVLEP 178
Cdd:cd07855  258 pvpwetLYPKADQqaldLLSQMLRFDPSERITVAEALQHPFLAKYHDP 305
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
22-175 6.91e-05

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 42.50  E-value: 6.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  22 QIVSAVAHCHQSAIVLGDLKLRKFVFSTEertqlrlesledTHIMKGEDDALSDKHGCPA-----------YVSPEILNT 90
Cdd:PLN00009 110 QILRGIAYCHSHRVLHRDLKPQNLLIDRR------------TNALKLADFGLARAFGIPVrtfthevvtlwYRAPEILLG 177
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  91 TGTYSgKAADVWSLGVmLYTLLVGRYPFH--DSDPSALFSKIR----------RGQFCIPEHIS--PKARC--------- 147
Cdd:PLN00009 178 SRHYS-TPVDIWSVGC-IFAEMVNQKPLFpgDSEIDELFKIFRilgtpneetwPGVTSLPDYKSafPKWPPkdlatvvpt 255
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 545477471 148 -------LIRSLLRREPSERLTAPEILLHPWFESV 175
Cdd:PLN00009 256 lepagvdLLSKMLRLDPSKRITARAALEHEYFKDL 290
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
69-166 1.06e-04

Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. TNNI3K, also called cardiac ankyrin repeat kinase (CARK), is a cardiac-specific troponin I-interacting kinase that promotes cardiac myogenesis, improves cardiac performance, and protects the myocardium from ischemic injury. It contains N-terminal ankyrin repeats, a catalytic kinase domain, and a C-terminal serine-rich domain. TNNI3K exerts a disease-accelerating effect on cardiac dysfunction and reduced survival in mouse models of cardiomyopathy. The TNNI3K subfamily is part of a larger superfamily that includes the catalytic domains of other protein serine/threonine PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270966 [Multi-domain]  Cd Length: 254  Bit Score: 41.75  E-value: 1.06e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  69 EDDALSDKHGCPAYVSPEILNTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKI--RRGQFCIPEHIsPKAr 146
Cdd:cd14064  149 DEDNMTKQPGNLRWMAPEVFTQCTRYSIKA-DVFSYALCLWELLTGEIPFAHLKPAAAAADMayHHIRPPIGYSI-PKP- 225
                         90       100
                 ....*....|....*....|....
gi 545477471 147 clIRSLLRR----EPSERLTAPEI 166
Cdd:cd14064  226 --ISSLLMRgwnaEPESRPSFVEI 247
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
82-171 1.16e-04

Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; 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 the MAPKKs Pek1/Skh1 from Schizosaccharomyces pombe and MKK2 from Saccharomyces cerevisiae, and related proteins. Both fission yeast Pek1 and baker's yeast MKK2 are components of the cell integrity MAPK pathway. In fission yeast, Pek1 phosphorylates and activates Pmk1/Spm1 and is regulated by the MAPKK kinase Mkh1. In baker's yeast, the pathway involves the MAPK Slt2, the MAPKKs MKK1 and MKK2, and the MAPKK kinase Bck1. The cell integrity MAPK cascade is activated by multiple stress conditions, and is essential in cell wall construction, morphogenesis, cytokinesis, and ion homeostasis. MAPK signaling pathways are important mediators of cellular responses to extracellular signals. 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: 270793 [Multi-domain]  Cd Length: 287  Bit Score: 42.02  E-value: 1.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILnTTGTYSGKAaDVWSLGVMLYTLLVGRYPF-HDSDPSA----LFSKIRRGQfcIPEHI---------SPKARC 147
Cdd:cd06621  169 YMAPERI-QGGPYSITS-DVWSLGLTLLEVAQNRFPFpPEGEPPLgpieLLSYIVNMP--NPELKdepengikwSESFKD 244
                         90       100
                 ....*....|....*....|....
gi 545477471 148 LIRSLLRREPSERLTAPEILLHPW 171
Cdd:cd06621  245 FIEKCLEKDGTRRPGPWQMLAHPW 268
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
69-184 1.33e-04

Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lyn is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lyn is expressed in B lymphocytes and myeloid cells. It exhibits both positive and negative regulatory roles in B cell receptor (BCR) signaling. Lyn, as well as Fyn and Blk, promotes B cell activation by phosphorylating ITAMs (immunoreceptor tyr activation motifs) in CD19 and in Ig components of BCR. It negatively regulates signaling by its unique ability to phosphorylate ITIMs (immunoreceptor tyr inhibition motifs) in cell surface receptors like CD22 and CD5. Lyn also plays an important role in G-CSF receptor signaling by phosphorylating a variety of adaptor molecules. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lyn subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 41.57  E-value: 1.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  69 EDDALSDKHGCP---AYVSPEILNTtGTYSGKAaDVWSLGVMLYTLLV-GRYPFHDSDPSALFSKIRRG-QFCIPEHISP 143
Cdd:cd05072  155 EDNEYTAREGAKfpiKWTAPEAINF-GSFTIKS-DVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRGyRMPRMENCPD 232
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 545477471 144 KARCLIRSLLRREPSERLTapeillHPWFESVLEPGYIDSE 184
Cdd:cd05072  233 ELYDIMKTCWKEKAEERPT------FDYLQSVLDDFYTATE 267
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
78-126 1.67e-04

Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) Kinase 1; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine (ST) or tyrosine residues on protein substrates. MEK1 is a dual-specificity PK and a MAPK kinase (MAPKK or MKK) that phosphorylates and activates the downstream targets, ERK1 and ERK2, on specific threonine and tyrosine residues. The ERK cascade starts with extracellular signals including growth factors, hormones, and neurotransmitters, which act through receptors and ion channels to initiate intracellular signaling that leads to the activation at the MAPKKK (Raf-1 or MOS) level, which leads to the transmission of signals to MEK1, and finally to ERK1/2. The ERK cascade plays an important role in cell proliferation, differentiation, oncogenic transformation, and cell cycle control, as well as in apoptosis and cell survival under certain conditions. Gain-of-function mutations in genes encoding ERK cascade proteins, including MEK1, cause cardiofaciocutaneous (CFC) syndrome, a condition leading to multiple congenital anomalies and mental retardation in patients. MEK1 also plays a role in cell cycle control. The MEK 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: 270816 [Multi-domain]  Cd Length: 319  Bit Score: 41.58  E-value: 1.67e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 545477471  78 GCPAYVSPEILNttGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSAL 126
Cdd:cd06650  164 GTRSYMSPERLQ--GTHYSVQSDIWSMGLSLVEMAVGRYPIPPPDAKEL 210
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
21-131 2.40e-04

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK 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: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 40.72  E-value: 2.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  21 KQIVSAVAHCHQS---AIVLGDLKLRKfVFSTEERT--------QLRLESLEDTHIMkgeddalSDKHGCPAYVSPEILn 89
Cdd:cd14066  100 KGIARGLEYLHEEcppPIIHGDIKSSN-ILLDEDFEpkltdfglARLIPPSESVSKT-------SAVKGTIGYLAPEYI- 170
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 545477471  90 TTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIR 131
Cdd:cd14066  171 RTGRVSTKS-DVYSFGVVLLELLTGKPAVDENRENASRKDLV 211
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
4-166 2.85e-04

Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRKs are also classified as ROCO proteins because they contain a ROC (Ras of complex proteins)/GTPase domain followed by a COR (C-terminal of ROC) domain of unknown function. In addition, LRRKs contain a catalytic kinase domain and protein-protein interaction motifs including a WD40 domain, LRRs and ankyrin (ANK) repeats. LRRKs possess both GTPase and kinase activities, with the ROC domain acting as a molecular switch for the kinase domain, cycling between a GTP-bound state which drives kinase activity and a GDP-bound state which decreases the activity. Vertebrates contain two members, LRRK1 and LRRK2, which show complementary expression in the brain. Mutations in LRRK2 are linked to both familial and sporadic forms of Parkinson's disease. The normal roles of LRRKs are not clearly defined. They may be involved in mitogen-activated protein kinase (MAPK) pathways, protein translation control, programmed cell death pathways, and cytoskeletal dynamics. The LRRK 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: 270902 [Multi-domain]  Cd Length: 275  Bit Score: 40.68  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLRLESLEDTHIMKGE-DDALSDKHGCPAY 82
Cdd:cd14000  102 DSRSFASLGRTLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVWTLYPNSAIIIKIADYGISRQCcRMGAKGSEGTPGF 181
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILNTTGTYSGKAaDVWSLGVMLYTLLVGRYPF--HDSDPSAL-FSKIRRGQFCIPEHISPKaRC--LIRSLLRREP 157
Cdd:cd14000  182 RAPEIARGNVIYNEKV-DVFSFGMLLYEILSGGAPMvgHLKFPNEFdIHGGLRPPLKQYECAPWP-EVevLMKKCWKENP 259

                 ....*....
gi 545477471 158 SERLTAPEI 166
Cdd:cd14000  260 QQRPTAVTV 268
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
78-138 3.08e-04

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK4 is a mitogen-activated protein kinase kinase kinase (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The specific function of MLK4 is yet to be determined. Mutations in the kinase domain of MLK4 have been detected in colorectal cancers. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK4 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: 271048 [Multi-domain]  Cd Length: 268  Bit Score: 40.41  E-value: 3.08e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545477471  78 GCPAYVSPEILNTTgTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIP 138
Cdd:cd14146  173 GTYAWMAPEVIKSS-LFS-KGSDIWSYGVLLWELLTGEVPYRGIDGLAVAYGVAVNKLTLP 231
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
81-172 3.30e-04

Catalytic domain of Male germ cell-Associated 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 of human MAK and MAK-related kinase (MRK), Saccharomyces cerevisiae Ime2p, Schizosaccharomyces pombe Mei4-dependent protein 3 (Mde3) and Pit1, Caenorhabditis elegans dyf-5, Arabidopsis thaliana MHK, and similar proteins. These proteins play important roles during meiosis. MAK is highly expressed in testicular cells specifically in the meiotic phase, but is not essential for spermatogenesis and fertility. It functions as a coactivator of the androgen receptor in prostate cells. MRK, also called Intestinal Cell Kinase (ICK), is expressed ubiquitously, with highest expression in the ovary and uterus. A missense mutation in MRK causes endocrine-cerebro-osteodysplasia, suggesting that this protein plays an important role in the development of many organs. MAK and MRK may be involved in regulating cell cycle and cell fate. Ime2p is a meiosis-specific kinase that is important during meiotic initiation and during the later stages of meiosis. Mde3 functions downstream of the transcription factor Mei-4 which is essential for meiotic prophase I. The MAK-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: 270824 [Multi-domain]  Cd Length: 283  Bit Score: 40.59  E-value: 3.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 AYVS------PEILNTTGTYSgKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI-------------------RRGQF 135
Cdd:cd07830  157 DYVStrwyraPEILLRSTSYS-SPVDIWALGCIMAELYTLRPLFPGSSEIDQLYKIcsvlgtptkqdwpegyklaSKLGF 235
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 545477471 136 CIPE-----------HISPKARCLIRSLLRREPSERLTAPEILLHPWF 172
Cdd:cd07830  236 RFPQfaptslhqlipNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
78-138 3.69e-04

Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLK3 is a mitogen-activated protein kinase kinase kinases (MAP3K, MKKK, MAPKKK), which phosphorylates and activates MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. MLK3 activates multiple MAPK pathways and plays a role in apoptosis, proliferation, migration, and differentiation, depending on the cellular context. It is highly expressed in breast cancer cells and its signaling through c-Jun N-terminal kinase has been implicated in the migration, invasion, and malignancy of cancer cells. MLK3 also functions as a negative regulator of Inhibitor of Nuclear Factor-KappaB Kinase (IKK) and consequently, it also impacts inflammation and immunity. Mammals have four MLKs, mostly conserved in vertebrates, which contain an SH3 domain, a catalytic kinase domain, a leucine zipper, a proline-rich region, and a CRIB domain that mediates binding to GTP-bound Cdc42 and Rac. MLKs play roles in immunity and inflammation, as well as in cell death, proliferation, and cell cycle regulation.The MLK3 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: 271049 [Multi-domain]  Cd Length: 267  Bit Score: 40.40  E-value: 3.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 545477471  78 GCPAYVSPEILNTTgTYsGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQFCIP 138
Cdd:cd14147  172 GTYAWMAPEVIKAS-TF-SKGSDVWSFGVLLWELLTGEVPYRGIDCLAVAYGVAVNKLTLP 230
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
8-171 3.78e-04

Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. They activate the MAPKs, p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating the respective MAP/ERK kinases (MEKs, also known as MKKs or MAPKKs), MEK3/MEK6 and MKK4/MKK7. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. Vertebrates contain three TAO subfamily members, named TAO1, TAO2, and TAO3. The TAO 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: 270784 [Multi-domain]  Cd Length: 258  Bit Score: 40.13  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   8 RKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLESLEDTHIMKGEDDALsdkhGCPAYVSPEI 87
Cdd:cd06607   95 KKPLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLT--EPGTVKLADFGSASLVCPANSFV----GTPYWMAPEV 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  88 LNTT--GTYSGKAaDVWSLGVMLYTLLVGRYP-FHDSDPSALFSkirrgqfcIPEHISPKA---------RCLIRSLLRR 155
Cdd:cd06607  169 ILAMdeGQYDGKV-DVWSLGITCIELAERKPPlFNMNAMSALYH--------IAQNDSPTLssgewsddfRNFVDSCLQK 239
                        170
                 ....*....|....*.
gi 545477471 156 EPSERLTAPEILLHPW 171
Cdd:cd06607  240 IPQDRPSAEDLLKHPF 255
PK_ILK cd14057
Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to ...
80-160 3.81e-04

Pseudokinase domain of Integrin Linked Kinase; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. ILK contains N-terminal ankyrin repeats, a Pleckstrin Homology (PH) domain, and a C-terminal pseudokinase domain. It is a component of the IPP (ILK/PINCH/Parvin) complex that couples beta integrins to the actin cytoskeleton, and plays important roles in cell adhesion, spreading, invasion, and migration. ILK was initially thought to be an active kinase despite the lack of key conserved residues because of in vitro studies showing that it can phosphorylate certain protein substrates. However, in vivo experiments in Caenorhabditis elegans, Drosophila melanogaster, and mice (ILK-null and knock-in) proved that ILK is not an active kinase. In addition to actin cytoskeleton regulation, ILK also influences the microtubule network and mitotic spindle orientation. The pseudokinase domain of ILK binds several adaptor proteins including the parvins and paxillin. The ILK subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270959 [Multi-domain]  Cd Length: 251  Bit Score: 40.16  E-value: 3.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  80 PAYVSPEILNTT-GTYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIR-RG-QFCIPEHISPKARCLIRSLLRRE 156
Cdd:cd14057  155 PAWMAPEALQKKpEDINRRSADMWSFAILLWELVTREVPFADLSNMEIGMKIAlEGlRVTIPPGISPHMCKLMKICMNED 234

                 ....
gi 545477471 157 PSER 160
Cdd:cd14057  235 PGKR 238
YegI COG4248
Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding ...
23-166 4.68e-04

Uncharacterized conserved protein YegI with protein kinase and helix-hairpin-helix DNA-binding domains [General function prediction only];


Pssm-ID: 443390 [Multi-domain]  Cd Length: 476  Bit Score: 40.46  E-value: 4.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  23 IVSAVAHCHQSAIVLGDLKLRKFVFSTEErtqlrLESLEDThimkgedDALSDKH---------GCPAYVSPEILNTTGT 93
Cdd:COG4248  130 LAAAVAALHAAGYVHGDVNPSNILVSDTA-----LVTLIDT-------DSFQVRDpgkvyrcvvGTPEFTPPELQGKSFA 197
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  94 YSGKAA--DVWSLGVMLYTLL-VGRYPF-----HDSDPSALFSKIRRGQFciPEHisPKARCLIRSlLRREPSERLTAPE 165
Cdd:COG4248  198 RVDRTEehDRFGLAVLIFQLLmEGRHPFsgvyqGDGDDPTLEERIAMGHF--VYH--PNRRVLIRP-PPRAIPYEILHPY 272

                 .
gi 545477471 166 I 166
Cdd:COG4248  273 L 273
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
3-173 4.95e-04

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIB myosin is expressed highly in retina. It is also present in the brain and testis. The human class IIIB myosin gene maps to a region that overlaps the locus for Bardet-Biedl syndrome, which is characterized by dysmorphic extremities, retinal dystrophy, obesity, male hypogenitalism, and renal abnormalities. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. They may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. They may also function as cargo carriers during light-dependent translocation, in photoreceptor cells, of proteins such as transducin and arrestin. The class III myosin 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: 270808 [Multi-domain]  Cd Length: 291  Bit Score: 39.98  E-value: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLR----LESLEDTHIMKgeddalSDKHG 78
Cdd:cd06639  117 GLLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVdfgvSAQLTSARLRR------NTSVG 190
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  79 CPAYVSPEILNTTGTYSGK---AADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRGQfcIPEHISPKARC-----LIR 150
Cdd:cd06639  191 TPFWMAPEVIACEQQYDYSydaRCDVWSLGITAIELADGDPPLFDMHPVKALFKIPRNP--PPTLLNPEKWCrgfshFIS 268
                        170       180
                 ....*....|....*....|...
gi 545477471 151 SLLRREPSERLTAPEILLHPWFE 173
Cdd:cd06639  269 QCLIKDFEKRPSVTHLLEHPFIK 291
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
4-169 5.11e-04

N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Class IIIA myosin is highly expressed in retina and in inner ear hair cells. It is localized to the distal ends of actin-bundled structures. Mutations in human myosin IIIA are responsible for progressive nonsyndromic hearing loss. Human myosin IIIA possesses ATPase and kinase activities, and the ability to move actin filaments in a motility assay. It may function as a cellular transporter capable of moving along actin bundles in sensory cells. Class III myosins are motor proteins containing an N-terminal kinase catalytic domain and a C-terminal actin-binding domain. Class III myosins may play an important role in maintaining the structural integrity of photoreceptor cell microvilli. In photoreceptor cells, they may also function as cargo carriers during light-dependent translocation of proteins such as transducin and arrestin. The class III myosin 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: 132969 [Multi-domain]  Cd Length: 286  Bit Score: 39.99  E-value: 5.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLR----LESLEDTHIMKgeddalSDKHGC 79
Cdd:cd06638  114 FLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVdfgvSAQLTSTRLRR------NTSVGT 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  80 PAYVSPEIL----NTTGTYSGKAaDVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG---QFCIPEHISPKARCLIRSL 152
Cdd:cd06638  188 PFWMAPEVIaceqQLDSTYDARC-DVWSLGITAIELGDGDPPLADLHPMRALFKIPRNpppTLHQPELWSNEFNDFIRKC 266
                        170
                 ....*....|....*..
gi 545477471 153 LRREPSERLTAPEILLH 169
Cdd:cd06638  267 LTKDYEKRPTVSDLLQH 283
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
9-170 5.22e-04

Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of fungal Wee1 proteins, also called Swe1 in budding yeast and Mik1 in fission yeast. Yeast Wee1 is required to control cell size. Wee1 is a cell cycle checkpoint kinase that helps keep the cyclin-dependent kinase CDK1 in an inactive state through phosphorylation of an N-terminal tyr (Y15) residue. During the late G2 phase, CDK1 is activated and mitotic entry is promoted by the removal of this inhibitory phosphorylation by the phosphatase Cdc25. Although Wee1 is functionally a tyr kinase, it is more closely related to serine/threonine kinases (STKs). It contains a catalytic kinase domain sandwiched in between N- and C-terminal regulatory domains. It is regulated by phosphorylation and degradation, and its expression levels are also controlled by circadian clock proteins. The fungal Wee1 subfamily is part of a larger superfamily that includes the catalytic domains of STKs, other PTKs, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270954 [Multi-domain]  Cd Length: 278  Bit Score: 39.71  E-value: 5.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   9 KRLREeeaARLFKQIV---SAVAHCHQSAIVLGDLKLRKfVFSTEERTqLRL------ESLEDTHIMKGEDDAlsdkhgc 79
Cdd:cd14052  101 GRLDE---FRVWKILVelsLGLRFIHDHHFVHLDLKPAN-VLITFEGT-LKIgdfgmaTVWPLIRGIEREGDR------- 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  80 pAYVSPEILnTTGTYsGKAADVWSLGVMLY----------------TLLVGRYPFHDSDPSALFSKIRRGQFCIPEHISP 143
Cdd:cd14052  169 -EYIAPEIL-SEHMY-DKPADIFSLGLILLeaaanvvlpdngdawqKLRSGDLSDAPRLSSTDLHSASSPSSNPPPDPPN 245
                        170       180       190
                 ....*....|....*....|....*....|...
gi 545477471 144 KAR------CLIRSLLRREPSERLTAPEILLHP 170
Cdd:cd14052  246 MPIlsgsldRVVRWMLSPEPDRRPTADDVLATP 278
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
22-128 5.47e-04

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Mutations in the gene encoding CDKL5, previously called STK9, are associated with early onset epilepsy and severe mental retardation [X-linked infantile spasm syndrome (ISSX) or West syndrome]. In addition, CDKL5 mutations also sometimes cause a phenotype similar to Rett syndrome (RTT), a progressive neurodevelopmental disorder. These pathogenic mutations are located in the N-terminal portion of the protein within the kinase domain. 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 CDKL5 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: 270838 [Multi-domain]  Cd Length: 287  Bit Score: 39.98  E-value: 5.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  22 QIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQLrLESLEDTHIMKGEDDALSDKHGCPAYVSPEILntTGTYSGKAADV 101
Cdd:cd07848  108 QLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKL-CDFGFARNLSEGSNANYTEYVATRWYRSPELL--LGAPYGKAVDM 184
                         90       100
                 ....*....|....*....|....*...
gi 545477471 102 WSLGVMLYTLLVGRYPF-HDSDPSALFS 128
Cdd:cd07848  185 WSVGCILGELSDGQPLFpGESEIDQLFT 212
KIND smart00750
kinase non-catalytic C-lobe domain; It is an interaction domain identified as being similar to ...
2-170 7.01e-04

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


Pssm-ID: 214801  Cd Length: 176  Bit Score: 38.92  E-value: 7.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471     2 HSYVRSRKR-LREEEAArlfkqivsAVahCHQSAIVL-GDLKLRKF--VFSTEERtqlrLESLEDTHIMKGEDDALSDkh 77
Cdd:smart00750   4 ADILEVRGRpLNEEEIW--------AV--CLQCLGALrELHRQAKSgnILLTWDG----LLKLDGSVAFKTPEQSRPD-- 67
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471    78 gcPAYVSPEILntTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDP-----SALFSKIRR---GQFCIPEHIS--PKARC 147
Cdd:smart00750  68 --PYFMAPEVI--QGQSYTEKADIYSLGITLYEALDYELPYNEERElsailEILLNGMPAddpRDRSNLEGVSaaRSFED 143
                          170       180
                   ....*....|....*....|...
gi 545477471   148 LIRSLLRREPSERLTAPEILLHP 170
Cdd:smart00750 144 FMRLCASRLPQRREAANHYLAHC 166
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
84-165 8.96e-04

Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They are PTKs, catalyzing the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jaks are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Most Jaks are expressed in a wide variety of tissues, except for Jak3, which is expressed only in hematopoietic cells. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). Jaks are also involved in regulating the surface expression of some cytokine receptors. The Jak-STAT pathway is involved in many biological processes including hematopoiesis, immunoregulation, host defense, fertility, lactation, growth, and embryogenesis. The Jak subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 39.29  E-value: 8.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  84 SPEILNTTGTYSgkAADVWSLGVMLYTLLVgrYPFHDSDPSALFSKIRRgqfciPEHISPKARCLIRSLlrrEPSERLTA 163
Cdd:cd05038  180 APECLRESRFSS--ASDVWSFGVTLYELFT--YGDPSQSPPALFLRMIG-----IAQGQMIVTRLLELL---KSGERLPR 247

                 ..
gi 545477471 164 PE 165
Cdd:cd05038  248 PP 249
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
78-172 1.05e-03

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 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: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 38.93  E-value: 1.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  78 GCPAYVSPEILNTtgtYSGKAADVWSLGVMLYTLLVGRYPFHDSDPSA-LFSKIRRG--QFCIPEHISPKARCLIRSLLR 154
Cdd:cd14031  176 GTPEFMAPEMYEE---HYDESVDVYAFGMCMLEMATSEYPYSECQNAAqIYRKVTSGikPASFNKVTDPEVKEIIEGCIR 252
                         90
                 ....*....|....*...
gi 545477471 155 REPSERLTAPEILLHPWF 172
Cdd:cd14031  253 QNKSERLSIKDLLNHAFF 270
PTKc_Aatyk3 cd14206
Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs ...
18-134 1.09e-03

Catalytic domain of the Protein Tyrosine Kinases, Apoptosis-associated tyrosine kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Aatyk3, also called lemur tyrosine kinase 3 (Lmtk3) is a receptor kinase containing a transmembrane segment and a long C-terminal cytoplasmic tail with a catalytic domain. The function of Aatyk3 is still unknown. The Aatyk3 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 271108 [Multi-domain]  Cd Length: 276  Bit Score: 38.78  E-value: 1.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  18 RLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEerTQLRLESLEDTHIMKGEDDALS-DKHGCP-AYVSPEIL-----NT 90
Cdd:cd14206  111 RMAYEITLGLLHLHKNNYIHSDLALRNCLLTSD--LTVRIGDYGLSHNNYKEDYYLTpDRLWIPlRWVAPELLdelhgNL 188
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 545477471  91 TGTYSGKAADVWSLGVMLYTLL-VGRYPF-HDSDPSALFSKIRRGQ 134
Cdd:cd14206  189 IVVDQSKESNVWSLGVTIWELFeFGAQPYrHLSDEEVLTFVVREQQ 234
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
84-167 1.35e-03

Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. Protein kinases catalyze the transfer of the gamma phosphate from nucleotide triphosphates (often ATP) to one or more amino acid residues in a protein substrate side chain, resulting in a conformational change affecting protein function. Phosphoprotein phosphatases catalyze the reverse process. Protein kinases fall into three broad classes, characterized with respect to substrate specificity; Serine/threonine-protein kinases, tyrosine-protein kinases, and dual specificity protein kinases (e.g. MEK - phosphorylates both Thr and Tyr on target proteins). This entry represents the catalytic domain found in a number of serine/threonine- and tyrosine-protein kinases. It does not include the catalytic domain of dual specificity kinases.


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 38.63  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   84 SPEILNTtGTYSGKAaDVWSLGVMLYTLL-VGRYPFHDSDPSALFSKIRRGQFC-IPEHISPKARCLIRSLLRREPSERL 161
Cdd:pfam07714 172 APESLKD-GKFTSKS-DVWSFGVLLWEIFtLGEQPYPGMSNEEVLEFLEDGYRLpQPENCPDELYDLMKQCWAYDPEDRP 249

                  ....*.
gi 545477471  162 TAPEIL 167
Cdd:pfam07714 250 TFSELV 255
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
4-169 1.52e-03

Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Itk, also known as Tsk or Emt, is a member of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Itk contains the Tec homology (TH) domain containing one proline-rich region and a zinc-binding region. Itk is expressed in T-cells and mast cells, and is important in their development and differentiation. Of the three Tec kinases expressed in T-cells, Itk plays the predominant role in T-cell receptor (TCR) signaling. It is activated by phosphorylation upon TCR crosslinking and is involved in the pathway resulting in phospholipase C-gamma1 activation and actin polymerization. It also plays a role in the downstream signaling of the T-cell costimulatory receptor CD28, the T-cell surface receptor CD2, and the chemokine receptor CXCR4. In addition, Itk is crucial for the development of T-helper(Th)2 effector responses. The Itk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 38.39  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   4 YVRSRK-RLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSteERTQLRLESLEDTHIMKgeDDALSDKHGCP-- 80
Cdd:cd05112   89 YLRTQRgLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVG--ENQVVKVSDFGMTRFVL--DDQYTSSTGTKfp 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  81 -AYVSPEILnTTGTYSGKAaDVWSLGVMLYTLLV-GRYPFHDSDPSALFSKIRRGQFCIPEHISPKARCLIRSLLRREPS 158
Cdd:cd05112  165 vKWSSPEVF-SFSRYSSKS-DVWSFGVLMWEVFSeGKIPYENRSNSEVVEDINAGFRLYKPRLASTHVYEIMNHCWKERP 242
                        170
                 ....*....|.
gi 545477471 159 ERLTAPEILLH 169
Cdd:cd05112  243 EDRPSFSLLLR 253
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
1-133 1.56e-03

Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. KSR2 interacts with the protein phosphatase calcineurin and functions in calcium-mediated ERK signaling. It also functions in energy metabolism by regulating AMP kinase and AMPK-dependent processes such as glucose uptake and fatty acid oxidation. KSR proteins act as scaffold proteins that function downstream of Ras and upstream of Raf in the Extracellular signal-Regulated Kinase (ERK) pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. KSR proteins regulate the assembly and activation of the Raf/MEK/ERK module upon Ras activation at the membrane by direct association of its components. They are widely regarded as pseudokinases. The KSR2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 38.45  E-value: 1.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   1 MHSYVRSRKRLREEEAARLFKQ-IVSAVAHCHQSAIVLGDLKlRKFVFSTEER---TQLRLESLEDTHIMKGEDDALSDK 76
Cdd:cd14153   83 LYSVVRDAKVVLDVNKTRQIAQeIVKGMGYLHAKGILHKDLK-SKNVFYDNGKvviTDFGLFTISGVLQAGRREDKLRIQ 161
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 545477471  77 HGCPAYVSPEILNTTGTYS-------GKAADVWSLGVMLYTLLVGRYPFHDSDPSALFSKIRRG 133
Cdd:cd14153  162 SGWLCHLAPEIIRQLSPETeedklpfSKHSDVFAFGTIWYELHAREWPFKTQPAEAIIWQVGSG 225
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
21-172 1.74e-03

Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called U2AF homology motif (UHM) kinase 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. KIS (or UHMK1) contains an N-terminal kinase domain and a C-terminal domain with a UHM motif, a protein interaction motif initially found in the pre-mRNA splicing factor U2AF. It phosphorylates the splicing factor SF1, which enhances binding to the splice site to promote spliceosome assembly. KIS was first identified as a kinase that interacts with stathmin, a phosphoprotein that plays a role in axon development and microtubule dynamics. It localizes in RNA granules in neurons and is important in neurite outgrowth. The KIS/UHMK1 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: 270922 [Multi-domain]  Cd Length: 285  Bit Score: 38.38  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  21 KQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTqlrlesledthiMKGEDDALSDKHG--------CPAYVSPEI----- 87
Cdd:cd14020  117 RDVLEALAFLHHEGYVHADLKPRNILWSAEDEC------------FKLIDFGLSFKEGnqdvkyiqTDGYRAPEAelqnc 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  88 LNTTGTYS----GKAADVWSLGVMLYTLLVGRYPFH-------DSDPSALFSKIRRGQFCIPEHISP-KARCLIRSLLRR 155
Cdd:cd14020  185 LAQAGLQSetecTSAVDLWSLGIVLLEMFSGMKLKHtvrsqewKDNSSAIIDHIFASNAVVNPAIPAyHLRDLIKSMLHN 264
                        170
                 ....*....|....*..
gi 545477471 156 EPSERLTAPEILLHPWF 172
Cdd:cd14020  265 DPGKRATAEAALCSPFF 281
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
11-132 2.40e-03

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKbeta is involved in the classical pathway of regulating Nuclear Factor-KappaB (NF-kB) proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. The classical pathway regulates the majority of genes activated by NF-kB including those encoding cytokines, chemokines, leukocyte adhesion molecules, and anti-apoptotic factors. It involves NEMO (NF-kB Essential MOdulator)- and IKKbeta-dependent phosphorylation and degradation of the Inhibitor of NF-kB (IkB), which liberates NF-kB dimers (typified by the p50-p65 heterodimer) from an inactive IkB/dimeric NF-kB complex, enabling them to migrate to the nucleus where they regulate gene transcription. The IKKbeta 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: 270940 [Multi-domain]  Cd Length: 290  Bit Score: 38.02  E-value: 2.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEErtQLRLESLEDTHIMKGEDDA--LSDKHGCPAYVSPEIL 88
Cdd:cd14038   98 LREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQQGE--QRLIHKIIDLGYAKELDQGslCTSFVGTLQYLAPELL 175
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 545477471  89 NTTgTYSgKAADVWSLGVMLYTLLVGRYPFHDS-DPSALFSKIRR 132
Cdd:cd14038  176 EQQ-KYT-VTVDYWSFGTLAFECITGFRPFLPNwQPVQWHGKVRQ 218
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
99-166 2.47e-03

Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. RET is a receptor PTK (RTK) containing an extracellular region with four cadherin-like repeats, a calcium-binding site, and a cysteine-rich domain, a transmembrane segment, and an intracellular catalytic domain. It is part of a multisubunit complex that binds glial-derived neurotropic factor (GDNF) family ligands (GFLs) including GDNF, neurturin, artemin, and persephin. GFLs bind RET along with four GPI-anchored coreceptors, bringing two RET molecules together, leading to autophosphorylation, activation, and intracellular signaling. RET is essential for the development of the sympathetic, parasympathetic and enteric nervous systems, and the kidney. RET disruption by germline mutations causes diseases in humans including congenital aganglionosis of the gastrointestinal tract (Hirschsprung's disease) and three related inherited cancers: multiple endocrine neoplasia type 2A (MEN2A), MEN2B, and familial medullary thyroid carcinoma. The RET subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 38.02  E-value: 2.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  99 ADVWSLGVMLYTLL-VGRYPFHDSDPSALFSKIRRG-QFCIPEHISPKARCLIRSLLRREPSERLTAPEI 166
Cdd:cd05045  210 SDVWSFGVLLWEIVtLGGNPYPGIAPERLFNLLKTGyRMERPENCSEEMYNLMLTCWKQEPDKRPTFADI 279
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
82-175 2.53e-03

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK 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: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 37.84  E-value: 2.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  82 YVSPEILNTTGTYSGKAADVWSLGVMLYTLLVGRYPF------HDSD---------PSALFSKIR-----------RGQF 135
Cdd:cd07859  172 YRAPELCGSFFSKYTPAIDIWSIGCIFAEVLTGKPLFpgknvvHQLDlitdllgtpSPETISRVRnekarrylssmRKKQ 251
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 545477471 136 CIP-----EHISPKARCLIRSLLRREPSERLTAPEILLHPWFESV 175
Cdd:cd07859  252 PVPfsqkfPNADPLALRLLERLLAFDPKDRPTAEEALADPYFKGL 296
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
11-118 2.94e-03

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 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: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 37.86  E-value: 2.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  11 LREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSTEERTQlRLESLEDTHIMK--GEDDALSDKHGCPAYVSPEIL 88
Cdd:cd13988   93 LPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRVIGEDGQ-SVYKLTDFGAARelEDDEQFVSLYGTEEYLHPDMY 171
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 545477471  89 ------NTTGTYSGKAADVWSLGVMLYTLLVGRYPF 118
Cdd:cd13988  172 eravlrKDHQKKYGATVDLWSIGVTFYHAATGSLPF 207
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
3-166 3.05e-03

Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. FAK is a cytoplasmic (or nonreceptor) PTK that contains an autophosphorylation site and a FERM domain at the N-terminus, a central tyr kinase domain, proline-rich regions, and a C-terminal FAT (focal adhesion targeting) domain. FAK activity is dependent on integrin-mediated cell adhesion, which facilitates N-terminal autophosphorylation. Full activation is achieved by the phosphorylation of its two adjacent A-loop tyrosines. FAK is important in mediating signaling initiated at sites of cell adhesions and at growth factor receptors. Through diverse molecular interactions, FAK functions as a biosensor or integrator to control cell motility. It is a key regulator of cell survival, proliferation, migration and invasion, and thus plays an important role in the development and progression of cancer. Src binds to autophosphorylated FAK forming the FAK-Src dual kinase complex, which is activated in a wide variety of tumor cells and generates signals promoting growth and metastasis. FAK is being developed as a target for cancer therapy. The FAK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 37.40  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471   3 SYVRSRKRLREEEAARlfkQIVSAVAHChqsaIVLGDLKLRKFvfsteertqlrlesLEDTHIMKGEDDALSDKhgcpaY 82
Cdd:cd05056  121 AYLESKRFVHRDIAAR---NVLVSSPDC----VKLGDFGLSRY--------------MEDESYYKASKGKLPIK-----W 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  83 VSPEILN----TTgtysgkAADVWSLGV-MLYTLLVGRYPFHDSDPSALFSKIRRGQ-FCIPEHISPKARCLIRSLLRRE 156
Cdd:cd05056  175 MAPESINfrrfTS------ASDVWMFGVcMWEILMLGVKPFQGVKNNDVIGRIENGErLPMPPNCPPTLYSLMTKCWAYD 248
                        170
                 ....*....|
gi 545477471 157 PSERLTAPEI 166
Cdd:cd05056  249 PSKRPRFTEL 258
pknD PRK13184
serine/threonine-protein kinase PknD;
18-143 3.64e-03

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 37.83  E-value: 3.64e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 545477471  18 RLFKQIVSAVAHCHQSAIVLGDLK-----LRKF-----------VFSTEERTQLRLESLEDTHIMKGEDDALSDKHGCPA 81
Cdd:PRK13184 117 SIFHKICATIEYVHSKGVLHRDLKpdnilLGLFgevvildwgaaIFKKLEEEDLLDIDVDERNICYSSMTIPGKIVGTPD 196
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 545477471  82 YVSPEILntTGTYSGKAADVWSLGVMLYTLLVGRYPFHDSDpsalFSKIR-RGQFCIPEHISP 143
Cdd:PRK13184 197 YMAPERL--LGVPASESTDIYALGVILYQMLTLSFPYRRKK----GRKISyRDVILSPIEVAP 253
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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