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Conserved domains on  [gi|1164769387|ref|NP_001336600|]
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ribosomal protein S6 kinase delta-1 isoform d [Homo sapiens]

Protein Classification

STKc_RPK118_like domain-containing protein( domain architecture ID 10144968)

STKc_RPK118_like domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
414-591 2.73e-131

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: 384.98  E-value: 2.73e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 414 DKEIHQIFEDLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSC 493
Cdd:cd05576    88 DKEIHQLFADLDERLAAASRFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSC 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 494 DSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVECHPAGINTHTTLNMPECVSEEARSLIQQLLQFNPLE 573
Cdd:cd05576   168 DSDAIENMYCAPEVGGISEETEACDWWSLGALLFELLTGKALVECHPAGINTHTTLNIPEWVSEEARSLLQQLLQFNPTE 247
                         170
                  ....*....|....*...
gi 1164769387 574 RLGAGVAGVEDIKSHPFF 591
Cdd:cd05576   248 RLGAGVAGVEDIKSHPFF 265
 
Name Accession Description Interval E-value
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
414-591 2.73e-131

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: 384.98  E-value: 2.73e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 414 DKEIHQIFEDLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSC 493
Cdd:cd05576    88 DKEIHQLFADLDERLAAASRFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSC 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 494 DSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVECHPAGINTHTTLNMPECVSEEARSLIQQLLQFNPLE 573
Cdd:cd05576   168 DSDAIENMYCAPEVGGISEETEACDWWSLGALLFELLTGKALVECHPAGINTHTTLNIPEWVSEEARSLLQQLLQFNPTE 247
                         170
                  ....*....|....*...
gi 1164769387 574 RLGAGVAGVEDIKSHPFF 591
Cdd:cd05576   248 RLGAGVAGVEDIKSHPFF 265
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
410-591 1.63e-33

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 128.42  E-value: 1.63e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387  410 VLEGDKEIHQIFE-----DLDKKLAlaSRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF- 483
Cdd:smart00220  65 VFEDEDKLYLVMEyceggDLFDLLK--KRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFg 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387  484 -SRWSEVEDSCDSDAIERMYCAPEVgaITEE--TEACDWWSLGAVLFELLTGKTL--------VECHPAGINTHTTLNMP 552
Cdd:smart00220 143 lARQLDPGEKLTTFVGTPEYMAPEV--LLGKgyGKAVDIWSLGVILYELLTGKPPfpgddqllELFKKIGKPKPPFPPPE 220
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1164769387  553 ECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:smart00220 221 WDISPEAKDLIRKLLVKDPEKRLTA-----EEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
410-591 4.62e-30

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 118.87  E-value: 4.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFE-----DLDKKLALasRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF- 483
Cdd:pfam00069  66 AFEDKDNLYLVLEyveggSLFDLLSE--KGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFg 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 484 -----SRWSEVEDSCDSdaieRMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVechPAGINTHTTLNM------- 551
Cdd:pfam00069 144 larqlNSGSSLTTFVGT----PWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPF---PGINGNEIYELIidqpyaf 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1164769387 552 ---PECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:pfam00069 217 pelPSNLSEEAKDLLKKLLKKDPSKRLTA-----TEALQHPWF 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
355-600 7.60e-28

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 114.53  E-value: 7.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 355 RICSpLSGANEYIAsTDTLKTEEVLLFTdQTDDLAKEepTSLFQRDSETKGESGLV-LEGDKEIHQIFE-----DLDKKL 428
Cdd:PTZ00263   35 RIAK-HKGTGEYYA-IKCLKKREILKMK-QVQHVAQE--KSILMELSHPFIVNMMCsFQDENRVYFLLEfvvggELFTHL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 429 ALASRFyiPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERMYCAPEVG 508
Cdd:PTZ00263  110 RKAGRF--PNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFTLCGTPEYLAPEVI 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 509 AITEETEACDWWSLGAVLFELLTGktlvecHP-----AGINTHTT-----LNMPECVSEEARSLIQQLLQFNPLERLGAG 578
Cdd:PTZ00263  188 QSKGHGKAVDWWTMGVLLYEFIAG------YPpffddTPFRIYEKilagrLKFPNWFDGRARDLVKGLLQTDHTKRLGTL 261
                         250       260
                  ....*....|....*....|..
gi 1164769387 579 VAGVEDIKSHPFFTPVDWAELM 600
Cdd:PTZ00263  262 KGGVADVKNHPYFHGANWDKLY 283
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
436-599 2.01e-17

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 84.41  E-value: 2.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHI----------QLTYFSRWSEVEDSCDSDAIERMYCAP 505
Cdd:COG0515    98 LSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVvklidfglakLLPDPGSTSSIPALPSTSVGTPGYMAP 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 506 EVGAITEE---TEACDWWSLGAVLFELLTGKTLVECHPAGINTHTTL-----------------NMPECVSEEARSLIQQ 565
Cdd:COG0515   178 EVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLkiilelptpslasplspSNPELISKAASDLLKK 257
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1164769387 566 LLQFNPLERLGAGVAGVEDIKSHPFFTPVDWAEL 599
Cdd:COG0515   258 LLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDL 291
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
443-533 5.94e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 49.02  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 443 RWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFsrwsevedscdsdAIER------M-----------YCAP 505
Cdd:NF033483  111 EIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDF-------------GIARalssttMtqtnsvlgtvhYLSP 177
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1164769387 506 EV---GAITEETeacDWWSLGAVLFELLTGK 533
Cdd:NF033483  178 EQargGTVDARS---DIYSLGIVLYEMLTGR 205
 
Name Accession Description Interval E-value
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
414-591 2.73e-131

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: 384.98  E-value: 2.73e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 414 DKEIHQIFEDLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSC 493
Cdd:cd05576    88 DKEIHQLFADLDERLAAASRFYIPEECIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSC 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 494 DSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVECHPAGINTHTTLNMPECVSEEARSLIQQLLQFNPLE 573
Cdd:cd05576   168 DSDAIENMYCAPEVGGISEETEACDWWSLGALLFELLTGKALVECHPAGINTHTTLNIPEWVSEEARSLLQQLLQFNPTE 247
                         170
                  ....*....|....*...
gi 1164769387 574 RLGAGVAGVEDIKSHPFF 591
Cdd:cd05576   248 RLGAGVAGVEDIKSHPFF 265
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
430-591 2.68e-71

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: 229.71  E-value: 2.68e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVE---DSCDSDAIERMYCAPE 506
Cdd:cd05123    84 LSKEGRFPEERARFYAAEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSsdgDRTYTFCGTPEYLAPE 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 507 VGAITEETEACDWWSLGAVLFELLTGKTLVECHPAGINTHT----TLNMPECVSEEARSLIQQLLQFNPLERLGAGvaGV 582
Cdd:cd05123   164 VLLGKGYGKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKilksPLKFPEYVSPEAKSLISGLLQKDPTKRLGSG--GA 241

                  ....*....
gi 1164769387 583 EDIKSHPFF 591
Cdd:cd05123   242 EEIKAHPFF 250
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
409-596 8.90e-40

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: 146.21  E-value: 8.90e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 409 LVLE----GD-KEIHQIFEDLDKKLAlasRFYIpegciqrwaAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF 483
Cdd:cd05579    70 LVMEylpgGDlYSLLENVGALDEDVA---RIYI---------AEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDF 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 484 --SRWSEVEDSCDSDAIERM----------------YCAPEVGAITEETEACDWWSLGAVLFELLTGKT-LVECHPAGIN 544
Cdd:cd05579   138 glSKVGLVRRQIKLSIQKKSngapekedrrivgtpdYLAPEILLGQGHGKTVDWWSLGVILYEFLVGIPpFHAETPEEIF 217
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1164769387 545 THTT---LNMPEC--VSEEARSLIQQLLQFNPLERLGAGvaGVEDIKSHPFFTPVDW 596
Cdd:cd05579   218 QNILngkIEWPEDpeVSDEAKDLISKLLTPDPEKRLGAK--GIEEIKNHPFFKGIDW 272
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
402-601 7.43e-38

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: 142.54  E-value: 7.43e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 402 ETKGESGLVLE----GDkeihqIFEDLDKKLALAS---RFYIpegciqrwaAEMVVALDALHREGIVCRDLNPNNILLND 474
Cdd:cd05582    67 QTEGKLYLILDflrgGD-----LFTRLSKEVMFTEedvKFYL---------AELALALDHLHSLGIIYRDLKPENILLDE 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 475 RGHIQLTYFSRWSEVEDSCDSD-----AIErmYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVEchpaGINTHTTL 549
Cdd:cd05582   133 DGHIKLTDFGLSKESIDHEKKAysfcgTVE--YMAPEVVNRRGHTQSADWWSFGVLMFEMLTGSLPFQ----GKDRKETM 206
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 550 N--------MPECVSEEARSLIQQLLQFNPLERLGAGVAGVEDIKSHPFFTPVDWAELMR 601
Cdd:cd05582   207 TmilkaklgMPQFLSPEAQSLLRALFKRNPANRLGAGPDGVEEIKRHPFFATIDWNKLYR 266
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
446-600 9.07e-35

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: 134.07  E-value: 9.07e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 446 AEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEvedSCDSDAIERMYC------APEVGAITEETEACDW 519
Cdd:cd05584   107 AEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLCKE---SIHDGTVTHTFCgtieymAPEILTRSGHGKAVDW 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 520 WSLGAVLFELLTG----------KTlvechpagINT--HTTLNMPECVSEEARSLIQQLLQFNPLERLGAGVAGVEDIKS 587
Cdd:cd05584   184 WSLGALMYDMLTGappftaenrkKT--------IDKilKGKLNLPPYLTNEARDLLKKLLKRNVSSRLGSGPGDAEEIKA 255
                         170
                  ....*....|...
gi 1164769387 588 HPFFTPVDWAELM 600
Cdd:cd05584   256 HPFFRHINWDDLL 268
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
430-591 2.88e-34

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: 130.98  E-value: 2.88e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDA------IErmYC 503
Cdd:cd05583    90 LYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRAysfcgtIE--YM 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 504 APEV--GAITEETEACDWWSLGAVLFELLTG-----------------KTLVECHPAginthttlnMPECVSEEARSLIQ 564
Cdd:cd05583   168 APEVvrGGSDGHDKAVDWWSLGVLTYELLTGaspftvdgernsqseisKRILKSHPP---------IPKTFSAEAKDFIL 238
                         170       180
                  ....*....|....*....|....*..
gi 1164769387 565 QLLQFNPLERLGAGVAGVEDIKSHPFF 591
Cdd:cd05583   239 KLLEKDPKKRLGAGPRGAHEIKEHPFF 265
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
410-591 1.63e-33

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 128.42  E-value: 1.63e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387  410 VLEGDKEIHQIFE-----DLDKKLAlaSRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF- 483
Cdd:smart00220  65 VFEDEDKLYLVMEyceggDLFDLLK--KRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFg 142
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387  484 -SRWSEVEDSCDSDAIERMYCAPEVgaITEE--TEACDWWSLGAVLFELLTGKTL--------VECHPAGINTHTTLNMP 552
Cdd:smart00220 143 lARQLDPGEKLTTFVGTPEYMAPEV--LLGKgyGKAVDIWSLGVILYELLTGKPPfpgddqllELFKKIGKPKPPFPPPE 220
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1164769387  553 ECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:smart00220 221 WDISPEAKDLIRKLLVKDPEKRLTA-----EEALQHPFF 254
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
432-601 1.84e-33

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: 130.13  E-value: 1.84e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYipegciqrwAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSevEDSCDSDAIERM-----YCAPE 506
Cdd:cd05575    98 ARFY---------AAEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLCK--EGIEPSDTTSTFcgtpeYLAPE 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 507 VGAITEETEACDWWSLGAVLFELLTG------KTLVECHPAGIntHTTLNMPECVSEEARSLIQQLLQFNPLERLGAGvA 580
Cdd:cd05575   167 VLRKQPYDRTVDWWCLGAVLYEMLYGlppfysRDTAEMYDNIL--HKPLRLRTNVSPSARDLLEGLLQKDRTKRLGSG-N 243
                         170       180
                  ....*....|....*....|.
gi 1164769387 581 GVEDIKSHPFFTPVDWAELMR 601
Cdd:cd05575   244 DFLEIKNHSFFRPINWDDLEA 264
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
435-596 6.00e-33

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: 127.21  E-value: 6.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 435 YIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDSCDSDAIERMYCAPEVGAITE 512
Cdd:cd05611    93 GLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFglSRNGLEKRHNKKFVGTPDYLAPETILGVG 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 513 ETEACDWWSLGAVLFELLTGKTlvechPAGINT---------HTTLNMPECV----SEEARSLIQQLLQFNPLERLGAGv 579
Cdd:cd05611   173 DDKMSDWWSLGCVIFEFLFGYP-----PFHAETpdavfdnilSRRINWPEEVkefcSPEAVDLINRLLCMDPAKRLGAN- 246
                         170
                  ....*....|....*..
gi 1164769387 580 aGVEDIKSHPFFTPVDW 596
Cdd:cd05611   247 -GYQEIKSHPFFKSINW 262
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
420-601 1.16e-32

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: 128.20  E-value: 1.16e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 420 IFEdldKKLAlasRFYIpegciqrwaAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFS-----RWSEvedscD 494
Cdd:cd05598    97 IFE---EDLA---RFYI---------AELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGlctgfRWTH-----D 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 495 SDAIERM-------YCAPEVGAITEETEACDWWSLGAVLFELLTGK------TLVECHPAGINTHTTLNMPECV--SEEA 559
Cdd:cd05598   157 SKYYLAHslvgtpnYIAPEVLLRTGYTQLCDWWSVGVILYEMLVGQppflaqTPAETQLKVINWRTTLKIPHEAnlSPEA 236
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1164769387 560 RSLIQQLLQfNPLERLGAGvaGVEDIKSHPFFTPVDWAELMR 601
Cdd:cd05598   237 KDLILRLCC-DAEDRLGRN--GADEIKAHPFFAGIDWEKLRK 275
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
435-601 2.59e-32

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: 126.97  E-value: 2.59e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 435 YIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--------------------SRWSEVED--- 491
Cdd:cd05574    99 RLPEEVARFYAAEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFdlskqssvtpppvrkslrkgSRRSSVKSiek 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 492 ---SCDSDAIERM------YCAPEVGAITEETEACDWWSLGAVLFELLTGKTlvechP-AGINTHTT--------LNMPE 553
Cdd:cd05574   179 etfVAEPSARSNSfvgteeYIAPEVIKGDGHGSAVDWWTLGILLYEMLYGTT-----PfKGSNRDETfsnilkkeLTFPE 253
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1164769387 554 --CVSEEARSLIQQLLQFNPLERLGAGvAGVEDIKSHPFFTPVDWAeLMR 601
Cdd:cd05574   254 spPVSSEAKDLIRKLLVKDPSKRLGSK-RGASEIKRHPFFRGVNWA-LIR 301
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
421-599 1.18e-31

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: 125.86  E-value: 1.18e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 421 FEDLDKKLAlasRFYIpegciqrwaAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLT--------------YFSRW 486
Cdd:cd05573    95 YDVFPEETA---RFYI---------AELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLAdfglctkmnksgdrESYLN 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 487 SEVEDSCDSDAIERM------------------YCAPEVGAITEETEACDWWSLGAVLFELLTG------KTLVECHPAG 542
Cdd:cd05573   163 DSVNTLFQDNVLARRrphkqrrvraysavgtpdYIAPEVLRGTGYGPECDWWSLGVILYEMLYGfppfysDSLVETYSKI 242
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1164769387 543 INTHTTLNMP--ECVSEEARSLIQQLLQfNPLERLGAgvagVEDIKSHPFFTPVDWAEL 599
Cdd:cd05573   243 MNWKESLVFPddPDVSPEAIDLIRRLLC-DPEDRLGS----AEEIKAHPFFKGIDWENL 296
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
428-599 7.87e-31

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: 122.84  E-value: 7.87e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 428 LALASRF--YIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrwsevedSC---DSDAIERM- 501
Cdd:cd05597    89 LTLLSKFedRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLADFG-------SClklREDGTVQSs 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 -------YCAPEVGAITEE------TEaCDWWSLGAVLFELLTGKT------LVECHPAGINTHTTLNMP---ECVSEEA 559
Cdd:cd05597   162 vavgtpdYISPEILQAMEDgkgrygPE-CDWWSLGVCMYEMLYGETpfyaesLVETYGKIMNHKEHFSFPddeDDVSEEA 240
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1164769387 560 RSLIQQLLQfNPLERLGAGvaGVEDIKSHPFFTPVDWAEL 599
Cdd:cd05597   241 KDLIRRLIC-SRERRLGQN--GIDDFKKHPFFEGIDWDNI 277
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
431-599 7.95e-31

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: 122.72  E-value: 7.95e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 431 ASRFYIpegciqrwaAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRwsevedsCDSDAIERM--------- 501
Cdd:cd05599   102 ETRFYI---------AETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGL-------CTGLKKSHLaystvgtpd 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 YCAPEVGAITEETEACDWWSLGAVLFELLTG------KTLVECHPAGINTHTTLNMPECV--SEEARSLIQQLLQfNPLE 573
Cdd:cd05599   166 YIAPEVFLQKGYGKECDWWSLGVIMYEMLIGyppfcsDDPQETCRKIMNWRETLVFPPEVpiSPEAKDLIERLLC-DAEH 244
                         170       180
                  ....*....|....*....|....*.
gi 1164769387 574 RLGAGvaGVEDIKSHPFFTPVDWAEL 599
Cdd:cd05599   245 RLGAN--GVEEIKSHPFFKGVDWDHI 268
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
433-596 1.53e-30

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: 121.15  E-value: 1.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 433 RFyiPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVED-------SCDsdaiermYCAP 505
Cdd:cd05580    97 RF--PNDVAKFYAAEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVKDrtytlcgTPE-------YLAP 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 506 EVGAITEETEACDWWSLGAVLFELLTG--------------KTLvechpAGInthttLNMPECVSEEARSLIQQLLQFNP 571
Cdd:cd05580   168 EIILSKGHGKAVDWWALGILIYEMLAGyppffdenpmkiyeKIL-----EGK-----IRFPSFFDPDAKDLIKRLLVVDL 237
                         170       180
                  ....*....|....*....|....*
gi 1164769387 572 LERLGAGVAGVEDIKSHPFFTPVDW 596
Cdd:cd05580   238 TKRLGNLKNGVEDIKNHPWFAGIDW 262
Pkinase pfam00069
Protein kinase domain;
410-591 4.62e-30

Protein kinase domain;


Pssm-ID: 425449 [Multi-domain]  Cd Length: 254  Bit Score: 118.87  E-value: 4.62e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFE-----DLDKKLALasRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF- 483
Cdd:pfam00069  66 AFEDKDNLYLVLEyveggSLFDLLSE--KGAFSEREAKFIMKQILEGLEYLHSNGIVHRDLKPENILIDEDGNLKITDFg 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 484 -----SRWSEVEDSCDSdaieRMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVechPAGINTHTTLNM------- 551
Cdd:pfam00069 144 larqlNSGSSLTTFVGT----PWYMAPEVLGGNPYGPKVDVWSLGCILYELLTGKPPF---PGINGNEIYELIidqpyaf 216
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1164769387 552 ---PECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:pfam00069 217 pelPSNLSEEAKDLLKKLLKKDPSKRLTA-----TEALQHPWF 254
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
436-599 4.97e-30

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: 119.38  E-value: 4.97e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEdscDSDAIE-RM----YCAPEVGAI 510
Cdd:cd05605    99 FEEERAVFYAAEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIP---EGETIRgRVgtvgYMAPEVVKN 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 511 TEETEACDWWSLGAVLFELLTGKTLVECHPAGINTH--------TTLNMPECVSEEARSLIQQLLQFNPLERLGAGVAGV 582
Cdd:cd05605   176 ERYTFSPDWWGLGCLIYEMIEGQAPFRARKEKVKREevdrrvkeDQEEYSEKFSEEAKSICSQLLQKDPKTRLGCRGEGA 255
                         170
                  ....*....|....*..
gi 1164769387 583 EDIKSHPFFTPVDWAEL 599
Cdd:cd05605   256 EDVKSHPFFKSINFKRL 272
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
436-596 5.12e-30

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: 119.43  E-value: 5.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--------SRWSEV-EDSCDSDAIERM----- 501
Cdd:cd05609    97 LPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFglskiglmSLTTNLyEGHIEKDTREFLdkqvc 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 ----YCAPEVGAITEETEACDWWSLGAVLFELLTGktlveCHPAGINTHTTL------------NMPECVSEEARSLIQQ 565
Cdd:cd05609   177 gtpeYIAPEVILRQGYGKPVDWWAMGIILYEFLVG-----CVPFFGDTPEELfgqvisdeiewpEGDDALPDDAQDLITR 251
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1164769387 566 LLQFNPLERLGAGvaGVEDIKSHPFFTPVDW 596
Cdd:cd05609   252 LLQQNPLERLGTG--GAEEVKQHPFFQDLDW 280
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
430-599 1.43e-29

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: 119.25  E-value: 1.43e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSR----WSEVEDSCDSDAIERMYCAP 505
Cdd:cd05614    96 LYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLskefLTEEKERTYSFCGTIEYMAP 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 506 E-VGAITEETEACDWWSLGAVLFELLTG-----------------KTLVECHPAginthttlnMPECVSEEARSLIQQLL 567
Cdd:cd05614   176 EiIRGKSGHGKAVDWWSLGILMFELLTGaspftlegekntqsevsRRILKCDPP---------FPSFIGPVARDLLQKLL 246
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1164769387 568 QFNPLERLGAGVAGVEDIKSHPFFTPVDWAEL 599
Cdd:cd05614   247 CKDPKKRLGAGPQGAQEIKEHPFFKGLDWEAL 278
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
432-601 5.18e-29

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: 117.32  E-value: 5.18e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYipegciqrwAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRwsevEDSCDsDAIERMYC------ 503
Cdd:cd05570    98 ARFY---------AAEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFgmCK----EGIWG-GNTTSTFCgtpdyi 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 504 APEVGAITEETEACDWWSLGAVLFELLTGKT---------LVEChpagINTHTTLnMPECVSEEARSLIQQLLQFNPLER 574
Cdd:cd05570   164 APEILREQDYGFSVDWWALGVLLYEMLAGQSpfegddedeLFEA----ILNDEVL-YPRWLSREAVSILKGLLTKDPARR 238
                         170       180
                  ....*....|....*....|....*..
gi 1164769387 575 LGAGVAGVEDIKSHPFFTPVDWAELMR 601
Cdd:cd05570   239 LGCGPKGEADIKAHPFFRNIDWDKLEK 265
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
430-599 2.24e-28

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: 115.10  E-value: 2.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEdscdSDAIERM-------- 501
Cdd:cd05613    96 LSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFL----LDENERAysfcgtie 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 YCAPEV--GAITEETEACDWWSLGAVLFELLTGKTlvechPAGI----NTHTTLN---------MPECVSEEARSLIQQL 566
Cdd:cd05613   172 YMAPEIvrGGDSGHDKAVDWWSLGVLMYELLTGAS-----PFTVdgekNSQAEISrrilkseppYPQEMSALAKDIIQRL 246
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1164769387 567 LQFNPLERLGAGVAGVEDIKSHPFFTPVDWAEL 599
Cdd:cd05613   247 LMKDPKKRLGCGPNGADEIKKHPFFQKINWDDL 279
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
440-591 2.91e-28

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: 114.23  E-value: 2.91e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 440 CIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--------SRWSEVEDSCDSDAIERM---------- 501
Cdd:cd05581   102 CTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFgtakvlgpDSSPESTKGDADSQIAYNqaraasfvgt 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 --YCAPEVgaITEE--TEACDWWSLGAVLFELLTGKTLVEchpaGINTHTTL--------NMPECVSEEARSLIQQLLQF 569
Cdd:cd05581   182 aeYVSPEL--LNEKpaGKSSDLWALGCIIYQMLTGKPPFR----GSNEYLTFqkivkleyEFPENFPPDAKDLIQKLLVL 255
                         170       180
                  ....*....|....*....|...
gi 1164769387 570 NPLERLGAG-VAGVEDIKSHPFF 591
Cdd:cd05581   256 DPSKRLGVNeNGGYDELKAHPFF 278
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
438-591 4.11e-28

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: 113.12  E-value: 4.11e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 438 EGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIE--RMYCAPEVGAITEETE 515
Cdd:cd05578    99 EETVKFYICEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLATSTSgtKPYMAPEVFMRAGYSF 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 516 ACDWWSLGAVLFELLTGKTLVECHPAGINT-------HTTLNMPECVSEEARSLIQQLLQFNPLERLGagvaGVEDIKSH 588
Cdd:cd05578   179 AVDWWSLGVTAYEMLRGKRPYEIHSRTSIEeirakfeTASVLYPAGWSEEAIDLINKLLERDPQKRLG----DLSDLKNH 254

                  ...
gi 1164769387 589 PFF 591
Cdd:cd05578   255 PYF 257
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
355-600 7.60e-28

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 114.53  E-value: 7.60e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 355 RICSpLSGANEYIAsTDTLKTEEVLLFTdQTDDLAKEepTSLFQRDSETKGESGLV-LEGDKEIHQIFE-----DLDKKL 428
Cdd:PTZ00263   35 RIAK-HKGTGEYYA-IKCLKKREILKMK-QVQHVAQE--KSILMELSHPFIVNMMCsFQDENRVYFLLEfvvggELFTHL 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 429 ALASRFyiPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERMYCAPEVG 508
Cdd:PTZ00263  110 RKAGRF--PNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAKKVPDRTFTLCGTPEYLAPEVI 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 509 AITEETEACDWWSLGAVLFELLTGktlvecHP-----AGINTHTT-----LNMPECVSEEARSLIQQLLQFNPLERLGAG 578
Cdd:PTZ00263  188 QSKGHGKAVDWWTMGVLLYEFIAG------YPpffddTPFRIYEKilagrLKFPNWFDGRARDLVKGLLQTDHTKRLGTL 261
                         250       260
                  ....*....|....*....|..
gi 1164769387 579 VAGVEDIKSHPFFTPVDWAELM 600
Cdd:PTZ00263  262 KGGVADVKNHPYFHGANWDKLY 283
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
432-601 8.49e-28

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: 113.99  E-value: 8.49e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYipegciqrwAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRwsevedsCDSD----AIERMYC---- 503
Cdd:cd05571    97 TRFY---------GAEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGL-------CKEEisygATTKTFCgtpe 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 504 --APEVGAITEETEACDWWSLGAVLFELLTGKTlvechPAGINTHTTL---------NMPECVSEEARSLIQQLLQFNPL 572
Cdd:cd05571   161 ylAPEVLEDNDYGRAVDWWGLGVVMYEMMCGRL-----PFYNRDHEVLfelilmeevRFPSTLSPEAKSLLAGLLKKDPK 235
                         170       180
                  ....*....|....*....|....*....
gi 1164769387 573 ERLGAGVAGVEDIKSHPFFTPVDWAELMR 601
Cdd:cd05571   236 KRLGGGPRDAKEIMEHPFFASINWDDLYQ 264
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
428-599 3.12e-27

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: 112.40  E-value: 3.12e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 428 LALASRF--YIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrwSEVEDSCDSDAIERM---- 501
Cdd:cd05601    89 LSLLSRYddIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFG--SAAKLSSDKTVTSKMpvgt 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 --YCAPEV----GAITEET--EACDWWSLGAVLFELLTGKT------LVECHPAGINTHTTLNMPE--CVSEEARSLIQQ 565
Cdd:cd05601   167 pdYIAPEVltsmNGGSKGTygVECDWWSLGIVAYEMLYGKTpftedtVIKTYSNIMNFKKFLKFPEdpKVSESAVDLIKG 246
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1164769387 566 LLQfNPLERLgagvaGVEDIKSHPFFTPVDWAEL 599
Cdd:cd05601   247 LLT-DAKERL-----GYEGLCCHPFFSGIDWNNL 274
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
431-596 6.30e-27

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: 110.01  E-value: 6.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 431 ASRFYIpegciqrwaAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDS------CDSDAiermYCA 504
Cdd:cd05572    94 TARFYT---------ACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGrktwtfCGTPE----YVA 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 505 PEVGAITEETEACDWWSLGAVLFELLTGK---TLVECHP--------AGINTHTtlnMPECVSEEARSLIQQLLQFNPLE 573
Cdd:cd05572   161 PEIILNKGYDFSVDYWSLGILLYELLTGRppfGGDDEDPmkiyniilKGIDKIE---FPKYIDKNAKNLIKQLLRRNPEE 237
                         170       180
                  ....*....|....*....|...
gi 1164769387 574 RLGAGVAGVEDIKSHPFFTPVDW 596
Cdd:cd05572   238 RLGYLKGGIRDIKKHKWFEGFDW 260
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
432-601 8.95e-27

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: 110.94  E-value: 8.95e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYipegciqrwAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWseVEDSCDsdaiERM---------Y 502
Cdd:cd05592    98 ARFY---------GAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMC--KENIYG----ENKastfcgtpdY 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 503 CAPEVGAITEETEACDWWSLGAVLFELLTGKT---------LVEChpagiNTHTTLNMPECVSEEARSLIQQLLQFNPLE 573
Cdd:cd05592   163 IAPEILKGQKYNQSVDWWSFGVLLYEMLIGQSpfhgededeLFWS-----ICNDTPHYPRWLTKEAASCLSLLLERNPEK 237
                         170       180
                  ....*....|....*....|....*...
gi 1164769387 574 RLGAGVAGVEDIKSHPFFTPVDWAELMR 601
Cdd:cd05592   238 RLGVPECPAGDIRDHPFFKTIDWDKLER 265
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
417-596 1.63e-26

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: 110.93  E-value: 1.63e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 417 IHQIFEDlDKKL-------------ALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF 483
Cdd:cd05596    91 LHYAFQD-DKYLymvmdympggdlvNLMSNYDVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADF 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 484 SRWSEVEDS----CDSDAIERMYCAPEV----GAITEETEACDWWSLGAVLFELLTGKT------LVECHPAGINTHTTL 549
Cdd:cd05596   170 GTCMKMDKDglvrSDTAVGTPDYISPEVlksqGGDGVYGRECDWWSVGVFLYEMLVGDTpfyadsLVGTYGKIMNHKNSL 249
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1164769387 550 NMPE--CVSEEARSLIQQLLQfNPLERLGAGvaGVEDIKSHPFFTPVDW 596
Cdd:cd05596   250 QFPDdvEISKDAKSLICAFLT-DREVRLGRN--GIEEIKAHPFFKNDQW 295
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
444-601 3.49e-26

Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. cPKCs are potent kinases for histones, myelin basic protein, and protamine. They depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. cPKCs contain a calcium-binding C2 region in their regulatory domain. There are four cPKC isoforms, named alpha, betaI, betaII, and gamma. PKC-gamma is mainly expressed in neuronal tissues. It plays a role in protection from ischemia. 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 cPKC 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: 270739 [Multi-domain]  Cd Length: 320  Bit Score: 109.40  E-value: 3.49e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 444 WAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEvedSCDSDAIERMYC------APEVGAITEETEAC 517
Cdd:cd05587   102 YAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMCKE---GIFGGKTTRTFCgtpdyiAPEIIAYQPYGKSV 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 518 DWWSLGAVLFELLTGKTLVECHP-----AGINTHTtLNMPECVSEEARSLIQQLLQFNPLERLGAGVAGVEDIKSHPFFT 592
Cdd:cd05587   179 DWWAYGVLLYEMLAGQPPFDGEDedelfQSIMEHN-VSYPKSLSKEAVSICKGLLTKHPAKRLGCGPTGERDIKEHPFFR 257

                  ....*....
gi 1164769387 593 PVDWAELMR 601
Cdd:cd05587   258 RIDWEKLER 266
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
444-599 9.66e-26

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: 107.23  E-value: 9.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 444 WAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIqltyfsRWSEVEDSCDSDAIERM--------YCAPEVgaITEE-- 513
Cdd:cd05577   100 YAAEIICGLEHLHNRFIVYRDLKPENILLDDHGHV------RISDLGLAVEFKGGKKIkgrvgthgYMAPEV--LQKEva 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 514 -TEACDWWSLGAVLFELLTGKTLVECHPAGINTHT----TLNM----PECVSEEARSLIQQLLQFNPLERLGAGVAGVED 584
Cdd:cd05577   172 yDFSVDWFALGCMLYEMIAGRSPFRQRKEKVDKEElkrrTLEMaveyPDSFSPEARSLCEGLLQKDPERRLGCRGGSADE 251
                         170
                  ....*....|....*
gi 1164769387 585 IKSHPFFTPVDWAEL 599
Cdd:cd05577   252 VKEHPFFRSLNWQRL 266
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
428-596 3.77e-25

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: 108.17  E-value: 3.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 428 LALASRF--YIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF-SRWSEVEDSCDSDAI---ERM 501
Cdd:cd05624   160 LTLLSKFedKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFgSCLKMNDDGTVQSSVavgTPD 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 YCAPEVGAITEETEA-----CDWWSLGAVLFELLTGKT------LVECHPAGINTHTTLNMPEC---VSEEARSLIQQLL 567
Cdd:cd05624   240 YISPEILQAMEDGMGkygpeCDWWSLGVCMYEMLYGETpfyaesLVETYGKIMNHEERFQFPSHvtdVSEEAKDLIQRLI 319
                         170       180
                  ....*....|....*....|....*....
gi 1164769387 568 qFNPLERLGAGvaGVEDIKSHPFFTPVDW 596
Cdd:cd05624   320 -CSRERRLGQN--GIEDFKKHAFFEGLNW 345
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
444-596 4.50e-25

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: 105.60  E-value: 4.50e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 444 WAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERMYCAPEVGAITEETEACDWWSLG 523
Cdd:cd05612   106 YASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAKKLRDRTWTLCGTPEYLAPEVIQSKGHNKAVDWWALG 185
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1164769387 524 AVLFELLTGK-TLVECHPAGINTHT---TLNMPECVSEEARSLIQQLLQFNPLERLGAGVAGVEDIKSHPFFTPVDW 596
Cdd:cd05612   186 ILIYEMLVGYpPFFDDNPFGIYEKIlagKLEFPRHLDLYAKDLIKKLLVVDRTRRLGNMKNGADDVKNHRWFKSVDW 262
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
411-596 6.55e-25

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: 107.01  E-value: 6.55e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 411 LEGDKEIHQIFE-----DLdkkLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSR 485
Cdd:cd05621   121 FQDDKYLYMVMEympggDL---VNLMSNYDVPEKWAKFYTAEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLADFGT 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 486 WSEVEDS----CDSDAIERMYCAPEV----GAITEETEACDWWSLGAVLFELLTGKT------LVECHPAGINTHTTLNM 551
Cdd:cd05621   198 CMKMDETgmvhCDTAVGTPDYISPEVlksqGGDGYYGRECDWWSVGVFLFEMLVGDTpfyadsLVGTYSKIMDHKNSLNF 277
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1164769387 552 PECV--SEEARSLIQQLLQFNPLeRLGAgvAGVEDIKSHPFFTPVDW 596
Cdd:cd05621   278 PDDVeiSKHAKNLICAFLTDREV-RLGR--NGVEEIKQHPFFRNDQW 321
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
435-601 6.89e-25

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: 105.81  E-value: 6.89e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 435 YIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSE---VEDSCDSDAIERMYCAPEVGAIT 511
Cdd:cd05604    93 SFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLCKEgisNSDTTTTFCGTPEYLAPEVIRKQ 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 512 EETEACDWWSLGAVLFELLTGKTLVEC---HPAGINT-HTTLNMPECVSEEARSLIQQLLQFNPLERLGAGvAGVEDIKS 587
Cdd:cd05604   173 PYDNTVDWWCLGSVLYEMLYGLPPFYCrdtAEMYENIlHKPLVLRPGISLTAWSILEELLEKDRQLRLGAK-EDFLEIKN 251
                         170
                  ....*....|....
gi 1164769387 588 HPFFTPVDWAELMR 601
Cdd:cd05604   252 HPFFESINWTDLVQ 265
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
432-600 8.20e-25

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: 105.35  E-value: 8.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYIpegciqrwaAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWS---EVEDSCDSDAIERMYCAPEVG 508
Cdd:cd05585    96 ARFYT---------AELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKlnmKDDDKTNTFCGTPEYLAPELL 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 509 AITEETEACDWWSLGAVLFELLTGktLVECHPAGINT------HTTLNMPECVSEEARSLIQQLLQFNPLERLGAGvaGV 582
Cdd:cd05585   167 LGHGYTKAVDWWTLGVLLYEMLTG--LPPFYDENTNEmyrkilQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLGYN--GA 242
                         170
                  ....*....|....*...
gi 1164769387 583 EDIKSHPFFTPVDWAELM 600
Cdd:cd05585   243 QEIKNHPFFDQIDWKRLL 260
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
437-599 1.66e-24

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: 103.56  E-value: 1.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 437 PEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEV-EDSCDSDAIERM-YCAPEVGAITEET 514
Cdd:cd05630   100 PEARAVFYAAEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVpEGQTIKGRVGTVgYMAPEVVKNERYT 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 515 EACDWWSLGAVLFELLTGKTLVECHPAGINTHTTLNMPECVSEE--------ARSLIQQLLQFNPLERLGAGVAGVEDIK 586
Cdd:cd05630   180 FSPDWWALGCLLYEMIAGQSPFQQRKKKIKREEVERLVKEVPEEysekfspqARSLCSMLLCKDPAERLGCRGGGAREVK 259
                         170
                  ....*....|...
gi 1164769387 587 SHPFFTPVDWAEL 599
Cdd:cd05630   260 EHPLFKKLNFKRL 272
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
438-601 1.72e-24

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: 103.29  E-value: 1.72e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 438 EGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIqltyfsRWSEVEDSCD-------SDAIERMYCAPEVGAI 510
Cdd:cd05606    97 EAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHV------RISDLGLACDfskkkphASVGTHGYMAPEVLQK 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 511 -TEETEACDWWSLGAVLFELLTGKTLVECHPAG----INTHT-TLN--MPECVSEEARSLIQQLLQFNPLERLGAGVAGV 582
Cdd:cd05606   171 gVAYDSSADWFSLGCMLYKLLKGHSPFRQHKTKdkheIDRMTlTMNveLPDSFSPELKSLLEGLLQRDVSKRLGCLGRGA 250
                         170
                  ....*....|....*....
gi 1164769387 583 EDIKSHPFFTPVDWAELMR 601
Cdd:cd05606   251 TEVKEHPFFKGVDWQQVYL 269
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
432-599 5.10e-24

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: 103.13  E-value: 5.10e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYipegciqrwAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF---SRWSEVEDSCDSDAIERMYCAPEVG 508
Cdd:cd05603    98 ARFY---------AAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFglcKEGMEPEETTSTFCGTPEYLAPEVL 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 509 AITEETEACDWWSLGAVLFELLTG------KTLVECHPAGIntHTTLNMPECVSEEARSLIQQLLQFNPLERLGAgVAGV 582
Cdd:cd05603   169 RKEPYDRTVDWWCLGAVLYEMLYGlppfysRDVSQMYDNIL--HKPLHLPGGKTVAACDLLQGLLHKDQRRRLGA-KADF 245
                         170
                  ....*....|....*..
gi 1164769387 583 EDIKSHPFFTPVDWAEL 599
Cdd:cd05603   246 LEIKNHVFFSPINWDDL 262
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
387-596 6.80e-24

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: 104.33  E-value: 6.80e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 387 DLAKEEPTSLF--QRDSETKGESGLVlegdKEIHQIFEDlDKKLALASRFYI---------------PEGCIQRWAAEMV 449
Cdd:cd05623   109 EMLKRAETACFreERDVLVNGDSQWI----TTLHYAFQD-DNNLYLVMDYYVggdlltllskfedrlPEDMARFYLAEMV 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 450 VALDALHREGIVCRDLNPNNILLNDRGHIQLTYF-SRWSEVEDSCDSDAIERM---YCAPEVGAITEETEA-----CDWW 520
Cdd:cd05623   184 LAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFgSCLKLMEDGTVQSSVAVGtpdYISPEILQAMEDGKGkygpeCDWW 263
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 521 SLGAVLFELLTGKT------LVECHPAGINTHTTLNMPEC---VSEEARSLIQQLLqFNPLERLGAGvaGVEDIKSHPFF 591
Cdd:cd05623   264 SLGVCMYEMLYGETpfyaesLVETYGKIMNHKERFQFPTQvtdVSENAKDLIRRLI-CSREHRLGQN--GIEDFKNHPFF 340

                  ....*
gi 1164769387 592 TPVDW 596
Cdd:cd05623   341 VGIDW 345
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
432-601 7.09e-24

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: 102.78  E-value: 7.09e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYipegciqrwAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEvedSCDSDAIERMYC------AP 505
Cdd:cd05595    97 ARFY---------GAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLCKE---GITDGATMKTFCgtpeylAP 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 506 EVGAITEETEACDWWSLGAVLFELLTGKTlvechPAGINTHTTL---------NMPECVSEEARSLIQQLLQFNPLERLG 576
Cdd:cd05595   165 EVLEDNDYGRAVDWWGLGVVMYEMMCGRL-----PFYNQDHERLfelilmeeiRFPRTLSPEAKSLLAGLLKKDPKQRLG 239
                         170       180
                  ....*....|....*....|....*
gi 1164769387 577 AGVAGVEDIKSHPFFTPVDWAELMR 601
Cdd:cd05595   240 GGPSDAKEVMEHRFFLSINWQDVVQ 264
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
444-599 1.13e-23

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: 101.22  E-value: 1.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 444 WAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDScdsdaiERM--------YCAPEVGAITEETE 515
Cdd:cd05631   107 YAAELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEG------ETVrgrvgtvgYMAPEVINNEKYTF 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 516 ACDWWSLGAVLFELLTGKTLVECHPAGIN--------THTTLNMPECVSEEARSLIQQLLQFNPLERLGAGVAGVEDIKS 587
Cdd:cd05631   181 SPDWWGLGCLIYEMIQGQSPFRKRKERVKreevdrrvKEDQEEYSEKFSEDAKSICRMLLTKNPKERLGCRGNGAAGVKQ 260
                         170
                  ....*....|..
gi 1164769387 588 HPFFTPVDWAEL 599
Cdd:cd05631   261 HPIFKNINFKRL 272
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
432-601 1.84e-23

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: 102.62  E-value: 1.84e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYIpegciqrwaAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERM---------- 501
Cdd:cd05629   103 TRFYM---------AECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTGFHKQHDSAYYQKLlqgksnknri 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 ----------------------------------------YCAPEVGAITEETEACDWWSLGAVLFELLTG------KTL 535
Cdd:cd05629   174 dnrnsvavdsinltmsskdqiatwkknrrlmaystvgtpdYIAPEIFLQQGYGQECDWWSLGAIMFECLIGwppfcsENS 253
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1164769387 536 VECHPAGINTHTTLNMPE--CVSEEARSLIQQLLQfNPLERLGAGvaGVEDIKSHPFFTPVDWAELMR 601
Cdd:cd05629   254 HETYRKIINWRETLYFPDdiHLSVEAEDLIRRLIT-NAENRLGRG--GAHEIKSHPFFRGVDWDTIRQ 318
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
410-590 3.07e-23

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: 99.13  E-value: 3.07e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFE-----DLDKKLAlaSRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF- 483
Cdd:cd14003    67 VIETENKIYLVMEyasggELFDYIV--NNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFg 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 484 -SRWSE----VEDSCDSDAiermYCAPEV-GAITEETEACDWWSLGAVLFELLTGK------TLVECHpaGINTHTTLNM 551
Cdd:cd14003   145 lSNEFRggslLKTFCGTPA----YAAPEVlLGRKYDGPKADVWSLGVILYAMLTGYlpfdddNDSKLF--RKILKGKYPI 218
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1164769387 552 PECVSEEARSLIQQLLQFNPLERLgagvaGVEDIKSHPF 590
Cdd:cd14003   219 PSHLSPDARDLIRRMLVVDPSKRI-----TIEEILNHPW 252
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
423-601 5.68e-23

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: 100.07  E-value: 5.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 423 DLDKKLALASRFYIPEGCIqrWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSE-VEDSCDSDAI--E 499
Cdd:cd05616    87 DLMYHIQQVGRFKEPHAVF--YAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMCKEnIWDGVTTKTFcgT 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 500 RMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVECHP-----AGINTHTtLNMPECVSEEARSLIQQLLQFNPLER 574
Cdd:cd05616   165 PDYIAPEIIAYQPYGKSVDWWAFGVLLYEMLAGQAPFEGEDedelfQSIMEHN-VAYPKSMSKEAVAICKGLMTKHPGKR 243
                         170       180
                  ....*....|....*....|....*..
gi 1164769387 575 LGAGVAGVEDIKSHPFFTPVDWAELMR 601
Cdd:cd05616   244 LGCGPEGERDIKEHAFFRYIDWEKLER 270
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
430-597 8.01e-23

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: 100.85  E-value: 8.01e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDS----CDSDAIERMYCAP 505
Cdd:cd05622   163 LMSNYDVPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCMKMNKEgmvrCDTAVGTPDYISP 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 506 EV----GAITEETEACDWWSLGAVLFELLTGKT------LVECHPAGINTHTTLNMPE--CVSEEARSLIQQLLQFNPLe 573
Cdd:cd05622   243 EVlksqGGDGYYGRECDWWSVGVFLYEMLVGDTpfyadsLVGTYSKIMNHKNSLTFPDdnDISKEAKNLICAFLTDREV- 321
                         170       180
                  ....*....|....*....|....
gi 1164769387 574 RLGAGvaGVEDIKSHPFFTPVDWA 597
Cdd:cd05622   322 RLGRN--GVEEIKRHLFFKNDQWA 343
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
436-591 1.75e-22

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: 96.89  E-value: 1.75e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDaieRM-----YCAPEVGAI 510
Cdd:cd05122    95 LTEQQIAYVCKEVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTRN---TFvgtpyWMAPEVIQG 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 511 TEETEACDWWSLGAVLFELLTGKT-LVECHP------AGINTHTTLNMPECVSEEARSLIQQLLQFNPLERlgagvAGVE 583
Cdd:cd05122   172 KPYGFKADIWSLGITAIEMAEGKPpYSELPPmkalflIATNGPPGLRNPKKWSKEFKDFLKKCLQKDPEKR-----PTAE 246

                  ....*...
gi 1164769387 584 DIKSHPFF 591
Cdd:cd05122   247 QLLKHPFI 254
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
433-589 3.41e-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: 95.03  E-value: 3.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 433 RFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDSCDSDA---IERMYCAPEV 507
Cdd:cd00180    86 KGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFglAKDLDSDDSLLKTTggtTPPYYAPPEL 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 508 GAITEETEACDWWSLGAVLFELltgktlvechpaginthttlnmpecvsEEARSLIQQLLQFNPLERLGAgvagvEDIKS 587
Cdd:cd00180   166 LGGRYYGPKVDIWSLGVILYEL---------------------------EELKDLIRRMLQYDPKKRPSA-----KELLE 213

                  ..
gi 1164769387 588 HP 589
Cdd:cd00180   214 HL 215
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
446-592 9.14e-22

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: 94.85  E-value: 9.14e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 446 AEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrWsevedSCDSDAIERM-------YCAPEVGAITEETEACD 518
Cdd:cd14007   107 YQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFG-W-----SVHAPSNRRKtfcgtldYLPPEMVEGKEYDYKVD 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 519 WWSLGAVLFELLTGKTlvechPAGINTHTT---------LNMPECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHP 589
Cdd:cd14007   181 IWSLGVLCYELLVGKP-----PFESKSHQEtykriqnvdIKFPSSVSPEAKDLISKLLQKDPSKRLSL-----EQVLNHP 250

                  ...
gi 1164769387 590 FFT 592
Cdd:cd14007   251 WIK 253
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
436-599 1.53e-21

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: 96.63  E-value: 1.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAI---ERMYCAPEVGAITE 512
Cdd:cd05617   113 LPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMCKEGLGPGDTTSTfcgTPNYIAPEILRGEE 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 513 ETEACDWWSLGAVLFELLTGKT---LVECHPaGINTHTTL---------NMPECVSEEARSLIQQLLQFNPLERLGAGV- 579
Cdd:cd05617   193 YGFSVDWWALGVLMFEMMAGRSpfdIITDNP-DMNTEDYLfqvilekpiRIPRFLSVKASHVLKGFLNKDPKERLGCQPq 271
                         170       180
                  ....*....|....*....|
gi 1164769387 580 AGVEDIKSHPFFTPVDWAEL 599
Cdd:cd05617   272 TGFSDIKSHTFFRSIDWDLL 291
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
432-600 1.96e-21

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: 95.45  E-value: 1.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYipegciqrwAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAierMYC------AP 505
Cdd:cd05589   103 AVFY---------AACVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLCKEGMGFGDRTS---TFCgtpeflAP 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 506 EVGAITEETEACDWWSLGAVLFELLTGktlvECHPAGINTH----TTLNM----PECVSEEARSLIQQLLQFNPLERLGA 577
Cdd:cd05589   171 EVLTDTSYTRAVDWWGLGVLIYEMLVG----ESPFPGDDEEevfdSIVNDevryPRFLSTEAISIMRRLLRKNPERRLGA 246
                         170       180
                  ....*....|....*....|...
gi 1164769387 578 GVAGVEDIKSHPFFTPVDWAELM 600
Cdd:cd05589   247 SERDAEDVKKQPFFRNIDWEALL 269
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
401-601 2.91e-21

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: 95.85  E-value: 2.91e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 401 SETKGESGLVLEGDKE----IHQIFEDLDK------------KLALASRFYI-PEGCIQRWAAEMVVALDALHREGIVCR 463
Cdd:cd05626    46 AHVKAERDILAEADNEwvvkLYYSFQDKDNlyfvmdyipggdMMSLLIRMEVfPEVLARFYIAELTLAIESVHKMGFIHR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 464 DLNPNNILLNDRGHIQLT---------------YFSR--------------WSEVEDSCDSDAIERM------------- 501
Cdd:cd05626   126 DIKPDNILIDLDGHIKLTdfglctgfrwthnskYYQKgshirqdsmepsdlWDDVSNCRCGDRLKTLeqratkqhqrcla 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 --------YCAPEVGAITEETEACDWWSLGAVLFELLTGK------TLVECHPAGINTHTTLNMPECV--SEEARSLIQQ 565
Cdd:cd05626   206 hslvgtpnYIAPEVLLRKGYTQLCDWWSVGVILFEMLVGQppflapTPTETQLKVINWENTLHIPPQVklSPEAVDLITK 285
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1164769387 566 LLqFNPLERLGAGvaGVEDIKSHPFFTPVDWAELMR 601
Cdd:cd05626   286 LC-CSAEERLGRN--GADDIKAHPFFSEVDFSSDIR 318
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
423-599 3.34e-21

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: 95.06  E-value: 3.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 423 DLDKKLALASRFYIPEGCIqrWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRwsevedsCDSDAIE--- 499
Cdd:cd05615    97 DLMYHIQQVGKFKEPQAVF--YAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGM-------CKEHMVEgvt 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 500 -RMYC------APEVGAITEETEACDWWSLGAVLFELLTGKTLVECHP-----AGINTHTtLNMPECVSEEARSLIQQLL 567
Cdd:cd05615   168 tRTFCgtpdyiAPEIIAYQPYGRSVDWWAYGVLLYEMLAGQPPFDGEDedelfQSIMEHN-VSYPKSLSKEAVSICKGLM 246
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1164769387 568 QFNPLERLGAGVAGVEDIKSHPFFTPVDWAEL 599
Cdd:cd05615   247 TKHPAKRLGCGPEGERDIREHAFFRRIDWDKL 278
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
444-600 4.44e-21

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: 94.70  E-value: 4.44e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 444 WAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSE-VEDSCDSDAI--ERMYCAPEVGAITEETEACDWW 520
Cdd:cd05602   113 YAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLCKEnIEPNGTTSTFcgTPEYLAPEVLHKQPYDRTVDWW 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 521 SLGAVLFELLTG------KTLVECHPAGINthTTLNMPECVSEEARSLIQQLLQFNPLERLGAGVAGVEdIKSHPFFTPV 594
Cdd:cd05602   193 CLGAVLYEMLYGlppfysRNTAEMYDNILN--KPLQLKPNITNSARHLLEGLLQKDRTKRLGAKDDFTE-IKNHIFFSPI 269

                  ....*.
gi 1164769387 595 DWAELM 600
Cdd:cd05602   270 NWDDLI 275
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
436-599 5.09e-21

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: 94.41  E-value: 5.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAI---ERMYCAPEVGAITE 512
Cdd:cd05588    93 LPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTfcgTPNYIAPEILRGED 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 513 ETEACDWWSLGAVLFELLTGKTlvechPAGINTHT------------------TLNMPECVSEEARSLIQQLLQFNPLER 574
Cdd:cd05588   173 YGFSVDWWALGVLMFEMLAGRS-----PFDIVGSSdnpdqntedylfqvilekPIRIPRSLSVKAASVLKGFLNKNPAER 247
                         170       180
                  ....*....|....*....|....*.
gi 1164769387 575 LGAGV-AGVEDIKSHPFFTPVDWAEL 599
Cdd:cd05588   248 LGCHPqTGFADIQSHPFFRTIDWEQL 273
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
436-591 5.37e-21

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: 92.58  E-value: 5.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWseVEDSCDSDAIERM-----YCAPEVG 508
Cdd:cd06606    96 LPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFgcAKR--LAEIATGEGTKSLrgtpyWMAPEVI 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 509 AITEETEACDWWSLGAVLFELLTGKtlvecHP-AGINTHTTL-----------NMPECVSEEARSLIQQLLQFNPLERlg 576
Cdd:cd06606   174 RGEGYGRAADIWSLGCTVIEMATGK-----PPwSELGNPVAAlfkigssgeppPIPEHLSEEAKDFLRKCLQRDPKKR-- 246
                         170
                  ....*....|....*
gi 1164769387 577 agvAGVEDIKSHPFF 591
Cdd:cd06606   247 ---PTADELLQHPFL 258
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
432-600 7.93e-21

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: 92.85  E-value: 7.93e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYipegciqrwAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERMYCAPEVGAIT 511
Cdd:cd14209   103 ARFY---------AAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKGRTWTLCGTPEYLAPEIILSK 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 512 EETEACDWWSLGAVLFELLTGKTlvechPAGINTHTTL---------NMPECVSEEARSLIQQLLQFNPLERLGAGVAGV 582
Cdd:cd14209   174 GYNKAVDWWALGVLIYEMAAGYP-----PFFADQPIQIyekivsgkvRFPSHFSSDLKDLLRNLLQVDLTKRFGNLKNGV 248
                         170
                  ....*....|....*...
gi 1164769387 583 EDIKSHPFFTPVDWAELM 600
Cdd:cd14209   249 NDIKNHKWFATTDWIAIY 266
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
401-601 2.51e-20

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: 93.19  E-value: 2.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 401 SETKGESGLVLEGDKE----IHQIFEDLDK------------KLALASRFYI-PEGCIQRWAAEMVVALDALHREGIVCR 463
Cdd:cd05625    46 AHVKAERDILAEADNEwvvrLYYSFQDKDNlyfvmdyipggdMMSLLIRMGVfPEDLARFYIAELTCAVESVHKMGFIHR 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 464 DLNPNNILLNDRGHIQLTYFS-----RWSE-----------VEDSCD-------------SDAIERM------------- 501
Cdd:cd05625   126 DIKPDNILIDRDGHIKLTDFGlctgfRWTHdskyyqsgdhlRQDSMDfsnewgdpencrcGDRLKPLerraarqhqrcla 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 --------YCAPEVGAITEETEACDWWSLGAVLFELLTG------KTLVECHPAGINTHTTLNMPEC--VSEEARSLIQQ 565
Cdd:cd05625   206 hslvgtpnYIAPEVLLRTGYTQLCDWWSVGVILFEMLVGqppflaQTPLETQMKVINWQTSLHIPPQakLSPEASDLIIK 285
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1164769387 566 LLQfNPLERLGAGvaGVEDIKSHPFFTPVDWAELMR 601
Cdd:cd05625   286 LCR-GPEDRLGKN--GADEIKAHPFFKTIDFSSDLR 318
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
433-601 2.81e-20

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: 91.89  E-value: 2.81e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 433 RFYIPEGCIqrWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSE-VEDSCDSDAI--ERMYCAPEVGA 509
Cdd:cd05590    92 RFDEARARF--YAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMCKEgIFNGKTTSTFcgTPDYIAPEILQ 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 510 ITEETEACDWWSLGAVLFELLTGKTLVECHPAGINTHTTLN----MPECVSEEARSLIQQLLQFNPLERLGAGVAGVED- 584
Cdd:cd05590   170 EMLYGPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNdevvYPTWLSQDAVDILKAFMTKNPTMRLGSLTLGGEEa 249
                         170
                  ....*....|....*..
gi 1164769387 585 IKSHPFFTPVDWAELMR 601
Cdd:cd05590   250 ILRHPFFKELDWEKLNR 266
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
444-599 1.32e-19

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: 90.47  E-value: 1.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 444 WAAEMVVALDALHRE-GIVCRDLNPNNILLNDRGHIQLTYFSRWSE-VEDScdsdAIERMYC------APEVGAITEETE 515
Cdd:cd05594   130 YGAEIVSALDYLHSEkNVVYRDLKLENLMLDKDGHIKITDFGLCKEgIKDG----ATMKTFCgtpeylAPEVLEDNDYGR 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 516 ACDWWSLGAVLFELLTGKTlvechPAGINTHTTL---------NMPECVSEEARSLIQQLLQFNPLERLGAGVAGVEDIK 586
Cdd:cd05594   206 AVDWWGLGVVMYEMMCGRL-----PFYNQDHEKLfelilmeeiRFPRTLSPEAKSLLSGLLKKDPKQRLGGGPDDAKEIM 280
                         170
                  ....*....|...
gi 1164769387 587 SHPFFTPVDWAEL 599
Cdd:cd05594   281 QHKFFAGIVWQDV 293
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
409-599 1.73e-19

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: 90.32  E-value: 1.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 409 LVLE----GD-KEIHQIFEDLDKKLAlasRFYIpegciqrwaAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF 483
Cdd:cd05610    81 LVMEyligGDvKSLLHIYGYFDEEMA---VKYI---------SEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDF 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 484 --SRWSEVEDSCDSDAI-------------------------------------------------ERM-----YCAPEV 507
Cdd:cd05610   149 glSKVTLNRELNMMDILttpsmakpkndysrtpgqvlslisslgfntptpyrtpksvrrgaarvegERIlgtpdYLAPEL 228
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 508 GAITEETEACDWWSLGAVLFELLTGKTLVECHPAGINTHTTLN--MP-----ECVSEEARSLIQQLLQFNPLERlgagvA 580
Cdd:cd05610   229 LLGKPHGPAVDWWALGVCLFEFLTGIPPFNDETPQQVFQNILNrdIPwpegeEELSVNAQNAIEILLTMDPTKR-----A 303
                         250
                  ....*....|....*....
gi 1164769387 581 GVEDIKSHPFFTPVDWAEL 599
Cdd:cd05610   304 GLKELKQHPLFHGVDWENL 322
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
436-599 1.88e-19

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: 90.50  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERM-------------- 501
Cdd:cd05627    99 LSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKKAHRTEFYRNLthnppsdfsfqnmn 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 ------------------------YCAPEVGAITEETEACDWWSLGAVLFELLTG------KTLVECHPAGINTHTTLNM 551
Cdd:cd05627   179 skrkaetwkknrrqlaystvgtpdYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGyppfcsETPQETYRKVMNWKETLVF 258
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1164769387 552 PECV--SEEARSLIQQLLqFNPLERLGAGvaGVEDIKSHPFFTPVDWAEL 599
Cdd:cd05627   259 PPEVpiSEKAKDLILRFC-TDAENRIGSN--GVEEIKSHPFFEGVDWEHI 305
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
433-601 2.02e-19

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: 89.60  E-value: 2.02e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 433 RFYIPEGCIqrWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEvedSCDSDAIERMYC------APE 506
Cdd:cd05619   102 KFDLPRATF--YAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKE---NMLGDAKTSTFCgtpdyiAPE 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 507 VGAITEETEACDWWSLGAVLFELLTGKTLVECHPA-----GINTHTTLnMPECVSEEARSLIQQLLQFNPLERLgaGVAG 581
Cdd:cd05619   177 ILLGQKYNTSVDWWSFGVLLYEMLIGQSPFHGQDEeelfqSIRMDNPF-YPRWLEKEAKDILVKLFVREPERRL--GVRG 253
                         170       180
                  ....*....|....*....|
gi 1164769387 582 veDIKSHPFFTPVDWAELMR 601
Cdd:cd05619   254 --DIRQHPFFREINWEALEE 271
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
444-599 3.40e-19

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: 88.49  E-value: 3.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 444 WAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVE--DSCDSDAIERMYCAPEVGAITEETEACDWWS 521
Cdd:cd05632   109 YAAEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPegESIRGRVGTVGYMAPEVLNNQRYTLSPDYWG 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 522 LGAVLFELLTGKTLVECHPAGIN--------THTTLNMPECVSEEARSLIQQLLQFNPLERLGAGVAGVEDIKSHPFFTP 593
Cdd:cd05632   189 LGCLIYEMIEGQSPFRGRKEKVKreevdrrvLETEEVYSAKFSEEAKSICKMLLTKDPKQRLGCQEEGAGEVKRHPFFRN 268

                  ....*.
gi 1164769387 594 VDWAEL 599
Cdd:cd05632   269 MNFKRL 274
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
432-599 3.73e-19

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: 88.70  E-value: 3.73e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYipegciqrwAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEvedSCDSDAIERMYC------AP 505
Cdd:cd05591    98 ARFY---------AAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMCKE---GILNGKTTTTFCgtpdyiAP 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 506 EVGAITEETEACDWWSLGAVLFELLTGKTLVECHPAGINTHTTLN----MPECVSEEARSLIQQLLQFNPLERLG-AGVA 580
Cdd:cd05591   166 EILQELEYGPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHddvlYPVWLSKEAVSILKAFMTKNPAKRLGcVASQ 245
                         170       180
                  ....*....|....*....|
gi 1164769387 581 GVED-IKSHPFFTPVDWAEL 599
Cdd:cd05591   246 GGEDaIRQHPFFREIDWEAL 265
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
444-601 4.44e-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: 88.46  E-value: 4.44e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 444 WAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEV---EDSCDSDAIERMYCAPEVGAITEETEACDWW 520
Cdd:cd05620   101 YAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENvfgDNRASTFCGTPDYIAPEILQGLKYTFSVDWW 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 521 SLGAVLFELLTGKT---------LVEchpaGINTHTTlNMPECVSEEARSLIQQLLQFNPLERLGAgvagVEDIKSHPFF 591
Cdd:cd05620   181 SFGVLLYEMLIGQSpfhgddedeLFE----SIRVDTP-HYPRWITKESKDILEKLFERDPTRRLGV----VGNIRGHPFF 251
                         170
                  ....*....|
gi 1164769387 592 TPVDWAELMR 601
Cdd:cd05620   252 KTINWTALEK 261
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
402-590 5.19e-19

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: 86.92  E-value: 5.19e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 402 ETKGESGLVLE-GDKEIHQIFEDlDKKLalasrfyiPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQL 480
Cdd:cd14002    70 ETKKEFVVVTEyAQGELFQILED-DGTL--------PEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKL 140
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 481 TYF--SRwsevEDSCDSDAIER-----MYCAPEVgaITEE--TEACDWWSLGAVLFELLTGK---------TLVEchpag 542
Cdd:cd14002   141 CDFgfAR----AMSCNTLVLTSikgtpLYMAPEL--VQEQpyDHTADLWSLGCILYELFVGQppfytnsiyQLVQ----- 209
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1164769387 543 INTHTTLNMPECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPF 590
Cdd:cd14002   210 MIVKDPVKWPSNMSPEFKSFLQGLLNKDPSKRLSW-----PDLLEHPF 252
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
433-599 5.97e-19

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: 88.94  E-value: 5.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 433 RFYIpegciqrwaAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFS----------------RWSEVED----- 491
Cdd:cd05600   114 RFYI---------AEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGlasgtlspkkiesmkiRLEEVKNtafle 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 492 --------------SCDSDAIERM-----YCAPEVGAITEETEACDWWSLGAVLFELLTG------KTLVECHPAGINTH 546
Cdd:cd05600   185 ltakerrniyramrKEDQNYANSVvgspdYMAPEVLRGEGYDLTVDYWSLGCILFECLVGfppfsgSTPNETWANLYHWK 264
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1164769387 547 TTLNMP--------ECVSEEARSLIQQLLQfNPLERLGagvaGVEDIKSHPFFTPVDWAEL 599
Cdd:cd05600   265 KTLQRPvytdpdleFNLSDEAWDLITKLIT-DPQDRLQ----SPEQIKNHPFFKNIDWDRL 320
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
441-591 6.99e-19

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: 86.52  E-value: 6.99e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLN-DRGHIQLTYF--SRWSeVEDSCDSDAIERMYCAPEV--GAiTEETE 515
Cdd:cd05118   103 IKSYLYQLLQALDFLHSNGIIHRDLKPENILINlELGQLKLADFglARSF-TSPPYTPYVATRWYRAPEVllGA-KPYGS 180
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1164769387 516 ACDWWSLGAVLFELLTGKTLVEchpaGINTHTTLNMPECV--SEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd05118   181 SIDIWSLGCILAELLTGRPLFP----GDSEVDQLAKIVRLlgTPEALDLLSKMLKYDPAKRITA-----SQALAHPYF 249
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
444-599 7.50e-19

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: 88.21  E-value: 7.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 444 WAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSE-VEDSCDSDAI--ERMYCAPEVGAITEETEACDWW 520
Cdd:cd05593   120 YGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLCKEgITDAATMKTFcgTPEYLAPEVLEDNDYGRAVDWW 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 521 SLGAVLFELLTGKTlvechPAGINTHTTL---------NMPECVSEEARSLIQQLLQFNPLERLGAGVAGVEDIKSHPFF 591
Cdd:cd05593   200 GLGVVMYEMMCGRL-----PFYNQDHEKLfelilmediKFPRTLSADAKSLLSGLLIKDPNKRLGGGPDDAKEIMRHSFF 274

                  ....*...
gi 1164769387 592 TPVDWAEL 599
Cdd:cd05593   275 TGVNWQDV 282
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
430-574 8.51e-19

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: 86.49  E-value: 8.51e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWseVEDSCDSDAIERM----YC 503
Cdd:cd14014    91 LRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFgiARA--LGDSGLTQTGSVLgtpaYM 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 504 APEVGAITEETEACDWWSLGAVLFELLTGK----------TLVECHPAGINTHTTLNMPecVSEEARSLIQQLLQFNPLE 573
Cdd:cd14014   169 APEQARGGPVDPRSDIYSLGVVLYELLTGRppfdgdspaaVLAKHLQEAPPPPSPLNPD--VPPALDAIILRALAKDPEE 246

                  .
gi 1164769387 574 R 574
Cdd:cd14014   247 R 247
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
438-596 1.72e-18

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: 86.64  E-value: 1.72e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 438 EGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIqltyfsRWSEVEDSCD-------SDAIERMYCAPEV--G 508
Cdd:cd14223   102 EAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHV------RISDLGLACDfskkkphASVGTHGYMAPEVlqK 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 509 AITEETEAcDWWSLGAVLFELLTGKTLVECHPAG-------INTHTTLNMPECVSEEARSLIQQLLQFNPLERLGAGVAG 581
Cdd:cd14223   176 GVAYDSSA-DWFSLGCMLFKLLRGHSPFRQHKTKdkheidrMTLTMAVELPDSFSPELRSLLEGLLQRDVNRRLGCMGRG 254
                         170
                  ....*....|....*
gi 1164769387 582 VEDIKSHPFFTPVDW 596
Cdd:cd14223   255 AQEVKEEPFFRGLDW 269
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
432-599 2.04e-18

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: 86.47  E-value: 2.04e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYIpegciqrwaAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFS-RWSEVEDSCDSDAI--ERMYCAPEVg 508
Cdd:cd05586    98 AKFYI---------AELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGlSKADLTDNKTTNTFcgTTEYLAPEV- 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 509 aITEE---TEACDWWSLGAVLFELLTGKTLVECHpagiNTHT--------TLNMPECV-SEEARSLIQQLLQFNPLERLG 576
Cdd:cd05586   168 -LLDEkgyTKMVDFWSLGVLVFEMCCGWSPFYAE----DTQQmyrniafgKVRFPKDVlSDEGRSFVKGLLNRNPKHRLG 242
                         170       180
                  ....*....|....*....|...
gi 1164769387 577 AgVAGVEDIKSHPFFTPVDWAEL 599
Cdd:cd05586   243 A-HDDAVELKEHPFFADIDWDLL 264
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
444-596 2.42e-18

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: 86.65  E-value: 2.42e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 444 WAAEMVVALDALHREGIVCRDLNPNNILLNDRGHiqltyfSRWSEVEDSCD-------SDAIERMYCAPEV-GAITEETE 515
Cdd:cd05633   113 YATEIILGLEHMHNRFVVYRDLKPANILLDEHGH------VRISDLGLACDfskkkphASVGTHGYMAPEVlQKGTAYDS 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 516 ACDWWSLGAVLFELLTGKTLVECHPAG-------INTHTTLNMPECVSEEARSLIQQLLQFNPLERLGAGVAGVEDIKSH 588
Cdd:cd05633   187 SADWFSLGCMLFKLLRGHSPFRQHKTKdkheidrMTLTVNVELPDSFSPELKSLLEGLLQRDVSKRLGCHGRGAQEVKEH 266

                  ....*...
gi 1164769387 589 PFFTPVDW 596
Cdd:cd05633   267 SFFKGIDW 274
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
436-596 2.77e-18

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: 86.63  E-value: 2.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAI---ERMYCAPEVGAITE 512
Cdd:cd05618   118 LPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGMCKEGLRPGDTTSTfcgTPNYIAPEILRGED 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 513 ETEACDWWSLGAVLFELLTGKTLVECHPAGINT-------------HTTLNMPECVSEEARSLIQQLLQFNPLERLGA-G 578
Cdd:cd05618   198 YGFSVDWWALGVLMFEMMAGRSPFDIVGSSDNPdqntedylfqvilEKQIRIPRSLSVKAASVLKSFLNKDPKERLGChP 277
                         170
                  ....*....|....*...
gi 1164769387 579 VAGVEDIKSHPFFTPVDW 596
Cdd:cd05618   278 QTGFADIQGHPFFRNVDW 295
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
437-590 9.80e-18

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: 83.51  E-value: 9.80e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 437 PEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrwSEVEDSCDSDAIER----------MYCAPE 506
Cdd:cd06626    97 DEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFG--SAVKLKNNTTTMAPgevnslvgtpAYMAPE 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 507 VgaITEETE-----ACDWWSLGAVLFELLTGKtlvecHP-------------AGINTHTTLNMPECVSEEARSLIQQLLQ 568
Cdd:cd06626   175 V--ITGNKGeghgrAADIWSLGCVVLEMATGK-----RPwseldnewaimyhVGMGHKPPIPDSLQLSPEGKDFLSRCLE 247
                         170       180
                  ....*....|....*....|..
gi 1164769387 569 FNPLERLGAgvagvEDIKSHPF 590
Cdd:cd06626   248 SDPKKRPTA-----SELLDHPF 264
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
410-590 1.04e-17

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: 83.04  E-value: 1.04e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFE-----DLDKklALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRG-HIQLTY- 482
Cdd:cd14009    60 VQKTEDFIYLVLEycaggDLSQ--YIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLSTSGdDPVLKIa 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 483 ---FSR----WSEVEDSCDSDaierMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTlvechPAGINTHTTL------ 549
Cdd:cd14009   138 dfgFARslqpASMAETLCGSP----LYMAPEILQFQKYDAKADLWSVGAILFEMLVGKP-----PFRGSNHVQLlrnier 208
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1164769387 550 -------NMPECVSEEARSLIQQLLQFNPLERLgagvaGVEDIKSHPF 590
Cdd:cd14009   209 sdavipfPIAAQLSPDCKDLLRRLLRRDPAERI-----SFEEFFAHPF 251
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
436-599 1.51e-17

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: 84.71  E-value: 1.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSR------------WSEVEDSCDSD-AIERM- 501
Cdd:cd05628    98 LTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLctglkkahrtefYRNLNHSLPSDfTFQNMn 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 ------------------------YCAPEVGAITEETEACDWWSLGAVLFELLTG------KTLVECHPAGINTHTTLNM 551
Cdd:cd05628   178 skrkaetwkrnrrqlafstvgtpdYIAPEVFMQTGYNKLCDWWSLGVIMYEMLIGyppfcsETPQETYKKVMNWKETLIF 257
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1164769387 552 PECV--SEEARSLIqqlLQFNPLERLGAGVAGVEDIKSHPFFTPVDWAEL 599
Cdd:cd05628   258 PPEVpiSEKAKDLI---LRFCCEWEHRIGAPGVEEIKTNPFFEGVDWEHI 304
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
436-591 1.85e-17

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: 82.62  E-value: 1.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLT--YFSRWSEVEDS-------CDSDAiermYCAPE 506
Cdd:cd14080    99 LSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSdfGFARLCPDDDGdvlsktfCGSAA----YAAPE 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 507 V--GaITEETEACDWWSLGAVLFELLTG---------KTLVECH-PAGINTHTTLnmpECVSEEARSLIQQLLQFNPLER 574
Cdd:cd14080   175 IlqG-IPYDPKKYDIWSLGVILYIMLCGsmpfddsniKKMLKDQqNRKVRFPSSV---KKLSPECKDLIDQLLEPDPTKR 250
                         170
                  ....*....|....*..
gi 1164769387 575 lgagvAGVEDIKSHPFF 591
Cdd:cd14080   251 -----ATIEEILNHPWL 262
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
436-599 2.01e-17

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 223589 [Multi-domain]  Cd Length: 384  Bit Score: 84.41  E-value: 2.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHI----------QLTYFSRWSEVEDSCDSDAIERMYCAP 505
Cdd:COG0515    98 LSESEALFILAQILSALEYLHSKGIIHRDIKPENILLDRDGRVvklidfglakLLPDPGSTSSIPALPSTSVGTPGYMAP 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 506 EVGAITEE---TEACDWWSLGAVLFELLTGKTLVECHPAGINTHTTL-----------------NMPECVSEEARSLIQQ 565
Cdd:COG0515   178 EVLLGLSLayaSSSSDIWSLGITLYELLTGLPPFEGEKNSSATSQTLkiilelptpslasplspSNPELISKAASDLLKK 257
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1164769387 566 LLQFNPLERLGAGVAGVEDIKSHPFFTPVDWAEL 599
Cdd:COG0515   258 LLAKDPKNRLSSSSDLSHDLLAHLKLKESDLSDL 291
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
437-590 2.86e-17

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: 81.96  E-value: 2.86e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 437 PEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrWSEVEDSCDSDAIERM--------------- 501
Cdd:cd14010    92 PESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFG-LARREGEILKELFGQFsdegnvnkvskkqak 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 -----YCAPEVGAITEETEACDWWSLGAVLFELLTGK---------TLVEchpaGINTHTTLNMPECVSEEA----RSLI 563
Cdd:cd14010   171 rgtpyYMAPELFQGGVHSFASDLWALGCVLYEMFTGKppfvaesftELVE----KILNEDPPPPPPKVSSKPspdfKSLL 246
                         170       180
                  ....*....|....*....|....*..
gi 1164769387 564 QQLLQFNPLERLGAgvagvEDIKSHPF 590
Cdd:cd14010   247 KGLLEKDPAKRLSW-----DELVKHPF 268
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
447-591 2.91e-17

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: 81.92  E-value: 2.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRW----SEVEDSCDSDaierMYCAPEVgaITEET---EAC 517
Cdd:cd14081   109 QIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFgmASLqpegSLLETSCGSP----HYACPEV--IKGEKydgRKA 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 518 DWWSLGAVLFELLTGKTLVEchpaGINTHTTLN--------MPECVSEEARSLIQQLLQFNPLERLgagvaGVEDIKSHP 589
Cdd:cd14081   183 DIWSCGVILYALLVGALPFD----DDNLRQLLEkvkrgvfhIPHFISPDAQDLLRRMLEVNPEKRI-----TIEEIKKHP 253

                  ..
gi 1164769387 590 FF 591
Cdd:cd14081   254 WF 255
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
437-599 3.75e-17

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: 82.24  E-value: 3.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 437 PEGCIqrWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSD---AIERMYCAPEVGAITEE 513
Cdd:cd05608   105 PRACF--YTAQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGQTKTkgyAGTPGFMAPELLLGEEY 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 514 TEACDWWSLGAVLFELLTGKTLVECHPAGINT--------HTTLNMPECVSEEARSLIQQLLQFNPLERLGAGVAGVEDI 585
Cdd:cd05608   183 DYSVDYFTLGVTLYEMIAARGPFRARGEKVENkelkqrilNDSVTYSEKFSPASKSICEALLAKDPEKRLGFRDGNCDGL 262
                         170
                  ....*....|....
gi 1164769387 586 KSHPFFTPVDWAEL 599
Cdd:cd05608   263 RTHPFFRDINWRKL 276
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
434-591 6.52e-17

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: 80.78  E-value: 6.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 434 FYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILL--NDRGHIQLTYFSRWSEVEDSCDSDAIERMYCAPEVGAIT 511
Cdd:cd14133    97 QYLSLPRIRKIAQQILEALVFLHSLGLIHCDLKPENILLasYSRCQIKIIDFGSSCFLTQRLYSYIQSRYYRAPEVILGL 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 512 EETEACDWWSLGAVLFELLTGK----------------TLVECHPAGINTHTTLNMPECVseearSLIQQLLQFNPLERL 575
Cdd:cd14133   177 PYDEKIDMWSLGCILAELYTGEplfpgasevdqlariiGTIGIPPAHMLDQGKADDELFV-----DFLKKLLEIDPKERP 251
                         170
                  ....*....|....*.
gi 1164769387 576 GAGVAgvediKSHPFF 591
Cdd:cd14133   252 TASQA-----LSHPWL 262
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
410-590 8.40e-17

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: 80.60  E-value: 8.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFE-----DL-DKklaLASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDR---GHIQL 480
Cdd:cd05117    67 VFEDDKNLYLVMElctggELfDR---IVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASKdpdSPIKI 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 481 TYF--SRW----SEVEDSCDSDAiermYCAPEVGAITEETEACDWWSLGAVLFELLTGktlveCHPAGINTHTTL----- 549
Cdd:cd05117   144 IDFglAKIfeegEKLKTVCGTPY----YVAPEVLKGKGYGKKCDIWSLGVILYILLCG-----YPPFYGETEQELfekil 214
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1164769387 550 ----NMPE----CVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPF 590
Cdd:cd05117   215 kgkySFDSpewkNVSEEAKDLIKRLLVVDPKKRLTA-----AEALNHPW 258
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
433-600 9.35e-17

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 81.95  E-value: 9.35e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 433 RFYIPEGCIqrWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERMYCAPEVGAITE 512
Cdd:PTZ00426  127 RFPNDVGCF--YAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDTRTYTLCGTPEYIAPEILLNVG 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 513 ETEACDWWSLGAVLFELLTGktlveCHPAGINT---------HTTLNMPECVSEEARSLIQQLLQFNPLERLGAGVAGVE 583
Cdd:PTZ00426  205 HGKAADWWTLGIFIYEILVG-----CPPFYANEplliyqkilEGIIYFPKFLDNNCKHLMKKLLSHDLTKRYGNLKKGAQ 279
                         170
                  ....*....|....*..
gi 1164769387 584 DIKSHPFFTPVDWAELM 600
Cdd:PTZ00426  280 NVKEHPWFGNIDWVSLL 296
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
436-591 1.66e-16

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: 79.90  E-value: 1.66e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRwSEVEDSCDsDAIER-----MYCAPEVGAI 510
Cdd:cd14008   105 LPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGV-SEMFEDGN-DTLQKtagtpAFLAPELCDG 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 511 TEET---EACDWWSLGAVLFELLTGK------TLVECHPAGINTHTTLNMPECVSEEARSLIQQLLQFNPLERLgagvaG 581
Cdd:cd14008   183 DSKTysgKAADIWALGVTLYCLVFGRlpfngdNILELYEAIQNQNDEFPIPPELSPELKDLLRRMLEKDPEKRI-----T 257
                         170
                  ....*....|
gi 1164769387 582 VEDIKSHPFF 591
Cdd:cd14008   258 LKEIKEHPWV 267
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
436-591 3.15e-15

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: 75.72  E-value: 3.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF---SRWSEVEDSCDSDAIERMYCAPEVGAITE 512
Cdd:cd06627    96 FPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFgvaTKLNEVEKDENSVVGTPYWMAPEVIEMSG 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 513 ETEACDWWSLGAVLFELLTGK-------------TLVEchpagiNTHTTLnmPECVSEEARSLIQQLLQFNPLERLGAgv 579
Cdd:cd06627   176 VTTASDIWSVGCTVIELLTGNppyydlqpmaalfRIVQ------DDHPPL--PENISPELRDFLLQCFQKDPTLRPSA-- 245
                         170
                  ....*....|..
gi 1164769387 580 agvEDIKSHPFF 591
Cdd:cd06627   246 ---KELLKHPWL 254
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
447-591 8.39e-15

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: 74.61  E-value: 8.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVED------SCDSD---AIE----RMYCAPEVgaitee 513
Cdd:cd14079   110 QIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDgeflktSCGSPnyaAPEvisgKLYAGPEV------ 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 514 teacDWWSLGAVLFELLTGK---------TLVECHPAGINThttlnMPECVSEEARSLIQQLLQFNPLERlgagvAGVED 584
Cdd:cd14079   184 ----DVWSCGVILYALLCGSlpfddehipNLFKKIKSGIYT-----IPSHLSPGARDLIKRMLVVDPLKR-----ITIPE 249

                  ....*..
gi 1164769387 585 IKSHPFF 591
Cdd:cd14079   250 IRQHPWF 256
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
433-591 1.30e-14

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: 74.13  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 433 RFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEdscdsDAIERM--------YCA 504
Cdd:cd14099    95 RKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLE-----YDGERKktlcgtpnYIA 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 505 PEV--GAITEETEAcDWWSLGAVLFELLTGKTLVEChpagINTHTTLN--------MPE--CVSEEARSLIQQLLQFNPL 572
Cdd:cd14099   170 PEVleKKKGHSFEV-DIWSLGVILYTLLVGKPPFET----SDVKETYKrikkneysFPShlSISDEAKDLIRSMLQPDPT 244
                         170
                  ....*....|....*....
gi 1164769387 573 ERLgagvaGVEDIKSHPFF 591
Cdd:cd14099   245 KRP-----SLDEILSHPFF 258
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
448-593 3.27e-14

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: 73.87  E-value: 3.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 448 MVVALDALHREGIVCRDLNPNNILL---NDRGHIQLT--YFSRWSEVEDSCDSDAIERMYCAPEV----GAITEETEACD 518
Cdd:cd14092   108 LVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVdfGFARLKPENQPLKTPCFTLPYAAPEVlkqaLSTQGYDESCD 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 519 WWSLGAVLFELLTGKtlVECHPAGINTHTTLNMP--------------ECVSEEARSLIQQLLQFNPLERLgagvaGVED 584
Cdd:cd14092   188 LWSLGVILYTMLSGQ--VPFQSPSRNESAAEIMKriksgdfsfdgeewKNVSSEAKSLIQGLLTVDPSKRL-----TMSE 260

                  ....*....
gi 1164769387 585 IKSHPFFTP 593
Cdd:cd14092   261 LRNHPWLQG 269
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
436-590 5.61e-14

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: 72.02  E-value: 5.61e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILL-NDRGH----IQLTY------FSRWSEVEDS----CDSDaier 500
Cdd:cd14120    89 LSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLsHNSGRkpspNDIRLkiadfgFARFLQDGMMaatlCGSP---- 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 501 MYCAPEVGAITEETEACDWWSLGAVLFELLTGKTlvechPAGINT----------HTTL--NMPECVSEEARSLIQQLLQ 568
Cdd:cd14120   165 MYMAPEVIMSLQYDAKADLWSIGTIVYQCLTGKA-----PFQAQTpqelkafyekNANLrpNIPSGTSPALKDLLLGLLK 239
                         170       180
                  ....*....|....*....|..
gi 1164769387 569 FNPLERLgagvaGVEDIKSHPF 590
Cdd:cd14120   240 RNPKDRI-----DFEDFFSHPF 256
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
449-593 4.70e-13

Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and similar MAPKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human MAPK15 is also called Extracellular signal Regulated Kinase 8 (ERK8) while the rat protein is called ERK7. ERK7 and ERK8 display both similar and different biochemical properties. They autophosphorylate and activate themselves and do not require upstream activating kinases. ERK7 is constitutively active and is not affected by extracellular stimuli whereas ERK8 shows low basal activity and is activated by DNA-damaging agents. ERK7 and ERK8 also have different substrate profiles. Genome analysis shows that they are orthologs with similar gene structures. ERK7 and ERK 8 may be involved in the signaling of some nuclear receptor transcription factors. ERK7 regulates hormone-dependent degradation of estrogen receptor alpha while ERK8 down-regulates the transcriptional co-activation androgen and glucocorticoid receptors. MAPKs are important mediators of cellular responses to extracellular signals. The MAPK15 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: 270841 [Multi-domain]  Cd Length: 337  Bit Score: 70.66  E-value: 4.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 449 VVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDSCDSDAI------ERMYCAPEV--GAiTEETEACD 518
Cdd:cd07852   117 LKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFglARSLSQLEEDDENPVltdyvaTRWYRAPEIllGS-TRYTKGVD 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 519 WWSLGAVLFELLTGKTL-------------VECHP-------AGINTHTTLNM----------------PECvSEEARSL 562
Cdd:cd07852   196 MWSVGCILGEMLLGKPLfpgtstlnqlekiIEVIGrpsaediESIQSPFAATMleslppsrpksldelfPKA-SPDALDL 274
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1164769387 563 IQQLLQFNPLERLGAgvagvEDIKSHPFFTP 593
Cdd:cd07852   275 LKKLLVFNPNKRLTA-----EEALRHPYVAQ 300
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
421-589 5.16e-13

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: 69.34  E-value: 5.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 421 FEDLDKKLA--LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTyfsrwseveDSCDSDAI 498
Cdd:cd08530    83 FGDLSKLISkrKKKRRLFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIG---------DLGISKVL 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 499 ER----------MYCAPEVGAITEETEACDWWSLGAVLFELLTGKTlvechPAGINTHTTLN----------MPECVSEE 558
Cdd:cd08530   154 KKnlaktqigtpLYAAPEVWKGRPYDYKSDIWSLGCLLYEMATFRP-----PFEARTMQELRykvcrgkfppIPPVYSQD 228
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1164769387 559 ARSLIQQLLQFNPLERLgagvaGVEDIKSHP 589
Cdd:cd08530   229 LQQIIRSLLQVNPKKRP-----SCDKLLQSP 254
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
423-574 6.54e-13

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: 69.03  E-value: 6.54e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 423 DLDKKLALASRF--YIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRwsEVEDSCDsdai 498
Cdd:cd08215    85 DLAQKIKKQKKKgqPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFgiSK--VLESTTD---- 158
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 499 erM---------YCAPEVgaiteeteaC---------DWWSLGAVLFELLTGKtlvecHP--AG--------INTHTTLN 550
Cdd:cd08215   159 --LaktvvgtpyYLSPEL---------CenkpynyksDIWALGCVLYELCTLK-----HPfeANnlpalvykIVKGQYPP 222
                         170       180
                  ....*....|....*....|....
gi 1164769387 551 MPECVSEEARSLIQQLLQFNPLER 574
Cdd:cd08215   223 IPSQYSSELRDLVNSMLQKDPEKR 246
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
442-592 7.08e-13

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: 68.83  E-value: 7.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 442 QRWAA---EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrWS-EVEDSCDSDAIERM-YCAPEVGAITEETEA 516
Cdd:cd14116   105 QRTATyitELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFG-WSvHAPSSRRTTLCGTLdYLPPEMIEGRMHDEK 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 517 CDWWSLGAVLFELLTGKTlvechPAGINTH---------TTLNMPECVSEEARSLIQQLLQFNPLERLgagvaGVEDIKS 587
Cdd:cd14116   184 VDLWSLGVLCYEFLVGKP-----PFEANTYqetykrisrVEFTFPDFVTEGARDLISRLLKHNPSQRP-----MLREVLE 253

                  ....*
gi 1164769387 588 HPFFT 592
Cdd:cd14116   254 HPWIT 258
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
442-590 9.28e-13

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: 68.63  E-value: 9.28e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 442 QRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQL------TYFSRWSEVEDSCDS---DAIE----RMYCAPEVg 508
Cdd:cd14077   116 RKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIidfglsNLYDPRRLLRTFCGSlyfAAPEllqaQPYTGPEV- 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 509 aiteeteacDWWSLGAVLFELLTGKTLV--ECHPAginTHT-----TLNMPECVSEEARSLIQQLLQFNPLERlgagvAG 581
Cdd:cd14077   195 ---------DVWSFGVVLYVLVCGKVPFddENMPA---LHAkikkgKVEYPSYLSSECKSLISRMLVVDPKKR-----AT 257

                  ....*....
gi 1164769387 582 VEDIKSHPF 590
Cdd:cd14077   258 LEQVLNHPW 266
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
410-591 1.05e-12

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: 68.66  E-value: 1.05e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFEDLDKKLA--LASRFY-IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--S 484
Cdd:cd07829    66 VIHTENKLYLVFEYCDQDLKkyLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFglA 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 485 RWSEVEDSCDSDAIERM-YCAPEV--GAiTEETEACDWWSLGAVLFELLTGKTL-------------------------- 535
Cdd:cd07829   146 RAFGIPLRTYTHEVVTLwYRAPEIllGS-KHYSTAVDIWSVGCIFAELITGKPLfpgdseidqlfkifqilgtpteeswp 224
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1164769387 536 -VECHPA---------GINTHTTLNmpeCVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd07829   225 gVTKLPDykptfpkwpKNDLEKVLP---RLDPEGIDLLSKMLQYNPAKRISA-----KEALKHPYF 282
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
436-591 1.07e-12

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: 68.51  E-value: 1.07e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF---SRWS------EVEDSCDSDAiermYCAPE 506
Cdd:cd14069    97 MPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFglaTVFRykgkerLLNKMCGTLP----YVAPE 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 507 VGAITE-ETEACDWWSLGAVLFELLTGKTlvechP------------AGINTHTTLNMP-ECVSEEARSLIQQLLQFNPL 572
Cdd:cd14069   173 LLAKKKyRAEPVDVWSCGIVLFAMLAGEL-----PwdqpsdscqeysDWKENKKTYLTPwKKIDTAALSLLRKILTENPN 247
                         170
                  ....*....|....*....
gi 1164769387 573 ERlgagvAGVEDIKSHPFF 591
Cdd:cd14069   248 KR-----ITIEDIKKHPWY 261
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
432-591 1.10e-12

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: 67.84  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrwseVEDSC----DSDAIER-----MY 502
Cdd:cd13976    77 SRKRLREPEAARLFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLES----LEDAVilegEDDSLSDkhgcpAY 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 503 CAPEV--GAITEETEACDWWSLGAVLFELLTGK-TLVECHPAGINT---HTTLNMPECVSEEARSLIQQLLQFNPLERLG 576
Cdd:cd13976   153 VSPEIlnSGATYSGKAADVWSLGVILYTMLVGRyPFHDSEPASLFAkirRGQFAIPETLSPRARCLIRSLLRREPSERLT 232
                         170
                  ....*....|....*
gi 1164769387 577 AgvagvEDIKSHPFF 591
Cdd:cd13976   233 A-----EDILLHPWL 242
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
446-581 1.66e-12

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: 67.58  E-value: 1.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 446 AEMVVALDALHREGIVCRDLNPNNILLN-DRGHIQLTYFSRWSEVEDS-------CDSDAiermYCAPEV-GAITEETEA 516
Cdd:cd14164   107 AQMVGAVNYLHDMNIVHRDLKCENILLSaDDRKIKIADFGFARFVEDYpelsttfCGSRA----YTPPEViLGTPYDPKK 182
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 517 CDWWSLGAVLFELLTGKTLVECHPAGINTHTT--LNMPECVS--EEARSLIQQLLQFNPLERLGAG-VAG 581
Cdd:cd14164   183 YDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQrgVLYPSGVAleEPCRALIRTLLQFNPSTRPSIQqVAG 252
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
447-592 1.69e-12

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: 68.16  E-value: 1.69e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVE---DSCDSDAIERMYCAPEvgAITEETE-----ACD 518
Cdd:cd14118   123 DIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFGVSNEFEgddALLSSTAGTPAFMAPE--ALSESRKkfsgkALD 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 519 WWSLGAVLFELLTGKT-LVECHPAGINT---HTTLNMPE--CVSEEARSLIQQLLQFNPLERLgagvaGVEDIKSHPFFT 592
Cdd:cd14118   201 IWAMGVTLYCFVFGRCpFEDDHILGLHEkikTDPVVFPDdpVVSEQLKDLILRMLDKNPSERI-----TLPEIKEHPWVT 275
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
402-591 2.50e-12

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: 67.64  E-value: 2.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 402 ETKGESGLVLE---GDKEIHQIFEDLDKKlalasrfyIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILL---NDR 475
Cdd:cd14198    78 ETTSEIILILEyaaGGEIFNLCVPDLAEM--------VSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLssiYPL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 476 GHIQLTYFSRWSEVEDSCDSDAI--ERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTlvechP-AGI-NTHTTLNM 551
Cdd:cd14198   150 GDIKIVDFGMSRKIGHACELREImgTPEYLAPEILNYDPITTATDMWNIGVIAYMLLTHES-----PfVGEdNQETFLNI 224
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1164769387 552 PEC-----------VSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd14198   225 SQVnvdyseetfssVSQLATDFIQKLLVKNPEKRPTA-----EICLSHSWL 270
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
436-590 3.19e-12

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: 67.05  E-value: 3.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILL-NDRGHIQLTYF--SRWSE----VEDSCDSDAiermYCAPEVg 508
Cdd:cd14074   100 LNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFgfSNKFQpgekLETSCGSLA----YSAPEI- 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 509 AITEETE--ACDWWSLGAVLFELLTGktlvecHP--AGINTHTTLNM--------PECVSEEARSLIQQLLQFNPLERlg 576
Cdd:cd14074   175 LLGDEYDapAVDIWSLGVILYMLVCG------QPpfQEANDSETLTMimdckytvPAHVSPECKDLIRRMLIRDPKKR-- 246
                         170
                  ....*....|....
gi 1164769387 577 agvAGVEDIKSHPF 590
Cdd:cd14074   247 ---ASLEEIENHPW 257
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
441-590 3.32e-12

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: 66.61  E-value: 3.32e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILL---NDRGHIQLTYFSRWSEVEDSCDSDAIERM----YCAPEVGAI-TE 512
Cdd:cd14012   106 ARRWTLQLLEALEYLHRNGVVHKSLHAGNVLLdrdAGTGIVKLTDYSLGKTLLDMCSRGSLDEFkqtyWLPPELAQGsKS 185
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1164769387 513 ETEACDWWSLGAVLFELLTGKTLVECHPAGINTHTTLNMPecvsEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPF 590
Cdd:cd14012   186 PTRKTDVWDLGLLFLQMLFGLDVLEKYTSPNPVLVSLDLS----ASLQDFLSKCLSLDPKKRPTA-----LELLPHEF 254
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
432-591 4.47e-12

Catalytic domain of Cyclin-Dependent protein Kinase 9-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 CDK9 and CDK12 from higher eukaryotes, yeast BUR1, C-type plant CDKs (CdkC), and similar proteins. CDK9, BUR1, and CdkC are functionally equivalent. They act as a kinase for the C-terminal domain of RNA polymerase II and participate in regulating mutliple steps of gene expression including transcription elongation and RNA processing. CDK9 and CdkC associate with T-type cyclins while BUR1 associates with the cyclin BUR2. CDK12 is a unique CDK that contains an arginine/serine-rich (RS) domain, which is predominantly found in splicing factors. CDK12 interacts with cyclins L1 and L2, and participates 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 CDK9-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: 270832 [Multi-domain]  Cd Length: 291  Bit Score: 66.82  E-value: 4.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYIPEgcIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDSCD--SDAIERMYCAPEV 507
Cdd:cd07840    99 VKFTESQ--IKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADFglARPYTKENNADytNRVITLWYRPPEL 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 508 --GAiTEETEACDWWSLGAVLFELLTGKTLVE-----------CHPAGinTHTTLNMP---------------------- 552
Cdd:cd07840   177 llGA-TRYGPEVDMWSVGCILAELFTGKPIFQgkteleqlekiFELCG--SPTEENWPgvsdlpwfenlkpkkpykrrlr 253
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1164769387 553 ----ECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd07840   254 evfkNVIDPSALDLLDKLLTLDPKKRISA-----DQALQHEYF 291
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
447-593 4.59e-12

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: 67.37  E-value: 4.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILL---NDRGHIQLT--YFSRWSEVEDS-CDSDAIERMYCAPEVGAITEETEACDWW 520
Cdd:cd14179   110 KLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIdfGFARLKPPDNQpLKTPCFTLHYAAPELLNYNGYDESCDLW 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 521 SLGAVLFELLTGKTLVECHPAGINTHTTLNMPE---------------CVSEEARSLIQQLLQFNPLERL-------GAG 578
Cdd:cd14179   190 SLGVILYTMLSGQVPFQCHDKSLTCTSAEEIMKkikqgdfsfegeawkNVSQEAKDLIQGLLTVDPNKRIkmsglryNEW 269
                         170
                  ....*....|....*
gi 1164769387 579 VAGVEDIKSHPFFTP 593
Cdd:cd14179   270 LQDGSQLSSNPLMTP 284
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
447-590 5.67e-12

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: 66.04  E-value: 5.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVE-------DSCDSDAiermYCAPEVGAITEETEACDW 519
Cdd:cd14186   110 QIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKmphekhfTMCGTPN----YISPEIATRSAHGLESDV 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 520 WSLGAVLFELLTGKTlvechPAGINT-HTTLN--------MPECVSEEARSLIQQLLQFNPLERLgagvaGVEDIKSHPF 590
Cdd:cd14186   186 WSLGCMFYTLLVGRP-----PFDTDTvKNTLNkvvladyeMPAFLSREAQDLIHQLLRKNPADRL-----SLSSVLDHPF 255
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
424-592 6.34e-12

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


Pssm-ID: 270782 [Multi-domain]  Cd Length: 265  Bit Score: 66.21  E-value: 6.34e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 424 LDKKLALASRfyIPEGCIQRWAAEMVVALDALHRE-GIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDS-CDSDAIERM 501
Cdd:cd06605    86 LDKILKEVGR--IPERILGKIAVAVVKGLIYLHEKhKIIHRDVKPSNILVNSRGQVKLCDFGVSGQLVDSlAKTFVGTRS 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 YCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVEchPAGINTHTT--------LNMP------ECVSEEARSLIQQLL 567
Cdd:cd06605   164 YMAPERISGGKYTVKSDIWSLGLSLVELATGRFPYP--PPNAKPSMMifellsyiVDEPppllpsGKFSPDFQDFVSQCL 241
                         170       180
                  ....*....|....*....|....*
gi 1164769387 568 QFNPLERlgagvAGVEDIKSHPFFT 592
Cdd:cd06605   242 QKDPTER-----PSYKELMEHPFIK 261
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
435-591 6.42e-12

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: 66.17  E-value: 6.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 435 YIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF-----------SRWSEVEDSCDSDAiermYC 503
Cdd:cd14162    96 ALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFgfargvmktkdGKPKLSETYCGSYA----YA 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 504 APEV-GAITEETEACDWWSLGAVLFELLTG---------KTLVEchpaGINTHTTLNMPECVSEEARSLIQQLLQFNPlE 573
Cdd:cd14162   172 SPEIlRGIPYDPFLSDIWSMGVVLYTMVYGrlpfddsnlKVLLK----QVQRRVVFPKNPTVSEECKDLILRMLSPVK-K 246
                         170
                  ....*....|....*...
gi 1164769387 574 RLgagvaGVEDIKSHPFF 591
Cdd:cd14162   247 RI-----TIEEIKRDPWF 259
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
447-592 6.82e-12

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: 66.51  E-value: 6.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDS---CDSDAIERMYCAPEVGAITEET---EACDWW 520
Cdd:cd14200   132 DIVLGIEYLHYQKIVHRDIKPSNLLLGDDGHVKIADFGVSNQFEGNdalLSSTAGTPAFMAPETLSDSGQSfsgKALDVW 211
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1164769387 521 SLGAVLFELLTGKT-LVECHPAGINT---HTTLNMPE--CVSEEARSLIQQLLQFNPLERLgagvaGVEDIKSHPFFT 592
Cdd:cd14200   212 AMGVTLYCFVYGKCpFIDEFILALHNkikNKPVEFPEepEISEELKDLILKMLDKNPETRI-----TVPEIKVHPWVT 284
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
436-590 7.22e-12

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: 66.08  E-value: 7.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHRE-GIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDsdaiermYCAPEVGAIT--- 511
Cdd:cd06623    96 IPEPVLAYIARQILKGLDYLHTKrHIIHRDIKPSNLLINSKGEVKIADFGISKVLENTLD-------QCNTFVGTVTyms 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 512 -EETE------ACDWWSLGAVLFELLTGKtlvecHP---AGINTHTTL----------NMP-ECVSEEARSLIQQLLQFN 570
Cdd:cd06623   169 pERIQgesysyAADIWSLGLTLLECALGK-----FPflpPGQPSFFELmqaicdgpppSLPaEEFSPEFRDFISACLQKD 243
                         170       180
                  ....*....|....*....|
gi 1164769387 571 PLERLGAgvagvEDIKSHPF 590
Cdd:cd06623   244 PKKRPSA-----AELLQHPF 258
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
442-590 7.67e-12

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: 65.78  E-value: 7.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 442 QRWAAEMV----VALDALHREGIVCRDLNPNNILL---NDRGHIQLT--YFSRWSEVEDSCDSDAIERMYCAPEVGAITE 512
Cdd:cd14172   102 EREASEIMrdigTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTdfGFAKETTVQNALQTPCYTPYYVAPEVLGPEK 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 513 ETEACDWWSLGAVLFELLTG------KTLVECHPaGINTHTTLNM-----PEC--VSEEARSLIQQLLQFNPLERLgagv 579
Cdd:cd14172   182 YDKSCDMWSLGVIMYILLCGfppfysNTGQAISP-GMKRRIRMGQygfpnPEWaeVSEEAKQLIRHLLKTDPTERM---- 256
                         170
                  ....*....|.
gi 1164769387 580 aGVEDIKSHPF 590
Cdd:cd14172   257 -TITQFMNHPW 266
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
441-594 9.09e-12

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: 66.39  E-value: 9.09e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRwSEVEDSCDSDAIE----RMYCAPEV-GAITEE 513
Cdd:cd07834   105 IQYFLYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFglAR-GVDPDEDKGFLTEyvvtRWYRAPELlLSSKKY 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 514 TEACDWWSLGAVLFELLTGKTL-------------VEC----HPAGINTHTTLNMPECV------------------SEE 558
Cdd:cd07834   184 TKAIDIWSVGCIFAELLTRKPLfpgrdyidqlnliVEVlgtpSEEDLKFISSEKARNYLkslpkkpkkplsevfpgaSPE 263
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1164769387 559 ARSLIQQLLQFNPLERLGAgvagvEDIKSHPFFTPV 594
Cdd:cd07834   264 AIDLLEKMLVFNPKKRITA-----DEALAHPYLAQL 294
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
451-591 1.13e-11

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: 65.45  E-value: 1.13e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDS------CDSDAiermYCAPEVGAITEETEA------CD 518
Cdd:cd14093   121 AVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGeklrelCGTPG----YLAPEVLKCSMYDNApgygkeVD 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 519 WWSLGAVLFELLTGktlveCHP-----------AGINTHTTLNMPEC--VSEEARSLIQQLLQFNPLERLGAgvagvEDI 585
Cdd:cd14093   197 MWACGVIMYTLLAG-----CPPfwhrkqmvmlrNIMEGKYEFGSPEWddISDTAKDLISKLLVVDPKKRLTA-----EEA 266

                  ....*.
gi 1164769387 586 KSHPFF 591
Cdd:cd14093   267 LEHPFF 272
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
437-590 1.40e-11

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


Pssm-ID: 270798 [Multi-domain]  Cd Length: 267  Bit Score: 65.25  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 437 PEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIER---------MYCAPEV 507
Cdd:cd06628   104 EESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEANSLSTKNNGarpslqgsvFWMAPEV 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 508 GAITEETEACDWWSLGAVLFELLTGKtlvecHPAG----------INTHTTLNMPECVSEEARSLIQQLLQFNPLERLGA 577
Cdd:cd06628   184 VKQTSYTRKADIWSLGCLVVEMLTGT-----HPFPdctqmqaifkIGENASPTIPSNISSEARDFLEKTFEIDHNKRPTA 258
                         170
                  ....*....|...
gi 1164769387 578 gvagvEDIKSHPF 590
Cdd:cd06628   259 -----DELLKHPF 266
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
419-591 1.42e-11

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: 65.38  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 419 QIFEDLDKKLALASRfyiPEGCIQRWAAEMVVALDALHregIVCRDLNPNNILLNDRGHIQLTYFSRwsevedSCDSDAI 498
Cdd:cd14181   102 ELFDYLTEKVTLSEK---ETRSIMRSLLEAVSYLHANN---IVHRDLKPENILLDDQLHIKLSDFGF------SCHLEPG 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 499 ERM--------YCAPEVGAIT-EET-----EACDWWSLGAVLFELLTG-------KTLVECHPAgINTHTTLNMPEC--V 555
Cdd:cd14181   170 EKLrelcgtpgYLAPEILKCSmDEThpgygKEVDLWACGVILFTLLAGsppfwhrRQMLMLRMI-MEGRYQFSSPEWddR 248
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1164769387 556 SEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd14181   249 SSTVKDLISRLLVVDPEIRLTA-----EQALQHPFF 279
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
443-574 1.44e-11

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


Pssm-ID: 270901 [Multi-domain]  Cd Length: 245  Bit Score: 64.87  E-value: 1.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 443 RWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRwseVEDSCDsdaiERM--------YCAPEVgaITE 512
Cdd:cd13999    95 KIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFglSR---IKNSTT----EKMtgvvgtprWMAPEV--LRG 165
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 513 E--TEACDWWSLGAVLFELLTGKTLVECHP------AGINTHTTLNMPECVSEEARSLIQQLLQFNPLER 574
Cdd:cd13999   166 EpyTEKADVYSFGIVLWELLTGEVPFKELSpiqiaaAVVQKGLRPPIPPDCPPELSKLIKRCWNEDPEKR 235
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
417-591 2.16e-11

Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 and CDK6 partner with D-type cyclins to regulate the early G1 phase of the cell cycle. They are the first kinases activated by mitogenic signals to release cells from the G0 arrested state. CDK4 and CDK6 are both expressed ubiquitously, associate with all three D cyclins (D1, D2 and D3), and phosphorylate the retinoblastoma (pRb) protein. They are also regulated by the INK4 family of inhibitors which associate with either the CDK alone or the CDK/cyclin complex. CDK4 and CDK6 show differences in subcellular localization, sensitivity to some inhibitors, timing in activation, tumor selectivity, and possibly substrate profiles. Although CDK4 and CDK6 seem to show some redundancy, they also have discrete, nonoverlapping functions. CDK6 plays an important role in cell differentiation. 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 CDK4/6-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: 270831 [Multi-domain]  Cd Length: 287  Bit Score: 64.99  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 417 IHQIFEDLDKKLALASRFY----IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVE 490
Cdd:cd07838    81 LTLVFEHVDQDLATYLDKCpkpgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFglARIYSFE 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 491 DSCDSDAIERMYCAPEVGAITEETEACDWWSLGAVLFEL---------------------LTGK------------TLVE 537
Cdd:cd07838   161 MALTSVVVTLWYRAPEVLLQSSYATPVDMWSVGCIFAELfnrrplfrgsseadqlgkifdVIGLpseeewprnsalPRSS 240
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1164769387 538 CHPAGINTHTTLnMPEcVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd07838   241 FPSYTPRPFKSF-VPE-IDEEGLDLLKKMLTFNPHKRISA-----FEALQHPYF 287
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
444-599 2.27e-11

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: 64.93  E-value: 2.27e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 444 WAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVED--SCDSDAIERMYCAPEVGAITEETEACDWWS 521
Cdd:cd05607   109 YSAQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEgkPITQRAGTNGYMAPEILKEESYSYPVDWFA 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 522 LGAVLFELLTGKTLVECHPAGINTHTTLNMP---------ECVSEEARSLIQQLLQFNPLERLGAGVAGvEDIKSHPFFT 592
Cdd:cd05607   189 MGCSIYEMVAGRTPFRDHKEKVSKEELKRRTledevkfehQNFTEEAKDICRLFLAKKPENRLGSRTND-DDPRKHEFFK 267

                  ....*..
gi 1164769387 593 PVDWAEL 599
Cdd:cd05607   268 SINFPRL 274
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
423-590 2.64e-11

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: 64.35  E-value: 2.64e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 423 DLDKKLALASRFyiPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrWSEVEDSCDSDAIERMY 502
Cdd:cd14663    86 ELFSKIAKNGRL--KEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFG-LSALSEQFRQDGLLHTT 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 503 C------APEV-------GAiteeteACDWWSLGAVLFELLTG------KTLVECHPAGINTHttLNMPECVSEEARSLI 563
Cdd:cd14663   163 CgtpnyvAPEVlarrgydGA------KADIWSCGVILFVLLAGylpfddENLMALYRKIMKGE--FEYPRWFSPGAKSLI 234
                         170       180
                  ....*....|....*....|....*..
gi 1164769387 564 QQLLQFNPLERlgagvAGVEDIKSHPF 590
Cdd:cd14663   235 KRILDPNPSTR-----ITVEQIMASPW 256
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
432-590 2.71e-11

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: 64.23  E-value: 2.71e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTY----FSRWSEVEDSCDSDAIERMYCAPEV 507
Cdd:cd14121    88 SRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNPVLKLadfgFAQHLKPNDEAHSLRGSPLYMAPEM 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 508 GAITEETEACDWWSLGAVLFELLTGK------TLVECHpAGINTHTTLNMPEC--VSEEARSLIQQLLQFNPLERLgagv 579
Cdd:cd14121   168 ILKKKYDARVDLWSVGVILYECLFGRapfasrSFEELE-EKIRSSKPIEIPTRpeLSADCRDLLLRLLQRDPDRRI---- 242
                         170
                  ....*....|.
gi 1164769387 580 aGVEDIKSHPF 590
Cdd:cd14121   243 -SFEEFFAHPF 252
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
411-577 7.33e-11

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: 62.68  E-value: 7.33e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 411 LEGDKEIHQIFE-----DLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSR 485
Cdd:cd08219    67 FEADGHLYIVMEycdggDLMQKIKLQRGKLFPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGS 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 486 W----SEVEDSCDSDAIErMYCAPEVGAITEETEACDWWSLGAVLFELLTGKtlvecHPAGINTHTTLNMPEC------- 554
Cdd:cd08219   147 ArlltSPGAYACTYVGTP-YYVPPEIWENMPYNNKSDIWSLGCILYELCTLK-----HPFQANSWKNLILKVCqgsykpl 220
                         170       180
                  ....*....|....*....|....*.
gi 1164769387 555 ---VSEEARSLIQQLLQFNPLERLGA 577
Cdd:cd08219   221 pshYSYELRSLIKQMFKRNPRSRPSA 246
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
447-589 9.01e-11

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: 62.80  E-value: 9.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILL---NDRGHIQLTYFSRWSEVEDscdsDAIERMYC------APEV---GAITEET 514
Cdd:cd14084   119 QMLLAVKYLHSNGIIHRDLKPENVLLssqEEECLIKITDFGLSKILGE----TSLMKTLCgtptylAPEVlrsFGTEGYT 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 515 EACDWWSLGAVLFELLTGktlvecHPAGINTHTTLNMPE---------------CVSEEARSLIQQLLQFNPLERLgagv 579
Cdd:cd14084   195 RAVDCWSLGVILFICLSG------YPPFSEEYTQMSLKEqilsgkytfipkawkNVSEEAKDLVKKMLVVDPSRRP---- 264
                         170
                  ....*....|
gi 1164769387 580 aGVEDIKSHP 589
Cdd:cd14084   265 -SIEEALEHP 273
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
416-589 9.99e-11

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: 62.41  E-value: 9.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 416 EIHQIFEDLDKKLA-------------LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQL-- 480
Cdd:cd14073    65 RIYEVFENKDKIVIvmeyasggelydyISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIad 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 481 ----TYFSRWSEVEDSCDSDaierMYCAPE-VGAITEETEACDWWSLGAVLFELLTGKTlvechPAGINTHTTLNM---- 551
Cdd:cd14073   145 fglsNLYSKDKLLQTFCGSP----LYASPEiVNGTPYQGPEVDCWSLGVLLYTLVYGTM-----PFDGSDFKRLVKqiss 215
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1164769387 552 -----PECVSeEARSLIQQLLQFNPLERlgagvAGVEDIKSHP 589
Cdd:cd14073   216 gdyrePTQPS-DASGLIRWMLTVNPKRR-----ATIEDIANHW 252
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
414-592 1.05e-10

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


Pssm-ID: 270833 [Multi-domain]  Cd Length: 298  Bit Score: 62.97  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 414 DKEIHQIFE----DL-----DKKLALAsrfyipEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF- 483
Cdd:cd07841    74 KSNINLVFEfmetDLekvikDKSIVLT------PADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFg 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 484 -SRwsevedSCDSD-------AIERMYCAPEV--GAiTEETEACDWWSLGAVLFELLTGKTL------------------ 535
Cdd:cd07841   148 lAR------SFGSPnrkmthqVVTRWYRAPELlfGA-RHYGVGVDMWSVGCIFAELLLRVPFlpgdsdidqlgkifealg 220
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1164769387 536 ---------VECHP--------AGINTHTTLNMpecVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFFT 592
Cdd:cd07841   221 tpteenwpgVTSLPdyvefkpfPPTPLKQIFPA---ASDDALDLLQRLLTLNPNKRITA-----RQALEHPYFS 286
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
421-533 1.11e-10

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: 62.77  E-value: 1.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 421 FEDLDKKLALASRFYIPEGCIQRWAAEMVVALDALHRE-GIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSC--DSDA 497
Cdd:cd06616    91 LDKFYKYVYEVLDSVIPEEILGKIAVATVKALNYLKEElKIIHRDVKPSNILLDRNGNIKLCDFGISGQLVDSIakTRDA 170
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1164769387 498 IERMYCAPEvgAITEETEA------CDWWSLGAVLFELLTGK 533
Cdd:cd06616   171 GCRPYMAPE--RIDPSASRdgydvrSDVWSLGITLYEVATGK 210
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
436-533 1.29e-10

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: 61.96  E-value: 1.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRG--HIQLTYFSRWSEVEDSCDSDAIERMYCAPEV-GAITE 512
Cdd:cd13987    88 LPEERVKRCAAQLASALDFMHSKNLVHRDIKPENVLLFDKDcrRVKLCDFGLTRRVGSTVKRVSGTIPYTAPEVcEAKKN 167
                          90       100
                  ....*....|....*....|....*
gi 1164769387 513 ETEAC----DWWSLGAVLFELLTGK 533
Cdd:cd13987   168 EGFVVdpsiDVWAFGVLLFCCLTGN 192
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
441-577 1.31e-10

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: 62.18  E-value: 1.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAemvvALDALHREGIVCRDLNPNNILL-------NDRGHIQLTYFS----RWSEVEDSCDSDAIERMYCAPEVGA 509
Cdd:cd14097   106 IQSLAS----AVAYLHKNDIVHRDLKLENILVkssiidnNDKLNIKVTDFGlsvqKYGLGEDMLQETCGTPIYMAPEVIS 181
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1164769387 510 ITEETEACDWWSLGAVLFELLTGK---------TLVECHPAGiNTHTTLNMPECVSEEARSLIQQLLQFNPLERLGA 577
Cdd:cd14097   182 AHGYSQQCDIWSIGVIMYMLLCGEppfvakseeKLFEEIRKG-DLTFTQSVWQSVSDAAKNVLQQLLKVDPAHRMTA 257
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
449-591 1.37e-10

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: 61.87  E-value: 1.37e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 449 VVALDALHREGIVCRDLNPNNILLN-DRGHIQLTYFSRWSEVEDSCDSDAI-ERMYCAPEvgaiteeteacdW------- 519
Cdd:cd14005   117 VEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCGALLKDSVYTDFDgTRVYSPPE------------Wirhgryh 184
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1164769387 520 ------WSLGAVLFELLTGKtLVECHPAGINTHTTLNMPEcVSEEARSLIQQLLQFNPLERLgagvaGVEDIKSHPFF 591
Cdd:cd14005   185 grpatvWSLGILLYDMLCGD-IPFENDEQILRGNVLFRPR-LSKECCDLISRCLQFDPSKRP-----SLEQILSHPWF 255
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
436-592 1.47e-10

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: 62.35  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SR--WSEVEDSCDSDAIERMYCAPEV--GA 509
Cdd:cd07832    97 LTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFglARlfSEEDPRLYSHQVATRWYRAPELlyGS 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 510 iTEETEACDWWSLGAVLFELLTGKTLVechpAG----------INTHTTLNM---------------------------- 551
Cdd:cd07832   177 -RKYDEGVDLWAVGCIFAELLNGSPLF----PGendieqlaivLRTLGTPNEktwpeltslpdynkitfpeskgirleei 251
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1164769387 552 -PECvSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFFT 592
Cdd:cd07832   252 fPDC-SPEAIDLLKGLLVYNPKKRLSA-----EEALRHPYFF 287
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
430-591 2.15e-10

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: 61.57  E-value: 2.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILL-----------NDRGHIQLTYFSRWSEVEDSCDSDAI 498
Cdd:cd14202    92 LHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLsysggrksnpnNIRIKIADFGFARYLQNNMMAATLCG 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 499 ERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVECH-PAGI------NTHTTLNMPECVSEEARSLIQQLLQFNP 571
Cdd:cd14202   172 SPMYMAPEVIMSQHYDAKADLWSIGTIIYQCLTGKAPFQASsPQDLrlfyekNKSLSPNIPRETSSHLRQLLLGLLQRNQ 251
                         170       180
                  ....*....|....*....|
gi 1164769387 572 LERLgagvaGVEDIKSHPFF 591
Cdd:cd14202   252 KDRM-----DFDEFFHHPFL 266
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
423-592 2.35e-10

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 62.09  E-value: 2.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 423 DLDKKLALASRFYIPE-GCIQRwaaEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SR---WSEVEDSCDSD 496
Cdd:PTZ00024  105 DLKKVVDRKIRLTESQvKCILL---QILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFglARrygYPPYSDTLSKD 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 497 AI----ERM--------YCAPEV--GAiTEETEACDWWSLGAVLFELLTGKTLV----ECHPAG-----INTHTTLNMPE 553
Cdd:PTZ00024  182 ETmqrrEEMtskvvtlwYRAPELlmGA-EKYHFAVDMWSVGCIFAELLTGKPLFpgenEIDQLGrifelLGTPNEDNWPQ 260
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1164769387 554 CV-----------------------SEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFFT 592
Cdd:PTZ00024  261 AKklplyteftprkpkdlktifpnaSDDAIDLLQSLLKLNPLERISA-----KEALKHEYFK 317
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
442-589 2.55e-10

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: 61.15  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 442 QRWAAEMV----VALDALHREGIVCRDLNPNNILLNDRGH---IQLTYFSRWSEVE--DSCDSDAIERMYCAPEVgaITE 512
Cdd:cd14089    99 EREAAEIMrqigSAVAHLHSMNIAHRDLKPENLLYSSKGPnaiLKLTDFGFAKETTtkKSLQTPCYTPYYVAPEV--LGP 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 513 ET--EACDWWSLGAVLFELLTGktlveCHPAGINTHTTLN--M-------------PE--CVSEEARSLIQQLLQFNPLE 573
Cdd:cd14089   177 EKydKSCDMWSLGVIMYILLCG-----YPPFYSNHGLAISpgMkkrirngqyefpnPEwsNVSEEAKDLIRGLLKTDPSE 251
                         170
                  ....*....|....*.
gi 1164769387 574 RLgagvaGVEDIKSHP 589
Cdd:cd14089   252 RL-----TIEEVMNHP 262
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
424-593 2.65e-10

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: 61.67  E-value: 2.65e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 424 LDK--KLALASRFYIPEGCIQRWAAEMVVALDALH-REGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSC--DSDAI 498
Cdd:cd06617    86 LDKfyKKVYDKGLTIPEDILGKIAVSIVKALEYLHsKLSVIHRDVKPSNVLINRNGQVKLCDFGISGYLVDSVakTIDAG 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 499 ERMYCAPEvgAITEETEA------CDWWSLGAVLFELLTG--------------KTLVEchpagiNTHTTLNMpECVSEE 558
Cdd:cd06617   166 CKPYMAPE--RINPELNQkgydvkSDVWSLGITMIELATGrfpydswktpfqqlKQVVE------EPSPQLPA-EKFSPE 236
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1164769387 559 ARSLIQQLLQFNPLERlgagvAGVEDIKSHPFFTP 593
Cdd:cd06617   237 FQDFVNKCLKKNYKER-----PNYPELLQHPFFEL 266
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
430-590 3.60e-10

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: 60.96  E-value: 3.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRfYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSE--------VEDSCDSDAierm 501
Cdd:cd14076    98 LARR-RLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTfdhfngdlMSTSCGSPC---- 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 YCAPEVGAITE--ETEACDWWSLGAVLFELLTGKTLVECHPAGIN-----------THTTLNMPECVSEEARSLIQQLLQ 568
Cdd:cd14076   173 YAAPELVVSDSmyAGRKADIWSCGVILYAMLAGYLPFDDDPHNPNgdnvprlyryiCNTPLIFPEYVTPKARDLLRRILV 252
                         170       180
                  ....*....|....*....|..
gi 1164769387 569 FNPLERlgagvAGVEDIKSHPF 590
Cdd:cd14076   253 PNPRKR-----IRLSAIMRHAW 269
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
440-535 4.08e-10

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK10, also called PISSLRE, is essential for cell growth and proliferation, and acts through the G2/M phase of the cell cycle. CDK10 has also been identified as an important factor in endocrine therapy resistance in breast cancer. CDK10 silencing increases the transcription of c-RAF and the activation of the p42/p44 MAPK pathway, which leads to antiestrogen resistance. Patients who express low levels of CDK10 relapse early on tamoxifen. 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 CDK10 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: 173742 [Multi-domain]  Cd Length: 309  Bit Score: 61.23  E-value: 4.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 440 CIQRwaaEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF---SRWSEVEDSCDSDAIERMYCAPEV--GAiTEET 514
Cdd:cd07845   112 CLML---QLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFglaRTYGLPAKPMTPKVVTLWYRAPELllGC-TTYT 187
                          90       100
                  ....*....|....*....|.
gi 1164769387 515 EACDWWSLGAVLFELLTGKTL 535
Cdd:cd07845   188 TAIDMWAVGCILAELLAHKPL 208
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
442-591 4.25e-10

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: 60.35  E-value: 4.25e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 442 QRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF------SRWSEvEDSCDSDAIERMYCAPEV--GAITEE 513
Cdd:cd14119   100 HGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFgvaealDLFAE-DDTCTTSQGSPAFQPPEIanGQDSFS 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 514 TEACDWWSLGAVLFELLTGKTLVEchpaGINTHT--------TLNMPECVSEEARSLIQQLLQFNPLERLgagvaGVEDI 585
Cdd:cd14119   179 GFKVDIWSAGVTLYNMTTGKYPFE----GDNIYKlfenigkgEYTIPDDVDPDLQDLLRGMLEKDPEKRF-----TIEQI 249

                  ....*.
gi 1164769387 586 KSHPFF 591
Cdd:cd14119   250 RQHPWF 255
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
435-591 4.57e-10

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: 60.63  E-value: 4.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 435 YIPEGCIQRWAAEMVVALDALHREG-----IVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDSCdsdAIERM----YC 503
Cdd:cd08217   101 YIPEEFIWKIFTQLLLALYECHNRSvgggkILHRDLKPANIFLDSDNNVKLGDFglARVLSHDSSF---AKTYVgtpyYM 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 504 APEVgaITEE--TEACDWWSLGAVLFELLTGKtlvecHPAGINTHTTLNM----------PECVSEEARSLIQQLLQFNP 571
Cdd:cd08217   178 SPEL--LNEQsyDEKSDIWSLGCLIYELCALH-----PPFQAANQLELAKkikegkfpriPSRYSSELNEVIKSMLNVDP 250
                         170       180
                  ....*....|....*....|
gi 1164769387 572 LERlgagvAGVEDIKSHPFF 591
Cdd:cd08217   251 DKR-----PSVEELLQLPLI 265
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
441-535 4.66e-10

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase; Protein Kinases (PKs), Dual-specificity tYrosine-phosphorylated and -Regulated Kinase (DYRK) subfamily, catalytic (c) domain. 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. The DYRK subfamily is part of a larger superfamily that includes the catalytic domains of other protein S/T PKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K). DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. Vertebrates contain multiple DYRKs (DYRK1-4) and mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A is involved in neuronal differentiation and is implicated in the pathogenesis of DS (Down syndrome). DYRK1B plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRK2 promotes apoptosis in response to DNA damage by phosphorylating the tumor suppressor p53, while DYRK3 promotes cell survival by phosphorylating SIRT1 and promoting p53 deacetylation. DYRK4 is a testis-specific kinase that may function during spermiogenesis.


Pssm-ID: 271112 [Multi-domain]  Cd Length: 311  Bit Score: 61.02  E-value: 4.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILL--NDRGHIQLTYF-SrwsevedSCDSDAI------ERMYCAPEV--GA 509
Cdd:cd14210   118 IRKFAKQILQALQFLHKLNIIHCDLKPENILLkqPSKSSIKVIDFgS-------SCFEGEKvytyiqSRFYRAPEVilGL 190
                          90       100
                  ....*....|....*....|....*.
gi 1164769387 510 itEETEACDWWSLGAVLFELLTGKTL 535
Cdd:cd14210   191 --PYDTAIDMWSLGCILAELYTGYPL 214
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
436-591 5.35e-10

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: 5.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERM-------YCAPEVg 508
Cdd:cd06610    99 LDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVSASLATGGDRTRKVRKtfvgtpcWMAPEV- 177
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 509 aITEE---TEACDWWSLGAVLFELLTGKT-LVECHPAGINTHTTLNMPECVSEEA---------RSLIQQLLQFNPLERL 575
Cdd:cd06610   178 -MEQVrgyDFKADIWSFGITAIELATGAApYSKYPPMKVLMLTLQNDPPSLETGAdykkysksfRKMISLCLQKDPSKRP 256
                         170
                  ....*....|....*.
gi 1164769387 576 GAgvagvEDIKSHPFF 591
Cdd:cd06610   257 TA-----EELLKHKFF 267
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
414-591 6.55e-10

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: 59.94  E-value: 6.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 414 DKEIHQIFEDLDKKLALA----SRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF---SRW 486
Cdd:cd14189    72 DAENIYIFLELCSRKSLAhiwkARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFglaARL 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 487 SEVEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGK------TLVECHPAGINTHTTLnmPECVSEEAR 560
Cdd:cd14189   152 EPPEQRKKTICGTPNYLAPEVLLRQGHGPESDVWSLGCVMYTLLCGNppfetlDLKETYRCIKQVKYTL--PASLSLPAR 229
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1164769387 561 SLIQQLLQFNPLERLgagvaGVEDIKSHPFF 591
Cdd:cd14189   230 HLLAGILKRNPGDRL-----TLDQILEHEFF 255
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
442-575 8.35e-10

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: 59.88  E-value: 8.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 442 QRWAAEMVVALDAL---HREGIVCRDLNPNNILLNDRGHIQLTYFSrWSevedsCDSDAIERM-------YCAPEVGAIT 511
Cdd:cd14117   106 QRTATFMEELADALhycHEKKVIHRDIKPENLLMGYKGELKIADFG-WS-----VHAPSLRRRtmcgtldYLPPEMIEGR 179
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1164769387 512 EETEACDWWSLGAVLFELLTGKTLVEChPAGINTH-----TTLNMPECVSEEARSLIQQLLQFNPLERL 575
Cdd:cd14117   180 THDEKVDLWCIGVLCYELLVGMPPFES-ASHTETYrrivkVDLKFPPFLSDGSRDLISKLLRYHPSERL 247
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
410-591 9.71e-10

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: 59.29  E-value: 9.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFE-DL-DKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLtyfsRWS 487
Cdd:cd14023    53 VILGDTKAYVFFEkDFgDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDEERTQL----RLE 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 488 EVEDS----CDSDAIER-----MYCAPEV--GAITEETEACDWWSLGAVLFELLTGK-TLVECHPAGINTHT---TLNMP 552
Cdd:cd14023   129 SLEDThimkGEDDALSDkhgcpAYVSPEIlnTTGTYSGKSADVWSLGVMLYTLLVGRyPFHDSDPSALFSKIrrgQFCIP 208
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1164769387 553 ECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd14023   209 DHVSPKARCLIRSLLRREPSERLTA-----PEILLHPWF 242
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
452-591 1.03e-09

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: 59.59  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 452 LDALHREGIVCRDLNPNNILL---NDRGHIQL---------------TYFSRWSEVEDSCDsdaiermYCAPEV---GAI 510
Cdd:cd13982   112 LAHLHSLNIVHRDLKPQNILIstpNAHGNVRAmisdfglckkldvgrSSFSRRSGVAGTSG-------WIAPEMlsgSTK 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 511 TEETEACDWWSLGAVLFELLTGKtlveCHPAGIN-------THTTLNMPECVSE-----EARSLIQQLLQFNPLERLGAg 578
Cdd:cd13982   185 RRQTRAVDIFSLGCVFYYVLSGG----SHPFGDKlereaniLKGKYSLDKLLSLgehgpEAQDLIERMIDFDPEKRPSA- 259
                         170
                  ....*....|...
gi 1164769387 579 vagvEDIKSHPFF 591
Cdd:cd13982   260 ----EEVLNHPFF 268
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
402-591 2.06e-09

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: 58.52  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 402 ETKGESGLVLE--GDKEIHQIfedLDKKLALasrfyiPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDR---G 476
Cdd:cd14106    78 ETRSELILILElaAGGELQTL---LDEEECL------TEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLTSEfplG 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 477 HIQLTYFSRWSEVEDSCDSDAI--ERMYCAPEVGAITEETEACDWWSLGAVLFELLTGktlveCHPAGINT--HTTLNMP 552
Cdd:cd14106   149 DIKLCDFGISRVIGEGEEIREIlgTPDYVAPEILSYEPISLATDMWSIGVLTYVLLTG-----HSPFGGDDkqETFLNIS 223
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1164769387 553 EC-----------VSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd14106   224 QCnldfpeelfkdVSPLAIDFIKRLLVKDPEKRLTA-----KECLEHPWL 268
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
430-591 2.54e-09

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: 58.48  E-value: 2.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTY-----------FSRWSEVEDSCDSDAI 498
Cdd:cd14201    96 LQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSYASRKKSSVsgirikiadfgFARYLQSNMMAATLCG 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 499 ERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVECH-PAGI------NTHTTLNMPECVSEEARSLIQQLLQFNP 571
Cdd:cd14201   176 SPMYMAPEVIMSQHYDAKADLWSIGTVIYQCLVGKPPFQANsPQDLrmfyekNKNLQPSIPRETSPYLADLLLGLLQRNQ 255
                         170       180
                  ....*....|....*....|
gi 1164769387 572 LERLgagvaGVEDIKSHPFF 591
Cdd:cd14201   256 KDRM-----DFEAFFSHPFL 270
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
447-590 3.51e-09

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-3 shows a restricted pattern of expression and is present in brain, kidney, and intestine. It is elevated in Alzheimer's disease (AD) and has been shown to associate with paired helical filaments (PHFs) and stimulate Tau phosphorylation. As AD progresses, phosphorylated Tau aggregates and forms PHFs, which leads to the formation of neurofibrillary tangles. In human glioma cells, PCTAIRE-3 induces cell cycle arrest and cell death. PCTAIRE-3 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-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: 270853 [Multi-domain]  Cd Length: 288  Bit Score: 58.10  E-value: 3.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDSCDSDAIERM-YCAPEV--GAiTEETEACDWWS 521
Cdd:cd07871   111 QLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFglARAKSVPTKTYSNEVVTLwYRPPDVllGS-TEYSTPIDMWG 189
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1164769387 522 LGAVLFELLTGKTLvechpaginthttlnMPECVSEEARSLIQQLLQfNPLERLGAGVAGVEDIKSHPF 590
Cdd:cd07871   190 VGCILYEMATGRPM---------------FPGSTVKEELHLIFRLLG-TPTEETWPGVTSNEEFRSYLF 242
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
402-574 4.28e-09

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: 57.52  E-value: 4.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 402 ETKGESGLVLE---GDKEIHQIFEDldKKLAlasrfyipEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHI 478
Cdd:cd14070    73 ETENSYYLVMElcpGGNLMHRIYDK--KRLE--------EREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNI 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 479 QLTYF-----SRWSEVEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVECHPAGINT-HTTL--- 549
Cdd:cd14070   143 KLIDFglsncAGILGYSDPFSTQCGSPAYAAPELLARKKYGPKVDVWSIGVNMYAMLTGTLPFTVEPFSLRAlHQKMvdk 222
                         170       180
                  ....*....|....*....|....*...
gi 1164769387 550 ---NMPECVSEEARSLIQQLLQFNPLER 574
Cdd:cd14070   223 emnPLPTDLSPGAISFLRSLLEPDPLKR 250
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
452-591 5.48e-09

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: 57.62  E-value: 5.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 452 LDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRwsevedSCDSDAIERM--------YCAPEVGAITEETE------AC 517
Cdd:cd14182   123 ICALHKLNIVHRDLKPENILLDDDMNIKLTDFGF------SCQLDPGEKLrevcgtpgYLAPEIIECSMDDNhpgygkEV 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 518 DWWSLGAVLFELLTG-------KTLVECHPAgINTHTTLNMPEC--VSEEARSLIQQLLQFNPLERLGAgvagvEDIKSH 588
Cdd:cd14182   197 DMWSTGVIMYTLLAGsppfwhrKQMLMLRMI-MSGNYQFGSPEWddRSDTVKDLISRFLVVQPQKRYTA-----EEALAH 270

                  ...
gi 1164769387 589 PFF 591
Cdd:cd14182   271 PFF 273
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
447-589 6.41e-09

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: 57.01  E-value: 6.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFS--------RWSEVEDSCDSDAiermYCAPEV--GAITEETEA 516
Cdd:cd14078   109 QIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGlcakpkggMDHHLETCCGSPA----YAAPELiqGKPYIGSEA 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 517 cDWWSLGAVLFELLTGKTlvechPAGINTHTTL---------NMPECVSEEARSLIQQLLQFNPLERLgagvaGVEDIKS 587
Cdd:cd14078   185 -DVWSMGVLLYALLCGFL-----PFDDDNVMALyrkiqsgkyEEPEWLSPSSKLLLDQMLQVDPKKRI-----TVKELLN 253

                  ..
gi 1164769387 588 HP 589
Cdd:cd14078   254 HP 255
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
410-591 6.77e-09

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-1 is expressed ubiquitously and is localized in the cytoplasm. Its kinase activity is cell cycle dependent and peaks at the S and G2 phases. PCTAIRE-1 is highly expressed in the brain and may play a role in regulating neurite outgrowth. It can also associate with Trap (Tudor repeat associator with PCTAIRE-2), a physiological partner of PCTAIRE-2; with p11, a small dimeric protein with similarity to S100; and with 14-3-3 proteins, mediators of phosphorylation-dependent interactions in many different proteins. PCTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-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: 270854 [Multi-domain]  Cd Length: 297  Bit Score: 57.32  E-value: 6.77e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFEDLDKKLalasRFYIpEGC--------IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLT 481
Cdd:cd07873    68 IIHTEKSLTLVFEYLDKDL----KQYL-DDCgnsinmhnVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLA 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 482 YF--SRWSEV-EDSCDSDAIERMYCAPEV--GAiTEETEACDWWSLGAVLFELLTGKTLV-------------------- 536
Cdd:cd07873   143 DFglARAKSIpTKTYSNEVVTLWYRPPDIllGS-TDYSTQIDMWGVGCIFYEMSTGRPLFpgstveeqlhfifrilgtpt 221
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 537 -ECHPaGINTH---TTLNMP----ECVSEEA-------RSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd07873   222 eETWP-GILSNeefKSYNYPkyraDALHNHAprldsdgADLLSKLLQFEGRKRISA-----EEAMKHPYF 285
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
440-591 7.26e-09

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: 57.57  E-value: 7.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 440 CIQRWAAEMVVALDALHREGIVCRDLNPNNILL-NDRGHIQLTYFSRWSE--VEDS----CD-----------SDAIE-R 500
Cdd:cd14134   116 HVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLvDSDYVKVYNPKKKRQIrvPKSTdiklIDfgsatfddeyhSSIVStR 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 501 MYCAPEVgaITEE--TEACDWWSLGAVLFELLTGKTLVECH----------------PA------------GINTHTTLN 550
Cdd:cd14134   196 HYRAPEV--ILGLgwSYPCDVWSIGCILVELYTGELLFQTHdnlehlammerilgplPKrmirrakkgakyFYFYHGRLD 273
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1164769387 551 MPE--------------------CVSEEARS---LIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd14134   274 WPEgsssgrsikrvckplkrlmlLVDPEHRLlfdLIRKMLEYDPSKRITA-----KEALKHPFF 332
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
432-592 7.97e-09

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: 56.84  E-value: 7.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVedscDSDAIER---------My 502
Cdd:cd06614    90 NPVRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFAAQL----TKEKSKRnsvvgtpywM- 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 503 cAPEVGAITEETEACDWWSLGAVLFELLTGK-TLVECHPAG----INTHTT--LNMPECVSEEARSLIQQLLQFNPLERl 575
Cdd:cd06614   165 -APEVIKRKDYGPKVDIWSLGIMCIEMAEGEpPYLEEPPLRalflITTKGIppLKNPEKWSPEFKDFLNKCLVKDPEKR- 242
                         170
                  ....*....|....*..
gi 1164769387 576 gagvAGVEDIKSHPFFT 592
Cdd:cd06614   243 ----PSAEELLQHPFLK 255
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
447-590 8.24e-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: 56.87  E-value: 8.24e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVedscdSDAIERM--------YCAPEVGAITEETEACD 518
Cdd:cd06609   106 EVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGVSGQL-----TSTMSKRntfvgtpfWMAPEVIKQSGYDEKAD 180
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1164769387 519 WWSLGAVLFELLTGKT-LVECHPAGI------NTHTTLNMPEcVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPF 590
Cdd:cd06609   181 IWSLGITAIELAKGEPpLSDLHPMRVlflipkNNPPSLEGNK-FSKPFKDFVELCLNKDPKERPSA-----KELLKHKF 253
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
413-583 8.50e-09

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: 56.62  E-value: 8.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 413 GDKEIHQIFEDLDKKLALASRFyipegciqRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDS 492
Cdd:cd13979    85 GNGTLQQLIYEGSEPLPLAHRI--------LISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGCSVKLGEG 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 493 CDSDAIERM------YCAPEVGAITEETEACDWWSLGAVLFELLTGKTlvechP-AGINTHTTLNM------PECVSEE- 558
Cdd:cd13979   157 NEVGTPRSHiggtytYRAPELLKGERVTPKADIYSFGITLWQMLTREL-----PyAGLRQHVLYAVvakdlrPDLSGLEd 231
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1164769387 559 ------ARSLIQQLLQFNPLERLGAGVAGVE 583
Cdd:cd13979   232 sefgqrLRSLISRCWSAQPAERPNADESLLK 262
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
432-574 9.57e-09

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: 56.53  E-value: 9.57e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDR-GHIQLTYFS---RWSEVEDSCDSDAIER------- 500
Cdd:cd13996   100 SSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGlatSIGNQKRELNNLNNNNngntsnn 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 501 -------MYCAPEVGAITEETEACDWWSLGAVLFELL-TGKTLVEchpagiNTHT-----TLNMPECVSE---EARSLIQ 564
Cdd:cd13996   180 svgigtpLYASPEQLDGENYNEKADIYSLGIILFEMLhPFKTAME------RSTIltdlrNGILPESFKAkhpKEADLIQ 253
                         170
                  ....*....|
gi 1164769387 565 QLLQFNPLER 574
Cdd:cd13996   254 SLLSKNPEER 263
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
447-590 1.00e-08

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: 56.54  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVedscDSDAIERMYC-------APEVGAITEETEA--- 516
Cdd:cd06608   121 ETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGVSAQL----DSTLGRRNTFigtpywmAPEVIACDQQPDAsyd 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 517 --CDWWSLGAVLFELLTGKT-LVECHPAGI------NTHTTLNMPECVSEEARSLIQQLLQFNPLERlgagvAGVEDIKS 587
Cdd:cd06608   197 arCDVWSLGITAIELADGKPpLCDMHPMRAlfkiprNPPPTLKSPEKWSKEFNDFISECLIKNYEQR-----PFTEELLE 271

                  ...
gi 1164769387 588 HPF 590
Cdd:cd06608   272 HPF 274
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
437-590 1.06e-08

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: 56.26  E-value: 1.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 437 PEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVED-----SCDSDAierMYCAPEVGA-- 509
Cdd:cd06632   100 EEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAfsfakSFKGSP---YWMAPEVIMqk 176
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 510 ITEETEACDWWSLGAVLFELLTGKT-LVECHPAGI-----NTHTTLNMPECVSEEARSLIQQLLQFNPLERLGAgvagvE 583
Cdd:cd06632   177 NSGYGLAVDIWSLGCTVLEMATGKPpWSQYEGVAAifkigNSGELPPIPDHLSPDAKDFIRLCLQRDPEDRPTA-----S 251

                  ....*..
gi 1164769387 584 DIKSHPF 590
Cdd:cd06632   252 QLLEHPF 258
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
451-591 1.12e-08

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: 56.55  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRwSEV------EDSCDSDAI--ERMYCAPEV-GAITEETEACDWWS 521
Cdd:cd13994   110 GVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGT-AEVfgmpaeKESPMSAGLcgSEPYMAPEVfTSGSYDGRAVDVWS 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 522 LGAVLFELLTGKtlvecHP----------------AGINTHTTLNMPECVS-EEARSLIQQLLQFNPLERLGAgvagvED 584
Cdd:cd13994   189 CGIVLFALFTGR-----FPwrsakksdsaykayekSGDFTNGPYEPIENLLpSECRRLIYRMLHPDPEKRITI-----DE 258

                  ....*..
gi 1164769387 585 IKSHPFF 591
Cdd:cd13994   259 ALNDPWV 265
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
441-535 1.16e-08

Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and -Regulated Kinases 2 and 3; 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 DYRK2 and DYRK3, and similar proteins. Drosophila DYRK2 interacts and phosphorylates the chromatin remodelling factor, SNR1 (Snf5-related 1), and also interacts with the essential chromatin component, trithorax. It may play a role in chromatin remodelling. Vertebrate DYRK2 phosphorylates and regulates the tumor suppressor p53 to induce apoptosis in response to DNA damage. It can also phosphorylate the transcription factor, nuclear factor of activated T cells (NFAT). DYRK2 is overexpressed in lung adenocarcinoma and esophageal carcinomas, and is a predictor for favorable prognosis in lung adenocarcinoma. DYRK3, also called regulatory erythroid kinase (REDK), is highly expressed in erythroid cells and the testis, and is also present in adult kidney and liver. It promotes cell survival by phosphorylating and activating SIRT1, an NAD(+)-dependent protein deacetylase, which promotes p53 deacetylation, resulting in the inhibition of apoptosis. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK2/3 subfamily is part of a larger superfamily that includes the catalytic domains of other S/T kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271126 [Multi-domain]  Cd Length: 380  Bit Score: 57.45  E-value: 1.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGH--IQLTYFSrwseveDSC-DSDAI-----ERMYCAPEVGAITE 512
Cdd:cd14224   170 VRKFAHSILQCLDALHRNKIIHCDLKPENILLKQQGRsgIKVIDFG------SSCyEHQRIytyiqSRFYRAPEVILGAR 243
                          90       100
                  ....*....|....*....|...
gi 1164769387 513 ETEACDWWSLGAVLFELLTGKTL 535
Cdd:cd14224   244 YGMPIDMWSFGCILAELLTGYPL 266
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
441-539 1.21e-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: 56.88  E-value: 1.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERMYCAPEV-GAITEETEACDW 519
Cdd:cd07880   120 IQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDSEMTGYVVTRWYRAPEViLNWMHYTQTVDI 199
                          90       100
                  ....*....|....*....|
gi 1164769387 520 WSLGAVLFELLTGKTLVECH 539
Cdd:cd07880   200 WSVGCIMAEMLTGKPLFKGH 219
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
447-591 1.26e-08

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: 55.81  E-value: 1.26e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLND--RGHIQL-----TYFSRWSEveDSCDSDAIERMYCAPEV--GAITEETEAC 517
Cdd:cd14022    92 QIASAVAHCHDGGLVLRDLKLRKFVFKDeeRTRVKLesledAYILRGHD--DSLSDKHGCPAYVSPEIlnTSGSYSGKAA 169
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1164769387 518 DWWSLGAVLFELLTGK-TLVECHPAGINTHT---TLNMPECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd14022   170 DVWSLGVMLYTMLVGRyPFHDIEPSSLFSKIrrgQFNIPETLSPKAKCLIRSILRREPSERLTS-----QEILDHPWF 242
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
433-591 1.43e-08

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: 56.13  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 433 RFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDrGHIQLTYFSrwsevedSCDSDAIE---------RMYC 503
Cdd:cd07831    94 KRPLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKD-DILKLADFG-------SCRGIYSKppyteyistRWYR 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 504 APEV----GAITEETeacDWWSLGAVLFELLT------GKTLVE----CH------PAGI------NTHTTLNMP----- 552
Cdd:cd07831   166 APEClltdGYYGPKM---DIWAVGCVFFEILSlfplfpGTNELDqiakIHdvlgtpDAEVlkkfrkSRHMNYNFPskkgt 242
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1164769387 553 --EC----VSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd07831   243 glRKllpnASAEGLDLLKKLLAYDPDERITA-----KQALRHPYF 282
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
301-531 1.55e-08

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 57.33  E-value: 1.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 301 KHYAQEDPRMLFV---AAVDHSSSGDmsllPSSDPKFQGLGVVESAVTANNTEESLFrICSPLSGAN----EYIASTDTL 373
Cdd:PTZ00267   17 NQYAKYFPHVLFTseeAFEKYCADLD----PEAYKKCVDLPEGEEVPESNNPREHMY-VLTTLVGRNpttaAFVATRGSD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 374 KTEEV-----LLFTDQTDDLAKEEPTSLFQRDsetkgESGLV-----LEGDKEIHQIFE-----DLDKKLALASRFYIPe 438
Cdd:PTZ00267   92 PKEKVvakfvMLNDERQAAYARSELHCLAACD-----HFGIVkhfddFKSDDKLLLIMEygsggDLNKQIKQRLKEHLP- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 439 gcIQRWAA-----EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERM-----YCAPEVG 508
Cdd:PTZ00267  166 --FQEYEVgllfyQIVLALDEVHSRKMMHRDLKSANIFLMPTGIIKLGDFGFSKQYSDSVSLDVASSFcgtpyYLAPELW 243
                         250       260
                  ....*....|....*....|...
gi 1164769387 509 AITEETEACDWWSLGAVLFELLT 531
Cdd:PTZ00267  244 ERKRYSKKADMWSLGVILYELLT 266
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
417-588 1.68e-08

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: 55.73  E-value: 1.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 417 IHQIFEDLDK---KLALASRF----YIPEGciQRWAA--------EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLT 481
Cdd:cd14161    67 VYEVFENSSKiviVMEYASRGdlydYISER--QRLSElearhffrQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIA 144
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 482 YFSrwseVEDSCDSDAIERMYCAPEVGAITEETEA-------CDWWSLGAVLFELLTG---------KTLVECHPAGINT 545
Cdd:cd14161   145 DFG----LSNLYNQDKFLQTYCGSPLYASPEIVNGrpyigpeVDSWSLGVLLYILVHGtmpfdghdyKILVKQISSGAYR 220
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1164769387 546 HTTLNMPECvseearSLIQQLLQFNPLERlgagvAGVEDIKSH 588
Cdd:cd14161   221 EPTKPSDAC------GLIRWLLMVNPERR-----ATLEDVASH 252
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
402-590 1.85e-08

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: 55.63  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 402 ETKGESGLVLEGDKEIHQIFEDLDKKLALasrfyiPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDR-GHIQL 480
Cdd:cd14101    77 EIPEGFLLVLERPQHCQDLFDYITERGAL------DESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRtGDIKL 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 481 TYFSRWSEVEDSCDSD-AIERMYCAPEvGAITEETEA--CDWWSLGAVLFELLTGKTLVECHPAGINTHTTLNMPecVSE 557
Cdd:cd14101   151 IDFGSGATLKDSMYTDfDGTRVYSPPE-WILYHQYHAlpATVWSLGILLYDMVCGDIPFERDTDILKAKPSFNKR--VSN 227
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1164769387 558 EARSLIQQLLQFNPLERlgagvAGVEDIKSHPF 590
Cdd:cd14101   228 DCRSLIRSCLAYNPSDR-----PSLEQILLHPW 255
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
430-590 1.97e-08

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: 55.52  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRF-YIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFS---RWSEVEDS-CDSDAIERM--- 501
Cdd:cd06631    93 ILARFgALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGcakRLCINLSSgSQSQLLKSMrgt 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 --YCAPEVGAITEETEACDWWSLGAVLFELLTGK-TLVECHPAG----INTHTTL--NMPECVSEEARSLIQQLLQFNPL 572
Cdd:cd06631   173 pyWMAPEVINETGHGRKSDIWSIGCTVFEMATGKpPWADMNPMAaifaIGSGRKPvpRLPDKFSPEARDFVHACLTRDQD 252
                         170
                  ....*....|....*...
gi 1164769387 573 ERLGAgvagvEDIKSHPF 590
Cdd:cd06631   253 ERPSA-----EQLLKHPF 265
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
432-590 2.14e-08

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: 55.27  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYfsrwSEVEDSC----DSDAIER-----MY 502
Cdd:cd14024    77 RRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFTDELRTKLVL----VNLEDSCplngDDDSLTDkhgcpAY 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 503 CAPEV--GAITEETEACDWWSLGAVLFELLTGK-TLVECHPAGINTHT---TLNMPECVSEEARSLIQQLLQFNPLERLG 576
Cdd:cd14024   153 VGPEIlsSRRSYSGKAADVWSLGVCLYTMLLGRyPFQDTEPAALFAKIrrgAFSLPAWLSPGARCLVSCMLRRSPAERLK 232
                         170
                  ....*....|....
gi 1164769387 577 AGvagveDIKSHPF 590
Cdd:cd14024   233 AS-----EILLHPW 241
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
452-591 2.32e-08

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: 55.35  E-value: 2.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 452 LDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSdaIERM-----YCAPEVgaITEE--TEACDWWSLGA 524
Cdd:cd06612   112 LEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGVSGQLTDTMAK--RNTVigtpfWMAPEV--IQEIgyNNKADIWSLGI 187
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1164769387 525 VLFELLTGK-TLVECHPA------GINTHTTLNMPECVSEEARSLIQQLLQFNPLERlgagvAGVEDIKSHPFF 591
Cdd:cd06612   188 TAIEMAEGKpPYSDIHPMraifmiPNKPPPTLSDPEKWSPEFNDFVKKCLVKDPEER-----PSAIQLLQHPFI 256
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
423-591 2.36e-08

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: 55.35  E-value: 2.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 423 DLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHI-QLTYFSRWSEVEDSCD---SDAI 498
Cdd:cd08225    85 DLMKRINRQRGVLFSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNGMVaKLGDFGIARQLNDSMElayTCVG 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 499 ERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKtlvecHPAGINTHTTLNMPEC----------VSEEARSLIQQLLQ 568
Cdd:cd08225   165 TPYYLSPEICQNRPYNNKTDIWSLGCVLYELCTLK-----HPFEGNNLHQLVLKICqgyfapispnFSRDLRSLISQLFK 239
                         170       180
                  ....*....|....*....|...
gi 1164769387 569 FNPLERlgagvAGVEDIKSHPFF 591
Cdd:cd08225   240 VSPRDR-----PSITSILKRPFL 257
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
447-578 2.67e-08

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: 55.49  E-value: 2.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGH-IQLTYF-------SRWSEVEDSCDSDAiermYCAPEVGAITE-ETEAC 517
Cdd:cd13974   140 DVVRVVEALHKKNIVHRDLKLGNMVLNKRTRkITITNFclgkhlvSEDDLLKDQRGSPA----YISPDVLSGKPyLGKPS 215
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1164769387 518 DWWSLGAVLFELLTGKtlvecHPAGINTHTTL---------NMPEC--VSEEARSLIQQLLQFNPLERLGAG 578
Cdd:cd13974   216 DMWALGVVLFTMLYGQ-----FPFYDSIPQELfrkikaaeyTIPEDgrVSENTVCLIRKLLVLNPQKRLTAS 282
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
447-577 2.73e-08

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: 55.45  E-value: 2.73e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF-----------SRWSEVEDSCDSDAIER----------MYCAP 505
Cdd:cd14046   112 QILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFglatsnklnveLATQDINKSTSAALGSSgdltgnvgtaLYVAP 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 506 EVGAITEET--EACDWWSLGAVLFELltgktlveCHPAG-----INTHTTL---------NMPECVSEEARSLIQQLLQF 569
Cdd:cd14046   192 EVQSGTKSTynEKVDMYSLGIIFFEM--------CYPFStgmerVQILTALrsvsiefppDFDDNKHSKQAKLIRWLLNH 263

                  ....*...
gi 1164769387 570 NPLERLGA 577
Cdd:cd14046   264 DPAKRPSA 271
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
410-591 2.86e-08

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: 55.20  E-value: 2.86e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFE----DLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF-- 483
Cdd:cd07860    67 VIHTENKLYLVFEflhqDLKKFMDASALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFgl 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 484 SRWSEVE-DSCDSDAIERMYCAPEV--GAITEETeACDWWSLGAVLFELLTGKTL---------------VECHPAGINT 545
Cdd:cd07860   147 ARAFGVPvRTYTHEVVTLWYRAPEIllGCKYYST-AVDIWSLGCIFAEMVTRRALfpgdseidqlfrifrTLGTPDEVVW 225
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1164769387 546 HTTLNMPE------------------CVSEEARSLIQQLLQFNPLERLGAGVAgvediKSHPFF 591
Cdd:cd07860   226 PGVTSMPDykpsfpkwarqdfskvvpPLDEDGRDLLSQMLHYDPNKRISAKAA-----LAHPFF 284
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
424-574 2.87e-08

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: 55.52  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 424 LDKKLALASRFyiPEGCIQRWAAEMVVALDALHRE-GIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDS-CDSDAIERM 501
Cdd:cd06620    91 LDKILKKKGPF--PEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGVSGELINSiADTFVGTST 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 YCAPEVGAITEETEACDWWSLGAVLFELLTGK---------TLVECHPAGINT--HTTLNMP-------ECVSEEARSLI 563
Cdd:cd06620   169 YMSPERIQGGKYSVKSDVWSLGLSIIELALGEfpfagsnddDDGYNGPMGILDllQRIVNEPpprlpkdRIFPKDLRDFV 248
                         170
                  ....*....|.
gi 1164769387 564 QQLLQFNPLER 574
Cdd:cd06620   249 DRCLLKDPRER 259
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
414-591 3.16e-08

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: 55.23  E-value: 3.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 414 DKEIHQIFEDLDKKLalasrfyIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEdSC 493
Cdd:cd07830    81 EGNLYQLMKDRKGKP-------FSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIR-SR 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 494 D--SDAIE-RMYCAPEVgaITEETE---ACDWWSLGAVLFELLTGKTL---------------------VECHPAGINTH 546
Cdd:cd07830   153 PpyTDYVStRWYRAPEI--LLRSTSyssPVDIWALGCIMAELYTLRPLfpgsseidqlykicsvlgtptKQDWPEGYKLA 230
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1164769387 547 TTLN--MPECV-----------SEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd07830   231 SKLGfrFPQFAptslhqlipnaSPEAIDLIKDMLRWDPKKRPTA-----SQALQHPYF 283
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
423-574 3.35e-08

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: 54.82  E-value: 3.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 423 DLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF------SRWSEVEDSCDSD 496
Cdd:cd08218    85 DLYKRINAQRGVLFPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFgiarvlNSTVELARTCIGT 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 497 AierMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVEchpAGINTHTTLNM--------PECVSEEARSLIQQLLQ 568
Cdd:cd08218   165 P---YYLSPEICENKPYNNKSDIWALGCVLYEMCTLKHAFE---AGNMKNLVLKIirgsyppvPSRYSYDLRSLVSQLFK 238

                  ....*.
gi 1164769387 569 FNPLER 574
Cdd:cd08218   239 RNPRDR 244
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
430-589 3.38e-08

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: 54.58  E-value: 3.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRG--HIQLTYFSRWSEVEDSCDSDAI----ErmYC 503
Cdd:cd14006    80 LAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLARKLNPGEELKEIfgtpE--FV 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 504 APEVgaITEE--TEACDWWSLGAVLFELLTGktlveCHP-AGINTHTTLN------------MPECVSEEARSLIQQLLQ 568
Cdd:cd14006   158 APEI--VNGEpvSLATDMWSIGVLTYVLLSG-----LSPfLGEDDQETLAnisacrvdfseeYFSSVSQEAKDFIRKLLV 230
                         170       180
                  ....*....|....*....|.
gi 1164769387 569 FNPLERLGAgvagvEDIKSHP 589
Cdd:cd14006   231 KEPRKRPTA-----QEALQHP 246
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
432-592 3.45e-08

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: 55.36  E-value: 3.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 432 SRFYIpegciqrwaAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEdscDSDAI------ERMYCAP 505
Cdd:cd14199   128 ARFYF---------QDLIKGIEYLHYQKIIHRDVKPSNLLVGEDGHIKIADFGVSNEFE---GSDALltntvgTPAFMAP 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 506 EVGAITEET---EACDWWSLGAVLFELLTGK-----TLVECHPAGINTHtTLNMPEC--VSEEARSLIQQLLQFNPLERL 575
Cdd:cd14199   196 ETLSETRKIfsgKALDVWAMGVTLYCFVFGQcpfmdERILSLHSKIKTQ-PLEFPDQpdISDDLKDLLFRMLDKNPESRI 274
                         170
                  ....*....|....*..
gi 1164769387 576 gagvaGVEDIKSHPFFT 592
Cdd:cd14199   275 -----SVPEIKLHPWVT 286
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
436-580 3.65e-08

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: 54.79  E-value: 3.65e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRG--HIQLTYFS------RWSEVEDSCDSDAiermYCAPEV 507
Cdd:cd14098    98 IPEQHARELTKQILEAMAYTHSMGITHRDLKPENILITQDDpvIVKISDFGlakvihTGTFLVTFCGTMA----YLAPEI 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 508 GAITEETE------ACDWWSLGAVLFELLTG---------KTLVECHPAGINTHTTLNMPEcVSEEARSLIQQLLQFNPL 572
Cdd:cd14098   174 LMSKEQNLqggysnLVDMWSVGCLVYVMLTGalpfdgssqLPVEKRIRKGRYTQPPLVDFN-ISEEAIDFILRLLDVDPE 252

                  ....*...
gi 1164769387 573 ERLGAGVA 580
Cdd:cd14098   253 KRMTAAQA 260
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
452-595 4.04e-08

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: 55.03  E-value: 4.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 452 LDALHREGIVCRDLNPNNILLNDRghiqltyfSRWSEVEDSCDSDAIERM---------------YCAPEVGAITEETEA 516
Cdd:cd14175   108 VEYLHSQGVVHRDLKPSNILYVDE--------SGNPESLRICDFGFAKQLraengllmtpcytanFVAPEVLKRQGYDEG 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 517 CDWWSLGAVLFELLTGKTLVECHP------------AGINTHTTLNMpECVSEEARSLIQQLLQFNPLERLGAgvagvED 584
Cdd:cd14175   180 CDIWSLGILLYTMLAGYTPFANGPsdtpeeiltrigSGKFTLSGGNW-NTVSDAAKDLVSKMLHVDPHQRLTA-----KQ 253
                         170
                  ....*....|.
gi 1164769387 585 IKSHPFFTPVD 595
Cdd:cd14175   254 VLQHPWITQKD 264
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
437-531 4.37e-08

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: 54.82  E-value: 4.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 437 PEGCIQRWAAEMVVALDALHRE-GIVCRDLNPNNILLNDRGHIQLTYF-----SRWSEVEDSCDSDAIerMYCAPEVGAI 510
Cdd:cd08528   111 TEDRIWNIFVQMVLALRYLHKEkQIVHRDLKPNNIMLGEDDKVTITDFglakqKGPESSKMTSVVGTI--LYSCPEIVQN 188
                          90       100
                  ....*....|....*....|.
gi 1164769387 511 TEETEACDWWSLGAVLFELLT 531
Cdd:cd08528   189 EPYGEKADIWALGCILYQMCT 209
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
423-591 4.81e-08

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: 54.44  E-value: 4.81e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 423 DLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDrGHIQLTYFSRWSEVEDSCDSDAIERM- 501
Cdd:cd14109    83 ELVRDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGIAHLDLRPEDILLQD-DKLKLADFGQSRRLLRGKLTTLIYGSp 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 -YCAPEVGAITEETEACDWWSLGAVLFELLTGKTlvechP-AGINTHTTL------------NMPECVSEEARSLIQQLL 567
Cdd:cd14109   162 eFVSPEIVNSYPVTLATDMWSVGVLTYVLLGGIS-----PfLGDNDRETLtnvrsgkwsfdsSPLGNISDDARDFIKKLL 236
                         170       180
                  ....*....|....*....|....
gi 1164769387 568 QFNPLERLgagvaGVEDIKSHPFF 591
Cdd:cd14109   237 VYIPESRL-----TVDEALNHPWF 255
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
414-591 4.87e-08

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK4 partners with all three D-type cyclins (D1, D2, and D3) and is also regulated by INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein and plays a role in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the nucleus. CDK4 also shows kinase activity towards Smad3, a signal transducer of TGF-beta signaling which modulates transcription and plays a role in cell proliferation and apoptosis. CDK4 is inhibited by the p21 inhibitor and is specifically mutated in human melanoma. 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 CDK4 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: 143368 [Multi-domain]  Cd Length: 288  Bit Score: 54.58  E-value: 4.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 414 DKEIH--QIFEDLDKKLalasRFYI--------PEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF 483
Cdd:cd07863    77 DRETKvtLVFEHVDQDL----RTYLdkvpppglPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADF 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 484 --SRWSEVEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVeCH----------------PAGINT 545
Cdd:cd07863   153 glARIYSCQMALTPVVVTLWYRAPEVLLQSTYATPVDMWSVGCIFAEMFRRKPLF-CGnseadqlgkifdliglPPEDDW 231
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1164769387 546 HTTLNMP-------------ECV---SEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd07863   232 PRDVTLPrgafsprgprpvqSVVpeiEESGAQLLLEMLTFNPHKRISA-----FRALQHPFF 288
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
410-590 5.99e-08

Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-2 is specifically expressed in neurons in the central nervous system, mainly in terminally differentiated neurons. It associates with Trap (Tudor repeat associator with PCTAIRE-2) and could play a role in regulating mitochondrial function in neurons. PCTAIRE-2 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PCTAIRE-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: 143377 [Multi-domain]  Cd Length: 309  Bit Score: 54.61  E-value: 5.99e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFEDLDKKLalasRFYIpEGC--------IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLT 481
Cdd:cd07872    72 IVHTDKSLTLVFEYLDKDL----KQYM-DDCgnimsmhnVKIFLYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 482 YF--SRWSEVEDSCDSDAIERM-YCAPEV--GAiTEETEACDWWSLGAVLFELLTGKTLvechpaginthttlnMPECVS 556
Cdd:cd07872   147 DFglARAKSVPTKTYSNEVVTLwYRPPDVllGS-SEYSTQIDMWGVGCIFFEMASGRPL---------------FPGSTV 210
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1164769387 557 EEARSLIQQLLQfNPLERLGAGVAGVEDIKSHPF 590
Cdd:cd07872   211 EDELHLIFRLLG-TPTEETWPGISSNDEFKNYNF 243
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
447-591 6.56e-08

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: 53.94  E-value: 6.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQL------TYFSRWSEVEDSCDSDAiermYCAPEV--GAITEETEAcD 518
Cdd:cd14071   107 QILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIadfgfsNFFKPGELLKTWCGSPP----YAAPEVfeGKEYEGPQL-D 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 519 WWSLGAVLFELLTGKTlvechPAGINTHTTLN---------MPECVSEEARSLIQQLLQFNPLERLgagvaGVEDIKSHP 589
Cdd:cd14071   182 IWSLGVVLYVLVCGAL-----PFDGSTLQTLRdrvlsgrfrIPFFMSTDCEHLIRRMLVLDPSKRL-----TIEQIKKHK 251

                  ..
gi 1164769387 590 FF 591
Cdd:cd14071   252 WM 253
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
447-590 8.48e-08

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: 53.84  E-value: 8.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILL---NDRGHIQLTYFSrWSEVED------SCDSDAiermYCAPEVGAITEETEAC 517
Cdd:cd14166   108 QVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFG-LSKMEQngimstACGTPG----YVAPEVLAQKPYSKAV 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 518 DWWSLGAVLFELLTG------KTLVECHPAGINTHTTLNMP--ECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHP 589
Cdd:cd14166   183 DCWSIGVITYILLCGyppfyeETESRLFEKIKEGYYEFESPfwDDISESAKDFIRHLLEKNPSKRYTC-----EKALSHP 257

                  .
gi 1164769387 590 F 590
Cdd:cd14166   258 W 258
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
410-591 9.16e-08

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK5 is unusual in that it is regulated by non-cyclin proteins, p35 and p39. It is highly expressed in the nervous system and is critical in normal neural development and function. It plays a role in neuronal migration and differentiation, and is also important in synaptic plasticity and learning. CDK5 also participates in protecting against cell death and promoting angiogenesis. Impaired CDK5 activity is implicated in Alzheimer's disease, amyotrophic lateral sclerosis, Parkinson's disease, Huntington's disease and acute neuronal injury. 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 CDK5 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: 143344 [Multi-domain]  Cd Length: 284  Bit Score: 53.98  E-value: 9.16e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFEDLD---KKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--S 484
Cdd:cd07839    67 VLHSDKKLTLVFEYCDqdlKKYFDSCNGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFglA 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 485 RWSEVEDSCDS-DAIERMYCAPEV--GAITEETeACDWWSLGAVLFELLTG----------------------------- 532
Cdd:cd07839   147 RAFGIPVRCYSaEVVTLWYRPPDVlfGAKLYST-SIDMWSAGCIFAELANAgrplfpgndvddqlkrifrllgtpteesw 225
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1164769387 533 ---------KTLVECHPAGINTHTTLNMpecvSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd07839   226 pgvsklpdyKPYPMYPATTSLVNVVPKL----NSTGRDLLQNLLVCNPVQRISA-----EEALQHPYF 284
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
451-591 9.83e-08

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: 53.87  E-value: 9.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALH-REGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERM--------------YCAPEVGAITEETE 515
Cdd:cd14011   126 ALSFLHnDVKLVHGNICPESVVINSNGEWKLAGFDFCISSEQATDQFPYFREydpnlpplaqpnlnYLAPEYILSKTCDP 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 516 ACDWWSLGAVLFELL-TGKTLVECHPAGIN--------THTTLNMPECVSEEARSLIQQLLQFNPLERLGAgvagvEDIK 586
Cdd:cd14011   206 ASDMFSLGVLIYAIYnKGKPLFDCVNNLLSykknsnqlRQLSLSLLEKVPEELRDHVKTLLNVTPEVRPDA-----EQLS 280

                  ....*
gi 1164769387 587 SHPFF 591
Cdd:cd14011   281 KIPFF 285
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
420-535 1.18e-07

Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase (also called MAPK13); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38delta/MAPK13 is found in skeletal muscle, heart, lung, testis, pancreas, and small intestine. It regulates microtubule function by phosphorylating Tau. It activates the c-jun promoter and plays a role in G2 cell cycle arrest. It also controls the degration of c-Myb, which is associated with myeloid leukemia and poor prognosis in colorectal cancer. p38delta is the main isoform involved in regulating the differentiation and apoptosis of keratinocytes. 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 p38delta 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: 143384 [Multi-domain]  Cd Length: 342  Bit Score: 54.14  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 420 IFEDLDKKLALasrfYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIE 499
Cdd:cd07879   102 MQTDLQKIMGH----PLSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADAEMTGYVVT 177
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1164769387 500 RMYCAPEV-GAITEETEACDWWSLGAVLFELLTGKTL 535
Cdd:cd07879   178 RWYRAPEViLNWMHYNQTVDIWSVGCIMAEMLTGKTL 214
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
441-532 1.21e-07

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 4; 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. DYRK4 is a testis-specific kinase with restricted expression to postmeiotic spermatids. It may function during spermiogenesis, however, it is not required for male fertility. DYRK4 has also been detected in a human teratocarcinoma cell line induced to produce postmitotic neurons. It may have a role in neuronal differentiation. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. They play important roles in cell proliferation, differentiation, survival, and development. The DYRK4 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: 271127 [Multi-domain]  Cd Length: 341  Bit Score: 53.94  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLtyfsrwsEVED---SCDSDAI------ERMYCAPEVGAIT 511
Cdd:cd14225   148 IRRFAISLLQCLRLLYRERIIHCDLKPENILLRQRGQSSI-------KVIDfgsSCYEHQRvytyiqSRFYRSPEVILGL 220
                          90       100
                  ....*....|....*....|.
gi 1164769387 512 EETEACDWWSLGAVLFELLTG 532
Cdd:cd14225   221 PYSMAIDMWSLGCILAELYTG 241
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
410-591 1.26e-07

Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of Plant B-type Cyclin-Dependent protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of CDK, CDK2, and CDK3. CDK1 is also called Cell division control protein 2 (Cdc2) or p34 protein kinase, and is regulated by cyclins A, B, and E. The CDK1/cyclin A complex controls G2 phase entry and progression while the CDK1/cyclin B complex is critical for G2 to M phase transition. 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. Studies in knockout mice revealed that CDK1 can compensate for the loss of the cdk2 gene as it can also bind cyclin E and drive 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. The plant-specific B-type CDKs are expressed from the late S to the M phase of the cell cycle. They are characterized by the cyclin binding motif PPT[A/T]LRE. They play a role in controlling mitosis and integrating developmental pathways, such as stomata and leaf development. CdkB has been shown to associate with both cyclin B, which controls G2/M transition, and cyclin D, which acts as a mediator in linking extracellular signals to the cell cycle. 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 CDK1 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: 270829 [Multi-domain]  Cd Length: 283  Bit Score: 53.45  E-value: 1.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFE----DLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF-- 483
Cdd:cd07835    66 VVHSENKLYLVFEfldlDLKKYMDSSPLTGLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFgl 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 484 SR---------WSEVedscdsdaIERMYCAPEV--GAITEETeACDWWSLGAVLFELLTGKTL----------------- 535
Cdd:cd07835   146 ARafgvpvrtyTHEV--------VTLWYRAPEIllGSKHYST-PVDIWSVGCIFAEMVTRRPLfpgdseidqlfrifrtl 216
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1164769387 536 ----------VECHPAGINTH-----TTLN--MPECvSEEARSLIQQLLQFNPLERLGAGVAgvediKSHPFF 591
Cdd:cd07835   217 gtpdedvwpgVTSLPDYKPTFpkwarQDLSkvVPSL-DEDGLDLLSQMLVYDPAKRISAKAA-----LQHPYF 283
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
441-568 1.28e-07

Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase (also called MAPK14); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38alpha/MAPK14 is expressed in most tissues and is the major isoform involved in the immune and inflammatory response. It is the central p38 MAPK involved in myogenesis. It plays a role in regulating cell cycle check-point transition and promoting cell differentiation. p38alpha also regulates cell proliferation and death through crosstalk with the JNK pathway. Its substrates include MAPK activated protein kinase 2 (MK2), MK5, and the transcription factors ATF2 and Mitf. p38 kinases 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 p38alpha 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: 143382 [Multi-domain]  Cd Length: 345  Bit Score: 53.89  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERMYCAPEVGA-ITEETEACDW 519
Cdd:cd07877   122 VQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEIMLnWMHYNQTVDI 201
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1164769387 520 WSLGAVLFELLTGKTLVechpAGINTHTTLNM---------PECV----SEEARSLIQQLLQ 568
Cdd:cd07877   202 WSVGCIMAELLTGRTLF----PGTDHIDQLKLilrlvgtpgAELLkkisSESARNYIQSLTQ 259
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
455-591 1.31e-07

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: 53.13  E-value: 1.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 455 LHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERM-----YCAPEVgaITEET--EACDWWSLGAVLF 527
Cdd:cd06625   118 LHSNMIVHRDIKGANILRDSNGNVKLGDFGASKRLQTICSSTGMKSVtgtpyWMSPEV--INGEGygRKADIWSVGCTVV 195
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 528 ELLTGK-TLVECHPAG----INTHTTL-NMPECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd06625   196 EMLTTKpPWAEFEPMAaifkIATQPTNpQLPPHVSEDARDFLSLIFVRNKKQRPSA-----EELLSHSFV 260
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
447-590 1.46e-07

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: 52.99  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDrGHIQLTYFSRWSEVEDscDSDAIER-------MYCAPEVGAITEETE---- 515
Cdd:cd14131   111 QMLEAVHTIHEEGIVHSDLKPANFLLVK-GRLKLIDFGIAKAIQN--DTTSIVRdsqvgtlNYMSPEAIKDTSASGegkp 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 516 ------ACDWWSLGAVLFELLTGKT-------LVECHPAGINTHTTLNMPECVSEEARSLIQQLLQFNPLERlgagvAGV 582
Cdd:cd14131   188 kskigrPSDVWSLGCILYQMVYGKTpfqhitnPIAKLQAIIDPNHEIEFPDIPNPDLIDVMKRCLQRDPKKR-----PSI 262

                  ....*...
gi 1164769387 583 EDIKSHPF 590
Cdd:cd14131   263 PELLNHPF 270
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
430-591 1.59e-07

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: 52.86  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLT--YFSRWSEVEDS---------CDSDAi 498
Cdd:cd14165    93 IKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTdfGFSKRCLRDENgrivlsktfCGSAA- 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 499 ermYCAPEV-GAITEETEACDWWSLGAVLFELLTG---------KTLVEchpagINTHTTLNMPECV--SEEARSLIQQL 566
Cdd:cd14165   172 ---YAAPEVlQGIPYDPRIYDIWSLGVILYIMVCGsmpyddsnvKKMLK-----IQKEHRVRFPRSKnlTSECKDLIYRL 243
                         170       180
                  ....*....|....*....|....*
gi 1164769387 567 LQFNPLERLgagvaGVEDIKSHPFF 591
Cdd:cd14165   244 LQPDVSQRL-----CIDEVLSHPWL 263
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
452-590 1.59e-07

Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NLK is an atypical mitogen-activated protein kinase (MAPK) that is not regulated by a MAPK kinase. It functions downstream of the MAPK kinase kinase Tak1, which also plays a role in activating the JNK and p38 MAPKs. The Tak1/NLK pathways are regulated by Wnts, a family of secreted proteins that is critical in the control of asymmetric division and cell polarity. NLK can phosphorylate transcription factors from the TCF/LEF family, inhibiting their ability to activate the transcription of target genes. In prostate cancer cells, NLK is involved in regulating androgen receptor-mediated transcription and its expression is altered during cancer progression. MAPKs are important mediators of cellular responses to extracellular signals. The NLK 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: 173748 [Multi-domain]  Cd Length: 372  Bit Score: 53.59  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 452 LDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDSCD--SDAIERMYCAPEV--GAiTEETEACDWWSLGAV 525
Cdd:cd07853   116 LKYLHSAGILHRDIKPGNLLVNSNCVLKICDFglARVEEPDESKHmtQEVVTQYYRAPEIlmGS-RHYTSAVDIWSVGCI 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 526 LFELLTGKTLVE--------------------------CHPAGINTHTTLNMPECVS----------EEARSLIQQLLQF 569
Cdd:cd07853   195 FAELLGRRILFQaqspiqqldlitdllgtpsleamrsaCEGARAHILRGPHKPPSLPvlytlssqatHEAVHLLCRMLVF 274
                         170       180
                  ....*....|....*....|.
gi 1164769387 570 NPLERLGAgvagvEDIKSHPF 590
Cdd:cd07853   275 DPDKRISA-----ADALAHPY 290
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
451-591 1.71e-07

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L1, also called PITSLRE, exists in different isoforms which are named using the alias CDK11(p). The CDC2L1 gene produces two protein products, CDK11(p110) and CDK11(p58). CDC2L1 is also represented by the caspase-processed CDK11(p46). CDK11(p110), the major isoform, associates with cyclin L and is expressed throughout the cell cycle. It is involved in RNA processing and the regulation of transcription. CDK11(p58) associates with cyclin D3 and is expressed during the G2/M phase of the cell cycle. It plays roles in spindle morphogenesis, centrosome maturation, sister chromatid cohesion, and the completion of mitosis. CDK11(p46) is formed from the larger isoforms by caspases during TNFalpha- and Fas-induced apoptosis. It functions as a downstream effector kinase in apoptotic signaling pathways and interacts with eukaryotic initiation factor 3f (eIF3f), p21-activated kinase (PAK1), and Ran-binding protein (RanBPM). 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 CDC2L1 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: 173741 [Multi-domain]  Cd Length: 293  Bit Score: 53.00  E-value: 1.71e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNILLNDRGHIQLTYFS---RWSEVEDSCDSDAIERMYCAPEV--GAiTEETEACDWWSLGAV 525
Cdd:cd07843   118 GVAHLHDNWILHRDLKTSNLLLNNRGILKICDFGlarEYGSPLKPYTQLVVTLWYRAPELllGA-KEYSTAIDMWSVGCI 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 526 LFELLTGKTL---------------------VECHPA-----GINTHTTLNMPEC----------VSEEARSLIQQLLQF 569
Cdd:cd07843   197 FAELLTKKPLfpgkseidqlnkifkllgtptEKIWPGfselpGAKKKTFTKYPYNqlrkkfpalsLSDNGFDLLNRLLTY 276
                         170       180
                  ....*....|....*....|..
gi 1164769387 570 NPLERLGAgvagvEDIKSHPFF 591
Cdd:cd07843   277 DPAKRISA-----EDALKHPYF 293
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
451-592 2.16e-07

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: 52.73  E-value: 2.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNILLNDR---GHIQLT--YFSRWSEVEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAV 525
Cdd:cd14170   113 AIQYLHSINIAHRDVKPENLLYTSKrpnAILKLTdfGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYDKSCDMWSLGVI 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 526 LFELLTGktlvecHPAGINTHTTLNMPEC------------------VSEEARSLIQQLLQFNPLERLgagvaGVEDIKS 587
Cdd:cd14170   193 MYILLCG------YPPFYSNHGLAISPGMktrirmgqyefpnpewseVSEEVKMLIRNLLKTEPTQRM-----TITEFMN 261

                  ....*
gi 1164769387 588 HPFFT 592
Cdd:cd14170   262 HPWIM 266
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
424-533 2.22e-07

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: 53.13  E-value: 2.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 424 LDKKLALASRfyIPEGCIQRWAAEMVVALDAL-HREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDS-CDSDAIERM 501
Cdd:cd06650    90 LDQVLKKAGR--IPEQILGKVSIAVIKGLTYLrEKHKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSmANSFVGTRS 167
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1164769387 502 YCAPEVGAITEETEACDWWSLGAVLFELLTGK 533
Cdd:cd06650   168 YMSPERLQGTHYSVQSDIWSMGLSLVEMAVGR 199
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
424-533 2.82e-07

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: 52.44  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 424 LDKKLALASRfyIPEGCIQRWAAEMVVALDALHRE-GIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDS-CDSDAIERM 501
Cdd:cd06615    86 LDQVLKKAGR--IPENILGKISIAVLRGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSmANSFVGTRS 163
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1164769387 502 YCAPEVGAITEETEACDWWSLGAVLFELLTGK 533
Cdd:cd06615   164 YMSPERLQGTHYTVQSDIWSLGLSLVEMAIGR 195
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
447-592 2.94e-07

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: 52.24  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEdsCDSDAIERM-----YCAPEVGAITEETEACDWWS 521
Cdd:cd14187   115 QIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVE--YDGERKKTLcgtpnYIAPEVLSKKGHSFEVDIWS 192
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1164769387 522 LGAVLFELLTGKTLVECHPAGiNTHTTL-----NMPECVSEEARSLIQQLLQFNPLERlgagvAGVEDIKSHPFFT 592
Cdd:cd14187   193 IGCIMYTLLVGKPPFETSCLK-ETYLRIkkneySIPKHINPVAASLIQKMLQTDPTAR-----PTINELLNDEFFT 262
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
436-532 3.14e-07

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: 52.09  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrwseVEDSCDSDAIERM-------YCAPEVg 508
Cdd:cd06917    98 IAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFG----VAASLNQNSSKRStfvgtpyWMAPEV- 172
                          90       100
                  ....*....|....*....|....*..
gi 1164769387 509 aITEETE---ACDWWSLGAVLFELLTG 532
Cdd:cd06917   173 -ITEGKYydtKADIWSLGITTYEMATG 198
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
424-574 3.19e-07

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: 52.23  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 424 LDKKLALASRFYIPEG--CIQRWAAEMVVALDALHREGIVCRDLNPNNILL-----NDRGHIQLTYF--SRWSEVEDSCD 494
Cdd:cd14000    95 LDHLLQQDSRSFASLGrtLQQRIALQVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAIIIKIADYgiSRQCCRMGAKG 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 495 SDAIERmYCAPEVGAITEE-TEACDWWSLGAVLFELLTGKTLVECH---PAGINTHT----TLNMPECVS-EEARSLIQQ 565
Cdd:cd14000   175 SEGTPG-FRAPEIARGNVIyNEKVDVFSFGMLLYEILSGGAPMVGHlkfPNEFDIHGglrpPLKQYECAPwPEVEVLMKK 253

                  ....*....
gi 1164769387 566 LLQFNPLER 574
Cdd:cd14000   254 CWKENPQQR 262
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
447-567 3.27e-07

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: 52.32  E-value: 3.27e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDS---CDSDAIERMYCAPEVGAITEETEA-----CD 518
Cdd:cd06638   132 EALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTrlrRNTSVGTPFWMAPEVIACEQQLDStydarCD 211
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1164769387 519 WWSLGAVLFELLTGK-TLVECHPAGI------NTHTTLNMPECVSEEARSLIQQLL 567
Cdd:cd06638   212 VWSLGITAIELGDGDpPLADLHPMRAlfkiprNPPPTLHQPELWSNEFNDFIRKCL 267
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
451-532 3.28e-07

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: 52.34  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNILL---NDRGHIQLTYFSRWSEVEDSCDSDAIER----------MYCAPE-VGAITEET-- 514
Cdd:cd14173   112 ALDFLHNKGIAHRDLKPENILCehpNQVSPVKICDFDLGSGIKLNSDCSPISTpelltpcgsaEYMAPEvVEAFNEEAsi 191
                          90       100
                  ....*....|....*....|
gi 1164769387 515 --EACDWWSLGAVLFELLTG 532
Cdd:cd14173   192 ydKRCDLWSLGVILYIMLSG 211
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
401-535 3.34e-07

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK6 is regulated by D-type cyclins and INK4 inhibitors. It is active towards the retinoblastoma (pRb) protein, implicating it to function in regulating the early G1 phase of the cell cycle. It is expressed ubiquitously and is localized in the cytoplasm. It is also present in the ruffling edge of spreading fibroblasts and may play a role in cell spreading. It binds to the p21 inhibitor without any effect on its own activity and it is overexpressed in squamous cell carcinomas and neuroblastomas. CDK6 has also been shown to inhibit cell differentiation in many cell types. 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 CDK6 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: 270846 [Multi-domain]  Cd Length: 290  Bit Score: 52.34  E-value: 3.34e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 401 SETKGESGLVLegdkeihqIFEDLDKKLAL----ASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRG 476
Cdd:cd07862    76 SRTDRETKLTL--------VFEHVDQDLTTyldkVPEPGVPTETIKDMMFQLLRGLDFLHSHRVVHRDLKPQNILVTSSG 147
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1164769387 477 HIQLTYF--SRWSEVEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTL 535
Cdd:cd07862   148 QIKLADFglARIYSFQMALTSVVVTLWYRAPEVLLQSSYATPVDLWSVGCIFAEMFRRKPL 208
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
447-591 3.65e-07

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 51.78  E-value: 3.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLND-RGHIQLTYFsRWSEVED--SCDSDAIErmYCAPEvgAITEE--TEACDWWS 521
Cdd:PHA03390  117 QLVEALNDLHKHNIIHNDIKLENVLYDRaKDRIYLCDY-GLCKIIGtpSCYDGTLD--YFSPE--KIKGHnyDVSFDWWA 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 522 LGAVLFELLTGKtlvecHPAGINT-------------HTTLNMPECVSEEARSLIQQLLQFNPLERLgagvAGVEDIKSH 588
Cdd:PHA03390  192 VGVLTYELLTGK-----HPFKEDEdeeldlesllkrqQKKLPFIKNVSKNANDFVQSMLKYNINYRL----TNYNEIIKH 262

                  ...
gi 1164769387 589 PFF 591
Cdd:PHA03390  263 PFL 265
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
441-566 4.01e-07

Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase (also called MAPK11); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38beta/MAPK11 is widely expressed in tissues and shows more similarity with p38alpha than with the other isoforms. Both are sensitive to pyridinylimidazoles and share some common substrates such as MAPK activated protein kinase 2 (MK2) and the transcription factors ATF2, c-Fos and, ELK-1. p38beta is involved in regulating the activation of the cyclooxygenase-2 promoter and the expression of TGFbeta-induced alpha-smooth muscle cell actin. p38 kinases are mitogen-activated protein kinases (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 p38beta 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: 143383 [Multi-domain]  Cd Length: 343  Bit Score: 52.36  E-value: 4.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERMYCAPEVGA-ITEETEACDW 519
Cdd:cd07878   120 VQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLARQADDEMTGYVATRWYRAPEIMLnWMHYNQTVDI 199
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1164769387 520 WSLGAVLFELLTGKTLVechPAG------------INTHTTLNMPECVSEEARSLIQQL 566
Cdd:cd07878   200 WSVGCIMAELLKGKALF---PGNdyidqlkrimevVGTPSPEVLKKISSEHARKYIQSL 255
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
399-589 4.29e-07

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: 51.56  E-value: 4.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 399 RDSETKGESGLVLE----GDkeihqIFEDLdkklALASRFyiPEgciqRWAAEMVV----ALDALHREGIVCRDLNPNNI 470
Cdd:cd14095    65 EEYDTDTELYLVMElvkgGD-----LFDAI----TSSTKF--TE----RDASRMVTdlaqALKYLHSLSIVHRDIKPENL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 471 LLNDRG----HIQLTYFSRWSEVEDS----CDSDAiermYCAPEVGAITEETEACDWWSLGAVLFELLTG---------- 532
Cdd:cd14095   130 LVVEHEdgskSLKLADFGLATEVKEPlftvCGTPT----YVAPEILAETGYGLKVDIWAAGVITYILLCGfppfrspdrd 205
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 533 -KTLVECHPAGintHTTLNMP--ECVSEEARSLIQQLLQFNPLERLGAGvagveDIKSHP 589
Cdd:cd14095   206 qEELFDLILAG---EFEFLSPywDNISDSAKDLISRMLVVDPEKRYSAG-----QVLDHP 257
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
414-590 4.33e-07

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: 51.77  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 414 DKEIHQIFEDLDK--------KLALASrFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILL---NDRGHIQLTY 482
Cdd:cd14094    77 DGMLYMVFEFMDGadlcfeivKRADAG-FVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGG 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 483 FSRWSEVEDScDSDAIERM----YCAPEVGAITEETEACDWWSLGAVLFELLTGK-----TLVECHPAGINTHTTLNMPE 553
Cdd:cd14094   156 FGVAIQLGES-GLVAGGRVgtphFMAPEVVKREPYGKPVDVWGCGVILFILLSGClpfygTKERLFEGIIKGKYKMNPRQ 234
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1164769387 554 C--VSEEARSLIQQLLQFNPLERLgagvaGVEDIKSHPF 590
Cdd:cd14094   235 WshISESAKDLVRRMLMLDPAERI-----TVYEALNHPW 268
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
438-590 4.35e-07

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: 51.64  E-value: 4.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 438 EGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLND-RGHIQLTYF---SRWSEVEDSCDSDAIERMYCAPEV------ 507
Cdd:cd06624   107 ENTIGYYTKQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFgtsKRLAGINPCTETFTGTLQYMAPEVidkgqr 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 508 --GAiteeteACDWWSLGAVLFELLTGKT----LVECHPA----GI-NTHTtlNMPECVSEEARSLIQQLLQFNPLERlg 576
Cdd:cd06624   187 gyGP------PADIWSLGCTIIEMATGKPpfieLGEPQAAmfkvGMfKIHP--EIPESLSEEAKSFILRCFEPDPDKR-- 256
                         170
                  ....*....|....
gi 1164769387 577 agvAGVEDIKSHPF 590
Cdd:cd06624   257 ---ATASDLLQDPF 267
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
455-595 4.64e-07

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: 51.94  E-value: 4.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 455 LHREGIVCRDLNPNNILLNDRG----HIQLTYFSRWSEVEDSCD---SDAIERMYCAPEVGAITEETEACDWWSLGAVLF 527
Cdd:cd14176   129 LHAQGVVHRDLKPSNILYVDESgnpeSIRICDFGFAKQLRAENGllmTPCYTANFVAPEVLERQGYDAACDIWSLGVLLY 208
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1164769387 528 ELLTGKTLVECHP--------AGINT---HTTLNMPECVSEEARSLIQQLLQFNPLERLGAGvagveDIKSHPFFTPVD 595
Cdd:cd14176   209 TMLTGYTPFANGPddtpeeilARIGSgkfSLSGGYWNSVSDTAKDLVSKMLHVDPHQRLTAA-----LVLRHPWIVHWD 282
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
447-591 4.72e-07

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: 51.23  E-value: 4.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVED---SCDSDAIErmYCAPEV--GAITEETEAcDWWS 521
Cdd:cd14004   117 QVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAYIKSgpfDTFVGTID--YAAPEVlrGNPYGGKEQ-DIWA 193
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1164769387 522 LGAVLFELLTGKTlvechPAgINTHTTLN----MPECVSEEARSLIQQLLQFNPLERlgagvAGVEDIKSHPFF 591
Cdd:cd14004   194 LGVLLYTLVFKEN-----PF-YNIEEILEadlrIPYAVSEDLIDLISRMLNRDVGDR-----PTIEELLTDPWL 256
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
438-591 4.83e-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: 51.65  E-value: 4.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 438 EGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEV--EDSCDSDAIERMY-CAPEVGAITEET 514
Cdd:cd06656   114 EGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpEQSKRSTMVGTPYwMAPEVVTRKAYG 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 515 EACDWWSLGAVLFELLTGK-------TLVECHPAGINTHTTLNMPECVSEEARSLIQQLLQFNpLERLGAGvagvEDIKS 587
Cdd:cd06656   194 PKVDIWSLGIMAIEMVEGEppylnenPLRALYLIATNGTPELQNPERLSAVFRDFLNRCLEMD-VDRRGSA----KELLQ 268

                  ....
gi 1164769387 588 HPFF 591
Cdd:cd06656   269 HPFL 272
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
436-590 5.72e-07

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: 51.42  E-value: 5.72e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAI-ERMYCAPEVGAITEET 514
Cdd:cd06619    92 IPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVNSIAKTYVgTNAYMAPERISGEQYG 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 515 EACDWWSLGAVLFELLTGKTlveCHPAGINTHTTLnMP----ECVSEEAR-------------SLIQQLLQFNPLERLGA 577
Cdd:cd06619   172 IHSDVWSLGISFMELALGRF---PYPQIQKNQGSL-MPlqllQCIVDEDPpvlpvgqfsekfvHFITQCMRKQPKERPAP 247
                         170
                  ....*....|...
gi 1164769387 578 gvagvEDIKSHPF 590
Cdd:cd06619   248 -----ENLMDHPF 255
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
436-601 6.00e-07

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: 51.27  E-value: 6.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAI-ERMYCAPEvgAITEE- 513
Cdd:cd06621   102 IGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGVSGELVNSLAGTFTgTSYYMAPE--RIQGGp 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 514 -TEACDWWSLGAVLFELLTGKTLVE---CHPAG-------INTHTTLNMPECV------SEEARSLIQQLLQFNPLERlg 576
Cdd:cd06621   180 ySITSDVWSLGLTLLEVAQNRFPFPpegEPPLGpiellsyIVNMPNPELKDEPengikwSESFKDFIEKCLEKDGTRR-- 257
                         170       180       190
                  ....*....|....*....|....*....|
gi 1164769387 577 agvAGVEDIKSHPFFT-----PVDWAELMR 601
Cdd:cd06621   258 ---PGPWQMLAHPWIKaqekkKVNMAKFVK 284
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
451-574 6.54e-07

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: 51.18  E-value: 6.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNIL---LNDRGHIQLTYFSrWSEVEDS-------CDSDAiermYCAPEVGAITEETEACDWW 520
Cdd:cd14167   113 AVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFG-LSKIEGSgsvmstaCGTPG----YVAPEVLAQKPYSKAVDCW 187
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1164769387 521 SLGAVLFELLTG------KTLVECHPAGINTHTTLNMP--ECVSEEARSLIQQLLQFNPLER 574
Cdd:cd14167   188 SIGVIAYILLCGyppfydENDAKLFEQILKAEYEFDSPywDDISDSAKDFIQHLMEKDPEKR 249
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
430-591 6.79e-07

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: 50.78  E-value: 6.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF---SRWSEVEDSCDSDAIERMYCAPE 506
Cdd:cd14188    92 LKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFglaARLEPLEHRRRTICGTPNYLSPE 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 507 VgaITEETEAC--DWWSLGAVLFELLTGKTLVEChpagINTHTT--------LNMPECVSEEARSLIQQLLQFNPLERlg 576
Cdd:cd14188   172 V--LNKQGHGCesDIWALGCVMYTMLLGRPPFET----TNLKETyrcirearYSLPSSLLAPAKHLIASMLSKNPEDR-- 243
                         170
                  ....*....|....*
gi 1164769387 577 agvAGVEDIKSHPFF 591
Cdd:cd14188   244 ---PSLDEIIRHDFF 255
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
447-590 7.48e-07

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: 50.92  E-value: 7.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGH---IQLTYFSRWSEVEDSCDSDAIERMYCAPEV------------GAIT 511
Cdd:cd14171   117 QIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKLCDFGFAKVDQGDLMTPQFTPYYVAPQVleaqrrhrkersGIPT 196
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 512 EET-----EACDWWSLGAVLFELLTG-KTLVECHPAGINTHT--------TLNMPE----CVSEEARSLIQQLLQFNPLE 573
Cdd:cd14171   197 SPTpytydKSCDMWSLGVIIYIMLCGyPPFYSEHPSRTITKDmkrkimtgSYEFPEeewsQISEMAKDIVRKLLCVDPEE 276
                         170
                  ....*....|....*..
gi 1164769387 574 RLgagvaGVEDIKSHPF 590
Cdd:cd14171   277 RM-----TIEEVLHHPW 288
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
424-533 8.16e-07

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: 50.84  E-value: 8.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 424 LDKKLALASRFyIPEGCIQRWAAEMVVALDALHRE-GIVCRDLNPNNILLNDRGHIQLTYFSRWSEVedsCDSDAIER-- 500
Cdd:cd06618   100 LDKLLKRIQGP-IPEDILGKMTVSIVKALHYLKEKhGVIHRDVKPSNILLDESGNVKLCDFGISGRL---VDSKAKTRsa 175
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1164769387 501 ---MYCAPEvgAITEETEA-----CDWWSLGAVLFELLTGK 533
Cdd:cd06618   176 gcaAYMAPE--RIDPPDNPkydirADVWSLGISLVELATGQ 214
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
419-580 8.88e-07

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: 50.88  E-value: 8.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 419 QIFEDLdkklaLASRFYI---PEGCIQrwaaEMVVALDALHREGIVCRDLNPNNILLNDR---GHIQLTYFSRWSEVEDS 492
Cdd:cd14086    86 ELFEDI-----VAREFYSeadASHCIQ----QILESVNHCHQNGIVHRDLKPENLLLASKskgAAVKLADFGLAIEVQGD 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 493 CDSD---AIERMYCAPEVGAITEETEACDWWSLGAVLFELLTG---------KTLVECHPAGINTHTTlnmPE--CVSEE 558
Cdd:cd14086   157 QQAWfgfAGTPGYLSPEVLRKDPYGKPVDIWACGVILYILLVGyppfwdedqHRLYAQIKAGAYDYPS---PEwdTVTPE 233
                         170       180
                  ....*....|....*....|..
gi 1164769387 559 ARSLIQQLLQFNPLERLGAGVA 580
Cdd:cd14086   234 AKDLINQMLTVNPAKRITAAEA 255
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
443-574 1.08e-06

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP1 harbors a C-terminal Death domain (DD), which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 can also recruit other kinases including MEKK1, MEKK3, and RIP3 through an intermediate domain (ID) that bears a RIP homotypic interaction motif (RHIM). RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accummulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. RIP kinases serve as essential sensors of cellular stress. The RIP1 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: 270929 [Multi-domain]  Cd Length: 267  Bit Score: 50.58  E-value: 1.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 443 RWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQ-----LTYFSRWS-----------EVEDSCDSDAIERMYCAPE 506
Cdd:cd14027    94 RIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKiadlgLASFKMWSkltkeehneqrEVDGTAKKNAGTLYYMAPE 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 507 -VGAI-TEETEACDWWSLGAVLFELLTGKTLVE----------CHPAGiNTHTTLNMPECVSEEARSLIQQLLQFNPLER 574
Cdd:cd14027   174 hLNDVnAKPTEKSDVYSFAIVLWAIFANKEPYEnainedqiimCIKSG-NRPDVDDITEYCPREIIDLMKLCWEANPEAR 252
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
437-590 1.12e-06

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: 50.70  E-value: 1.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 437 PEGC----IQRWAAEMVVALDALHREGIVCRDLNPNNILLN-DRGHIQLTYFSrWSEVEDSCDSDAIER-MYCAPE---- 506
Cdd:cd14020   104 NQGCsmwmIQHCARDVLEALAFLHHEGYVHADLKPRNILWSaEDECFKLIDFG-LSFKEGNQDVKYIQTdGYRAPEaelq 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 507 -------VGAITEETEACDWWSLGAVLFELLTGKTLVEC--------HPAGINTH----TTLNMPECVSEEARSLIQQLL 567
Cdd:cd14020   183 nclaqagLQSETECTSAVDLWSLGIVLLEMFSGMKLKHTvrsqewkdNSSAIIDHifasNAVVNPAIPAYHLRDLIKSML 262
                         170       180
                  ....*....|....*....|...
gi 1164769387 568 QFNPLERLGAGVAGVEDIKSHPF 590
Cdd:cd14020   263 HNDPGKRATAEAALCSPFFSIPF 285
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
447-574 1.13e-06

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 51.41  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrWSEVEDSCDSDAIERMYC------APEVGAITEETEACDWW 520
Cdd:PTZ00283  151 QVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFG-FSKMYAATVSDDVGRTFCgtpyyvAPEIWRRKPYSKKADMF 229
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1164769387 521 SLGAVLFELLTGKTLVEchpaGINTHTTLN---------MPECVSEEARSLIQQLLQFNPLER 574
Cdd:PTZ00283  230 SLGVLLYELLTLKRPFD----GENMEEVMHktlagrydpLPPSISPEMQEIVTALLSSDPKRR 288
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
404-535 1.20e-06

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: 50.39  E-value: 1.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 404 KGESGLVLE-GDKEIHQIFEdldkklalASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLT- 481
Cdd:cd07833    72 KGRLYLVFEyVERTLLELLE--------ASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCd 143
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1164769387 482 -YFSRW--SEVEDSCDSDAIERMYCAPE--VGAiTEETEACDWWSLGAVLFELLTGKTL 535
Cdd:cd07833   144 fGFARAltARPASPLTDYVATRWYRAPEllVGD-TNYGKPVDVWAIGCIMAELLDGEPL 201
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
438-591 1.22e-06

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: 50.31  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 438 EGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEV--EDSCDSDAIERMY-CAPEVGAITEET 514
Cdd:cd06647   102 EGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpEQSKRSTMVGTPYwMAPEVVTRKAYG 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 515 EACDWWSLGAVLFELLTGK-------TLVECHPAGINTHTTLNMPECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKS 587
Cdd:cd06647   182 PKVDIWSLGIMAIEMVEGEppylnenPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMDVEKRGSA-----KELLQ 256

                  ....
gi 1164769387 588 HPFF 591
Cdd:cd06647   257 HPFL 260
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
436-574 1.22e-06

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: 50.23  E-value: 1.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHRE-GIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIE-RMYCAPE---VGAI 510
Cdd:cd06622    99 IPEDVLRRITYAVVKGLKFLKEEhNIIHRDVKPTNVLVNGNGQVKLCDFGVSGNLVASLAKTNIGcQSYMAPErikSGGP 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 511 TEE---TEACDWWSLGAVLFELLTGktlveCHPAGINTHTTL-------------NMPECVSEEARSLIQQLLQFNPLER 574
Cdd:cd06622   179 NQNptyTVQSDVWSLGLSILEMALG-----RYPYPPETYANIfaqlsaivdgdppTLPSGYSDDAQDFVAKCLNKIPNRR 253
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
452-577 1.25e-06

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: 50.40  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 452 LDALHREGIVCRDLNPNNILLNDRG----HIQLTYFSRWSEVEDSCD---SDAIERMYCAPEVGAITEETEACDWWSLGA 524
Cdd:cd14178   110 VEYLHSQGVVHRDLKPSNILYMDESgnpeSIRICDFGFAKQLRAENGllmTPCYTANFVAPEVLKRQGYDAACDIWSLGI 189
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1164769387 525 VLFELLTGKTLVECHP------------AGINTHTTLNMpECVSEEARSLIQQLLQFNPLERLGA 577
Cdd:cd14178   190 LLYTMLAGFTPFANGPddtpeeilarigSGKYALSGGNW-DSISDAAKDIVSKMLHVDPHQRLTA 253
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
452-591 1.52e-06

Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PCTAIRE-like proteins show unusual expression patterns with high levels in post-mitotic tissues, suggesting that they may be involved in regulating post-mitotic cellular events. They share sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The association of PCTAIRE-like proteins with cyclins has not been widely studied, although PFTAIRE-1 has been shown to function as a CDK which is regulated by cyclin D3 as well as the membrane-associated cyclin Y. The PCTAIRE-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: 270835 [Multi-domain]  Cd Length: 286  Bit Score: 50.07  E-value: 1.52e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 452 LDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEV-EDSCDSDAIERMYCAPEV--GAiTEETEACDWWSLGAVL 526
Cdd:cd07844   111 LAYCHQRRVLHRDLKPQNLLISERGELKLADFglARAKSVpSKTYSNEVVTLWYRPPDVllGS-TEYSTSLDMWGVGCIF 189
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 527 FELLTGKTLV----------------------ECHPaGIN---THTTLNMPECVSE-------------EARSLIQQLLQ 568
Cdd:cd07844   190 YEMATGRPLFpgstdvedqlhkifrvlgtpteETWP-GVSsnpEFKPYSFPFYPPRplinhaprldripHGEELALKFLQ 268
                         170       180
                  ....*....|....*....|...
gi 1164769387 569 FNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd07844   269 YEPKKRISA-----AEAMKHPYF 286
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
436-571 1.61e-06

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: 50.04  E-value: 1.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVC---RDLNPNNILL-----ND---RGHIQLTYFSRWSEVEDSCD-SDAIERMYC 503
Cdd:cd14146    99 IPPHILVNWAVQIARGMLYLHEEAVVPilhRDLKSSNILLlekieHDdicNKTLKITDFGLAREWHRTTKmSAAGTYAWM 178
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1164769387 504 APEVGAITEETEACDWWSLGAVLFELLTGKT-------LVECHPAGINThTTLNMPECVSEEARSLIQQLLQFNP 571
Cdd:cd14146   179 APEVIKSSLFSKGSDIWSYGVLLWELLTGEVpyrgidgLAVAYGVAVNK-LTLPIPSTCPEPFAKLMKECWEQDP 252
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
424-533 1.71e-06

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: 50.43  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 424 LDKKLALASRfyIPEGCIQRWAAEMVVALDAL-HREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDS-CDSDAIERM 501
Cdd:cd06649    90 LDQVLKEAKR--IPEEILGKVSIAVLRGLAYLrEKHQIMHRDVKPSNILVNSRGEIKLCDFGVSGQLIDSmANSFVGTRS 167
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1164769387 502 YCAPEVGAITEETEACDWWSLGAVLFELLTGK 533
Cdd:cd06649   168 YMSPERLQGTHYSVQSDIWSMGLSLVELAIGR 199
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
436-591 1.79e-06

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 50.42  E-value: 1.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGH-IQLTYFSRWSEVEDSCDSDA--IERMYCAPE--VGAi 510
Cdd:PTZ00036  167 LPLFLVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDPNTHtLKLCDFGSAKNLLAGQRSVSyiCSRFYRAPElmLGA- 245
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 511 TEETEACDWWSLGAVLFELLTGKTLVECHPA-----------GINTHTTLN----------------------MPECVSE 557
Cdd:PTZ00036  246 TNYTTHIDLWSLGCIIAEMILGYPIFSGQSSvdqlvriiqvlGTPTEDQLKemnpnyadikfpdvkpkdlkkvFPKGTPD 325
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1164769387 558 EARSLIQQLLQFNPLERLGAgVAGVEDikshPFF 591
Cdd:PTZ00036  326 DAINFISQFLKYEPLKRLNP-IEALAD----PFF 354
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
436-589 1.83e-06

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: 49.61  E-value: 1.83e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEV--EDSCDSDAIERMYCAPEV--GAIt 511
Cdd:cd14050    97 LPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELdkEDIHDAQEGDPRYMAPELlqGSF- 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 512 eeTEACDWWSLGAVLFELLTGKTLVEchpAGINTHTTLN--MPE----CVSEEARSLIQQLLQFNPLERlgagvAGVEDI 585
Cdd:cd14050   176 --TKAADIFSLGITILELACNLELPS---GGDGWHQLRQgyLPEeftaGLSPELRSIIKLMMDPDPERR-----PTAEDL 245

                  ....
gi 1164769387 586 KSHP 589
Cdd:cd14050   246 LALP 249
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
437-592 1.88e-06

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: 49.74  E-value: 1.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 437 PEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRG-HIQLTYFSRWSEVEdSCDSDAIERM--------YCAPEV 507
Cdd:cd06630   101 SENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTGqRLRIADFGAAARLA-SKGTGAGEFQgqllgtiaFMAPEV 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 508 GAITEETEACDWWSLGAVLFELLTGKtlvecHPAG---INTHTTL-----------NMPECVSEEARSLIQQLLQFNPLE 573
Cdd:cd06630   180 LRGEQYGRSCDVWSVGCVIIEMATAK-----PPWNaekISNHLALifkiasattppPIPEHLSPGLRDVTLRCLELQPED 254
                         170
                  ....*....|....*....
gi 1164769387 574 RLGAgvagvEDIKSHPFFT 592
Cdd:cd06630   255 RPPA-----RELLKHPVFT 268
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
409-590 1.94e-06

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: 49.58  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 409 LVLEGDKEIHQIFEDLDKKLALasrfyiPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLN-DRGHIQLTYFSRWS 487
Cdd:cd14100    82 LVLERPEPVQDLFDFITERGAL------PEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGA 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 488 EVEDSCDSDAI-ERMYCAPE-VGAITEETEACDWWSLGAVLFELLTGKTLVECHPAGINTHTTLNmpECVSEEARSLIQQ 565
Cdd:cd14100   156 LLKDTVYTDFDgTRVYSPPEwIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEHDEEIIRGQVFFR--QRVSSECQHLIKW 233
                         170       180
                  ....*....|....*....|....*
gi 1164769387 566 LLQFNPLERlgagvAGVEDIKSHPF 590
Cdd:cd14100   234 CLALRPSDR-----PSFEDIQNHPW 253
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
406-591 2.03e-06

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Pho85 is a multifunctional CDK in yeast. It is regulated by 10 different cyclins (Pcls) and plays a role in G1 progression, cell polarity, phosphate and glycogen metabolism, gene expression, and in signaling changes in the environment. It is not essential for yeast viability and is the functional homolog of mammalian CDK5, which plays a role in central nervous system development. 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 Pho85 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: 143341 [Multi-domain]  Cd Length: 284  Bit Score: 49.79  E-value: 2.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 406 ESGLVLegdkeihqIFEDLDKKL-----ALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQL 480
Cdd:cd07836    70 ENKLML--------VFEYMDKDLkkymdTHGVRGALDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKL 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 481 TYF--SRWSEVE-DSCDSDAIERMYCAPEV--GAITEETeACDWWSLGAVLFELLTGKTLVechpAGIN----------- 544
Cdd:cd07836   142 ADFglARAFGIPvNTFSNEVVTLWYRAPDVllGSRTYST-SIDIWSVGCIMAEMITGRPLF----PGTNnedqllkifri 216
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1164769387 545 --THTTLNMPECV-SEEAR-----------------------SLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd07836   217 mgTPTESTWPGISqLPEYKptfpryppqdlqqlfphadplgiDLLHRLLQLNPELRISA-----HDALQHPWF 284
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
441-535 2.07e-06

Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PRP4 phosphorylates a number of factors involved in the formation of active spliceosomes, which catalyze pre-mRNA splicing. It phosphorylates PRP6 and PRP31, components of the U4/U6-U5 tri-small nuclear ribonucleoprotein (snRNP), during spliceosomal complex formation. In fission yeast, PRP4 phosphorylates the splicing factor PRP1 (U5-102 kD in mammals). Thus, PRP4 plays a key role in regulating spliceosome assembly and pre-mRNA splicing. It also plays an important role in mitosis by acting as a spindle assembly checkpoint kinase that is required for chromosome alignment and the recruitment of the checkpoint proteins MPS1, MAD1, and MAD2 at kinetochores. The PRP4 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: 271037 [Multi-domain]  Cd Length: 318  Bit Score: 49.91  E-value: 2.07e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLN-DRGHIQLTYFSRWSEVEdscDSDAIE----RMYCAPEV--GAITEe 513
Cdd:cd14135   107 VRSYAQQLFLALKHLKKCNILHADIKPDNILVNeKKNTLKLCDFGSASDIG---ENEITPylvsRFYRAPEIilGLPYD- 182
                          90       100
                  ....*....|....*....|..
gi 1164769387 514 tEACDWWSLGAVLFELLTGKTL 535
Cdd:cd14135   183 -YPIDMWSVGCTLYELYTGKIL 203
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
429-533 2.29e-06

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: 49.21  E-value: 2.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 429 ALASRfYIPEGCIQRWAAEMVVALDALHREGIVC---RDLNPNNILLNDRGH--------IQLTYFSRWSEVEDSCD-SD 496
Cdd:cd14148    83 ALAGK-KVPPHVLVNWAVQIARGMNYLHNEAIVPiihRDLKSSNILILEPIEnddlsgktLKITDFGLAREWHKTTKmSA 161
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1164769387 497 AIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGK 533
Cdd:cd14148   162 AGTYAWMAPEVIRLSLFSKSSDVWSFGVLLWELLTGE 198
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
418-591 2.30e-06

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: 49.14  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 418 HQIFEDLDKKLALASrfyipegcIQRWAAEMVVALDALHREGIVCRDLNPNNILLN-DRGHIQLTYFSRwseVEDSCDSD 496
Cdd:cd14019    88 HDDFRDFYRKMSLTD--------IRIYLRNLFKALKHVHSFGIIHRDVKPGNFLYNrETGKGVLVDFGL---AQREEDRP 156
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 497 AIE------RMYCAPEV-GAITEETEACDWWSLGAVLFELLTGktlveCHPAGINTHTTLNMPECVS----EEARSLIQQ 565
Cdd:cd14019   157 EQRapragtRGFRAPEVlFKCPHQTTAIDIWSAGVILLSILSG-----RFPFFFSSDDIDALAEIATifgsDEAYDLLDK 231
                         170       180
                  ....*....|....*....|....*.
gi 1164769387 566 LLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd14019   232 LLELDPSKRITA-----EEALKHPFF 252
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
452-595 2.44e-06

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: 49.63  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 452 LDALHREGIVCRDLNPNNIL-LNDRGH---IQLTYFSRWSEVEDSCD---SDAIERMYCAPEVGAITEETEACDWWSLGA 524
Cdd:cd14177   111 VDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLRGENGlllTPCYTANFVAPEVLMRQGYDAACDIWSLGV 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 525 VLFELLTGKTLVECHPAGINTHTTLNMP-----------ECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFFTP 593
Cdd:cd14177   191 LLYTMLAGYTPFANGPNDTPEEILLRIGsgkfslsggnwDTVSDAAKDLLSHMLHVDPHQRYTA-----EQVLKHSWIAC 265

                  ..
gi 1164769387 594 VD 595
Cdd:cd14177   266 RD 267
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
441-593 2.45e-06

Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-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 the mitogen-activated protein kinases (MAPKs) ERK1, ERK2, baker's yeast Fus3, and similar proteins. MAPK pathways are important mediators of cellular responses to extracellular signals. ERK1/2 activation is preferentially by mitogenic factors, differentiation stimuli, and cytokines, through a kinase cascade involving the MAPK kinases MEK1/2 and a MAPK kinase kinase from the Raf family. ERK1/2 have numerous substrates, many of which are nuclear and participate in transcriptional regulation of many cellular processes. They regulate cell growth, cell proliferation, and cell cycle progression from G1 to S phase. Although the distinct roles of ERK1 and ERK2 have not been fully determined, it is known that ERK2 can maintain most functions in the absence of ERK1, and that the deletion of ERK2 is embryonically lethal. The MAPK, Fus3, regulates yeast mating processes including mating-specific gene expression, G1 arrest, mating projection, and cell fusion. This ERK1/2-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: 270839 [Multi-domain]  Cd Length: 336  Bit Score: 49.61  E-value: 2.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLN----------------DRGHI---QLTYF--SRWsevedscdsdaie 499
Cdd:cd07849   108 IQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNtncdlkicdfglariaDPEHDhtgFLTEYvaTRW------------- 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 500 rmYCAPEVGAITEE-TEACDWWSLGAVLFELLTGKTLVechpAGINTHTTLNM-------P-----ECV-SEEARS---- 561
Cdd:cd07849   175 --YRAPEIMLNSKGyTKAIDIWSVGCILAEMLSNRPLF----PGKDYLHQLNLilgilgtPsqedlNCIiSLKARNyiks 248
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1164769387 562 ----------------------LIQQLLQFNPLERLgagvaGVEDIKSHPFFTP 593
Cdd:cd07849   249 lpfkpkvpwnklfpnadpkaldLLDKMLTFNPHKRI-----TVEEALAHPYLEQ 297
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
455-574 2.78e-06

Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. They can be classified into receptor and non-receptor tyr kinases. PTKs play important roles in many cellular processes including, lymphocyte activation, epithelium growth and maintenance, metabolism control, organogenesis regulation, survival, proliferation, differentiation, migration, adhesion, motility, and morphogenesis. Receptor tyr kinases (RTKs) are integral membrane proteins which contain an extracellular ligand-binding region, a transmembrane segment, and an intracellular tyr kinase domain. RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain, leading to intracellular signaling. Some RTKs are orphan receptors with no known ligands. Non-receptor (or cytoplasmic) tyr kinases are distributed in different intracellular compartments and are usually multi-domain proteins containing a catalytic tyr kinase domain as well as various regulatory domains such as SH3 and SH2. PTKs are usually autoinhibited and require a mechanism for activation. In many PTKs, the phosphorylation of tyr residues in the activation loop is essential for optimal activity. Aberrant expression of PTKs is associated with many development abnormalities and cancers.The PTK family is part of a larger superfamily that includes the catalytic domains of serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270623 [Multi-domain]  Cd Length: 262  Bit Score: 49.07  E-value: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 455 LHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDSCDSDAIERM---YCAPEvgAITEE--TEACDWWSLGAVLF 527
Cdd:cd00192   121 LASKKFVHRDLAARNCLVGEDLVVKISDFglSRDIYDDDYYRKKTGGKLpirWMAPE--SLKDGifTSKSDVWSFGVLLW 198
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1164769387 528 ELLT-GKTlvechP-AGINTHTT---------LNMPECVSEEARSLIQQLLQFNPLER 574
Cdd:cd00192   199 EIFTlGAT-----PyPGLSNEEVleylrkgyrLPKPENCPDELYELMLSCWQLDPEDR 251
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
451-591 2.86e-06

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: 48.98  E-value: 2.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVedscdSDAIER--------MYCAPEVgaITEE---TEAcDW 519
Cdd:cd06648   115 ALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFCAQV-----SKEVPRrkslvgtpYWMAPEV--ISRLpygTEV-DI 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 520 WSLGAVLFELLTG-------------KTLVECHPAginthtTLNMPECVSEEARSLIQQLLQFNPLERlgagvAGVEDIK 586
Cdd:cd06648   187 WSLGIMVIEMVDGeppyfnepplqamKRIRDNEPP------KLKNLHKVSPRLRSFLDRMLVRDPAQR-----ATAAELL 255

                  ....*
gi 1164769387 587 SHPFF 591
Cdd:cd06648   256 NHPFL 260
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
435-574 2.92e-06

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: 48.96  E-value: 2.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 435 YIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHI-QLTYFSRWSEVedSCDSDAIERM----YCAPEVGA 509
Cdd:cd08220    97 LLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKIL--SSKSKAYTVVgtpcYISPELCE 174
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 510 ITEETEACDWWSLGAVLFELLTGKTLVECH--PA---GINTHTTLNMPECVSEEARSLIQQLLQFNPLER 574
Cdd:cd08220   175 GKPYNQKSDIWALGCVLYELASLKRAFEAAnlPAlvlKIMRGTFAPISDRYSEELRHLILSMLHLDPNKR 244
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
446-580 3.01e-06

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: 49.42  E-value: 3.01e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 446 AEMVVALDALHREGIVCRDLNPNNILL--------------------NDRGHIQLTYFSRWSEVEDSCDSDAIERMYCAP 505
Cdd:cd14018   145 LQLLEGVDHLVRHGIAHRDLKSDNILLeldfdgcpwlviadfgcclaDDSIGLQLPFSSWYVDRGGNACLMAPEVSTAVP 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 506 EVGAITEETEAcDWWSLGAVLFELLTGKTLVECHPAGINTHTTLN------MPECVSEEARSLIQQLLQFNPLERLGAGV 579
Cdd:cd14018   225 GPGVVINYSKA-DAWAVGAIAYEIFGLSNPFYGLGDTMLESRSYQesqlpaLPSAVPPDVRQVVKDLLQRDPNKRVSARV 303

                  .
gi 1164769387 580 A 580
Cdd:cd14018   304 A 304
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
451-532 3.10e-06

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: 49.37  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNILLNDRGH------IQLTYFSRWSEVEdSCDSDAIERMYCAPEVGAITEETEACDWWSLGA 524
Cdd:cd13989   114 AISYLHENRIIHRDLKPENIVLQQGGGrviyklIDLGYAKELDQGS-LCTSFVGTLQYLAPELFESKKYTCTVDYWSFGT 192

                  ....*...
gi 1164769387 525 VLFELLTG 532
Cdd:cd13989   193 LAFECITG 200
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
449-567 3.12e-06

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: 49.22  E-value: 3.12e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 449 VVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrwseVEDSCDSDAIER-------MYCAPEVGAITEETEA----- 516
Cdd:cd06639   138 LLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFG----VSAQLTSARLRRntsvgtpFWMAPEVIACEQQYDYsydar 213
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1164769387 517 CDWWSLGAVLFELLTGK-TLVECHPAGI------NTHTTLNMPECVSEEARSLIQQLL 567
Cdd:cd06639   214 CDVWSLGITAIELADGDpPLFDMHPVKAlfkiprNPPPTLLNPEKWCRGFSHFISQCL 271
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
435-574 3.75e-06

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: 48.83  E-value: 3.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 435 YIPEGCIQRWAAEMVVALDALH---REGIVCRDLNPNNILLNDRGHIQLTYFSRWS----EVEDScdSDAIER------- 500
Cdd:cd13986   102 FFPEDRILHIFLGICRGLKAMHepeLVPYAHRDIKPGNVLLSEDDEPILMDLGSMNpariEIEGR--REALALqdwaaeh 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 501 ---MYCAPEV-----GAITeeTEACDWWSLGAVLFELLTGKT---LVECHPAGIN---THTTLNMPEC--VSEEARSLIQ 564
Cdd:cd13986   180 ctmPYRAPELfdvksHCTI--DEKTDIWSLGCTLYALMYGESpfeRIFQKGDSLAlavLSGNYSFPDNsrYSEELHQLVK 257
                         170
                  ....*....|
gi 1164769387 565 QLLQFNPLER 574
Cdd:cd13986   258 SMLVVNPAER 267
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
441-535 3.80e-06

Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p38 kinases are mitogen-activated protein kinases (MAPKs), serving as important mediators of cellular responses to extracellular signals. They function in the regulation of the cell cycle, cell development, cell differentiation, senescence, tumorigenesis, apoptosis, pain development and pain progression, and immune responses. p38 kinases 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. p38 substrates include other protein kinases and factors that regulate transcription, nuclear export, mRNA stability and translation. p38 kinases are drug targets for the inflammatory diseases psoriasis, rheumatoid arthritis, and chronic pulmonary disease. Vertebrates contain four isoforms of p38, named alpha, beta, gamma, and delta, which show varying substrate specificity and expression patterns. p38alpha and p38beta are ubiquitously expressed, p38gamma is predominantly found in skeletal muscle, and p38delta is found in the heart, lung, testis, pancreas, and small intestine. The p38 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: 143356 [Multi-domain]  Cd Length: 343  Bit Score: 49.21  E-value: 3.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERMYCAPEVgaI---TEETEAC 517
Cdd:cd07851   120 IQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLARHTDDEMTGYVATRWYRAPEI--MlnwMHYNQTV 197
                          90
                  ....*....|....*...
gi 1164769387 518 DWWSLGAVLFELLTGKTL 535
Cdd:cd07851   198 DIWSVGCIMAELLTGKTL 215
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
436-533 4.19e-06

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: 48.26  E-value: 4.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCD--SDAIERMYCAPEVgaITEE 513
Cdd:cd14059    78 ITPSLLVDWSKQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTkmSFAGTVAWMAPEV--IRNE 155
                          90       100
                  ....*....|....*....|..
gi 1164769387 514 --TEACDWWSLGAVLFELLTGK 533
Cdd:cd14059   156 pcSEKVDIWSFGVVLWELLTGE 177
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
441-535 4.20e-06

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: 49.03  E-value: 4.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDS--CDSDAIERMYCAPEVgAITEE--T 514
Cdd:cd07864   118 IKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLADFglARLYNSEESrpYTNKVITLWYRPPEL-LLGEEryG 196
                          90       100
                  ....*....|....*....|.
gi 1164769387 515 EACDWWSLGAVLFELLTGKTL 535
Cdd:cd07864   197 PAIDVWSCGCILGELFTKKPI 217
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
436-593 4.68e-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: 49.01  E-value: 4.68e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLND----------------------RGHIQLTYFSRWsevedsc 493
Cdd:cd07854   111 LSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINTedlvlkigdfglarivdphyshKGYLSEGLVTKW------- 183
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 494 dsdaiermYCAPE-VGAITEETEACDWWSLGAVLFELLTGKTLV-------------------------EC---HPAGIN 544
Cdd:cd07854   184 --------YRSPRlLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFagaheleqmqlilesvpvvreedrnELlnvIPSFVR 255
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1164769387 545 THTTLN-------MPEcVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFFTP 593
Cdd:cd07854   256 NDGGEPrrplrdlLPG-VNPEALDFLEQILTFNPMDRLTA-----EEALMHPYMSC 305
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
438-532 4.75e-06

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: 48.81  E-value: 4.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 438 EGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNdRGHIQLTY------FSRWSEVEDSCDSDAIERMYCAPEVGAIT 511
Cdd:cd14038   100 EGAILTLLSDISSALRYLHENRIIHRDLKPENIVLQ-QGEQRLIHkiidlgYAKELDQGSLCTSFVGTLQYLAPELLEQQ 178
                          90       100
                  ....*....|....*....|.
gi 1164769387 512 EETEACDWWSLGAVLFELLTG 532
Cdd:cd14038   179 KYTVTVDYWSFGTLAFECITG 199
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
441-593 5.13e-06

Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases Sty1 and Hog1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs Sty1 from Schizosaccharomyces pombe, Hog1 from Saccharomyces cerevisiae, and similar proteins. Sty1 and Hog1 are stress-activated MAPKs that partipate in transcriptional regulation in response to stress. Sty1 is activated in response to oxidative stress, osmotic stress, and UV radiation. It is regulated by the MAP2K Wis1, which is activated by the MAP3Ks Wis4 and Win1, which receive signals of the stress condition from membrane-spanning histidine kinases Mak1-3. Activated Sty1 stabilizes the Atf1 transcription factor and induces transcription of Atf1-dependent genes of the core environmetal stress response. Hog1 is the key element in the high osmolarity glycerol (HOG) pathway and is activated upon hyperosmotic stress. Activated Hog1 accumulates in the nucleus and regulates stress-induced transcription. The HOG pathway is mediated by two transmembrane osmosensors, Sln1 and Sho1. MAPKs are important mediators of cellular responses to extracellular signals. The Sty1/Hog1 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: 270843 [Multi-domain]  Cd Length: 328  Bit Score: 48.72  E-value: 5.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrWSEVEDSCDSDAIE-RMYCAPEVGAITEE-TEACD 518
Cdd:cd07856   110 IQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFG-LARIQDPQMTGYVStRYYRAPEIMLTWQKyDVEVD 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 519 WWSLGAVLFELLTGKTLV----ECHPAGINTHTTLNMPECVSE-------------------------------EARSLI 563
Cdd:cd07856   189 IWSAGCIFAEMLEGKPLFpgkdHVNQFSIITELLGTPPDDVINticsentlrfvqslpkrervpfsekfknadpDAIDLL 268
                         170       180       190
                  ....*....|....*....|....*....|
gi 1164769387 564 QQLLQFNPLERLGAGvagveDIKSHPFFTP 593
Cdd:cd07856   269 EKMLVFDPKKRISAA-----EALAHPYLAP 293
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
443-533 5.94e-06

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 411126 [Multi-domain]  Cd Length: 563  Bit Score: 49.02  E-value: 5.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 443 RWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFsrwsevedscdsdAIER------M-----------YCAP 505
Cdd:NF033483  111 EIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDF-------------GIARalssttMtqtnsvlgtvhYLSP 177
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1164769387 506 EV---GAITEETeacDWWSLGAVLFELLTGK 533
Cdd:NF033483  178 EQargGTVDARS---DIYSLGIVLYEMLTGR 205
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
445-580 6.33e-06

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: 47.91  E-value: 6.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 445 AAEMVV-ALDALHREGIVCRDLNPNNILLNDRGH---IQLTYFSRWSE--------VEDSCDSDAiermYCAPEVGAITE 512
Cdd:cd14087   102 VLQMVLdGVKYLHGLGITHRDLKPENLLYYHPGPdskIMITDFGLASTrkkgpnclMKTTCGTPE----YIAPEILLRKP 177
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1164769387 513 ETEACDWWSLGAVLFELLTG--------KTLVECHPAGINTHTTLNMPECVSEEARSLIQQLLQFNPLERLGAGVA 580
Cdd:cd14087   178 YTQSVDMWAVGVIAYILLSGtmpfdddnRTRLYRQILRAKYSYSGEPWPSVSNLAKDFIDRLLTVNPGERLSATQA 253
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
455-590 6.99e-06

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: 47.76  E-value: 6.99e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 455 LHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERM-----YCAPEVGAITEE--TEACDWWSLGAVLF 527
Cdd:cd06629   124 LHSKGILHRDLKADNILVDLEGICKISDFGISKKSDDIYGNNGATSMqgsvfWMAPEVIHSQGQgySAKVDIWSLGCVVL 203
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1164769387 528 ELLTGK------TLVECHPAGINTHTTLNMPECV--SEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPF 590
Cdd:cd06629   204 EMLAGRrpwsddEAIAAMFKLGNKRSAPPVPEDVnlSPEALDFLNACFAIDPRDRPTA-----AELLSHPF 269
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
436-591 7.37e-06

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: 47.58  E-value: 7.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILL--NDRGHIQLTYFSRWSEVEDSCD--SDAIERMYCAPEVGAIT 511
Cdd:cd14107    95 VTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQEITPSEHqfSKYGSPEFVAPEIVHQE 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 512 EETEACDWWSLGAVLFELLTGKtlveCHPAGINTHTTL----------NMPECV--SEEARSLIQQLLQFNPLERLGAGv 579
Cdd:cd14107   175 PVSAATDIWALGVIAYLSLTCH----SPFAGENDRATLlnvaegvvswDTPEIThlSEDAKDFIKRVLQPDPEKRPSAS- 249
                         170
                  ....*....|..
gi 1164769387 580 agveDIKSHPFF 591
Cdd:cd14107   250 ----ECLSHEWF 257
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
411-535 7.65e-06

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK1 is expressed in every cell and tissue type. It specifically binds with JAMP (JNK1-associated membrane protein), which regulates the duration of JNK1 activity in response to stimuli. Specific JNK1 substrates include Itch and SG10, which are implicated in Th2 responses and airway inflammation, and microtubule dynamics and axodendritic length, respectively. Mice deficient in JNK1 are protected against arthritis, obesity, type 2 diabetes, cardiac cell death, and non-alcoholic liver disease, suggesting that JNK1 may play roles in the pathogenesis of these diseases. Initially, it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK1 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: 143380 [Multi-domain]  Cd Length: 364  Bit Score: 48.50  E-value: 7.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 411 LEGDKEIHQIFEDLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSE 488
Cdd:cd07875    98 LEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFglARTAG 177
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1164769387 489 VEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTL 535
Cdd:cd07875   178 TSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMIKGGVL 224
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
424-574 7.93e-06

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: 47.76  E-value: 7.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 424 LDKKLALASRF-YIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERMY 502
Cdd:cd13997    87 LQDALEELSPIsKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGLATRLETSGDVEEGDSRY 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 503 CAPEVGA-ITEETEACDWWSLGAVLFELLTGKTLvechPAGINTHTTLNM------PECV-SEEARSLIQQLLQFNPLER 574
Cdd:cd13997   167 LAPELLNeNYTHLPKADIFSLGVTVYEAATGEPL----PRNGQQWQQLRQgklplpPGLVlSQELTRLLKVMLDPDPTRR 242
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
410-535 1.03e-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: 47.42  E-value: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFEDLDKKLaLASRFYIPEGC----IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSR 485
Cdd:cd07846    68 VFRRKKRWYLVFEFVDHTV-LDDLEKYPNGLdesrVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGF 146
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1164769387 486 WSEVE---DSCDSDAIERMYCAPE--VGAiTEETEACDWWSLGAVLFELLTGKTL 535
Cdd:cd07846   147 ARTLAapgEVYTDYVATRWYRAPEllVGD-TKYGKAVDVWAVGCLVTEMLTGEPL 200
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
402-591 1.08e-05

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: 47.24  E-value: 1.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 402 ETKGESGLVLE---GDKEIHQIFEDLDKKLAlasrfyipEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDR--- 475
Cdd:cd14197    79 ETASEMILVLEyaaGGEIFNQCVADREEAFK--------EKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSEspl 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 476 GHIQLTYFSRWSEVEDSCDSDAIERM--YCAPEVGAITEETEACDWWSLGAVLFELLTG--------KTLVECHPAGINT 545
Cdd:cd14197   151 GDIKIVDFGLSRILKNSEELREIMGTpeYVAPEILSYEPISTATDMWSIGVLAYVMLTGispflgddKQETFLNISQMNV 230
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1164769387 546 HTTLNMPECVSEEARSLIQQLLQFNPLERlgagvAGVEDIKSHPFF 591
Cdd:cd14197   231 SYSEEEFEHLSESAIDFIKTLLIKKPENR-----ATAEDCLKHPWL 271
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
429-574 1.13e-05

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: 47.00  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 429 ALASRfYIPEGCIQRWAAEMVVALDALHREG---IVCRDLNPNNILLNDR---GHIQ-----LTYFSRWSEVEDSCD-SD 496
Cdd:cd14061    83 VLAGR-KIPPHVLVDWAIQIARGMNYLHNEApvpIIHRDLKSSNILILEAienEDLEnktlkITDFGLAREWHKTTRmSA 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 497 AIERMYCAPEVgaITEET--EACDWWSLGAVLFELLTGKT-------LVECHPAGINThTTLNMPECVSEEARSLIQQLL 567
Cdd:cd14061   162 AGTYAWMAPEV--IKSSTfsKASDVWSYGVLLWELLTGEVpykgidgLAVAYGVAVNK-LTLPIPSTCPEPFAQLMKDCW 238

                  ....*..
gi 1164769387 568 QFNPLER 574
Cdd:cd14061   239 QPDPHDR 245
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
447-591 1.17e-05

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: 47.41  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEV--EDSCDSDAIERMY-CAPEVGAITEETEACDWWSLG 523
Cdd:cd06655   123 ECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFCAQItpEQSKRSTMVGTPYwMAPEVVTRKAYGPKVDIWSLG 202
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1164769387 524 AVLFELLTGK-------TLVECHPAGINTHTTLNMPECVSEEARSLIQQLLQFNpLERLGAGvagvEDIKSHPFF 591
Cdd:cd06655   203 IMAIEMVEGEppylnenPLRALYLIATNGTPELQNPEKLSPIFRDFLNRCLEMD-VEKRGSA----KELLQHPFL 272
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
451-574 1.49e-05

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: 46.94  E-value: 1.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREG--IVCRDLNPNNILLNDRGHIQLTYFS----------RWSEVEDScdSDAIER----MYCAPEVG------ 508
Cdd:cd13985   115 AVGHLHSQSppIIHRDIKIENILFSNTGRFKLCDFGsattehypleRAEEVNII--EEEIQKnttpMYRAPEMIdlyskk 192
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1164769387 509 AITEETeacDWWSLGAVLFELLTGKT-LVECHPAGINThTTLNMPEC--VSEEARSLIQQLLQFNPLER 574
Cdd:cd13985   193 PIGEKA---DIWALGCLLYKLCFFKLpFDESSKLAIVA-GKYSIPEQprYSPELHDLIRHMLTPDPAER 257
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
452-591 1.61e-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: 47.36  E-value: 1.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 452 LDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVedscDSDAIE-----------RMYCAPEVG-AITEETEACDW 519
Cdd:cd07855   122 LKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMARGL----CTSPEEhkyfmteyvatRWYRAPELMlSLPEYTQAIDM 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 520 WSLGAVLFE------LLTGKTLVecHPAGInTHTTLNMPE--------------------------------CVSEEARS 561
Cdd:cd07855   198 WSVGCIFAEmlgrrqLFPGKNYV--HQLQL-ILTVLGTPSqavinaigadrvrryiqnlpnkqpvpwetlypKADQQALD 274
                         170       180       190
                  ....*....|....*....|....*....|
gi 1164769387 562 LIQQLLQFNPLERLgagvaGVEDIKSHPFF 591
Cdd:cd07855   275 LLSQMLRFDPSERI-----TVAEALQHPFL 299
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
436-591 1.76e-05

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: 46.52  E-value: 1.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRgHIQLTYFSRWSEVEDS--------CDSDAiermYCAPEV 507
Cdd:cd14163    98 LPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALLQGF-TLKLTDFGFAKQLPKGgrelsqtfCGSTA----YAAPEV 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 508 -GAITEETEACDWWSLGAVLFELLTGKTLVE--------CH-PAGINTHTTLNmpecVSEEARSLIQQLLQFNPLERlga 577
Cdd:cd14163   173 lQGVPHDSRKGDIWSMGVVLYVMLCAQLPFDdtdipkmlCQqQKGVSLPGHLG----VSRTCQDLLKRLLEPDMVLR--- 245
                         170
                  ....*....|....
gi 1164769387 578 gvAGVEDIKSHPFF 591
Cdd:cd14163   246 --PSIEEVSWHPWL 257
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
429-533 1.80e-05

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: 46.56  E-value: 1.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 429 ALASRfYIPEGCIQRWAAEMVVALDALHREGIVC---RDLNPNNILLNDRGH--------IQLTYFSRWSEVEDSCD-SD 496
Cdd:cd14147    92 ALAGR-RVPPHVLVNWAVQIARGMHYLHCEALVPvihRDLKSNNILLLQPIEnddmehktLKITDFGLAREWHKTTQmSA 170
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1164769387 497 AIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGK 533
Cdd:cd14147   171 AGTYAWMAPEVIKASTFSKGSDVWSFGVLLWELLTGE 207
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
441-535 1.95e-05

Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and -Regulated Kinase 1; 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. Mammals contain two types of DYRK1 proteins, DYRK1A and DYRK1B. DYRK1A was previously called minibrain kinase homolog (MNBH) or dual-specificity YAK1-related kinase. It phosphorylates various substrates and is involved in many cellular events. It phosphorylates and inhibits the transcription factors, nuclear factor of activated T cells (NFAT) and forkhead in rhabdomyosarcoma (FKHR). It regulates neuronal differentiation by targetting CREB (cAMP response element-binding protein). It also targets many endocytic proteins including dynamin and amphiphysin and may play a role in the endocytic pathway. The gene encoding DYRK1A is located in the DSCR (Down syndrome critical region) of human chromosome 21 and DYRK1A has been implicated in the pathogenesis of DS. DYRK1B, also called minibrain-related kinase (MIRK), is highly expressed in muscle and plays a critical role in muscle differentiation by regulating transcription, cell motility, survival, and cell cycle progression. It is overexpressed in many solid tumors where it acts as a tumor survival factor. DYRKs autophosphorylate themselves on tyrosine residues and phosphorylate their substrates exclusively on S/T residues. The DYRK1 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: 271128 [Multi-domain]  Cd Length: 339  Bit Score: 46.93  E-value: 1.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREG---IVCrDLNPNNILLND--RGHIQLTYFSrwseveDSCDSDaiERMYC--------APEV 507
Cdd:cd14226   118 TRKFAQQLCTALLFLSTPElsiIHC-DLKPENILLCNpkRSAIKIIDFG------SSCQLG--QRIYQyiqsrfyrSPEV 188
                          90       100
                  ....*....|....*....|....*...
gi 1164769387 508 GAITEETEACDWWSLGAVLFELLTGKTL 535
Cdd:cd14226   189 LLGLPYDLAIDMWSLGCILVEMHTGEPL 216
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
437-574 2.33e-05

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: 46.41  E-value: 2.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 437 PEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSE---------VEDSCDSDAIE------RM 501
Cdd:cd14048   116 ELFVCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVTAmdqgepeqtVLTPMPAYAKHtgqvgtRL 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 YCAPEVGAITEETEACDWWSLGAVLFELLTG--------KTLVECHPAGINTHTTLNMPecvseEARSLIQQLLQFNPLE 573
Cdd:cd14048   196 YMSPEQIHGNQYSEKVDIFALGLILFELIYSfstqmeriRTLTDVRKLKFPALFTNKYP-----EERDMVQQMLSPSPSE 270

                  .
gi 1164769387 574 R 574
Cdd:cd14048   271 R 271
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
451-532 2.38e-05

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: 46.21  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNIL---LNDRGHIQLTYFSrWSEVEDS------CDSDAiermYCAPEVGAITEETEACDWWS 521
Cdd:cd14083   113 AVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFG-LSKMEDSgvmstaCGTPG----YVAPEVLAQKPYGKAVDCWS 187
                          90
                  ....*....|.
gi 1164769387 522 LGAVLFELLTG 532
Cdd:cd14083   188 IGVISYILLCG 198
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
452-593 2.62e-05

Catalytic domain of the Serine/Threonine Kinases, Plant TEY 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 TEY subtype of plant MAPKs and is further subdivided into three groups (A, B, and C). Group A is represented by AtMPK3, AtMPK6, Nicotiana tabacum BTF4 (NtNTF4), among others. They are mostly involved in environmental and hormonal responses. AtMPK3 and AtMPK6 are also key regulators for stomatal development and patterning. Group B is represented by AtMPK4, AtMPK13, and NtNTF6, among others. They may be involved in both cell division and environmental stress response. AtMPK4 also participates in regulating innate immunity. Group C is represented by AtMPK1, AtMPK2, NtNTF3, Oryza sativa MAPK4 (OsMAPK4), among others. They may also be involved in stress responses. AtMPK1 and AtMPK2 are activated following mechanical injury and in the presence of stress chemicals such as jasmonic acid, hydrogen peroxide and abscisic acid. OsMAPK4 is also called OsMSRMK3 for Multiple Stress-Responsive MAPK3. 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. The TEY MAPK 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: 143363 [Multi-domain]  Cd Length: 337  Bit Score: 46.59  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 452 LDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRW-SEVEDSCDSDAIERMYCAPEVGAITEE-TEACDWWSLGAVLF 527
Cdd:cd07858   121 LKYIHSANVLHRDLKPSNLLLNANCDLKICDFglARTtSEKGDFMTEYVVTRWYRAPELLLNCSEyTTAIDVWSVGCIFA 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 528 ELLTGKTLV---EC-HPAG-----INTHTTLNMPECVSEEARSLIQQL--------------------------LQFNPL 572
Cdd:cd07858   201 ELLGRKPLFpgkDYvHQLKlitelLGSPSEEDLGFIRNEKARRYIRSLpytprqsfarlfphanplaidllekmLVFDPS 280
                         170       180
                  ....*....|....*....|.
gi 1164769387 573 ERLgagvaGVEDIKSHPFFTP 593
Cdd:cd07858   281 KRI-----TVEEALAHPYLAS 296
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
451-591 2.64e-05

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: 46.52  E-value: 2.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEdscdSDAIER-------MYCAPEVGAITEETEACDWWSLG 523
Cdd:cd06659   129 ALAYLHSQGVIHRDIKSDSILLTLDGRVKLSDFGFCAQIS----KDVPKRkslvgtpYWMAPEVISRCPYGTEVDIWSLG 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 524 AVLFELLTG-------------KTLVECHPAGI-NTHTtlnmpecVSEEARSLIQQLLQFNPLERlgagvAGVEDIKSHP 589
Cdd:cd06659   205 IMVIEMVDGeppyfsdspvqamKRLRDSPPPKLkNSHK-------ASPVLRDFLERMLVRDPQER-----ATAQELLDHP 272

                  ..
gi 1164769387 590 FF 591
Cdd:cd06659   273 FL 274
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
436-533 2.77e-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: 46.19  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVC---RDLNPNNILLNDRGH--------IQLTYFSRWSEVEDSCD-SDAIERMYC 503
Cdd:cd14145   101 IPPDILVNWAVQIARGMNYLHCEAIVPvihRDLKSSNILILEKVEngdlsnkiLKITDFGLAREWHRTTKmSAAGTYAWM 180
                          90       100       110
                  ....*....|....*....|....*....|
gi 1164769387 504 APEVGAITEETEACDWWSLGAVLFELLTGK 533
Cdd:cd14145   181 APEVIRSSMFSKGSDVWSYGVLLWELLTGE 210
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
455-590 2.83e-05

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 46.36  E-value: 2.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 455 LHREGIVCRDLNPNNILLNDRGHIQLTYF--SR-WSEVEDSCDSDAIERMYCAPEvgAITEETE-------ACDWWSLGA 524
Cdd:PLN00034  184 LHRRHIVHRDIKPSNLLINSAKNVKIADFgvSRiLAQTMDPCNSSVGTIAYMSPE--RINTDLNhgaydgyAGDIWSLGV 261
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1164769387 525 VLFELLTGKtlvecHPAGINTH-------TTLNM------PECVSEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPF 590
Cdd:PLN00034  262 SILEFYLGR-----FPFGVGRQgdwaslmCAICMsqppeaPATASREFRHFISCCLQREPAKRWSA-----MQLLQHPF 330
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
423-590 3.09e-05

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: 45.88  E-value: 3.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 423 DLDKKLA--LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNdRGHIQLTYFSRWSEVEDSCD---SDA 497
Cdd:cd08222    88 DLDDKISeyKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLK-NNVIKVGDFGISRILMGTSDlatTFT 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 498 IERMYCAPEVGAITEETEACDWWSLGAVLFELLT------GKTLVECHPAgINTHTTLNMPECVSEEARSLIQQLLQFNP 571
Cdd:cd08222   167 GTPYYMSPEVLKHEGYNSKSDIWSLGCILYEMCClkhafdGQNLLSVMYK-IVEGETPSLPDKYSKELNAIYSRMLNKDP 245
                         170
                  ....*....|....*....
gi 1164769387 572 LERLGAGvagveDIKSHPF 590
Cdd:cd08222   246 ALRPSAA-----EILKIPF 259
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
435-590 3.13e-05

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: 46.16  E-value: 3.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 435 YIPEGCIQRWAAEMVVALDAL--HREGIVCRDLNPNNILL---NDRGHIQLTYF--SRWSEvEDSCDSDAIERM------ 501
Cdd:cd13990   101 SIPEREARSIIMQVVSALKYLneIKPPIIHYDLKPGNILLhsgNVSGEIKITDFglSKIMD-DESYNSDGMELTsqgagt 179
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 502 --YCAPEVGAITEE----TEACDWWSLGAVLFELLTGKtlvecHPAGINT--------HTTLNMPEC-------VSEEAR 560
Cdd:cd13990   180 ywYLPPECFVVGKTppkiSSKVDVWSVGVIFYQMLYGR-----KPFGHNQsqeaileeNTILKATEVefpskpvVSSEAK 254
                         170       180       190
                  ....*....|....*....|....*....|
gi 1164769387 561 SLIQQLLQFNPLERlgagvAGVEDIKSHPF 590
Cdd:cd13990   255 DFIRRCLTYRKEDR-----PDVLQLANDPY 279
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
455-574 3.54e-05

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 45.60  E-value: 3.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387  455 LHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDSCDSDAiERM---YCAPEvgAITEE--TEACDWWSLGAVLF 527
Cdd:smart00219 118 LESKNFIHRDLAARNCLVGENLVVKISDFglSRDLYDDDYYRKRG-GKLpirWMAPE--SLKEGkfTSKSDVWSFGVLLW 194
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1164769387  528 ELLT-GKTLvechPAGINTHTTLN---------MPECVSEEARSLIQQLLQFNPLER 574
Cdd:smart00219 195 EIFTlGEQP----YPGMSNEEVLEylkngyrlpQPPNCPPELYDLMLQCWAEDPEDR 247
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
436-532 3.73e-05

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK3 is a Fas-interacting protein that induces FADD (Fas-associated death domain) phosphorylation and mediates FasL-induced JNK activation. Overexpression of HIPK3 does not affect cell death, however its expression in prostate cancer cells contributes to increased resistance to Fas receptor-mediated apoptosis. HIPK3 also plays a role in regulating steroidogenic gene expression. In response to cAMP, HIPK3 activates the phosphorylation of JNK and c-Jun, leading to increased activity of the transcription factor SF-1 (Steroidogenic factor 1), a key regulator for steroid biosynthesis in the gonad and adrenal gland. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK3 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: 271131 [Multi-domain]  Cd Length: 330  Bit Score: 46.18  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDR----GHIQLTYFSRWSEVEDS-CDSDAIERMYCAPEVGAI 510
Cdd:cd14229    99 LPLKVIRPILQQVATALKKLKSLGLIHADLKPENIMLVDPvrqpYRVKVIDFGSASHVSKTvCSTYLQSRYYRAPEIILG 178
                          90       100
                  ....*....|....*....|..
gi 1164769387 511 TEETEACDWWSLGAVLFELLTG 532
Cdd:cd14229   179 LPFCEAIDMWSLGCVIAELFLG 200
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
438-591 3.80e-05

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: 45.87  E-value: 3.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 438 EGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEV--EDSCDSDAIERMY-CAPEVGAITEET 514
Cdd:cd06654   115 EGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFCAQItpEQSKRSTMVGTPYwMAPEVVTRKAYG 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 515 EACDWWSLGAVLFELLTGK-------TLVECHPAGINTHTTLNMPECVSEEARSLIQQLLQFNpLERLGAGvagvEDIKS 587
Cdd:cd06654   195 PKVDIWSLGIMAIEMIEGEppylnenPLRALYLIATNGTPELQNPEKLSAIFRDFLNRCLEMD-VEKRGSA----KELLQ 269

                  ....
gi 1164769387 588 HPFF 591
Cdd:cd06654   270 HQFL 273
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
361-535 3.84e-05

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: 45.76  E-value: 3.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 361 SGANEYIASTdTLKtEEVLLFTDQTDDLAkeEPTSLFQRdsetKGESGLVLEG-DKEIHQIFEDLDKKlalasrfyIPEG 439
Cdd:cd07848    37 SEENEEVKET-TLR-ELKMLRTLKQENIV--ELKEAFRR----RGKLYLVFEYvEKNMLELLEEMPNG--------VPPE 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 440 CIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIE----RMYCAPEVGAITEETE 515
Cdd:cd07848   101 KVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGSNANYTEyvatRWYRSPELLLGAPYGK 180
                         170       180
                  ....*....|....*....|
gi 1164769387 516 ACDWWSLGAVLFELLTGKTL 535
Cdd:cd07848   181 AVDMWSVGCILGELSDGQPL 200
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
438-595 3.87e-05

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: 45.89  E-value: 3.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 438 EGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDSCDSDAIERMY-CAPEVGAI-TEE 513
Cdd:cd06611   102 EPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFgvSAKNKSTLQKRDTFIGTPYwMAPEVVACeTFK 181
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 514 TEACDW----WSLGAVLFELLTGKtlvechPAGINTHT-------------TLNMPECVSEEARSLIQQLLQFNPLERLG 576
Cdd:cd06611   182 DNPYDYkadiWSLGITLIELAQME------PPHHELNPmrvllkilkseppTLDQPSKWSSSFNDFLKSCLVKDPDDRPT 255
                         170
                  ....*....|....*....
gi 1164769387 577 AGvagveDIKSHPFFTPVD 595
Cdd:cd06611   256 AA-----ELLKHPFVSDQS 269
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
452-533 4.14e-05

Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Raf kinases 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. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. Aberrant expression or activation of components in this pathway are associated with tumor initiation, progression, and metastasis. Raf proteins contain a Ras binding domain, a zinc finger cysteine-rich domain, and a catalytic kinase domain. Vertebrates have three Raf isoforms (A-, B-, and C-Raf) with different expression profiles, modes of regulation, and abilities to function in the ERK cascade, depending on cellular context and stimuli. They have essential and non-overlapping roles during embryo- and organogenesis. Knockout of each isoform results in a lethal phenotype or abnormality in most mouse strains. The Raf 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: 270964 [Multi-domain]  Cd Length: 253  Bit Score: 45.46  E-value: 4.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 452 LDALHREGIVCRDLNPNNILLNDRGHIQLTYF------SRWSEVEDSCD-SDAIERMycAPEVGAITEE---TEACDWWS 521
Cdd:cd14062   102 MDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFglatvkTRWSGSQQFEQpTGSILWM--APEVIRMQDEnpySFQSDVYA 179
                          90
                  ....*....|..
gi 1164769387 522 LGAVLFELLTGK 533
Cdd:cd14062   180 FGIVLYELLTGQ 191
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
441-539 4.89e-05

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK2 plays a role in hepatic insulin signaling and glucose metabolism. It is induced by the insulin/Akt pathway as part of the hepatic refeeding reponse, and it directly phosphorylates the SR domain of PGC-1alpha, which results in decreased gluconeogenic gene expression and glucose output. 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 serine/threonine residues. The CLK2 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: 271117 [Multi-domain]  Cd Length: 330  Bit Score: 45.78  E-value: 4.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHiQLTYFSRWSEVEDSCDSDAIE--------------------R 500
Cdd:cd14215   118 VRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNSDY-ELTYNLEKKRDERSVKSTAIRvvdfgsatfdhehhstivstR 196
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1164769387 501 MYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVECH 539
Cdd:cd14215   197 HYRAPEVILELGWSQPCDVWSIGCIIFEYYVGFTLFQTH 235
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
441-590 4.93e-05

Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of the MAPKs MPK1 from Saccharomyces cerevisiae, Pmk1 from Schizosaccharomyces pombe, and similar proteins. MPK1 (also called Slt2) and Pmk1 (also called Spm1) are stress-activated MAPKs that regulate the cell wall integrity pathway, and are therefore important in the maintainance of cell shape, cell wall construction, morphogenesis, and ion homeostasis. MPK1 is activated in response to cell wall stress including heat stimulation, osmotic shock, UV irradiation, and any agents that interfere with cell wall biogenesis such as chitin antagonists, caffeine, or zymolase. MPK1 is regulated by the MAP2Ks Mkk1/2, which are regulated by the MAP3K Bck1. Pmk1 is also activated by multiple stresses including elevated temperatures, hyper- or hypotonic stress, glucose deprivation, exposure to cell-wall damaging compounds, and oxidative stress. It is regulated by the MAP2K Pek1, which is regulated by the MAP3K Mkh1. MAPKs are important mediators of cellular responses to extracellular signals. The MPK1 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: 173750 [Multi-domain]  Cd Length: 332  Bit Score: 45.86  E-value: 4.93e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SR-WSEVEDSCDSDAIE----RMYCAPEVG-AITE 512
Cdd:cd07857   107 FQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFglARgFSENPGENAGFMTEyvatRWYRAPEIMlSFQS 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 513 ETEACDWWSLGAVLFELLTGKTLVE-----------CHPAGINTHTTL----------------NMPEC--------VSE 557
Cdd:cd07857   187 YTKAIDVWSVGCILAELLGRKPVFKgkdyvdqlnqiLQVLGTPDEETLsrigspkaqnyirslpNIPKKpfesifpnANP 266
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1164769387 558 EARSLIQQLLQFNPLERLgagvaGVEDIKSHPF 590
Cdd:cd07857   267 LALDLLEKLLAFDPTKRI-----SVEEALEHPY 294
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
411-535 5.56e-05

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK3 is expressed primarily in the brain, and to a lesser extent in the heart and testis. Mice deficient in JNK3 are protected against kainic acid-induced seizures, stroke, sciatic axotomy neural death, and neuronal death due to NGF deprivation, oxidative stress, or exposure to beta-amyloid peptide. This suggests that JNK3 may play roles in the pathogenesis of these diseases. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK3 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: 143379 [Multi-domain]  Cd Length: 355  Bit Score: 45.46  E-value: 5.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 411 LEGDKEIHQIFEDLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSE 488
Cdd:cd07874    91 LEEFQDVYLVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFglARTAG 170
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1164769387 489 VEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTL 535
Cdd:cd07874   171 TSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGEMVRHKIL 217
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
436-535 6.23e-05

Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDKL1, also called p42 KKIALRE, is a glial protein that is upregulated in gliosis. It is present in neuroblastoma and A431 human carcinoma cells, and may be implicated in neoplastic transformation. The function of CDKL4 is unknown. 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 CDKL1/4 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: 270837 [Multi-domain]  Cd Length: 286  Bit Score: 45.06  E-value: 6.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLT--YFSRWSEVEDSCDSDAI-ERMYCAPE--VGAi 510
Cdd:cd07847    97 VPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCdfGFARILTGPGDDYTDYVaTRWYRAPEllVGD- 175
                          90       100
                  ....*....|....*....|....*
gi 1164769387 511 TEETEACDWWSLGAVLFELLTGKTL 535
Cdd:cd07847   176 TQYGPPVDVWAIGCVFAELLTGQPL 200
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
447-574 7.40e-05

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: 44.82  E-value: 7.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAI--ERMYCAPEV--GAITEETEAcDWWSL 522
Cdd:cd14072   107 QIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLDTFcgSPPYAAPELfqGKKYDGPEV-DVWSL 185
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1164769387 523 GAVLFELLTG---------KTLVECHPAGinthtTLNMPECVSEEARSLIQQLLQFNPLER 574
Cdd:cd14072   186 GVILYTLVSGslpfdgqnlKELRERVLRG-----KYRIPFYMSTDCENLLKKFLVLNPSKR 241
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
405-533 7.46e-05

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: 44.75  E-value: 7.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 405 GESGLVLE----GDkeIHQIFEDLDKKLALASRFyipegciqRWAAEMVVALDALH--REGIVCRDLNPNNILLNDRGHI 478
Cdd:cd13978    65 RSLGLVMEymenGS--LKSLLEREIQDVPWSLRF--------RIIHEIALGMNFLHnmDPPLLHHDLKPENILLDNHFHV 134
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1164769387 479 QLTYF--SRW------SEVEDSCDSDAIERMYCAPEvgAITE----ETEACDWWSLGAVLFELLTGK 533
Cdd:cd13978   135 KISDFglSKLgmksisANRRRGTENLGGTPIYMAPE--AFDDfnkkPTSKSDVYSFAIVIWAVLTRK 199
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
455-574 7.52e-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: 44.46  E-value: 7.52e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387  455 LHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDScDSDAIERM---YCAPEvgAITEE--TEACDWWSLGAVLF 527
Cdd:smart00221 119 LESKNFIHRDLAARNCLVGENLVVKISDFglSRDLYDDDY-YKVKGGKLpirWMAPE--SLKEGkfTSKSDVWSFGVLLW 195
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1164769387  528 ELLT-GKTLvechPAGINTHTTLN----------MPECvSEEARSLIQQLLQFNPLER 574
Cdd:smart00221 196 EIFTlGEEP----YPGMSNAEVLEylkkgyrlpkPPNC-PPELYKLMLQCWAEDPEDR 248
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
411-537 8.61e-05

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNK2 is expressed in every cell and tissue type. It is specifically translocated to the mitochondria during dopaminergic cell death. Specific substrates include the microtubule-associated proteins DCX and Tau, as well as TIF-IA which is involved in ribosomal RNA synthesis regulation. Mice deficient in Jnk2 show protection against arthritis, type 1 diabetes, atherosclerosis, abdominal aortic aneurysm, cardiac cell death, TNF-induced liver damage, and tumor growth, indicating that JNK2 may play roles in the pathogenesis of these diseases. Initially it was thought that JNK1 and JNK2 were functionally redundant as mice deficient in either genes could survive but disruption of both genes resulted in lethality. However, recent studies have shown that JNK1 and JNK2 perform distinct functions through specific binding partners and substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. The JNK2 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: 143381 [Multi-domain]  Cd Length: 359  Bit Score: 45.02  E-value: 8.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 411 LEGDKEIHQIFEDLDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSE 488
Cdd:cd07876    95 LEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFglARTAC 174
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1164769387 489 VEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVE 537
Cdd:cd07876   175 TNFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGCIMGELVKGSVIFQ 223
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
440-575 8.84e-05

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: 44.81  E-value: 8.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 440 CIQRWAAEMVVALDALHREG--IVCRDLNPNNILLNDRGHIQLTYFS-----------RWSEVEDSCDSDAIER----MY 502
Cdd:cd14036   109 TVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFGsatteahypdySWSAQKRSLVEDEITRnttpMY 188
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 503 CAPEVGAITEE---TEACDWWSLGAVLFELLTGKtlvecHP-------AGINTHTTLNMPECVSEEARSLIQQLLQFNPL 572
Cdd:cd14036   189 RTPEMIDLYSNypiGEKQDIWALGCILYLLCFRK-----HPfedgaklRIINAKYTIPPNDTQYTVFHDLIRSTLKVNPE 263

                  ...
gi 1164769387 573 ERL 575
Cdd:cd14036   264 ERL 266
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
447-592 8.90e-05

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. 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 MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 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: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 44.65  E-value: 8.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSC---DSDAIERMYCAPEVGAITEE---TEACDWW 520
Cdd:cd06645   116 ETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGVSAQITATIakrKSFIGTPYWMAPEVAAVERKggyNQLCDIW 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 521 SLGAVLFELLTGK-TLVECHPAG---INTHTTLNMPECV-----SEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFF 591
Cdd:cd06645   196 AVGITAIELAELQpPMFDLHPMRalfLMTKSNFQPPKLKdkmkwSNSFHHFVKMALTKNPKKRPTA-----EKLLQHPFV 270

                  .
gi 1164769387 592 T 592
Cdd:cd06645   271 T 271
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
451-592 9.26e-05

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: 44.36  E-value: 9.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVeDSCDSDAIERMYCAPEVGAITEE---TEACDWWSLGAVLF 527
Cdd:cd06607   113 GLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFGSASLV-CPANSFVGTPYWMAPEVILAMDEgqyDGKVDVWSLGITCI 191
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1164769387 528 ElltgktLVECHPAGINT-------HTTLNMPECV-----SEEARSLIQQLLQFNPLERLGAgvagvEDIKSHPFFT 592
Cdd:cd06607   192 E------LAERKPPLFNMnamsalyHIAQNDSPTLssgewSDDFRNFVDSCLQKIPQDRPSA-----EDLLKHPFVT 257
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
447-535 1.01e-04

Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. JNKs are mitogen-activated protein kinases (MAPKs) that are involved in many stress-activated responses including those during inflammation, neurodegeneration, apoptosis, and persistent pain sensitization, among others. They are also essential regulators of physiological and pathological processes and are involved in the pathogenesis of several diseases such as diabetes, atherosclerosis, stroke, Parkinson's and Alzheimer's. Vetebrates harbor three different JNK genes (Jnk1, Jnk2, and Jnk3) that are alternatively spliced to produce at least 10 isoforms. JNKs are specifically activated by the MAPK kinases MKK4 and MKK7, which are in turn activated by upstream MAPK kinase kinases as a result of different stimuli including stresses such as ultraviolet (UV) irradiation, hyperosmolarity, heat shock, or cytokines. JNKs activate a large number of different substrates based on specific stimulus, cell type, and cellular condition, and may be implicated in seemingly contradictory functions. The JNK 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: 270840 [Multi-domain]  Cd Length: 337  Bit Score: 44.71  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGA 524
Cdd:cd07850   110 QMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFglARTAGTSFMMTPYVVTRYYRAPEVILGMGYKENVDIWSVGC 189
                          90
                  ....*....|.
gi 1164769387 525 VLFELLTGKTL 535
Cdd:cd07850   190 IMGEMIRGTVL 200
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
435-533 1.34e-04

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: 44.19  E-value: 1.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 435 YIPEGCI--QRWAAEMVVALDALHREGIVCRDLNPNNIL---LNDRGHIQLTY----FSRWSEVEDSCDSDAIERmYCAP 505
Cdd:cd14067   108 FMPLGHMltFKIAYQIAAGLAYLHKKNIIFCDLKSDNILvwsLDVQEHINIKLsdygISRQSFHEGALGVEGTPG-YQAP 186
                          90       100
                  ....*....|....*....|....*...
gi 1164769387 506 EVGAITEETEACDWWSLGAVLFELLTGK 533
Cdd:cd14067   187 EIRPRIVYDEKVDMFSYGMVLYELLSGQ 214
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
447-543 1.38e-04

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: 43.91  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDScdsdAIER-------MYCAPEVGAITEETEACDW 519
Cdd:cd06641   109 EILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGVAGQLTDT----QIKRn*fvgtpFWMAPEVIKQSAYDSKADI 184
                          90       100
                  ....*....|....*....|....*
gi 1164769387 520 WSLGAVLFELLTGK-TLVECHPAGI 543
Cdd:cd06641   185 WSLGITAIELARGEpPHSELHPMKV 209
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
410-577 1.51e-04

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: 43.78  E-value: 1.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 410 VLEGDKEIHQIFE-----DLDKKLALASRFYIPEgciqrwAAEMVV----ALDALHREGIVCRDLNPNNILL--NDRGH- 477
Cdd:cd14185    66 VYETEKEIYLILEyvrggDLFDAIIESVKFTEHD------AALMIIdlceALVYIHSKHIVHRDLKPENLLVqhNPDKSt 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 478 -IQLTYFSRWSEVEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTG-----------KTLVECHPAGint 545
Cdd:cd14185   140 tLKLADFGLAKYVTGPIFTVCGTPTYVAPEILSEKGYGLEVDMWAAGVILYILLCGfppfrsperdqEELFQIIQLG--- 216
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1164769387 546 HTTLNMP--ECVSEEARSLIQQLLQFNPLERLGA 577
Cdd:cd14185   217 HYEFLPPywDNISEAAKDLISRLLVVDPEKRYTA 250
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
451-532 1.75e-04

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: 43.88  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNILL---NDRGHIQLTYF--SRWSEVEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAV 525
Cdd:cd14168   120 AVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFglSKMEGKGDVMSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVI 199

                  ....*..
gi 1164769387 526 LFELLTG 532
Cdd:cd14168   200 AYILLCG 206
PTZ00284 PTZ00284
protein kinase; Provisional
450-571 1.81e-04

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 44.19  E-value: 1.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 450 VALDALHRE-GIVCRDLNPNNILL--NDRGHIQLTYFS--------RWSEVEDSCDS----DAI--ERMYCAPEVGAITE 512
Cdd:PTZ00284  242 VALDYFHTElHLMHTDLKPENILMetSDTVVDPVTNRAlppdpcrvRICDLGGCCDErhsrTAIvsTRHYRSPEVVLGLG 321
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1164769387 513 ETEACDWWSLGAVLFELLTGKTLVECHPAGINTH----TTLNMPE-----CVSEEARSLIQQLLQFNP 571
Cdd:PTZ00284  322 WMYSTDMWSMGCIIYELYTGKLLYDTHDNLEHLHlmekTLGRLPSewagrCGTEEARLLYNSAGQLRP 389
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
441-539 2.00e-04

Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK3 is predominantly expressed in mature spermatozoa, and might play a role in the fertilization process. 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 serine/threonine residues. The CLK3 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: 271116 [Multi-domain]  Cd Length: 331  Bit Score: 43.84  E-value: 2.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDrGHIQLTYFSRWSEVEDSCDSDAIE--------------------R 500
Cdd:cd14214   119 IRHMAYQLCHALKFLHENQLTHTDLKPENILFVN-SEFDTLYNESKSCEEKSVKNTSIRvadfgsatfdhehhttivatR 197
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1164769387 501 MYCAPEVGAITEETEACDWWSLGAVLFELLTGKTLVECH 539
Cdd:cd14214   198 HYRPPEVILELGWAQPCDVWSLGCILFEYYRGFTLFQTH 236
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
436-545 2.02e-04

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK8 can act as a negative or positive regulator of transcription, depending on the scenario. Together with its regulator, cyclin C, it reversibly associates with the multi-subunit core Mediator complex, a cofactor that is involved in regulating RNA polymerase II (RNAP II)-dependent transcription. CDK8 phosphorylates cyclin H, a subunit of the general transcription factor TFIIH, which results in the inhibition of TFIIH-dependent phosphorylation of the C-terminal domain of RNAP II, facilitating the inhibition of transcription. It has also been shown to promote transcription by a mechanism that is likely to involve RNAP II phosphorylation. CDK8 also functions as a stimulus-specific positive coregulator of p53 transcriptional responses. 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 CDK8 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: 270851 [Multi-domain]  Cd Length: 333  Bit Score: 43.89  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILL----NDRGHIQLT--YFSRW--SEVEDSCDSD--AIERMYCAP 505
Cdd:cd07868   121 LPRGMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIAdmGFARLfnSPLKPLADLDpvVVTFWYRAP 200
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1164769387 506 EV--GAiTEETEACDWWSLGAVLFELLTGKTLVECHPAGINT 545
Cdd:cd07868   201 ELllGA-RHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKT 241
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
445-532 2.05e-04

Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. A-Raf cooperates with C-Raf in regulating ERK transient phosphorylation that is associated with cyclin D expression and cell cycle progression. Mice deficient in A-Raf are born alive but show neurological and intestinal defects. A-Raf demonstrates low kinase activity to MEK, compared with B- and C-Raf, and may also have alternative functions other than in the ERK signaling cascade. It regulates the M2 type pyruvate kinase, a key glycolytic enzyme. It also plays a role in endocytic membrane trafficking. A-Raf 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. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The A-Raf 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: 271052 [Multi-domain]  Cd Length: 265  Bit Score: 43.47  E-value: 2.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 445 AAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF------SRWS---EVEDSCDSdaieRMYCAPEVGAITEE-- 513
Cdd:cd14150   102 ARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFglatvkTRWSgsqQVEQPSGS----ILWMAPEVIRMQDTnp 177
                          90       100
                  ....*....|....*....|
gi 1164769387 514 -TEACDWWSLGAVLFELLTG 532
Cdd:cd14150   178 ySFQSDVYAYGVVLYELMSG 197
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
409-590 2.27e-04

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: 43.02  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 409 LVLEGDKEIHQIFEDLDKKLALasrfyiPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDR-GHIQLTYFSRWS 487
Cdd:cd14102    81 IVMERPEPVKDLFDFITEKGAL------DEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDLRtGELKLIDFGSGA 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 488 EVEDSCDSDAI-ERMYCAPE-VGAITEETEACDWWSLGAVLFELLTGKTLVECHPAGINTHttLNMPECVSEEARSLIQQ 565
Cdd:cd14102   155 LLKDTVYTDFDgTRVYSPPEwIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQDEEILRGR--LYFRRRVSPECQQLIKW 232
                         170       180
                  ....*....|....*....|....*
gi 1164769387 566 LLQFNPLERlgagvAGVEDIKSHPF 590
Cdd:cd14102   233 CLSLRPSDR-----PTLEQIFDHPW 252
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
445-528 2.29e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 43.73  E-value: 2.29e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 445 AAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF-------SRWSE-----VEDSCDSDaiermycAPEVGAITE 512
Cdd:PHA03211  266 ARQLLSAIDYIHGEGIIHRDIKTENVLVNGPEDICLGDFgaacfarGSWSTpfhygIAGTVDTN-------APEVLAGDP 338
                          90
                  ....*....|....*.
gi 1164769387 513 ETEACDWWSLGAVLFE 528
Cdd:PHA03211  339 YTPSVDIWSAGLVIFE 354
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
447-592 2.65e-04

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: 43.28  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGH---IQLTYFSRWSEVEDSCDSDAI--ERMYCAPEVGAITEETEACDWWS 521
Cdd:cd14085   106 QILEAVAYLHENGIVHRDLKPENLLYATPAPdapLKIADFGLSKIVDQQVTMKTVcgTPGYCAPEILRGCAYGPEVDMWS 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 522 LGAVLFELLTG--------------KTLVECHPAGINthttlnmP--ECVSEEARSLIQQLLQFNPLERLGAgvagvEDI 585
Cdd:cd14085   186 VGVITYILLCGfepfydergdqymfKRILNCDYDFVS-------PwwDDVSLNAKDLVKKLIVLDPKKRLTT-----QQA 253

                  ....*..
gi 1164769387 586 KSHPFFT 592
Cdd:cd14085   254 LQHPWVT 260
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
441-601 2.77e-04

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: 43.10  E-value: 2.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF---SRWSEVEDSCDSDAIERMYCAPEVGAITEETEA- 516
Cdd:cd06644   112 IQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFgvsAKNVKTLQRRDSFIGTPYWMAPEVVMCETMKDTp 191
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 517 ----CDWWSLGAVLFELLTGK-TLVECHPAGI------NTHTTLNMPECVSEEARSLIQQLLQFNPLERLGAGvagveDI 585
Cdd:cd06644   192 ydykADIWSLGITLIEMAQIEpPHHELNPMRVllkiakSEPPTLSQPSKWSMEFRDFLKTALDKHPETRPSAA-----QL 266
                         170
                  ....*....|....*.
gi 1164769387 586 KSHPFFTPVDWAELMR 601
Cdd:cd06644   267 LEHPFVSSVTSNRPLR 282
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
447-562 2.88e-04

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: 43.12  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDScdsdAIER-------MYCAPEVGAITEETEACDW 519
Cdd:cd06640   109 EILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDT----QIKRntfvgtpFWMAPEVIQQSAYDSKADI 184
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1164769387 520 WSLGAVLFELLTGKTL-VECHPAGINTHT-TLNMPECVSEEARSL 562
Cdd:cd06640   185 WSLGITAIELAKGEPPnSDMHPMRVLFLIpKNNPPTLVGDFSKPF 229
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
447-532 3.00e-04

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-1 is widely expressed except in the spleen and thymus. It is highly expressed in the brain, heart, pancreas, testis, and ovary, and is localized in the cytoplasm. It is regulated by cyclin D3 and is inhibited by the p21 cell cycle inhibitor. It has also been shown to interact with the membrane-associated cyclin Y, which recruits the protein to the plasma membrane. PFTAIRE-1 shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-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: 143374 [Multi-domain]  Cd Length: 303  Bit Score: 43.14  E-value: 3.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDSCDSDAIERM-YCAPEVGAITEETEAC-DWWSL 522
Cdd:cd07869   111 QLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFglARAKSVPSHTYSNEVVTLwYRPPDVLLGSTEYSTClDMWGV 190
                          90
                  ....*....|
gi 1164769387 523 GAVLFELLTG 532
Cdd:cd07869   191 GCIFVEMIQG 200
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
447-532 3.07e-04

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors including homeodomain proteins (Nkx and HOX families), Smad1-4, Pax6, c-Myb, AML1, the histone acetyltransferase p300, and the tumor repressor p53, among others. It regulates gene transcription during development and in DNA damage response (DDR), and mediates cell processes such as apoptosis, survival, differentiation, and proliferation. HIPK2 mediates apoptosis by phosphorylating and activating p53 during DDR, resulting in the activation of apoptotic genes. In the absence of p53, HIPK2 targets the anti-apoptotic corepressor C-terminal binding protein (CtBP), leading to CtBP's degradation and the promotion of apoptosis. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK2 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: 271129 [Multi-domain]  Cd Length: 355  Bit Score: 43.15  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGH----IQLTYFSRWSEVEDS-CDSDAIERMYCAPEVGAITEETEACDWWS 521
Cdd:cd14227   125 QVATALMKLKSLGLIHADLKPENIMLVDPSRqpyrVKVIDFGSASHVSKAvCSTYLQSRYYRAPEIILGLPFCEAIDMWS 204
                          90
                  ....*....|.
gi 1164769387 522 LGAVLFELLTG 532
Cdd:cd14227   205 LGCVIAELFLG 215
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
441-533 3.18e-04

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: 42.72  E-value: 3.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLN-DRGHIQLTYF-----SRWSeVEDSCDSDaierMYCAPE----VGAI 510
Cdd:cd13993   109 IKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSqDEGTVKLCDFglattEKIS-MDFGVGSE----FYMAPEcfdeVGRS 183
                          90       100
                  ....*....|....*....|....*
gi 1164769387 511 TEE--TEACDWWSLGAVLFELLTGK 533
Cdd:cd13993   184 LKGypCAAGDIWSLGIILLNLTFGR 208
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
447-535 3.36e-04

Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PFTAIRE-2 is also referred to as ALS2CR7 (amyotrophic lateral sclerosis 2 (juvenile) chromosome region candidate 7). It may be associated with amyotrophic lateral sclerosis 2 (ALS2), an autosomal recessive form of juvenile ALS. The function of PFTAIRE-2 is not yet known. It shares sequence similarity with Cyclin-Dependent Kinases (CDKs), which belong to a large family of STKs that are regulated by their cognate cyclins. Together, CDKs and cyclins are involved in the control of cell-cycle progression, transcription, and neuronal function. The PFTAIRE-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: 270852 [Multi-domain]  Cd Length: 286  Bit Score: 43.03  E-value: 3.36e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEV-EDSCDSDAIERMYCAPEV--GAiTEETEACDWWS 521
Cdd:cd07870   106 QLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFglARAKSIpSQTYSSEVVTLWYRPPDVllGA-TDYSSALDIWG 184
                          90
                  ....*....|....
gi 1164769387 522 LGAVLFELLTGKTL 535
Cdd:cd07870   185 AGCIFIEMLQGQPA 198
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
436-590 3.60e-04

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: 42.70  E-value: 3.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDS-DAIERM-----YCAPEVGA 509
Cdd:cd06653   103 LTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRIQTICMSgTGIKSVtgtpyWMSPEVIS 182
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 510 ITEETEACDWWSLGAVLFELLTGK---TLVECHPA--GINTH-TTLNMPECVSEEARSLIQQLlqFNPLERlgagVAGVE 583
Cdd:cd06653   183 GEGYGRKADVWSVACTVVEMLTEKppwAEYEAMAAifKIATQpTKPQLPDGVSDACRDFLRQI--FVEEKR----RPTAE 256

                  ....*..
gi 1164769387 584 DIKSHPF 590
Cdd:cd06653   257 FLLRHPF 263
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
445-533 4.63e-04

Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. C-Raf, also known as Raf-1 or c-Raf-1, is ubiquitously expressed and was the first Raf identified. It was characterized as the acquired oncogene from an acutely transforming murine sarcoma virus (3611-MSV) and the transforming agent from the avian retrovirus MH2. C-Raf-deficient mice embryos die around midgestation with increased apoptosis of embryonic tissues, especially in the fetal liver. One of the main functions of C-Raf is restricting caspase activation to promote survival in response to specific stimuli such as Fas stimulation, macrophage apoptosis, and erythroid differentiation. C-Raf 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. It functions in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The C-Raf 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: 271051 [Multi-domain]  Cd Length: 283  Bit Score: 42.33  E-value: 4.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 445 AAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF------SRWS---EVEDSCDSdaieRMYCAPEVGAITEETE 515
Cdd:cd14149   114 ARQTAQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFglatvkSRWSgsqQVEQPTGS----ILWMAPEVIRMQDNNP 189
                          90       100
                  ....*....|....*....|.
gi 1164769387 516 ---ACDWWSLGAVLFELLTGK 533
Cdd:cd14149   190 fsfQSDVYSYGIVLYELMTGE 210
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
424-574 4.69e-04

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: 42.03  E-value: 4.69e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 424 LDKKLALASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrWSEVEDS----CDSDAIE 499
Cdd:cd08221    86 LHDKIAQQKNQLFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFG-ISKVLDSessmAESIVGT 164
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 500 RMYCAPEVGAITEETEACDWWSLGAVLFELLT-GKTLVECHP----AGINTHTTLNMPECVSEEARSLIQQLLQFNPLER 574
Cdd:cd08221   165 PYYMSPELVQGVKYNFKSDIWAVGCVLYELLTlKRTFDATNPlrlaVKIVQGEYEDIDEQYSEEIIQLVHDCLHQDPEDR 244
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
412-532 5.41e-04

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: 42.15  E-value: 5.41e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 412 EGDKEIHQIFE-----DLDKKLAlASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDR--GHIQLTYF- 483
Cdd:cd14104    66 ESHEELVMIFEfisgvDIFERIT-TARFELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRrgSYIKIIEFg 144
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1164769387 484 -SRWSEVEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAVLFELLTG 532
Cdd:cd14104   145 qSRQLKPGDKFRLQYTSAEFYAPEVHQHESVSTATDMWSLGCLVYVLLSG 194
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
436-532 5.43e-04

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). They show speckled localization in the nucleus, apart from the nucleoles. They play roles in the regulation of many nuclear pathways including gene transcription, cell survival, proliferation, differentiation, development, and DNA damage response. Vertebrates contain three HIPKs (HIPK1-3) and mammals harbor an additional family member HIPK4, which does not contain a homeobox-interacting domain and is localized in the cytoplasm. HIPK2, the most studied HIPK, is a coregulator of many transcription factors and cofactors and it regulates gene transcription during development and in DNA damage response. The HIPK 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: 271113 [Multi-domain]  Cd Length: 329  Bit Score: 42.44  E-value: 5.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRG----HIQLTYFSRWSEVEDSCDSDAIE-RMYCAPEVGAI 510
Cdd:cd14211    98 LPLKYIRPILQQVLTALLKLKSLGLIHADLKPENIMLVDPVrqpyRVKVIDFGSASHVSKAVCSTYLQsRYYRAPEIILG 177
                          90       100
                  ....*....|....*....|..
gi 1164769387 511 TEETEACDWWSLGAVLFELLTG 532
Cdd:cd14211   178 LPFCEAIDMWSLGCVIAELFLG 199
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
455-532 5.61e-04

Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase (IKK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IKKalpha is involved in the non-canonical or alternative 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 non-canonical pathway functions in cells lacking NEMO (NF-kB Essential MOdulator) and IKKbeta. It is induced by a subset of TNFR family members including CD40, RANK, and B cell-activating factor receptor. IKKalpha processes the Inhibitor of NF-kB (IkB)-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus. This pathway is dependent on NIK (NF-kB Inducing Kinase) which phosphorylates and activates IKKalpha. The IKKalpha 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: 270941 [Multi-domain]  Cd Length: 289  Bit Score: 42.21  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 455 LHREGIVCRDLNPNNILLNDRG----H--IQLTYfSRWSEVEDSCDSDAIERMYCAPEVGAITEETEACDWWSLGAVLFE 528
Cdd:cd14039   115 LHENKIIHRDLKPENIVLQEINgkivHkiIDLGY-AKDLDQGSLCTSFVGTLQYLAPELFENKSYTVTVDYWSFGTMVFE 193

                  ....
gi 1164769387 529 LLTG 532
Cdd:cd14039   194 CIAG 197
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
436-532 6.19e-04

Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HIPK1 has been implicated in regulating eye size, lens formation, and retinal morphogenesis during late embryogenesis. It also contributes to the regulation of haematopoiesis and leukaemogenesis by phosphorylating and repressing the transcription factor c-Myb, which is crucial in T- and B-cell development. In glucose-deprived conditions, HIPK1 phosphorylates Daxx, leading to its relocalization from the nucleus to the cytoplasm, where it binds and stabilizes ASK1 (apoptosis signal-regulating kinase 1), a mitogen-activated protein kinase (MAPK) kinase kinase that activates the JNK and p38 MAPK pathways. HIPKs, originally identified by their ability to bind homeobox factors, are nuclear proteins containing catalytic kinase and homeobox-interacting domains as well as a PEST region overlapping with the speckle-retention signal (SRS). The HIPK1 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: 271130 [Multi-domain]  Cd Length: 355  Bit Score: 42.38  E-value: 6.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDR----GHIQLTYFSRWSEVEDS-CDSDAIERMYCAPEVGAI 510
Cdd:cd14228   114 LPLKYIRPILQQVATALMKLKSLGLIHADLKPENIMLVDPvrqpYRVKVIDFGSASHVSKAvCSTYLQSRYYRAPEIILG 193
                          90       100
                  ....*....|....*....|..
gi 1164769387 511 TEETEACDWWSLGAVLFELLTG 532
Cdd:cd14228   194 LPFCEAIDMWSLGCVIAELFLG 215
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
399-475 7.10e-04

Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SNT7 is a plant thylakoid-associated kinase that is essential in short- and long-term acclimation responses to cope with various light conditions in order to maintain photosynthetic redox poise for optimal photosynthetic performance. Short-term response involves state transitions over periods of minutes while the long-term response (LTR) occurs over hours to days and involves changing the relative amounts of photosystems I and II. SNT7 acts as a redox sensor and a signal transducer for both responses, which are triggered by the redox state of the plastoquinone (PQ) pool. It is positioned at the top of a phosphorylation cascade that induces state transitions by phosphorylating light-harvesting complex II (LHCII), and triggers the LTR through the phosphorylation of chloroplast proteins. The SNT7 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: 270915 [Multi-domain]  Cd Length: 318  Bit Score: 42.04  E-value: 7.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 399 RDSETKGESGLV--LEGDKEIHQIFEDLD-----KKLALASRFYIPEGCIQRWAA------EMVVALDALHREGIVCRDL 465
Cdd:cd14013    67 SKKFTKPSLWLVwkYEGDATLADLMQGKEfpynlEPIIFGRVLIPPRGPKRENVIiksimrQILVALRKLHSTGIVHRDV 146
                          90
                  ....*....|
gi 1164769387 466 NPNNILLNDR 475
Cdd:cd14013   147 KPQNIIVSEG 156
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
447-533 7.51e-04

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: 41.58  E-value: 7.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDScdsdAIER-------MYCAPEVGAITEETEACDW 519
Cdd:cd06642   109 EILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDT----QIKRntfvgtpFWMAPEVIKQSAYDFKADI 184
                          90
                  ....*....|....
gi 1164769387 520 WSLGAVLFELLTGK 533
Cdd:cd06642   185 WSLGITAIELAKGE 198
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
441-530 7.79e-04

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: 41.71  E-value: 7.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVedscdSDAIERM-------YCAPEVGAITEE 513
Cdd:cd14047   119 ALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVKIGDFGLVTSL-----KNDGKRTkskgtlsYMSPEQISSQDY 193
                          90
                  ....*....|....*..
gi 1164769387 514 TEACDWWSLGAVLFELL 530
Cdd:cd14047   194 GKEVDIYALGLILFELL 210
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
451-533 8.35e-04

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: 41.56  E-value: 8.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAI---ERMYCAPEVGAITEETEACDWWSLGAVLF 527
Cdd:cd06658   130 ALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFCAQVSKEVPKRKSlvgTPYWMAPEVISRLPYGTEVDIWSLGIMVI 209

                  ....*.
gi 1164769387 528 ELLTGK 533
Cdd:cd06658   210 EMIDGE 215
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
446-528 8.58e-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: 41.64  E-value: 8.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 446 AEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF---SRW---SEVEDSCDsdaieRMYCAPEVGAITEETEACDW 519
Cdd:cd14052   113 VELSLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFgmaTVWpliRGIEREGD-----REYIAPEILSEHMYDKPADI 187

                  ....*....
gi 1164769387 520 WSLGAVLFE 528
Cdd:cd14052   188 FSLGLILLE 196
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
433-575 8.97e-04

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: 41.41  E-value: 8.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 433 RFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLN---DRGHIQLTYFSrWSEVEDS------CDSDAiermYC 503
Cdd:cd14169    95 RGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYAtpfEDSKIMISDFG-LSKIEAQgmlstaCGTPG----YV 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 504 APEVGAITEETEACDWWSLGAVLFELLTG------KTLVECHPAGINTHTTLNMP--ECVSEEARSLIQQLLQFNPLERL 575
Cdd:cd14169   170 APELLEQKPYGKAVDVWAIGVISYILLCGyppfydENDSELFNQILKAEYEFDSPywDDISESAKDFIRHLLERDPEKRF 249
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
436-545 9.46e-04

Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDC2L6 is also called CDK8-like and was previously referred to as CDK11. However, this is a confusing nomenclature as CDC2L6 is distinct from CDC2L1, which is represented by the two protein products from its gene, called CDK11(p110) and CDK11(p58), as well as the caspase-processed CDK11(p46). CDK11(p110), CDK11(p58), and CDK11(p46)do not belong to this subfamily. CDC2L6 is an associated protein of Mediator, a multiprotein complex that provides a platform to connect transcriptional and chromatin regulators and cofactors, in order to activate and mediate RNA polymerase II transcription. CDC2L6 is localized mainly in the nucleus amd exerts an opposing effect to CDK8 in VP16-dependent transcriptional activation by being a negative regulator. 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 CDC2L6 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: 270850 [Multi-domain]  Cd Length: 318  Bit Score: 41.59  E-value: 9.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILL----NDRGHIQLT--YFSRW--SEVEDSCDSD--AIERMYCAP 505
Cdd:cd07867   106 LPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIAdmGFARLfnSPLKPLADLDpvVVTFWYRAP 185
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1164769387 506 EV--GAiTEETEACDWWSLGAVLFELLTGKTLVECHPAGINT 545
Cdd:cd07867   186 ELllGA-RHYTKAIDIWAIGCIFAELLTSEPIFHCRQEDIKT 226
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
451-601 9.56e-04

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: 41.55  E-value: 9.56e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVedscdSDAIER--------MYCAPEVGAITEETEACDWWSL 522
Cdd:cd06657   128 ALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFCAQV-----SKEVPRrkslvgtpYWMAPELISRLPYGPEVDIWSL 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 523 GAVLFELLTGKTLVECHPA-------GINTHTTLNMPECVSEEARSLIQQLLQFNPLERlgagvAGVEDIKSHPFFT--- 592
Cdd:cd06657   203 GIMVIEMVDGEPPYFNEPPlkamkmiRDNLPPKLKNLHKVSPSLKGFLDRLLVRDPAQR-----ATAAELLKHPFLAkag 277
                         170
                  ....*....|
gi 1164769387 593 -PVDWAELMR 601
Cdd:cd06657   278 pPSCIVPLMR 287
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
436-590 1.03e-03

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: 41.22  E-value: 1.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 436 IPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIER------MYCAPEVGA 509
Cdd:cd06651   108 LTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQTICMSGTGIRsvtgtpYWMSPEVIS 187
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 510 ITEETEACDWWSLGAVLFELLTGKTLVECHPA-----GINTH-TTLNMPECVSEEARSLIQQLLqFNPLERLGAgvagvE 583
Cdd:cd06651   188 GEGYGRKADVWSLGCTVVEMLTEKPPWAEYEAmaaifKIATQpTNPQLPSHISEHARDFLGCIF-VEARHRPSA-----E 261

                  ....*..
gi 1164769387 584 DIKSHPF 590
Cdd:cd06651   262 ELLRHPF 268
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
430-574 1.11e-03

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: 40.98  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQ--LTYFSRWSEVEDSCDSDAIERM-YCAPE 506
Cdd:cd14112    90 FSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSVRSWQvkLVDFGRAQKVSKLGKVPVDGDTdWASPE 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 507 VgaITEETEA---CDWWSLGAVLFELLTGktlveCHP--AGINTHTTL------------NMPECVSEEARSLIQQLLQF 569
Cdd:cd14112   170 F--HNPETPItvqSDIWGLGVLTFCLLSG-----FHPftSEYDDEEETkenvifvkcrpnLIFVEATQEALRFATWALKK 242

                  ....*
gi 1164769387 570 NPLER 574
Cdd:cd14112   243 SPTRR 247
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
445-533 1.18e-03

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: 40.98  E-value: 1.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 445 AAEMVVALDA------LHR--EGIVCRDLNPNNILLNDRGHIQLTYF--SRW--SEVEDSCDSDAIERMYCAPEV-GAIT 511
Cdd:cd14064    93 QSKLIIAVDVakgmeyLHNltQPIIHRDLNSHNILLYEDGHAVVADFgeSRFlqSLDEDNMTKQPGNLRWMAPEVfTQCT 172
                          90       100
                  ....*....|....*....|..
gi 1164769387 512 EETEACDWWSLGAVLFELLTGK 533
Cdd:cd14064   173 RYSIKADVFSYALCLWELLTGE 194
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
445-533 1.28e-03

Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. B-Raf activates ERK with the strongest magnitude, compared with other Raf kinases. Mice embryos deficient in B-Raf die around midgestation due to vascular hemorrhage caused by apoptotic endothelial cells. Mutations in B-Raf have been implicated in initiating tumorigenesis and tumor progression, and are found in malignant cutaneous melanoma, papillary thyroid cancer, as well as in ovarian and colorectal carcinomas. Most oncogenic B-Raf mutations are located at the activation loop of the kinase and surrounding regions; the V600E mutation accounts for around 90% of oncogenic mutations. The V600E mutant constitutively activates MEK, resulting in sustained activation of ERK. B-Raf 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. They function in the linear Ras-Raf-MEK-ERK pathway that regulates many cellular processes including cycle regulation, proliferation, differentiation, survival, and apoptosis. The B-Raf 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: 271053 [Multi-domain]  Cd Length: 274  Bit Score: 40.81  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 445 AAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYF------SRWSevedscDSDAIER-----MYCAPEVGAITEE 513
Cdd:cd14151   110 ARQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFglatvkSRWS------GSHQFEQlsgsiLWMAPEVIRMQDK 183
                          90       100
                  ....*....|....*....|...
gi 1164769387 514 TE---ACDWWSLGAVLFELLTGK 533
Cdd:cd14151   184 NPysfQSDVYAFGIVLYELMTGQ 206
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
441-574 1.29e-03

Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated protein Triple Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLTK, also called zipper sterile-alpha-motif kinase (ZAK), contains a catalytic kinase domain and a leucine zipper. There are two alternatively-spliced variants, MLTK-alpha and MLTK-beta. MLTK-alpha contains a sterile-alpha-motif (SAM) at the C-terminus. MLTK regulates the c-Jun N-terminal kinase, extracellular signal-regulated kinase, p38 MAPK, and NF-kB pathways. ZAK is the MAP3K involved in the signaling cascade that leads to the ribotoxic stress response initiated by cellular damage due to Shiga toxins and ricin. It may also play a role in cell transformation and cancer development. 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 MLTK 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: 270962 [Multi-domain]  Cd Length: 242  Bit Score: 40.71  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 441 IQRWAAEMVVALDALHREG---IVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCDSDAIERM-YCAPEVGAITEETEA 516
Cdd:cd14060    86 IMTWATDIAKGMHYLHMEApvkVIHRDLKSRNVVIAADGVLKICDFGASRFHSHTTHMSLVGTFpWMAPEVIQSLPVSET 165
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1164769387 517 CDWWSLGAVLFELLT------GKTLVECHPAGINTHTTLNMPECVSEEARSLIQQLLQFNPLER 574
Cdd:cd14060   166 CDTYSYGVVLWEMLTrevpfkGLEGLQVAWLVVEKNERPTIPSSCPRSFAELMRRCWEADVKER 229
Kinase-like pfam14531
Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. ...
416-527 1.31e-03

Kinase-like; This family includes the pseudokinases ROP2 and ROP8 from Toxoplasma gondii. These proteins have a typical bilobed protein kinase fold, but lack catalytic actvity.


Pssm-ID: 405254 [Multi-domain]  Cd Length: 288  Bit Score: 40.94  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 416 EIHQIFEDL------DKKLALASRFYIPEGCIqRWAAemvvaldALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEV 489
Cdd:pfam14531 123 DLQLLGEVLlshsstHKSLVHHARLQLTLQLI-RLAA-------NLQHYGLVHGQFTVDNFFLDQRGGVFLGGFEHLVRD 194
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1164769387 490 EDSCDSDAIERMYCAPEVGA---------ITEETEACDWWSLGAVLF 527
Cdd:pfam14531 195 GTKVVASEVPRGFAPPELLGsrggytmknTTLMTHAFDAWQLGLVIY 241
Pkinase_Tyr pfam07714
Protein tyrosine kinase;
455-574 1.38e-03

Protein tyrosine kinase;


Pssm-ID: 429616 [Multi-domain]  Cd Length: 258  Bit Score: 40.94  E-value: 1.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 455 LHREGIVCRDLNPNNILLNDRGHIQLTYF--SRWSEVEDSCDSDAIERM---YCAPEVGAITEETEACDWWSLGAVLFEL 529
Cdd:pfam07714 118 LESKNFVHRDLAARNCLVSENLVVKISDFglSRDIYDDDYYRKRGGGKLpikWMAPESLKDGKFTSKSDVWSFGVLLWEI 197
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1164769387 530 LT-GKTlvechP-AGINTHTTLNM---------PECVSEEARSLIQQLLQFNPLER 574
Cdd:pfam07714 198 FTlGEQ-----PyPGMSNEEVLEYledgyrlpqPENCPDELYDLMKQCWAYDPEDR 248
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
442-540 1.81e-03

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: 40.47  E-value: 1.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 442 QRWAA----EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSC---DSDAIERMYCAPEVGAITEET 514
Cdd:cd06637   110 EEWIAyicrEILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVSAQLDRTVgrrNTFIGTPYWMAPEVIACDENP 189
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1164769387 515 EAC-----DWWSLGAVLFELLTGK-TLVECHP 540
Cdd:cd06637   190 DATydfksDLWSLGITAIEMAEGApPLCDMHP 221
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
451-532 1.89e-03

Catalytic domain of the Dual-specificity protein kinase, YAK1; 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 proteins with similarity to Saccharomyces cerevisiae YAK1 (or Yak1p), a dual-specificity kinase that autophosphorylates at tyrosine residues and phosphorylates substrates on S/T residues. YAK1 phosphorylates and activates the transcription factors Hsf1 and Msn2, which play important roles in cellular homeostasis during stress conditions including heat shock, oxidative stress, and nutrient deficiency. It also phosphorylates the protein POP2, a component of a complex that regulates transcription, under glucose-deprived conditions. It functions as a part of a glucose-sensing system that is involved in controlling growth in yeast. The YAK1 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: 271114 [Multi-domain]  Cd Length: 330  Bit Score: 40.70  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 451 ALDALHREGIVCRDLNPNNILLNDRGhiqltyfSRWSEVED---SCDSDA-----IE-RMYCAPEVGAITEETEACDWWS 521
Cdd:cd14212   115 ALSVLKDARIIHCDLKPENILLVNLD-------SPEIKLIDfgsACFENYtlytyIQsRFYRSPEVLLGLPYSTAIDMWS 187
                          90
                  ....*....|.
gi 1164769387 522 LGAVLFELLTG 532
Cdd:cd14212   188 LGCIAAELFLG 198
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
438-540 2.26e-03

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: 40.38  E-value: 2.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 438 EGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSrwseVEDSCDSDAIER-------MYCAPEVGAI 510
Cdd:cd06636   120 EDWIAYICREILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFG----VSAQLDRTVGRRntfigtpYWMAPEVIAC 195
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1164769387 511 TEETEA-----CDWWSLGAVLFELLTGK-TLVECHP 540
Cdd:cd06636   196 DENPDAtydyrSDIWSLGITAIEMAEGApPLCDMHP 231
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
434-575 2.49e-03

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: 39.99  E-value: 2.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 434 FYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNIL-LNDRG-HIQLTYFSRWSEVEDSCDSDAI--ERMYCAPEVGA 509
Cdd:cd14191    95 FELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMcVNKTGtKIKLIDFGLARRLENAGSLKVLfgTPEFVAPEVIN 174
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1164769387 510 ITEETEACDWWSLGAVLFELLTGKTLVechpAGINTHTTL-NMPEC-----------VSEEARSLIQQLLQFNPLERL 575
Cdd:cd14191   175 YEPIGYATDMWSIGVICYILVSGLSPF----MGDNDNETLaNVTSAtwdfddeafdeISDDAKDFISNLLKKDMKARL 248
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
447-529 2.78e-03

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 5; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K5, also called germinal center kinase-related enzyme (GCKR), has been shown to activate the MAPK c-Jun N-terminal kinase (JNK). MAP4K5 also facilitates Wnt signaling in B cells, and may therefore be implicated in the control of cell fate, proliferation, and polarity. MAP4Ks are involved in some MAPK signaling pathways by activating a MAPK kinase kinase. 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 MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K5 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: 270813 [Multi-domain]  Cd Length: 268  Bit Score: 40.01  E-value: 2.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 447 EMVVALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSC---DSDAIERMYCAPEVGAITEE---TEACDWW 520
Cdd:cd06646   114 ETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGVAAKITATIakrKSFIGTPYWMAPEVAAVEKNggyNQLCDIW 193

                  ....*....
gi 1164769387 521 SLGAVLFEL 529
Cdd:cd06646   194 AVGITAIEL 202
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
445-541 2.86e-03

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: 40.03  E-value: 2.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 445 AAEMVVALDALHREGIVCRDLNPNNILLnDRGHIQLTYF-----SRWSEVEDSCDSDAIER---MYCAPEV-GAITEE-- 513
Cdd:cd14063   103 AQQICQGMGYLHAKGIIHKDLKSKNIFL-ENGRVVITDFglfslSGLLQPGRREDTLVIPNgwlCYLAPEIiRALSPDld 181
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1164769387 514 -------TEACDWWSLGAVLFELLTGKTLVECHPA 541
Cdd:cd14063   182 feeslpfTKASDVYAFGTVWYELLAGRWPFKEQPA 216
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
444-537 3.16e-03

Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily includes three leucine-rich repeat receptor-like kinases (LRR-RLKs): Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1), and Physcomitrella patens CLL1B clavata1-like receptor S/T protein kinase. BAK1 functions in various signaling pathways. It plays a role in BR (brassinosteroid)-regulated plant development as a co-receptor of BRASSINOSTEROID (BR) INSENSITIVE 1 (BRI1), the receptor for BRs, and is required for full activation of BR signaling. It also modulates pathways involved in plant resistance to pathogen infection (pattern-triggered immunity, PTI) and herbivore attack (wound- or herbivore feeding-induced accumulation of jasmonic acid (JA) and JA-isoleucine. 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 STK_BAK1-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: 271134 [Multi-domain]  Cd Length: 270  Bit Score: 39.79  E-value: 3.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 444 WAAEMVVALDA------LHREG---IVCRDLNPNNILLND--RGHIQLTYFSRWSEVEDSCDSDAIERM--YCAPEVGAI 510
Cdd:cd14664    93 WETRQRIALGSarglayLHHDCsplIIHRDVKSNNILLDEefEAHVADFGLAKLMDDKDSHVMSSVAGSygYIAPEYAYT 172
                          90       100
                  ....*....|....*....|....*..
gi 1164769387 511 TEETEACDWWSLGAVLFELLTGKTLVE 537
Cdd:cd14664   173 GKVSEKSDVYSYGVVLLELITGKRPFD 199
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
418-573 3.45e-03

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 40.21  E-value: 3.45e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 418 HQIFEDLDKK--LALASRFYIPEGCIQrwaaemvvALDALHREGIVCRDLNPNNILLNDRGHIQLTYFSRWSEVEDSCD- 494
Cdd:PHA03207  170 CDLFTYVDRSgpLPLEQAITIQRRLLE--------ALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAACKLDAHPDt 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 495 ------SDAIERMycAPEVGAITEETEACDWWSLGAVLFELLTGK-TLVechpaGINTHTTlnmpecvSEEARSLIqQLL 567
Cdd:PHA03207  242 pqcygwSGTLETN--SPELLALDPYCAKTDIWSAGLVLFEMSVKNvTLF-----GKQVKSS-------SSQLRSII-RCM 306

                  ....*.
gi 1164769387 568 QFNPLE 573
Cdd:PHA03207  307 QVHPLE 312
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
460-593 6.92e-03

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: 38.88  E-value: 6.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 460 IVCRDLNPNNILLNDR---GHIQLTYFSRWSEVEDscDSDAIERM-----------YCAPEVGAITEE----TEACDWWS 521
Cdd:cd14040   134 IIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDD--DSYGVDGMdltsqgagtywYLPPECFVVGKEppkiSNKVDVWS 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 522 LGAVLFELLTGKTlvechPAGIN---------------THTTLNMPECVSEEARSLIQQLLQFNPLERLgagvaGVEDIK 586
Cdd:cd14040   212 VGVIFFQCLYGRK-----PFGHNqsqqdilqentilkaTEVQFPVKPVVSNEAKAFIRRCLAYRKEDRF-----DVHQLA 281

                  ....*..
gi 1164769387 587 SHPFFTP 593
Cdd:cd14040   282 SDPYLLP 288
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
430-591 7.59e-03

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: 38.34  E-value: 7.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 430 LASRFYIPEGCIQRWAAEMVVALDALHREGIVCRDLNPNNILLNDRG--HIQLTYFSRWSEVEDScdsdaiERMYC---- 503
Cdd:cd14108    88 ITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMADQKtdQVRICDFGNAQELTPN------EPQYCkygt 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1164769387 504 ----APEVGAITEETEACDWWSLGAVLFELLTGKTLVechpAGINTHTTL------------NMPECVSEEARSLIQQLL 567
Cdd:cd14108   162 pefvAPEIVNQSPVSKVTDIWPVGVIAYLCLTGISPF----VGENDRTTLmnirnynvafeeSMFKDLCREAKGFIIKVL 237
                         170       180
                  ....*....|....*....|....
gi 1164769387 568 QFNPLErlgagvAGVEDIKSHPFF 591
Cdd:cd14108   238 VSDRLR------PDAEETLEHPWF 255
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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