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Conserved domains on  [gi|211971036|ref|NP_001130026|]
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serine/threonine-protein kinase tousled-like 1 isoform 2 [Homo sapiens]

Protein Classification

serine/threonine-protein kinase tousled-like 1( domain architecture ID 19853017)

serine/threonine-protein kinase tousled-like 1 (TLK1) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
401-699 0e+00

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: 636.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 401 HPTLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFS 480
Cdd:cd14040    1 HPTLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 481 LDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTACGEIKITDF 560
Cdd:cd14040   81 LDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTACGEIKITDF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 561 GLSKIMDDDSYGVDGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENT 640
Cdd:cd14040  161 GLSKIMDDDSYGVDGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENT 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 641 ILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLPHMRRSNSSGNL 699
Cdd:cd14040  241 ILKATEVQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLLPHMRRSNSSGNL 299
EnvC super family cl34844
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
157-378 7.97e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


The actual alignment was detected with superfamily member COG4942:

Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 7.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 157 KQLSFKIIQTDLTMLKLAALESNKIQDLEKKEGRIDDLLRANCDLRRQIDEQQKLLEKYKERLNKcisMSKKLlieKSTQ 236
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAEL---EAQK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 237 EKLSSREKSMQDRLRLGHFTTVRHGASFTEQWTDGFAFQNLVKQQEwvnQQREDIERQRKLLAKRKPPTANNSQAPSTNS 316
Cdd:COG4942  104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALRAELEAERAELEALL 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 317 EPKQRKNKAVNGAENDpfvrpnlpQLLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLER 378
Cdd:COG4942  181 AELEEERAALEALKAE--------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
 
Name Accession Description Interval E-value
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
401-699 0e+00

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: 636.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 401 HPTLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFS 480
Cdd:cd14040    1 HPTLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 481 LDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTACGEIKITDF 560
Cdd:cd14040   81 LDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTACGEIKITDF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 561 GLSKIMDDDSYGVDGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENT 640
Cdd:cd14040  161 GLSKIMDDDSYGVDGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENT 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 641 ILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLPHMRRSNSSGNL 699
Cdd:cd14040  241 ILKATEVQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLLPHMRRSNSSGNL 299
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
419-686 1.44e-73

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 238.58  E-value: 1.44e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036   419 FSEVYKAFDLYEQRYAAVKIhqLNKswrdEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:smart00220  12 FGKVYLARDKKTGKLVAIKV--IKK----KKIKKDRERILREIKILKKLKHPNIVRLYDVF-EDEDKLYLVMEYCEGGDL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036   499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSygvdgmdL 578
Cdd:smart00220  85 FDLLKKRGRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENILL---DEDGHVKLADFGLARQLDPGE-------K 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036   579 TSQGAGTYWYLPPECfVVGKeppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQenTILKATEVQFPVKPVVSSE 658
Cdd:smart00220 153 LTTFVGTPEYMAPEV-LLGK---GYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFK--KIGKPKPPFPPPEWDISPE 226
                          250       260
                   ....*....|....*....|....*...
gi 211971036   659 AKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:smart00220 227 AKDLIRKLLVKDPEKRLTAEEALQHPFF 254
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
419-683 3.20e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 177.13  E-value: 3.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHkhacREYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCEGNDL 498
Cdd:COG0515   20 MGVVYLARDLRLGRPVALKVLRPELAADPEARERFR----REARALARLNHPNIVRVYDVGEED-GRPYLVMEYVEGESL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIkpPIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSygvdgMDL 578
Cdd:COG0515   95 ADLLRRRGPLPPAEALRILAQLAEALAAAHAA--GIVHRDIKPANILLTPD---GRVKLIDFGIARALGGAT-----LTQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPECFvVGKEPpkiSNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQentILKATEVQFP-VKPVVSS 657
Cdd:COG0515  165 TGTVVGTPGYMAPEQA-RGEPV---DPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRA---HLREPPPPPSeLRPDLPP 237
                        250       260
                 ....*....|....*....|....*..
gi 211971036 658 EAKAFIRRCLAYRKEDRF-DVHQLAND 683
Cdd:COG0515  238 ALDAIVLRALAKDPEERYqSAAELAAA 264
Pkinase pfam00069
Protein kinase domain;
419-686 9.28e-41

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 148.55  E-value: 9.28e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036  419 FSEVYKAFDLYEQRYAAVKIhqLNKSwrdEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:pfam00069  12 FGTVYKAKHRDTGKIVAIKK--IKKE---KIKKKKDKNILREIKILKKLNHPNIVRLYDAF-EDKDNLYLVLEYVEGGSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036  499 DFYLKQHKLMSEKEARSIVMQIVNALRylneikppiihydlkpgnillvdgtacGEIKITDFglskimdddsygvdgmdl 578
Cdd:pfam00069  86 FDLLSEKGAFSEREAKFIMKQILEGLE---------------------------SGSSLTTF------------------ 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036  579 tsqgAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQentILKATEVQFPVKPVVSSE 658
Cdd:pfam00069 121 ----VGTPWYMAPE--VLGGNP--YGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEL---IIDQPYAFPELPSNLSEE 189
                         250       260
                  ....*....|....*....|....*...
gi 211971036  659 AKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:pfam00069 190 AKDLLKKLLKKDPSKRLTATQALQHPWF 217
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
447-686 2.05e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 101.25  E-value: 2.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 447 DEKKENYhkhACREYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCEGNDLDFYLKQ----HKLMSEKEARSIVMQIVN 522
Cdd:PTZ00267 105 DERQAAY---ARSELHCLAACDHFGIVKHFDDFKSD-DKLLLIMEYGSGGDLNKQIKQrlkeHLPFQEYEVGLLFYQIVL 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 523 ALRYLNEIKppIIHYDLKPGNILLVdgtACGEIKITDFGLSKIMDDDSygvdGMDLTSQGAGTYWYLPPECFvvgkEPPK 602
Cdd:PTZ00267 181 ALDEVHSRK--MMHRDLKSANIFLM---PTGIIKLGDFGFSKQYSDSV----SLDVASSFCGTPYYLAPELW----ERKR 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 603 ISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntILKATEVQFPVKpvVSSEAKAFIRRCLAYRKEDRFDVHQLAN 682
Cdd:PTZ00267 248 YSKKADMWSLGVILYELLTLHRPF-KGPSQREIMQQ--VLYGKYDPFPCP--VSSGMKALLDPLLSKNPALRPTTQQLLH 322

                 ....
gi 211971036 683 DPYL 686
Cdd:PTZ00267 323 TEFL 326
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
420-626 2.93e-20

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 95.25  E-value: 2.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 420 SEVYKAFDLYEQRYAAVKIHQLNKSwRDEkkeNYHKhacreyRIHKE------LDHPRIVKLYD--------YFsldtdt 485
Cdd:NF033483  21 AEVYLAKDTRLDRDVAVKVLRPDLA-RDP---EFVA------RFRREaqsaasLSHPNIVSVYDvgedggipYI------ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 486 fctVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKI 565
Cdd:NF033483  85 ---VMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNG--IVHRDIKPQNILI---TKDGRVKVTDFGIARA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 566 MDDDSygvdgMDLTSQGAGTYWYLPPECfVVGKeppKISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:NF033483 157 LSSTT-----MTQTNSVLGTVHYLSPEQ-ARGG---TVDARSDIYSLGIVLYEMLTGRPPF 208
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
157-378 7.97e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 7.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 157 KQLSFKIIQTDLTMLKLAALESNKIQDLEKKEGRIDDLLRANCDLRRQIDEQQKLLEKYKERLNKcisMSKKLlieKSTQ 236
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAEL---EAQK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 237 EKLSSREKSMQDRLRLGHFTTVRHGASFTEQWTDGFAFQNLVKQQEwvnQQREDIERQRKLLAKRKPPTANNSQAPSTNS 316
Cdd:COG4942  104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALRAELEAERAELEALL 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 317 EPKQRKNKAVNGAENDpfvrpnlpQLLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLER 378
Cdd:COG4942  181 AELEEERAALEALKAE--------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
 
Name Accession Description Interval E-value
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
401-699 0e+00

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: 636.71  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 401 HPTLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFS 480
Cdd:cd14040    1 HPTLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 481 LDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTACGEIKITDF 560
Cdd:cd14040   81 LDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTACGEIKITDF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 561 GLSKIMDDDSYGVDGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENT 640
Cdd:cd14040  161 GLSKIMDDDSYGVDGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENT 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 641 ILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLPHMRRSNSSGNL 699
Cdd:cd14040  241 ILKATEVQFPVKPVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLLPHMRRSNSSGNL 299
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
419-685 0e+00

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: 571.57  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFCTVLEYCEGNDL 498
Cdd:cd13990   13 FSEVYKAFDLVEQRYVACKIHQLNKDWSEEKKQNYIKHALREYEIHKSLDHPRIVKLYDVFEIDTDSFCTVLEYCDGNDL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSYGVDGMDL 578
Cdd:cd13990   93 DFYLKQHKSIPEREARSIIMQVVSALKYLNEIKPPIIHYDLKPGNILLHSGNVSGEIKITDFGLSKIMDDESYNSDGMEL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQFPVKPVVSSE 658
Cdd:cd13990  173 TSQGAGTYWYLPPECFVVGKTPPKISSKVDVWSVGVIFYQMLYGRKPFGHNQSQEAILEENTILKATEVEFPSKPVVSSE 252
                        250       260
                 ....*....|....*....|....*..
gi 211971036 659 AKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd13990  253 AKDFIRRCLTYRKEDRPDVLQLANDPY 279
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
401-707 0e+00

Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TLKs play important functions during the cell cycle and are implicated in chromatin remodeling, DNA replication and repair, and mitosis. They phosphorylate and regulate Anti-silencing function 1 protein (Asf1), a histone H3/H4 chaperone that helps facilitate the assembly of chromatin following DNA replication during S phase. TLKs also phosphorylate the H3 histone tail and are essential in transcription. Vertebrates contain two subfamily members, TLK1 and TLK2. The TLK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270943 [Multi-domain]  Cd Length: 309  Bit Score: 570.08  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 401 HPTLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFS 480
Cdd:cd14041    1 HPTLNDRYLLLHLLGRGGFSEVYKAFDLTEQRYVAVKIHQLNKNWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 481 LDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTACGEIKITDF 560
Cdd:cd14041   81 LDTDSFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKPPIIHYDLKPGNILLVNGTACGEIKITDF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 561 GLSKIMDDDSYG-VDGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQEN 639
Cdd:cd14041  161 GLSKIMDDDSYNsVDGMELTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFYQCLYGRKPFGHNQSQQDILQEN 240
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 640 TILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLPHMRRS-NSSGNLHMAGLTAS 707
Cdd:cd14041  241 TILKATEVQFPPKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLLPHIRKSvSTSSPAGAAVASTS 309
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
419-686 1.44e-73

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 238.58  E-value: 1.44e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036   419 FSEVYKAFDLYEQRYAAVKIhqLNKswrdEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:smart00220  12 FGKVYLARDKKTGKLVAIKV--IKK----KKIKKDRERILREIKILKKLKHPNIVRLYDVF-EDEDKLYLVMEYCEGGDL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036   499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSygvdgmdL 578
Cdd:smart00220  85 FDLLKKRGRLSEDEARFYLRQILSALEYLHSKG--IVHRDLKPENILL---DEDGHVKLADFGLARQLDPGE-------K 152
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036   579 TSQGAGTYWYLPPECfVVGKeppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQenTILKATEVQFPVKPVVSSE 658
Cdd:smart00220 153 LTTFVGTPEYMAPEV-LLGK---GYGKAVDIWSLGVILYELLTGKPPFPGDDQLLELFK--KIGKPKPPFPPPEWDISPE 226
                          250       260
                   ....*....|....*....|....*...
gi 211971036   659 AKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:smart00220 227 AKDLIRKLLVKDPEKRLTAEEALQHPFF 254
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
419-684 1.48e-58

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: 198.85  E-value: 1.48e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKhacREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL 498
Cdd:cd05117   13 FGVVRLAVHKKTGEEYAVKI--IDKKKLKSEDEEMLR---REIEILKRLDHPNIVKLYEVFE-DDKNLYLVMELCTGGEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDsygvdgmDL 578
Cdd:cd05117   87 FDRIVKKGSFSEREAAKIMKQILSAVAYLHSQG--IVHRDLKPENILLASKDPDSPIKIIDFGLAKIFEEG-------EK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNqSQQDILQEntILKAT-EVQFPVKPVVSS 657
Cdd:cd05117  158 LKTVCGTPYYVAPEVL----KGKGYGKKCDIWSLGVILYILLCGYPPFYGE-TEQELFEK--ILKGKySFDSPEWKNVSE 230
                        250       260
                 ....*....|....*....|....*..
gi 211971036 658 EAKAFIRRCLAYRKEDRFDVHQLANDP 684
Cdd:cd05117  231 EAKDLIKRLLVVDPKKRLTAAEALNHP 257
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
419-684 1.08e-54

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: 186.71  E-value: 1.08e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSwrdekkENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd00180    6 FGKVYKARDKETGKKVAVKVIPKEKL------KKLLEELLREIEILKKLNHPNIVKLYDVF-ETENFLYLVMEYCEGGSL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQH-KLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGVDGMD 577
Cdd:cd00180   79 KDLLKENkGPLSEEEALSILRQLLSALEYLHSNG--IIHRDLKPENILL---DSDGTVKLADFGLAKDLDSDDSLLKTTG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 ltsqGAGTYWYLPPECfvvgKEPPKISNKVDVWSVGVIFFQClygrkpfghnqsqqdilqentilkatevqfpvkpvvsS 657
Cdd:cd00180  154 ----GTTPPYYAPPEL----LGGRYYGPKVDIWSLGVILYEL-------------------------------------E 188
                        250       260
                 ....*....|....*....|....*..
gi 211971036 658 EAKAFIRRCLAYRKEDRFDVHQLANDP 684
Cdd:cd00180  189 ELKDLIRRMLQYDPKKRPSAKELLEHL 215
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
419-683 2.23e-51

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: 179.32  E-value: 2.23e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHkhacREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL 498
Cdd:cd14014   13 MGEVYRARDTLLGRPVAIKVLRPELAEDEEFRERFL----REARALARLSHPNIVRVYDVGEDDGRPY-IVMEYVEGGSL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDdsygvDGMDL 578
Cdd:cd14014   88 ADLLRERGPLPPREALRILAQIADALAAAHR--AGIVHRDIKPANILL---TEDGRVKLTDFGIARALGD-----SGLTQ 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPEcFVVGKEPpkiSNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQFPvkPVVSSE 658
Cdd:cd14014  158 TGSVLGTPAYMAPE-QARGGPV---DPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSPLN--PDVPPA 231
                        250       260
                 ....*....|....*....|....*.
gi 211971036 659 AKAFIRRCLAYRKEDRF-DVHQLAND 683
Cdd:cd14014  232 LDAIILRALAKDPEERPqSAAELLAA 257
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
419-687 4.32e-49

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: 172.66  E-value: 4.32e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSwrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFCtVLEYCEGNDL 498
Cdd:cd14007   13 FGNVYLAREKKSGFIVALKV--ISKS--QLQKSGLEHQLRREIEIQSHLRHPNILRLYGYFEDKKRIYL-ILEYAPNGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsygvdgMDL 578
Cdd:cd14007   88 YKELKKQKRFDEKEAAKYIYQLALALDYLHSKN--IIHRDIKPENILL---GSNGELKLADFGWSVHAPSN------RRK 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSqgAGTYWYLPPEcFVVGKEppkISNKVDVWSVGVIFFQCLYGRKPFGHNqSQQDILQEntILKAtEVQFPvkPVVSSE 658
Cdd:cd14007  157 TF--CGTLDYLPPE-MVEGKE---YDYKVDIWSLGVLCYELLVGKPPFESK-SHQETYKR--IQNV-DIKFP--SSVSPE 224
                        250       260
                 ....*....|....*....|....*....
gi 211971036 659 AKAFIRRCLAYRKEDRFDVHQLANDPYLL 687
Cdd:cd14007  225 AKDLISKLLQKDPSKRLSLEQVLNHPWIK 253
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
419-685 8.59e-49

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: 171.93  E-value: 8.59e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKhacREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd14003   13 FGKVKLARHKLTGEKVAIKI--IDKSKLKEEIEEKIK---REIEIMKLLNHPNIIKLYEVI-ETENKIYLVMEYASGGEL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvDGTacGEIKITDFGLSKIMDDDSYgvdgmdL 578
Cdd:cd14003   87 FDYIVNNGRLSEDEARRFFQQLISAVDYCHSNG--IVHRDLKLENILL-DKN--GNLKIIDFGLSNEFRGGSL------L 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQgAGTYWYLPPECFvVGKepPKISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQ--QDILQEntilkatevQFPVKPVV 655
Cdd:cd14003  156 KTF-CGTPAYAAPEVL-LGR--KYDGPKADVWSLGVILYAMLTGYLPFdDDNDSKlfRKILKG---------KYPIPSHL 222
                        250       260       270
                 ....*....|....*....|....*....|
gi 211971036 656 SSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14003  223 SPDARDLIRRMLVVDPSKRITIEEILNHPW 252
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
419-683 3.20e-48

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 177.13  E-value: 3.20e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHkhacREYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCEGNDL 498
Cdd:COG0515   20 MGVVYLARDLRLGRPVALKVLRPELAADPEARERFR----REARALARLNHPNIVRVYDVGEED-GRPYLVMEYVEGESL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIkpPIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSygvdgMDL 578
Cdd:COG0515   95 ADLLRRRGPLPPAEALRILAQLAEALAAAHAA--GIVHRDIKPANILLTPD---GRVKLIDFGIARALGGAT-----LTQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPECFvVGKEPpkiSNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQentILKATEVQFP-VKPVVSS 657
Cdd:COG0515  165 TGTVVGTPGYMAPEQA-RGEPV---DPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRA---HLREPPPPPSeLRPDLPP 237
                        250       260
                 ....*....|....*....|....*..
gi 211971036 658 EAKAFIRRCLAYRKEDRF-DVHQLAND 683
Cdd:COG0515  238 ALDAIVLRALAKDPEERYqSAAELAAA 264
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
419-686 2.42e-46

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: 165.80  E-value: 2.42e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSwRDEKKENYHKHAC----------REYRIHKELDHPRIVKLYDYF-SLDTDTFC 487
Cdd:cd14008    6 FGKVKLALDTETGQLYAIKI--FNKS-RLRKRREGKNDRGkiknalddvrREIAIMKKLDHPNIVRLYEVIdDPESDKLY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 488 TVLEYCEGNDLDFYLKQHKL--MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKI 565
Cdd:cd14008   83 LVLEYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENG--IVHRDIKPENLLL---TADGTVKISDFGVSEM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 566 MDDDSygvdgmDLTSQGAGTYWYLPPECFVVGkEPPKISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQqdilQENTILKA 644
Cdd:cd14008  158 FEDGN------DTLQKTAGTPAFLAPELCDGD-SKTYSGKAADIWALGVTLYCLVFGRLPFnGDNILE----LYEAIQNQ 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 211971036 645 tEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14008  227 -NDEFPIPPELSPELKDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
419-675 1.62e-45

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: 162.69  E-value: 1.62e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL 498
Cdd:cd05123    6 FGKVLLVRKKDTGKLYAMKV--LRK--KEIIKRKEVEHTLNERNILERVNHPFIVKLHYAFQ-TEEKLYLVLDYVPGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddsYGVDGMDL 578
Cdd:cd05123   81 FSHLSKEGRFPEERARFYAAEIVLALEYLHSLG--IIYRDLKPENILL---DSDGHIKLTDFGLAK------ELSSDGDR 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPEcFVVGKEppkISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDIlqENTILKAtEVQFPVKpvVSSE 658
Cdd:cd05123  150 TYTFCGTPEYLAPE-VLLGKG---YGKAVDWWSLGVLLYEMLTGKPPF-YAENRKEI--YEKILKS-PLKFPEY--VSPE 219
                        250
                 ....*....|....*..
gi 211971036 659 AKAFIRRCLAYRKEDRF 675
Cdd:cd05123  220 AKSLISGLLQKDPTKRL 236
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
419-685 4.47e-43

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: 156.23  E-value: 4.47e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKI---HQLNKSWRDEKKenyhkhacREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEG 495
Cdd:cd14009    6 FATVWKGRHKQTGEVVAIKEisrKKLNKKLQENLE--------SEIAILKSIKHPNIVRLYD-VQKTEDFIYLVLEYCAG 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 NDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSygvdg 575
Cdd:cd14009   77 GDLSQYIRKRGRLPEAVARHFMQQLASGLKFLRSKN--IIHRDLKPQNLLLSTSGDDPVLKIADFGFARSLQPAS----- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 mdLTSQGAGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQqdiLQENTILKATEVQFPVKPV 654
Cdd:cd14009  150 --MAETLCGSPLYMAPE--ILQFQ--KYDAKADLWSVGAILFEMLVGKPPFrGSNHVQ---LLRNIERSDAVIPFPIAAQ 220
                        250       260       270
                 ....*....|....*....|....*....|.
gi 211971036 655 VSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14009  221 LSPDCKDLLRRLLRRDPAERISFEEFFAHPF 251
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
419-686 3.75e-41

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: 151.08  E-value: 3.75e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKEnyhkhACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd08215   13 FGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREE-----ALNEVKLLSKLKHPNIVKYYESF-EENGKLCIVMEYADGGDL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHK----LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsygvd 574
Cdd:cd08215   87 AQKIKKQKkkgqPFPEEQILDWFVQICLALKYLHSRK--ILHRDLKTQNIFL---TKDGVVKLGDFGISKVLEST----- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 575 gMDLTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNqSQQDILQEntILKAtevQF-PVKP 653
Cdd:cd08215  157 -TDLAKTVVGTPYYLSPE--LCENKP--YNYKSDIWALGCVLYELCTLKHPFEAN-NLPALVYK--IVKG---QYpPIPS 225
                        250       260       270
                 ....*....|....*....|....*....|...
gi 211971036 654 VVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd08215  226 QYSSELRDLVNSMLQKDPEKRPSANEILSSPFI 258
Pkinase pfam00069
Protein kinase domain;
419-686 9.28e-41

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 148.55  E-value: 9.28e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036  419 FSEVYKAFDLYEQRYAAVKIhqLNKSwrdEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:pfam00069  12 FGTVYKAKHRDTGKIVAIKK--IKKE---KIKKKKDKNILREIKILKKLNHPNIVRLYDAF-EDKDNLYLVLEYVEGGSL 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036  499 DFYLKQHKLMSEKEARSIVMQIVNALRylneikppiihydlkpgnillvdgtacGEIKITDFglskimdddsygvdgmdl 578
Cdd:pfam00069  86 FDLLSEKGAFSEREAKFIMKQILEGLE---------------------------SGSSLTTF------------------ 120
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036  579 tsqgAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQentILKATEVQFPVKPVVSSE 658
Cdd:pfam00069 121 ----VGTPWYMAPE--VLGGNP--YGPKVDVWSLGCILYELLTGKPPFPGINGNEIYEL---IIDQPYAFPELPSNLSEE 189
                         250       260
                  ....*....|....*....|....*...
gi 211971036  659 AKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:pfam00069 190 AKDLLKKLLKKDPSKRLTATQALQHPWF 217
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
419-686 3.09e-40

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: 148.47  E-value: 3.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSwrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFsldTDTFCT--VLEYCEGN 496
Cdd:cd14099   14 FAKCYEVTDMSTGKVYAGKV--VPKS--SLTKPKQREKLKSEIKIHRSLKHPNIVKFHDCF---EDEENVyiLLELCSNG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 497 DLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsyGVDGM 576
Cdd:cd14099   87 SLMELLKRRKALTEPEVRYFMRQILSGVKYLHSNR--IIHRDLKLGNLFL---DENMNVKIGDFGLAARLEYD--GERKK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 577 DLtsqgAGTYWYLPPEcfVVGKEPPKiSNKVDVWSVGVIFFQCLYGRKPFghnqsqQDILQENTI--LKATEVQFPVKPV 654
Cdd:cd14099  160 TL----CGTPNYIAPE--VLEKKKGH-SFEVDIWSLGVILYTLLVGKPPF------ETSDVKETYkrIKKNEYSFPSHLS 226
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 655 VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14099  227 ISDEAKDLIRSMLQPDPTKRPSLDEILSHPFF 258
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
419-686 3.56e-40

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: 148.05  E-value: 3.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihQLnkswrdEKKENYHKHA---CREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEG 495
Cdd:cd06606   13 FGSVYLALNLDTGELMAVK--EV------ELSGDSEEELealEREIRILSSLKHPNIVRYLG-TERTENTLNIFLEYVPG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 NDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNIlLVDGTacGEIKITDFGLSKIMDDDSYGVDG 575
Cdd:cd06606   84 GSLASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNG--IVHRDIKGANI-LVDSD--GVVKLADFGCAKRLAEIATGEGT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 MDLtsqgAGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILqeNTILKATEV-QFPVKpv 654
Cdd:cd06606  159 KSL----RGTPYWMAPE--VIRGE--GYGRAADIWSLGCTVIEMATGKPPWSELGNPVAAL--FKIGSSGEPpPIPEH-- 226
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 655 VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06606  227 LSEEAKDFLRKCLQRDPKKRPTADELLQHPFL 258
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
419-686 4.06e-40

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: 148.12  E-value: 4.06e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKswrDEKKENYHkhacREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL 498
Cdd:cd05122   13 FGVVYKARHKKTGQIVAIKKINLES---KEKKESIL----NEIAILKKCKHPNIVKYYGSYLKKDELW-IVMEFCSGGSL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQH-KLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDddsygvDGMD 577
Cdd:cd05122   85 KDLLKNTnKTLTEQQIAYVCKEVLKGLEYLHSHG--IIHRDIKAANILLTSD---GEVKLIDFGLSAQLS------DGKT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQgAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFghnqsqqdilQENTILKAT-------EVQFP 650
Cdd:cd05122  154 RNTF-VGTPYWMAPE--VIQGKP--YGFKADIWSLGITAIEMAEGKPPY----------SELPPMKALfliatngPPGLR 218
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 211971036 651 VKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd05122  219 NPKKWSKEFKDFLKKCLQKDPEKRPTAEQLLKHPFI 254
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
404-686 2.49e-38

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: 143.69  E-value: 2.49e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 404 LNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYH-KHACREYRIHKELDHPRIVKLYDYFSLD 482
Cdd:cd14084    4 LRKKYIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFTIGSRREINKpRNIETEIEILKKLSHPCIIKIEDFFDAE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 483 TDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGL 562
Cdd:cd14084   84 DDYY-IVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNG--IIHRDLKPENVLLSSQEEECLIKITDFGL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 563 SKIMDDDSygvdgmdLTSQGAGTYWYLPPECFV-VGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDIlqENTI 641
Cdd:cd14084  161 SKILGETS-------LMKTLCGTPTYLAPEVLRsFGTEG--YTRAVDCWSLGVILFICLSGYPPFSEEYTQMSL--KEQI 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 211971036 642 LKAtEVQF--PVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14084  230 LSG-KYTFipKAWKNVSEEAKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
419-686 5.18e-37

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: 138.91  E-value: 5.18e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnkswrdekKENYHKHACREYRIHKEL----DHPRIVKLYDYFSLDTDT-FCTVLEYC 493
Cdd:cd05118   12 FGTVWLARDKVTGEKVAIKKIKN--------DFRHPKAALREIKLLKHLndveGHPNIVKLLDVFEHRGGNhLCLVFELM 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 494 EGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVdgTACGEIKITDFGLSKIMDDDSYgv 573
Cdd:cd05118   84 GMNLYELIKDYPRGLPLDLIKSYLYQLLQALDFLHSNG--IIHRDLKPENILIN--LELGQLKLADFGLARSFTSPPY-- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 574 dgmdlTSQGAgTYWYLPPECfVVGKEPpkISNKVDVWSVGVIFFQcLYGRKPF--GHNQSQQdiLQENTILKATEvqfpv 651
Cdd:cd05118  158 -----TPYVA-TRWYRAPEV-LLGAKP--YGSSIDIWSLGCILAE-LLTGRPLfpGDSEVDQ--LAKIVRLLGTP----- 220
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 211971036 652 kpvvssEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd05118  221 ------EALDLLSKMLKYDPAKRITASQALAHPYF 249
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
419-685 8.50e-37

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: 139.15  E-value: 8.50e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihQLNKS---WRDEKKENYHkhacREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEG 495
Cdd:cd14098   13 FAEVKKAVEVETGKMRAIK--QIVKRkvaGNDKNLQLFQ----REINILKSLEHPGIVRLIDWYE-DDQHIYLVMEYVEG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 NDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACgEIKITDFGLSKIMDDDSYgvdg 575
Cdd:cd14098   86 GDLMDFIMAWGAIPEQHARELTKQILEAMAYTH--SMGITHRDLKPENILITQDDPV-IVKISDFGLAKVIHTGTF---- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 mdLTSQgAGTYWYLPPEcFVVGKE---PPKISNKVDVWSVGVIFFQCLYGRKPFghNQSQQDILQEnTILKATEVQFPVK 652
Cdd:cd14098  159 --LVTF-CGTMAYLAPE-ILMSKEqnlQGGYSNLVDMWSVGCLVYVMLTGALPF--DGSSQLPVEK-RIRKGRYTQPPLV 231
                        250       260       270
                 ....*....|....*....|....*....|....
gi 211971036 653 PV-VSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14098  232 DFnISEEAIDFILRLLDVDPEKRMTAAQALDHPW 265
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
419-690 6.99e-36

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: 136.58  E-value: 6.99e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL 498
Cdd:cd05581   14 YSTVVLAKEKETGKEYAIKV--LDK--RHIIKEKKVKYVTIEKEVLSRLAHPGIVKLYYTFQ-DESKLYFVLEYAPNGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGV-DGMD 577
Cdd:cd05581   89 LEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKG--IIHRDLKPENILL---DEDMHIKITDFGTAKVLGPDSSPEsTKGD 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQGA----------GTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntILKAtEV 647
Cdd:cd05581  164 ADSQIAynqaraasfvGTAEYVSPE--LLNEKP--AGKSSDLWALGCIIYQMLTGKPPF-RGSNEYLTFQK--IVKL-EY 235
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 211971036 648 QFPvkPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLPHM 690
Cdd:cd05581  236 EFP--ENFPPDAKDLIQKLLVLDPSKRLGVNENGGYDELKAHP 276
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
419-635 2.79e-34

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: 131.12  E-value: 2.79e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFdlYEQRYAAVKIHQLNkSWRDEKKENYhkhaCREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDL 498
Cdd:cd13999    6 FGEVYKGK--WRGTDVAIKKLKVE-DDNDELLKEF----RREVSILSKLRHPNIVQFIG-ACLSPPPLCIVTEYMPGGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYL-KQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMdddsygVDGMD 577
Cdd:cd13999   78 YDLLhKKKIPLSWSLRLKIALDIARGMNYLHS--PPIIHRDLKSLNILLDEN---FTVKIADFGLSRIK------NSTTE 146
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 578 LTSQGAGTYWYLPPECFvvGKEPpkISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQDI 635
Cdd:cd13999  147 KMTGVVGTPRWMAPEVL--RGEP--YTEKADVYSFGIVLWELLTGEVPFkELSPIQIAA 201
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
419-686 3.11e-34

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: 131.22  E-value: 3.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVK-IHQLNKSWRDEKkeNYHkhacREYRIHKELDHPRIVKLYDYFSLDTDtFCTVLEYCEGnD 497
Cdd:cd14002   14 FGKVYKGRRKYTGQVVALKfIPKRGKSEKELR--NLR----QEIEILRKLNHPNIIEMLDSFETKKE-FVVVTEYAQG-E 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSygvdgMD 577
Cdd:cd14002   86 LFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNR--IIHRDMKPQNILI---GKGGVVKLCDFGFARAMSCNT-----LV 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQgAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDIlqeNTILKATeVQFPvkPVVSS 657
Cdd:cd14002  156 LTSI-KGTPLYMAPE--LVQEQP--YDHTADLWSLGCILYELFVGQPPFYTNSIYQLV---QMIVKDP-VKWP--SNMSP 224
                        250       260
                 ....*....|....*....|....*....
gi 211971036 658 EAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14002  225 EFKSFLQGLLNKDPSKRLSWPDLLEHPFV 253
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
419-685 4.95e-34

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: 130.49  E-value: 4.95e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQR-YAAVKIHQ---LNKSWRDekkenyhkHACREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCE 494
Cdd:cd14121    8 YATVYKAYRKSGAReVVAVKCVSkssLNKASTE--------NLLTEIELLKKLKHPHIVELKD-FQWDEEHIYLIMEYCS 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 GNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcGEIKITDFGLSKIM--DDDSYG 572
Cdd:cd14121   79 GGDLSRFIRSRRTLPESTVRRFLQQLASALQFLREHN--ISHMDLKPQNLLLSSRYN-PVLKLADFGFAQHLkpNDEAHS 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 573 VDGMDLtsqgagtywYLPPEcFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDIlqENTILKATEVQFPVK 652
Cdd:cd14121  156 LRGSPL---------YMAPE-MILKK---KYDARVDLWSVGVILYECLFGRAPF-ASRSFEEL--EEKIRSSKPIEIPTR 219
                        250       260       270
                 ....*....|....*....|....*....|...
gi 211971036 653 PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14121  220 PELSADCRDLLLRLLQRDPDRRISFEEFFAHPF 252
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
446-667 1.89e-33

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: 128.92  E-value: 1.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 446 RDEKKENyhkhACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALR 525
Cdd:cd14006   29 RDKKKEA----VLREISILNQLQHPRIIQLHEAY-ESPTELVLILELCSGGELLDRLAERGSLSEEEVRTYMRQLLEGLQ 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 526 YLNEIKppIIHYDLKPGNILLVDGTAcGEIKITDFGLSKIMDDDsygvdgmDLTSQGAGTYWYLPPEcfVVGKEPpkISN 605
Cdd:cd14006  104 YLHNHH--ILHLDLKPENILLADRPS-PQIKIIDFGLARKLNPG-------EELKEIFGTPEFVAPE--IVNGEP--VSL 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 211971036 606 KVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntiLKATEVQF--PVKPVVSSEAKAFIRRCL 667
Cdd:cd14006  170 ATDMWSIGVLTYVLLSGLSPF-LGEDDQETLAN---ISACRVDFseEYFSSVSQEAKDFIRKLL 229
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
419-686 3.89e-33

Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of fungal STKs including Saccharomyces cerevisiae RCK1 and RCK2, Schizosaccharomyces pombe Sty1-regulated kinase 1 (Srk1), and similar proteins. RCK1, RCK2 (or Rck2p), and Srk1 are MAPK-activated protein kinases. RCK1 and RCK2 are involved in oxidative and metal stress resistance in budding yeast. RCK2 also regulates rapamycin sensitivity in both S. cerevisiae and Candida albicans. Srk1 is activated by Sty1/Spc1 and is involved in negatively regulating cell cycle progression by inhibiting Cdc25. The RCK1-like subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270998 [Multi-domain]  Cd Length: 295  Bit Score: 129.48  E-value: 3.89e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDL-YEQRYAAVKI---HQLNKSWRDEK-KENYHKhacrEYRIHKELDHPRIVKLYDYFslDTDTFC-TVLEY 492
Cdd:cd14096   14 FSNVYKAVPLrNTGKPVAIKVvrkADLSSDNLKGSsRANILK----EVQIMKRLSHPNIVKLLDFQ--ESDEYYyIVLEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 493 CEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILL-------------------------- 546
Cdd:cd14096   88 ADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIG--VVHRDIKPENLLFepipfipsivklrkadddetkvdege 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 547 ----VDGTACGEIKITDFGLSKIMDDDSygvdgmdlTSQGAGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYG 622
Cdd:cd14096  166 fipgVGGGGIGIVKLADFGLSKQVWDSN--------TKTPCGTVGYTAPE--VVKDE--RYSKKVDMWALGCVLYTLLCG 233
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 623 RKPF---GHNQSQQDILQ-ENTILKatevqfPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14096  234 FPPFydeSIETLTEKISRgDYTFLS------PWWDEISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
427-667 5.07e-33

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: 128.49  E-value: 5.07e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 427 DLYeqryaAVKIhqLNKswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHK 506
Cdd:cd05579   19 DLY-----AIKV--IKK--RDMIRKNQVDSVLAERNILSQAQNPFVVKLYYSFQ-GKKNLYLVMEYLPGGDLYSLLENVG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 507 LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKI-MDDDSYGVDGMDLTSQGA-- 583
Cdd:cd05579   89 ALDEDVARIYIAEIVLALEYLHSHG--IIHRDLKPDNILI---DANGHLKLTDFGLSKVgLVRRQIKLSIQKKSNGAPek 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 584 ------GTYWYLPPEcFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntILKAtEVQFPVKPVVSS 657
Cdd:cd05579  164 edrrivGTPDYLAPE-ILLGQ---GHGKTVDWWSLGVILYEFLVGIPPF-HAETPEEIFQN--ILNG-KIEWPEDPEVSD 235
                        250
                 ....*....|
gi 211971036 658 EAKAFIRRCL 667
Cdd:cd05579  236 EAKDLISKLL 245
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
422-636 9.52e-33

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: 127.98  E-value: 9.52e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKIHQLnkswrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSldTDTFCT-VLEYCEgNDLDF 500
Cdd:cd07829   15 VYKAKDKKTGEIVALKKIRL-----DNEEEGIPSTALREISLLKELKHPNIVKLLDVIH--TENKLYlVFEYCD-QDLKK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 501 YLKQHKL-MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddSYGVDGMDLT 579
Cdd:cd07829   87 YLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHR--ILHRDLKPQNLLI---NRDGVLKLADFGLAR-----AFGIPLRTYT 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 580 SQGAgTYWYLPPEcFVVGKepPKISNKVDVWSVGVIFFQCLYGrKPFGHNQSQQDIL 636
Cdd:cd07829  157 HEVV-TLWYRAPE-ILLGS--KHYSTAVDIWSVGCIFAELITG-KPLFPGDSEIDQL 208
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
419-686 1.77e-32

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: 126.55  E-value: 1.77e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKswrdekKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd06623   14 SGVVYKVRHKPTGKIYALKKIHVDG------DEEFRKQLLRELKTLRSCESPYVVKCYGAF-YKEGEISIVLEYMDGGSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPpIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDddsygvDGMDL 578
Cdd:cd06623   87 ADLLKKVGKIPEPVLAYIARQILKGLDYLHTKRH-IIHRDIKPSNLLI---NSKGEVKIADFGISKVLE------NTLDQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQ--DILQEntILKaTEVQFPVKPVVS 656
Cdd:cd06623  157 CNTFVGTVTYMSPERI----QGESYSYAADIWSLGLTLLECALGKFPFLPPGQPSffELMQA--ICD-GPPPSLPAEEFS 229
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 657 SEAKAFIRRCLayRKE--DRFDVHQLANDPYL 686
Cdd:cd06623  230 PEFRDFISACL--QKDpkKRPSAAELLQHPFI 259
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
419-686 2.40e-32

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


Pssm-ID: 270885 [Multi-domain]  Cd Length: 258  Bit Score: 126.19  E-value: 2.40e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAA---VKIHQLNKSWRDEKKEnyhkhacrEYRIHKELDHPRIVKLYDY-FSLDTDTFCTVLEYCE 494
Cdd:cd13983   14 FKTVYRAFDTEEGIEVAwneIKLRKLPKAERQRFKQ--------EIEILKSLKHPNIIKFYDSwESKSKKEVIFITELMT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 GNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNIlLVDGTAcGEIKITDFGLSKIMDDD-SYGV 573
Cdd:cd13983   86 SGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDPPIIHRDLKCDNI-FINGNT-GEVKIGDLGLATLLRQSfAKSV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 574 dgmdltsqgAGTYWYLPPECFVVGKEPpkisnKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQentilKATEVQFPV-- 651
Cdd:cd13983  164 ---------IGTPEFMAPEMYEEHYDE-----KVDIYAFGMCLLEMATGEYPYSECTNAAQIYK-----KVTSGIKPEsl 224
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 211971036 652 KPVVSSEAKAFIRRCLAyRKEDRFDVHQLANDPYL 686
Cdd:cd13983  225 SKVKDPELKDFIEKCLK-PPDERPSARELLEHPFF 258
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
419-686 4.73e-32

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: 125.37  E-value: 4.73e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAF--DLYEQRYAAVKIhqLNKswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGN 496
Cdd:cd14080   13 YSKVKLAEytKSGLKEKVACKI--IDK--KKAPKDFLEKFLPRELEILRKLRHPNIIQVYSIFE-RGSKVFIFMEYAEHG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 497 DLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsygvDGM 576
Cdd:cd14080   88 DLLEYIQKRGALSESQARIWFRQLALAVQYLHSLD--IAHRDLKCENILL---DSNNNVKLSDFGFARLCPDD----DGD 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 577 DLTSQGAGTYWYLPPEcfVVGKEP--PKISnkvDVWSVGVIFFQCLYGRKPFG-------HNQSQQDilqentilkatEV 647
Cdd:cd14080  159 VLSKTFCGSAAYAAPE--ILQGIPydPKKY---DIWSLGVILYIMLCGSMPFDdsnikkmLKDQQNR-----------KV 222
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 211971036 648 QFPVKPV-VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14080  223 RFPSSVKkLSPECKDLIDQLLEPDPTKRATIEEILNHPWL 262
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
430-629 5.94e-32

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: 125.11  E-value: 5.94e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 430 EQRYAaVKIhqLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMS 509
Cdd:cd13994   20 GVLYA-VKE--YRRRDDESKRKDYVKRLTSEYIISSKLHHPNIVKVLDLCQDLHGKWCLVMEYCPGGDLFTLIEKADSLS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 510 EKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMdddSYGVDGMDLTSQGA-GTYWY 588
Cdd:cd13994   97 LEEKDCFFKQILRGVAYLHSHG--IAHRDLKPENILL---DEDGVLKLTDFGTAEVF---GMPAEKESPMSAGLcGSEPY 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 211971036 589 LPPECFVVGKEPPKIsnkVDVWSVGVIFFQCLYGRKPFGHN 629
Cdd:cd13994  169 MAPEVFTSGSYDGRA---VDVWSCGIVLFALFTGRFPWRSA 206
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
419-686 7.10e-32

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: 124.72  E-value: 7.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDyfSLDTDT-FCTVLEYCEGND 497
Cdd:cd14162   13 YAVVKKAYSTKHKCKVAIKI----VSKKKAPEDYLQKFLPREIEVIKGLKHPNLICFYE--AIETTSrVYIIMELAENGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvDGTacGEIKITDFGLSKimdDDSYGVDGMD 577
Cdd:cd14162   87 LLDYIRKNGALPEPQARRWFRQLVAGVEYCH--SKGVVHRDLKCENLLL-DKN--NNLKITDFGFAR---GVMKTKDGKP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQG-AGTYWYLPPECFVVGKEPPKISnkvDVWSVGVIFFQCLYGRKPFGhNQSQQDILQEntilKATEVQFPVKPVVS 656
Cdd:cd14162  159 KLSETyCGSYAYASPEILRGIPYDPFLS---DIWSMGVVLYTMVYGRLPFD-DSNLKVLLKQ----VQRRVVFPKNPTVS 230
                        250       260       270
                 ....*....|....*....|....*....|
gi 211971036 657 SEAKAFIRRCLAYRKEdRFDVHQLANDPYL 686
Cdd:cd14162  231 EECKDLILRMLSPVKK-RITIEEIKRDPWF 259
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
431-686 4.60e-31

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: 122.36  E-value: 4.60e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 431 QRYAaVKIhqLNKSWRDEKKENyhKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSE 510
Cdd:cd05578   26 KMFA-MKY--MNKQKCIEKDSV--RNVLNELEILQELEHPFLVNLWYSFQDEEDMY-MVVDLLLGGDLRYHLQQKVKFSE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 511 KEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSygvdgmdLTSQGAGTYWYLP 590
Cdd:cd05578  100 ETVKFYICEIVLALDYLHSKN--IIHRDIKPDNILL---DEQGHVHITDFNIATKLTDGT-------LATSTSGTKPYMA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 591 PECFVvgkePPKISNKVDVWSVGVIFFQCLYGRKPF-GH-NQSQQDILQentILKATEVQFPvkPVVSSEAKAFIRRCLA 668
Cdd:cd05578  168 PEVFM----RAGYSFAVDWWSLGVTAYEMLRGKRPYeIHsRTSIEEIRA---KFETASVLYP--AGWSEEAIDLINKLLE 238
                        250
                 ....*....|....*....
gi 211971036 669 YRKEDRF-DVHQLANDPYL 686
Cdd:cd05578  239 RDPQKRLgDLSDLKNHPYF 257
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
419-686 1.17e-30

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. The MLCK1 gene expresses three transcripts in a cell-specific manner: a short MLCK1 which contains three immunoglobulin (Ig)-like and one fibronectin type III (FN3) domains, PEVK and actin-binding regions, and a kinase domain near the C-terminus; a long MLCK1 containing six additional Ig-like domains at the N-terminus compared to the short MLCK1; and the C-terminal Ig module. MLCK2, MLCK3, and MLCK4 share a simpler domain architecture of a single kinase domain near the C-terminus and the absence of Ig-like or FN3 domains. The MLCK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271005 [Multi-domain]  Cd Length: 250  Bit Score: 120.79  E-value: 1.17e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSwrdEKKENyhkhACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL 498
Cdd:cd14103    6 FGTVYRCVEKATGKELAAKFIKCRKA---KDRED----VRNEIEIMNQLRHPRLLQLYDAFE-TPREMVLVMEYVAGGEL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 -------DFYLkqhklmSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTAcGEIKITDFGLSKIMDDDSy 571
Cdd:cd14103   78 fervvddDFEL------TERDCILFMRQICEGVQYMH--KQGILHLDLKPENILCVSRTG-NQIKIIDFGLARKYDPDK- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 572 gvdgmDLTSQgAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPF-GHNqsqqDILQENTILKAT-EVQF 649
Cdd:cd14103  148 -----KLKVL-FGTPEFVAPE--VVNYEP--ISYATDMWSVGVICYVLLSGLSPFmGDN----DAETLANVTRAKwDFDD 213
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 211971036 650 PVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14103  214 EAFDDISDEAKDFISKLLVKDPRKRMSAAQCLQHPWL 250
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
419-675 1.19e-30

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: 123.55  E-value: 1.19e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKHACREyrIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd05573   14 FGEVWLVRDKDTGQVYAMKI--LRKSDMLKREQIAHVRAERD--ILADADSPWIVRLHYAF-QDEDHLYLVMEYMPGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDD----SYGVD 574
Cdd:cd05573   89 MNLLIKYDVFPEETARFYIAELVLALDSLHKLG--FIHRDIKPDNILL---DADGHIKLADFGLCTKMNKSgdreSYLND 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 575 GMDLTSQG-------------------AGTYWYLPPEcfVVGKEPPkiSNKVDVWSVGVIFFQCLYGRKPF---GHNQSQ 632
Cdd:cd05573  164 SVNTLFQDnvlarrrphkqrrvraysaVGTPDYIAPE--VLRGTGY--GPECDWWSLGVILYEMLYGFPPFysdSLVETY 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 211971036 633 QDILQENTILkatevQFPVKPVVSSEAKAFIRRCLAyRKEDRF 675
Cdd:cd05573  240 SKIMNWKESL-----VFPDDPDVSPEAIDLIRRLLC-DPEDRL 276
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
458-686 3.02e-30

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: 120.15  E-value: 3.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 458 CREYRIHK----EL--DHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIK 531
Cdd:cd14106   50 CRNEILHEiavlELckDCPRVVNLHEVYETRSELI-LILELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERN 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 532 ppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMdddSYGVDGMDLtsqgAGTYWYLPPEcfVVGKEPpkISNKVDVWS 611
Cdd:cd14106  129 --IVHLDLKPQNILLTSEFPLGDIKLCDFGISRVI---GEGEEIREI----LGTPDYVAPE--ILSYEP--ISLATDMWS 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 612 VGVIFFQCLYGRKPFGHNQSQQdilqenTILKATEVQ--FPVK--PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14106  196 IGVLTYVLLTGHSPFGGDDKQE------TFLNISQCNldFPEElfKDVSPLAIDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
460-686 4.77e-30

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: 119.57  E-value: 4.77e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFsLDTD--TFCTVLEYCEGNDLDFYLKQHK----LMSEKEARSIVMQIVNALR---YLNEI 530
Cdd:cd08217   49 EVNILRELKHPNIVRYYDRI-VDRAntTLYIVMEYCEGGDLAQLIKKCKkenqYIPEEFIWKIFTQLLLALYechNRSVG 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 531 KPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYgvdgmdLTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVW 610
Cdd:cd08217  128 GGKILHRDLKPANIFL---DSDNNVKLGDFGLARVLSHDSS------FAKTYVGTPYYMSPE--LLNEQS--YDEKSDIW 194
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036 611 SVGVIFFQCLYGRKPFghNQSQQDILQENtiLKATEVQfPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd08217  195 SLGCLIYELCALHPPF--QAANQLELAKK--IKEGKFP-RIPSRYSSELNEVIKSMLNVDPDKRPSVEELLQLPLI 265
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
419-686 5.07e-30

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: 119.63  E-value: 5.07e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAavkIHQLNKSWRDEK-KENYhkhaCREYRIHKEL-DHPRIVKLYDY-FSLDTDTFCTVLEYCEG 495
Cdd:cd14131   14 SSKVYKVLNPKKKIYA---LKRVDLEGADEQtLQSY----KNEIELLKKLkGSDRIIQLYDYeVTDEDDYLYMVMECGEI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 nDLDFYLKQH--KLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacgEIKITDFGLSKIMDDDSYGV 573
Cdd:cd14131   87 -DLATILKKKrpKPIDPNFIRYYWKQMLEAVHTIHEEG--IVHSDLKPANFLLVKG----RLKLIDFGIAKAIQNDTTSI 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 574 dgmdLTSQGAGTYWYLPPECFV------VGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQenTIL-KATE 646
Cdd:cd14131  160 ----VRDSQVGTLNYMSPEAIKdtsasgEGKPKSKIGRPSDVWSLGCILYQMVYGKTPFQHITNPIAKLQ--AIIdPNHE 233
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 211971036 647 VQFPvkPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14131  234 IEFP--DIPNPDLIDVMKRCLQRDPKKRPSIPELLNHPFL 271
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
419-686 1.07e-29

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


Pssm-ID: 270868 [Multi-domain]  Cd Length: 256  Bit Score: 118.28  E-value: 1.07e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKEnyhkhACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd08529   13 FGVVYKVVRKVDGRVYALKQIDISRMSRKMREE-----AIDEARVLSKLNSPYVIKYYDSF-VDKGKLNIVMEYAENGDL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQH--KLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsygvdgM 576
Cdd:cd08529   87 HSLIKSQrgRPLPEDQIWKFFIQTLLGLSHLHSKK--ILHRDIKSMNIFL---DKGDNVKIGDLGVAKILSDT------T 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 577 DLTSQGAGTYWYLPPE-CfvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQsqqdilQENTILKATEVQFPvkPVV 655
Cdd:cd08529  156 NFAQTIVGTPYYLSPElC-----EDKPYNEKSDVWALGCVLYELCTGKHPFEAQN------QGALILKIVRGKYP--PIS 222
                        250       260       270
                 ....*....|....*....|....*....|....
gi 211971036 656 SSEAKAF---IRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd08529  223 ASYSQDLsqlIDSCLTKDYRQRPDTTELLRNPSL 256
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
435-686 2.23e-29

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: 117.37  E-value: 2.23e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIhqLNKswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEAR 514
Cdd:cd14079   31 AVKI--LNR--QKIKSLDMEEKIRREIQILKLFRHPHIIRLYEVIETPTDIF-MVMEYVSGGELFDYIVQKGRLSEDEAR 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 515 SIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYgvdgmdL-TSQGAGTYwylppec 593
Cdd:cd14079  106 RFFQQIISGVEYCHRHM--VVHRDLKPENLLL---DSNMNVKIADFGLSNIMRDGEF------LkTSCGSPNY------- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 594 fvvgKEPPKISNK------VDVWSVGVIFFQCLYGRKPFghnqSQQDIlqENTILKATEVQFPVKPVVSSEAKAFIRRCL 667
Cdd:cd14079  168 ----AAPEVISGKlyagpeVDVWSCGVILYALLCGSLPF----DDEHI--PNLFKKIKSGIYTIPSHLSPGARDLIKRML 237
                        250
                 ....*....|....*....
gi 211971036 668 AYRKEDRFDVHQLANDPYL 686
Cdd:cd14079  238 VVDPLKRITIPEIRQHPWF 256
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
419-686 5.12e-29

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: 116.20  E-value: 5.12e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLD-TDTFCTVLEYCEGND 497
Cdd:cd14119    6 YGKVKEVLDTETLCRRAVKIL---KKRKLRRIPNGEANVKREIQILRRLNHRNVIKLVDVLYNEeKQKLYMVMEYCVGGL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLK-QHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDddSYGVDGM 576
Cdd:cd14119   83 QEMLDSaPDKRLPIWQAHGYFVQLIDGLEYLHSQG--IIHKDIKPGNLLL---TTDGTLKISDFGVAEALD--LFAEDDT 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 577 DLTSQGAGTYwylppecfvvgkEPPKISN--------KVDVWSVGVIFFQCLYGRKPF-GHNQSqqdILQENtiLKATEV 647
Cdd:cd14119  156 CTTSQGSPAF------------QPPEIANgqdsfsgfKVDIWSAGVTLYNMTTGKYPFeGDNIY---KLFEN--IGKGEY 218
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 211971036 648 QFPvkPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14119  219 TIP--DDVDPDLQDLLRGMLEKDPEKRFTIEQIRQHPWF 255
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
450-685 1.03e-28

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: 115.54  E-value: 1.03e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 450 KENYHKHAC---REYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRY 526
Cdd:cd14120   29 KKNLSKSQNllgKEIKILKELSHENVVALLDCQETSSSVY-LVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMKA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 527 LNEikPPIIHYDLKPGNILLVDGTACG------EIKITDFGLSKIMDDDSygvdgMDLTSqgAGTYWYLPPECFVvgkeP 600
Cdd:cd14120  108 LHS--KGIVHRDLKPQNILLSHNSGRKpspndiRLKIADFGFARFLQDGM-----MAATL--CGSPMYMAPEVIM----S 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 601 PKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDIlqENTILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQL 680
Cdd:cd14120  175 LQYDAKADLWSIGTIVYQCLTGKAPF-QAQTPQEL--KAFYEKNANLRPNIPSGTSPALKDLLLGLLKRNPKDRIDFEDF 251

                 ....*
gi 211971036 681 ANDPY 685
Cdd:cd14120  252 FSHPF 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
432-686 1.19e-28

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: 115.43  E-value: 1.19e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 432 RYAAVKIhqLNKswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEK 511
Cdd:cd14081   27 QKVAIKI--VNK--EKLSKESVLMKVEREIAIMKLIEHPNVLKLYDVYENKKYLY-LVLEYVSGGELFDYLVKKGRLTEK 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 512 EARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSygvdgMDLTSqgAGTYWYLPP 591
Cdd:cd14081  102 EARKFFRQIISALDYCH--SHSICHRDLKPENLLLDEK---NNIKIADFGMASLQPEGS-----LLETS--CGSPHYACP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 592 EcfVVGKEPPKiSNKVDVWSVGVIFFQCLYGRKPFGhnqsQQDIlqENTILKATEVQFPVKPVVSSEAKAFIRRCLAYRK 671
Cdd:cd14081  170 E--VIKGEKYD-GRKADIWSCGVILYALLVGALPFD----DDNL--RQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNP 240
                        250
                 ....*....|....*
gi 211971036 672 EDRFDVHQLANDPYL 686
Cdd:cd14081  241 EKRITIEEIKKHPWF 255
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
419-668 1.59e-28

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: 115.01  E-value: 1.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihQLNKS----WRDEKkenyhkHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCE 494
Cdd:cd05572    6 FGRVELVQLKSKGRTFALK--CVKKRhivqTRQQE------HIFSEKEILEECNSPFIVKLYRTFK-DKKYLYMLMEYCL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 GNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYgvd 574
Cdd:cd05572   77 GGELWTILRDRGLFDEYTARFYTACVVLAFEYLHSRG--IIYRDLKPENLLL---DSNGYVKLVDFGFAKKLGSGRK--- 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 575 gmdlTSQGAGTYWYLPPECfvvgkeppkISNK-----VDVWSVGVIFFQCLYGRKPFGHNQSQQdILQENTILKATE-VQ 648
Cdd:cd05572  149 ----TWTFCGTPEYVAPEI---------ILNKgydfsVDYWSLGILLYELLTGRPPFGGDDEDP-MKIYNIILKGIDkIE 214
                        250       260
                 ....*....|....*....|
gi 211971036 649 FPvkPVVSSEAKAFIRRCLA 668
Cdd:cd05572  215 FP--KYIDKNAKNLIKQLLR 232
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
455-686 1.82e-28

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: 114.79  E-value: 1.82e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 455 KHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPI 534
Cdd:cd14073   46 VRIRREIEIMSSLNHPHIIRIYEVFE-NKDKIVIVMEYASGGELYDYISERRRLPEREARRIFRQIVSAVHYCH--KNGV 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 535 IHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDsygvdgmDLTSQGAGTYWYLPPEcFVVGKepPKISNKVDVWSVGV 614
Cdd:cd14073  123 VHRDLKLENILLDQN---GNAKIADFGLSNLYSKD-------KLLQTFCGSPLYASPE-IVNGT--PYQGPEVDCWSLGV 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 615 IFFQCLYGRKPFG---HNQSQQDIlqentilkaTEVQF--PVKPvvsSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14073  190 LLYTLVYGTMPFDgsdFKRLVKQI---------SSGDYrePTQP---SDASGLIRWMLTVNPKRRATIEDIANHWWV 254
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
460-685 2.21e-28

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: 114.73  E-value: 2.21e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDL 539
Cdd:cd14095   48 EVAILRRVKHPNIVQLIEEYDTDTELY-LVMELVKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLS--IVHRDI 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 540 KPGNILLV---DGTACgeIKITDFGLSKIMDDDSYGVdgmdltsqgAGTYWYLPPEcfvvgkeppkISN------KVDVW 610
Cdd:cd14095  125 KPENLLVVeheDGSKS--LKLADFGLATEVKEPLFTV---------CGTPTYVAPE----------ILAetgyglKVDIW 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 611 SVGVIFFQCLYGRKPF-GHNQSQQDILQentILKATEVQFPvKPV---VSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14095  184 AAGVITYILLCGFPPFrSPDRDQEELFD---LILAGEFEFL-SPYwdnISDSAKDLISRMLVVDPEKRYSAGQVLDHPW 258
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
419-637 2.51e-28

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 114.55  E-value: 2.51e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036   419 FSEVYKAFdlYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYdYFSLDTDTFCTVLEYCEGNDL 498
Cdd:smart00219  12 FGEVYKGK--LKGKGGKKKVEVAVKTLKEDASEQQIEEFLREARIMRKLDHPNVVKLL-GVCTEEEPLYIVMEYMEGGDL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036   499 DFYLKQHKL-MSEKEARSIVMQIVNALRYLNEIkpPIIHYDLKPGNILLVDGtacGEIKITDFGLSK-IMDDDSYGVDGM 576
Cdd:smart00219  89 LSYLRKNRPkLSLSDLLSFALQIARGMEYLESK--NFIHRDLAARNCLVGEN---LVVKISDFGLSRdLYDDDYYRKRGG 163
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036   577 DLTsqgagTYWyLPPECFVVGkeppKISNKVDVWSVGViffqCLY-----GRKPFGhNQSQQDILQ 637
Cdd:smart00219 164 KLP-----IRW-MAPESLKEG----KFTSKSDVWSFGV----LLWeiftlGEQPYP-GMSNEEVLE 214
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
422-674 4.60e-28

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: 113.98  E-value: 4.60e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKIhqLNKSWRDEKK-ENYHKH-ACREYRIHKEL-DHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL 498
Cdd:cd13993   16 VYLAVDLRTGRKYAIKC--LYKSGPNSKDgNDFQKLpQLREIDLHRRVsRHPNIITLHDVFETEVAIY-IVLEYCPNGDL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 dFYL---KQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacGEIKITDFGLSkIMDDDSYGVdg 575
Cdd:cd13993   93 -FEAiteNRIYVGKTELIKNVFLQLIDAVKHCHSLG--IYHRDIKPENILLSQDE--GTVKLCDFGLA-TTEKISMDF-- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 mdltsqGAGTYWYLPPECF--VVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQENTILKATEVqFPVKP 653
Cdd:cd13993  165 ------GVGSEFYMAPECFdeVGRSLKGYPCAAGDIWSLGIILLNLTFGRNPW-KIASESDPIFYDYYLNSPNL-FDVIL 236
                        250       260
                 ....*....|....*....|.
gi 211971036 654 VVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd13993  237 PMSDDFYNLLRQIFTVNPNNR 257
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
419-674 6.24e-28

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


Pssm-ID: 462242 [Multi-domain]  Cd Length: 258  Bit Score: 113.36  E-value: 6.24e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036  419 FSEVYKA---FDLYEQRY-AAVKIhqLNKSWRDEKKENYHkhacREYRIHKELDHPRIVKLYdYFSLDTDTFCTVLEYCE 494
Cdd:pfam07714  12 FGEVYKGtlkGEGENTKIkVAVKT--LKEGADEEEREDFL----EEASIMKKLDHPNIVKLL-GVCTQGEPLYIVTEYMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036  495 GNDLDFYLKQHK-LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSK-IMDDDSYG 572
Cdd:pfam07714  85 GGDLLDFLRKHKrKLTLKDLLSMALQIAKGMEYLESKN--FVHRDLAARNCLVSEN---LVVKISDFGLSRdIYDDDYYR 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036  573 VDGMDLTSQgagtYWYlPPECFVVGkeppKISNKVDVWSVGV----IFfqcLYGRKPFGhNQSQQDILQ---ENTILKAt 645
Cdd:pfam07714 160 KRGGGKLPI----KWM-APESLKDG----KFTSKSDVWSFGVllweIF---TLGEQPYP-GMSNEEVLEfleDGYRLPQ- 225
                         250       260
                  ....*....|....*....|....*....
gi 211971036  646 evqfPvkPVVSSEAKAFIRRCLAYRKEDR 674
Cdd:pfam07714 226 ----P--ENCPDELYDLMKQCWAYDPEDR 248
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
446-686 6.25e-28

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: 113.70  E-value: 6.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 446 RDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALR 525
Cdd:cd14077   49 RLEKEISRDIRTIREAALSSLLNHPHICRLRDFLRTPNHYY-MLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 526 YLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsygvdgmDLTSQGAGTYWYLPPECFvvgKEPPKISN 605
Cdd:cd14077  128 YLH--RNSIVHRDLKIENILI---SKSGNIKIIDFGLSNLYDPR-------RLLRTFCGSLYFAAPELL---QAQPYTGP 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 606 KVDVWSVGVIFFQCLYGRKPFGHNQSQqdILQENtiLKATEVQFPvkPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14077  193 EVDVWSFGVVLYVLVCGKVPFDDENMP--ALHAK--IKKGKVEYP--SYLSSECKSLISRMLVVDPKKRATLEQVLNHPW 266

                 .
gi 211971036 686 L 686
Cdd:cd14077  267 M 267
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
419-684 7.48e-28

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: 112.87  E-value: 7.48e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnKSWRDEKKENyhkhACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd08530   13 YGSVYKVKRLSDNQVYALKEVNL-GSLSQKERED----SVNEIRLLASVNHPNIIRYKEAF-LDGNRLCIVMEYAPFGDL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYL----KQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDdsygvd 574
Cdd:cd08530   87 SKLIskrkKKRRLFPEDDIWRIFIQMLRGLKALHDQK--ILHRDLKSANILLSAG---DLVKIGDLGISKVLKK------ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 575 gmDLTSQGAGTYWYLPPEcfvVGKEPPkISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQentilKATEVQFP-VKP 653
Cdd:cd08530  156 --NLAKTQIGTPLYAAPE---VWKGRP-YDYKSDIWSLGCLLYEMATFRPPF-EARTMQELRY-----KVCRGKFPpIPP 223
                        250       260       270
                 ....*....|....*....|....*....|.
gi 211971036 654 VVSSEAKAFIRRCLAYRKEDRFDVHQLANDP 684
Cdd:cd08530  224 VYSQDLQQIIRSLLQVNPKKRPSCDKLLQSP 254
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
419-700 1.20e-27

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: 113.29  E-value: 1.20e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNK-SWRDEKKENyhkhacREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGND 497
Cdd:cd14086   14 FSVVRRCVQKSTGQEFAAKIINTKKlSARDHQKLE------REARICRLLKHPNIVRLHDSIS-EEGFHYLVFDLVTGGE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSYGVDGMd 577
Cdd:cd14086   87 LFEDIVAREFYSEADASHCIQQILESVNHCHQNG--IVHRDLKPENLLLASKSKGAAVKLADFGLAIEVQGDQQAWFGF- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 ltsqgAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntiLKATEVQFPvKP---V 654
Cdd:cd14086  164 -----AGTPGYLSPE--VLRKDP--YGKPVDIWACGVILYILLVGYPPF-WDEDQHRLYAQ---IKAGAYDYP-SPewdT 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 211971036 655 VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLphmRRSNSSGNLH 700
Cdd:cd14086  230 VTPEAKDLINQMLTVNPAKRITAAEALKHPWIC---QRDRVASMVH 272
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
418-685 1.26e-27

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: 112.47  E-value: 1.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 418 GFSEVYKAFDLYEQRYAAVK-IHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGN 496
Cdd:cd14083   15 AFSEVVLAEDKATGKLVAIKcIDKKALKGKEDSLEN-------EIAVLRKIKHPNIVQLLDIYE-SKSHLYLVMELVTGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 497 DLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDddsygvDGM 576
Cdd:cd14083   87 ELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLG--IVHRDLKPENLLYYSPDEDSKIMISDFGLSKMED------SGV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 577 dlTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntILKAtEVQF--PVKPV 654
Cdd:cd14083  159 --MSTACGTPGYVAPE--VLAQKP--YGKAVDCWSIGVISYILLCGYPPF-YDENDSKLFAQ--ILKA-EYEFdsPYWDD 228
                        250       260       270
                 ....*....|....*....|....*....|.
gi 211971036 655 VSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14083  229 ISDSAKDFIRHLMEKDPNKRYTCEQALEHPW 259
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
422-689 2.10e-27

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: 112.05  E-value: 2.10e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKIHQLNKswrDEKKEnyhKHACREYRIHKELDHPRIVKLYDYFSLDTDTF-CtvLEYCEGNDLDF 500
Cdd:cd06605   17 VSKVRHRPSGQIMAVKVIRLEI---DEALQ---KQILRELDVLHKCNSPYIVGFYGAFYSEGDISiC--MEYMDGGSLDK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 501 YLKQHKLMSEKEARSIVMQIVNALRYLNEiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMdddsygVDGMDLTS 580
Cdd:cd06605   89 ILKEVGRIPERILGKIAVAVVKGLIYLHE-KHKIIHRDVKPSNILV---NSRGQVKLCDFGVSGQL------VDSLAKTF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 581 qgAGTYWYLPPECFVvgkePPKISNKVDVWSVGVIFFQCLYGRKPF---GHNQSQQDILQENTILKATEVQFPVKPvVSS 657
Cdd:cd06605  159 --VGTRSYMAPERIS----GGKYTVKSDIWSLGLSLVELATGRFPYpppNAKPSMMIFELLSYIVDEPPPLLPSGK-FSP 231
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 658 EAKAFIRRCLAYRKEDRFDVHQLANDPYLLPH 689
Cdd:cd06605  232 DFQDFVSQCLQKDPTERPSYKELMEHPFIKRY 263
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
459-686 2.28e-27

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: 111.49  E-value: 2.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLDTDTFCTVLEYCEgNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYD 538
Cdd:cd14164   49 RELSILRRVNHPNIVQMFECIEVANGRLYIVMEAAA-TDLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMN--IVHRD 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLvdgTACGE-IKITDFGLSKIMDDDSygvdgmDLTSQGAGTYWYLPPECFVVGKEPPKisnKVDVWSVGVIFF 617
Cdd:cd14164  126 LKCENILL---SADDRkIKIADFGFARFVEDYP------ELSTTFCGSRAYTPPEVILGTPYDPK---KYDVWSLGVVLY 193
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 618 QCLYGRKPFGHNQSQQDILQENTILkatevqFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14164  194 VMVTGTMPFDETNVRRLRLQQRGVL------YPSGVALEEPCRALIRTLLQFNPSTRPSIQQVAGNSWL 256
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
419-686 3.79e-27

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: 111.32  E-value: 3.79e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNK--SWRDEKKENYHKHACR-EYRIHKELDHPRIVKlYDYFSLDTDTFCTVLEYCEG 495
Cdd:cd06629   14 YGRVYLAMNATTGEMLAVKQVELPKtsSDRADSRQKTVVDALKsEIDTLKDLDHPNIVQ-YLGFEETEDYFSIFLEYVPG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 NDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACgeiKITDFGLSKiMDDDSYGVDG 575
Cdd:cd06629   93 GSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLH--SKGILHRDLKADNILVDLEGIC---KISDFGISK-KSDDIYGNNG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 mDLTSQGagTYWYLPPEcfVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATevqfPVKP-- 653
Cdd:cd06629  167 -ATSMQG--SVFWMAPE--VIHSQGQGYSAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAP----PVPEdv 237
                        250       260       270
                 ....*....|....*....|....*....|...
gi 211971036 654 VVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06629  238 NLSPEALDFLNACFAIDPRDRPTAAELLSHPFL 270
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
419-685 4.52e-27

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: 110.57  E-value: 4.52e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSwrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL 498
Cdd:cd14663   13 FAKVKFARNTKTGESVAIKI--IDKE--QVAREGMVEQIKREIAIMKLLRHPNIVELHEVMATKTKIF-FVMELVTGGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDddsyGVDGMDL 578
Cdd:cd14663   88 FSKIAKNGRLKEDKARKYFQQLIDAVDYCH--SRGVFHRDLKPENLLL---DEDGNLKISDFGLSALSE----QFRQDGL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPECFvvgKEPPKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQentilKATEVQFPVKPVVSSE 658
Cdd:cd14663  159 LHTTCGTPNYVAPEVL---ARRGYDGAKADIWSCGVILFVLLAGYLPF-DDENLMALYR-----KIMKGEFEYPRWFSPG 229
                        250       260
                 ....*....|....*....|....*..
gi 211971036 659 AKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14663  230 AKSLIKRILDPNPSTRITVEQIMASPW 256
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
419-686 4.63e-27

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: 111.62  E-value: 4.63e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL 498
Cdd:cd14166   16 FSEVYLVKQRSTGKLYALKCIKKSPLSRDSSLEN-------EIAVLKRIKHENIVTLEDIYE-STTHYYLVMQLVSGGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDdsygvdgmDL 578
Cdd:cd14166   88 FDRILERGVYTEKDASRVINQVLSAVKYLHE--NGIVHRDLKPENLLYLTPDENSKIMITDFGLSKMEQN--------GI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFghNQSQQDILQENTILKATEVQFPVKPVVSSE 658
Cdd:cd14166  158 MSTACGTPGYVAPE--VLAQKP--YSKAVDCWSIGVITYILLCGYPPF--YEETESRLFEKIKEGYYEFESPFWDDISES 231
                        250       260
                 ....*....|....*....|....*...
gi 211971036 659 AKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14166  232 AKDFIRHLLEKNPSKRYTCEKALSHPWI 259
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
459-686 4.89e-27

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: 110.87  E-value: 4.89e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYD 538
Cdd:cd14202   50 KEIKILKELKHENIVALYDFQEIANSVY-LVMEYCNGGDLADYLHTMRTLSEDTIRLFLQQIAGAMKMLHS--KGIIHRD 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLVDGTACGE------IKITDFGLSKIMDDDSygvdgmdLTSQGAGTYWYLPPECFVvgkePPKISNKVDVWSV 612
Cdd:cd14202  127 LKPQNILLSYSGGRKSnpnnirIKIADFGFARYLQNNM-------MAATLCGSPMYMAPEVIM----SQHYDAKADLWSI 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 613 GVIFFQCLYGRKPFgHNQSQQDILQentilkATEVQFPVKPVVSSEAKAFIRR----CLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14202  196 GTIIYQCLTGKAPF-QASSPQDLRL------FYEKNKSLSPNIPRETSSHLRQlllgLLQRNQKDRMDFDEFFHHPFL 266
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
459-685 5.45e-27

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: 110.91  E-value: 5.45e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYfsLD---TDTFCTVLEYCEGNDLdFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppII 535
Cdd:cd14118   63 REIAILKKLDHPNVVKLVEV--LDdpnEDNLYMVFELVDKGAV-MEVPTDNPLSEETARSYFRDIVLGIEYLHYQK--II 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 536 HYDLKPGNILLVDGtacGEIKITDFGLSkimdDDSYGVDgmDLTSQGAGTYWYLPPECFVVGKEppKISNK-VDVWSVGV 614
Cdd:cd14118  138 HRDIKPSNLLLGDD---GHVKIADFGVS----NEFEGDD--ALLSSTAGTPAFMAPEALSESRK--KFSGKaLDIWAMGV 206
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 615 IFFQCLYGRKPFghnqSQQDILQENTILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14118  207 TLYCFVFGRCPF----EDDHILGLHEKIKTDPVVFPDDPVVSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
419-674 5.99e-27

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: 110.71  E-value: 5.99e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKA--FDLYEQRYA-AVKIHQLNKSwRDEKKEnyhkhACREYRIHKELDHPRIVKLYDYfSLDTDTFCTVLEYCEG 495
Cdd:cd00192    8 FGEVYKGklKGGDGKTVDvAVKTLKEDAS-ESERKD-----FLKEARVMKKLGHPNVVRLLGV-CTEEEPLYLVMEYMEG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 NDLDFYLKQHKL---------MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIM 566
Cdd:cd00192   81 GDLLDFLRKSRPvfpspepstLSLKDLLSFAIQIAKGMEYLASKK--FVHRDLAARNCLVGED---LVVKISDFGLSRDI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 567 DDDSYGVDGmdlTSQGAGTYWyLPPECFVVGkeppKISNKVDVWSVGVIFFQCL-YGRKPFGhNQSQQDILQenTILKAT 645
Cdd:cd00192  156 YDDDYYRKK---TGGKLPIRW-MAPESLKDG----IFTSKSDVWSFGVLLWEIFtLGATPYP-GLSNEEVLE--YLRKGY 224
                        250       260
                 ....*....|....*....|....*....
gi 211971036 646 EVQFPvkPVVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd00192  225 RLPKP--ENCPDELYELMLSCWQLDPEDR 251
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
419-637 7.82e-27

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: 109.95  E-value: 7.82e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036   419 FSEVYKAF----DLYEQRYAAVKIHQLNKSwrDEKKENYhkhaCREYRIHKELDHPRIVKLYdYFSLDTDTFCTVLEYCE 494
Cdd:smart00221  12 FGEVYKGTlkgkGDGKEVEVAVKTLKEDAS--EQQIEEF----LREARIMRKLDHPNIVKLL-GVCTEEEPLMIVMEYMP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036   495 GNDLDFYLKQHK--LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSK-IMDDDSY 571
Cdd:smart00221  85 GGDLLDYLRKNRpkELSLSDLLSFALQIARGMEYLESKN--FIHRDLAARNCLVGEN---LVVKISDFGLSRdLYDDDYY 159
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036   572 GVDGMDLTsqgagTYWyLPPECFVVGkeppKISNKVDVWSVGViffqCLY-----GRKPFGhNQSQQDILQ 637
Cdd:smart00221 160 KVKGGKLP-----IRW-MAPESLKEG----KFTSKSDVWSFGV----LLWeiftlGEEPYP-GMSNAEVLE 215
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
435-686 9.01e-27

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: 109.81  E-value: 9.01e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIhqLNKSWRDEKKEnyhKHACREYRIHKELDHPRIVKLYDYfsLDTDT-FCTVLEYCEGNDL-DFYLKQHKLMSEKE 512
Cdd:cd14074   32 AVKV--IDKTKLDDVSK---AHLFQEVRCMKLVQHPNVVRLYEV--IDTQTkLYLILELGDGGDMyDYIMKHENGLNEDL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 513 ARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacGEIKITDFGLSkimddDSYGVDGMDLTSqgAGTYWYLPPE 592
Cdd:cd14074  105 ARKYFRQIVSAISYCHKLH--VVHRDLKPENVVFFEKQ--GLVKLTDFGFS-----NKFQPGEKLETS--CGSLAYSAPE 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 593 cFVVGKE--PPKisnkVDVWSVGVIFFQCLYGRKPFghnQSQQDilqENTILKATEVQFPVKPVVSSEAKAFIRRCLAYR 670
Cdd:cd14074  174 -ILLGDEydAPA----VDIWSLGVILYMLVCGQPPF---QEAND---SETLTMIMDCKYTVPAHVSPECKDLIRRMLIRD 242
                        250
                 ....*....|....*.
gi 211971036 671 KEDRFDVHQLANDPYL 686
Cdd:cd14074  243 PKKRASLEEIENHPWL 258
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
469-686 9.81e-27

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: 110.14  E-value: 9.81e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFslDTDTFC-TVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLV 547
Cdd:cd14093   68 HPNIIELHDVF--ESPTFIfLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLN--IVHRDLKPENILLD 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 548 DGtacGEIKITDFGLSKIMDDDSYgvdgmdlTSQGAGTYWYLPPECFVVGKEP--PKISNKVDVWSVGVIFFQCLYGRKP 625
Cdd:cd14093  144 DN---LNVKISDFGFATRLDEGEK-------LRELCGTPGYLAPEVLKCSMYDnaPGYGKEVDMWACGVIMYTLLAGCPP 213
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 626 FGHNqsQQDILQENTILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14093  214 FWHR--KQMVMLRNIMEGKYEFGSPEWDDISDTAKDLISKLLVVDPKKRLTAEEALEHPFF 272
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
407-686 1.11e-26

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: 109.82  E-value: 1.11e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 407 RYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTF 486
Cdd:cd08222    1 RYRVVRKLGSGNFGTVYLVSDLKATADEELKV--LKEISVGELQPDETVDANREAKLLSKLDHPAIVKFHDSF-VEKESF 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 487 CTVLEYCEGNDLDFYLKQHKLMSEKEARSIVM----QIVNALRYLNEIKppIIHYDLKPGNILLVDGTacgeIKITDFGL 562
Cdd:cd08222   78 CIVTEYCEGGDLDDKISEYKKSGTTIDENQILdwfiQLLLAVQYMHERR--ILHRDLKAKNIFLKNNV----IKVGDFGI 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 563 SKIMDDDSygvdgmDLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQ--CLygrkpfGHNQSQQDILqeNT 640
Cdd:cd08222  152 SRILMGTS------DLATTFTGTPYYMSPEVL----KHEGYNSKSDIWSLGCILYEmcCL------KHAFDGQNLL--SV 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 211971036 641 ILKATEVQFPVKP-VVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd08222  214 MYKIVEGETPSLPdKYSKELNAIYSRMLNKDPALRPSAAEILKIPFI 260
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
431-686 1.19e-26

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. It is Ca2+/calmodulin (CaM)-regulated and actin-associated protein that contains an N-terminal kinase domain followed by an autoinhibitory CaM binding region and a large C-terminal extension with multiple functional domains including ankyrin (ANK) repeats, a cytoskeletal binding domain, a Death domain, and a serine-rich tail. Loss of DAPK1 expression, usually because of DNA methylation, is implicated in many tumor types. DAPK1 is highly abundant in the brain and has also been associated with neurodegeneration. The DAPK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271096 [Multi-domain]  Cd Length: 269  Bit Score: 110.11  E-value: 1.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 431 QRYAA--VKIHQLNKSWRDEKKENYHkhacREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLM 508
Cdd:cd14194   31 LQYAAkfIKKRRTKSSRRGVSREDIE----REVSILKEIQHPNVITLHEVYENKTDVI-LILELVAGGELFDFLAEKESL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 509 SEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACG-EIKITDFGLSKIMDddsYGVDGMDLTsqgaGTYW 587
Cdd:cd14194  106 TEEEATEFLKQILNGVYYLHSLQ--IAHFDLKPENIMLLDRNVPKpRIKIIDFGLAHKID---FGNEFKNIF----GTPE 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 588 YLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQFPVKpvVSSEAKAFIRRCL 667
Cdd:cd14194  177 FVAPE--IVNYEP--LGLEADMWSIGVITYILLSGASPFLGDTKQETLANVSAVNYEFEDEYFSN--TSALAKDFIRRLL 250
                        250
                 ....*....|....*....
gi 211971036 668 AYRKEDRFDVHQLANDPYL 686
Cdd:cd14194  251 VKDPKKRMTIQDSLQHPWI 269
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
419-686 1.26e-26

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: 109.73  E-value: 1.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVK-IHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGND 497
Cdd:cd14167   16 FSEVVLAEEKRTQKLVAIKcIAKKALEGKETSIEN-------EIAVLHKIKHPNIVALDDIYESGGHLY-LIMQLVSGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSygvdgmd 577
Cdd:cd14167   88 LFDRIVEKGFYTERDASKLIFQILDAVKYLHDMG--IVHRDLKPENLLYYSLDEDSKIMISDFGLSKIEGSGS------- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntILKAtEVQF--PVKPVV 655
Cdd:cd14167  159 VMSTACGTPGYVAPE--VLAQKP--YSKAVDCWSIGVIAYILLCGYPPF-YDENDAKLFEQ--ILKA-EYEFdsPYWDDI 230
                        250       260       270
                 ....*....|....*....|....*....|.
gi 211971036 656 SSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14167  231 SDSAKDFIQHLMEKDPEKRFTCEQALQHPWI 261
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
419-681 1.53e-26

Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases and related STKs; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. Some IRAKs may also play roles in T- and B-cell signaling, and adaptive immunity. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK-1, -2, and -4 are ubiquitously expressed and are active kinases, while IRAK-M is only induced in monocytes and macrophages and is an inactive kinase. Variations in IRAK genes are linked to diverse diseases including infection, sepsis, cancer, and autoimmune diseases. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase domain in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. This subfamily includes plant receptor-like kinases (RLKs) including Arabidopsis thaliana BAK1 and CLAVATA1 (CLV1). BAK1 functions in BR (brassinosteroid)-regulated plant development and in pathways involved in plant resistance to pathogen infection and herbivore attack. CLV1, directly binds small signaling peptides, CLAVATA3 (CLV3) and CLAVATA3/EMBRYO SURROUNDING REGI0N (CLE), to restrict stem cell proliferation: the CLV3-CLV1-WUS (WUSCHEL) module influences stem cell maintenance in the shoot apical meristem, and the CLE40 (CLAVATA3/EMBRYO SURROUNDING REGION40) -ACR4 (CRINKLY4) -CLV1- WOX5 (WUSCHEL-RELATED HOMEOBOX5) module at the root apical meristem. The IRAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270968 [Multi-domain]  Cd Length: 272  Bit Score: 109.67  E-value: 1.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFdLYEQRYAAVKIhqlnksWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd14066    6 FGTVYKGV-LENGTVVAVKR------LNEMNCAASKKEFLTELEMLGRLRHPNLVRLLGYC-LESDEKLLVYEYMPNGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKlmSEK----EAR-SIVMQIVNALRYLN-EIKPPIIHYDLKPGNILLVDgtaCGEIKITDFGLSKIMDDDsyg 572
Cdd:cd14066   78 EDRLHCHK--GSPplpwPQRlKIAKGIARGLEYLHeECPPPIIHGDIKSSNILLDE---DFEPKLTDFGLARLIPPS--- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 573 vDGMDLTSQGAGTYWYLPPEcFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQ------DILQENTILKATE 646
Cdd:cd14066  150 -ESVSKTSAVKGTIGYLAPE-YIRTG---RVSTKSDVYSFGVVLLELLTGKPAVDENRENAsrkdlvEWVESKGKEELED 224
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 211971036 647 V--QFPVKPVVS--SEAKAFIR---RCLAYRKEDRFDVHQLA 681
Cdd:cd14066  225 IldKRLVDDDGVeeEEVEALLRlalLCTRSDPSLRPSMKEVV 266
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
419-685 2.85e-26

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: 109.58  E-value: 2.85e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCEGnDL 498
Cdd:cd07841   13 YAVVYKARDKETGRIVAIKKIKLGE--RKEAKDGINFTALREIKLLQELKHPNIIGLLDVFGHK-SNINLVFEFMET-DL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKL-MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddSYGVDGMD 577
Cdd:cd07841   89 EKVIKDKSIvLTPADIKSYMLMTLRGLEYLHSNW--ILHRDLKPNNLLI---ASDGVLKLADFGLAR-----SFGSPNRK 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQgAGTYWYLPPECFVVGKeppKISNKVDVWSVGVIFFQCLYgRKPFghNQSQQDILQENTILKA----TE------- 646
Cdd:cd07841  159 MTHQ-VVTRWYRAPELLFGAR---HYGVGVDMWSVGCIFAELLL-RVPF--LPGDSDIDQLGKIFEAlgtpTEenwpgvt 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 211971036 647 -----VQF------PVK---PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd07841  232 slpdyVEFkpfpptPLKqifPAASDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
422-686 5.61e-26

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: 109.54  E-value: 5.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKihQLNKSWRDEKkenYHKHACREYRIHKELDHPRIVKLYDYF-SLDTDTFCT---VLEYCEgND 497
Cdd:cd07834   16 VCSAYDKRTGRKVAIK--KISNVFDDLI---DAKRILREIKILRHLKHENIIGLLDILrPPSPEEFNDvyiVTELME-TD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdGTACgEIKITDFGLSKIMDDDSygvDGMD 577
Cdd:cd07834   90 LHKVIKSPQPLTDDHIQYFLYQILRGLKYLHSAG--VIHRDLKPSNILV--NSNC-DLKICDFGLARGVDPDE---DKGF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTsQGAGTYWYLPPECFVVGKeppKISNKVDVWSVGVIFFQCLyGRKPF--GH---NQ-----------SQQDILQENTi 641
Cdd:cd07834  162 LT-EYVVTRWYRAPELLLSSK---KYTKAIDIWSVGCIFAELL-TRKPLfpGRdyiDQlnlivevlgtpSEEDLKFISS- 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036 642 LKATE--VQFPVK---------PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd07834  236 EKARNylKSLPKKpkkplsevfPGASPEAIDLLEKMLVFNPKKRITADEALAHPYL 291
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
431-667 6.30e-26

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: 108.44  E-value: 6.30e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 431 QRYAAVKIhqLNKSWRDEKKENyhKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSE 510
Cdd:cd05580   26 GKYYALKI--LKKAKIIKLKQV--EHVLNEKRILSEVRHPFIVNLLGSFQ-DDRNLYMVMEYVPGGELFSLLRRSGRFPN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 511 KEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGVdgmdltsqgAGTYWYLP 590
Cdd:cd05580  101 DVAKFYAAEVVLALEYLHSLD--IVYRDLKPENLLL---DSDGHIKITDFGFAKRVKDRTYTL---------CGTPEYLA 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 591 PECfvvgkeppkISNK-----VDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntILKAtEVQFPVKpvVSSEAKAFIRR 665
Cdd:cd05580  167 PEI---------ILSKghgkaVDWWALGILIYEMLAGYPPF-FDENPMKIYEK--ILEG-KIRFPSF--FDPDAKDLIKR 231

                 ..
gi 211971036 666 CL 667
Cdd:cd05580  232 LL 233
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
422-686 6.83e-26

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: 108.13  E-value: 6.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVK-IHQLNkswrDEkkENYHKHACREYRIHKELD---HPRIVKLYDYFS---LDTDTFCT-VLEYC 493
Cdd:cd07838   15 VYKARDLQDGRFVALKkVRVPL----SE--EGIPLSTIREIALLKQLEsfeHPNVVRLLDVCHgprTDRELKLTlVFEHV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 494 EgNDLDFYLKQH--KLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsy 571
Cdd:cd07838   89 D-QDLATYLDKCpkPGLPPETIKDLMRQLLRGLDFLHSHR--IVHRDLKPQNILV---TSDGQVKLADFGLARIYSFE-- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 572 gvdgMDLTSQGAgTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFFQcLYGRKPFGHNQSQQDILQE--NTILKATEVQF 649
Cdd:cd07838  161 ----MALTSVVV-TLWYRAPE--VLLQSSYATP--VDMWSVGCIFAE-LFNRRPLFRGSSEADQLGKifDVIGLPSEEEW 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 650 PVK--------------------PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd07838  231 PRNsalprssfpsytprpfksfvPEIDEEGLDLLKKMLTFNPHKRISAFEALQHPYF 287
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
419-686 7.53e-26

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: 107.31  E-value: 7.53e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKEnyhkhaCR-EYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGND 497
Cdd:cd06627   13 FGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKS------VMgEIDLLKKLNHPNIVKYIGSV-KTKDSLYIILEYVENGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDdsygVDGMD 577
Cdd:cd06627   86 LASIIKKFGKFPESLVAVYIYQVLEGLAYLHEQG--VIHRDIKGANILT---TKDGLVKLADFGVATKLNE----VEKDE 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQGAgTYWyLPPEcfVVGKEPPkiSNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntILKATEVQFPvkPVVSS 657
Cdd:cd06627  157 NSVVGT-PYW-MAPE--VIEMSGV--TTASDIWSVGCTVIELLTGNPPY-YDLQPMAALFR--IVQDDHPPLP--ENISP 225
                        250       260
                 ....*....|....*....|....*....
gi 211971036 658 EAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06627  226 ELRDFLLQCFQKDPTLRPSAKELLKHPWL 254
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
450-683 9.40e-26

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: 108.48  E-value: 9.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 450 KENYHKHACREYRIHKELDHPRIVKLydYFSLDTDTF-CTVLEYCEGNDLdFYLKQ---HKLMSEKEARSIVMQIVNALR 525
Cdd:cd05574   41 KRNKVKRVLTEREILATLDHPFLPTL--YASFQTSTHlCFVMDYCPGGEL-FRLLQkqpGKRLPEEVARFYAAEVLLALE 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 526 YLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSK--------IMDDDSYGVDGMDL---------TSQGA----- 583
Cdd:cd05574  118 YLHLLG--FVYRDLKPENILL---HESGHIMLTDFDLSKqssvtpppVRKSLRKGSRRSSVksieketfvAEPSArsnsf 192
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 584 -GTYWYLPPECFV-VGKeppkiSNKVDVWSVGVIFFQCLYGRKPF-GHNQsqqdilQE--NTILKAtEVQFPVKPVVSSE 658
Cdd:cd05574  193 vGTEEYIAPEVIKgDGH-----GSAVDWWTLGILLYEMLYGTTPFkGSNR------DEtfSNILKK-ELTFPESPPVSSE 260
                        250       260
                 ....*....|....*....|....*
gi 211971036 659 AKAFIRRCLAYRKEDRFDVHQLAND 683
Cdd:cd05574  261 AKDLIRKLLVKDPSKRLGSKRGASE 285
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
459-686 9.88e-26

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: 107.40  E-value: 9.88e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYD 538
Cdd:cd14201   54 KEIKILKELQHENIVALYDVQEMPNSVF-LVMEYCNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHS--KGIIHRD 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLV-----DGTACG-EIKITDFGLSKIMDDDSygvdgmdLTSQGAGTYWYLPPECFVvgkePPKISNKVDVWSV 612
Cdd:cd14201  131 LKPQNILLSyasrkKSSVSGiRIKIADFGFARYLQSNM-------MAATLCGSPMYMAPEVIM----SQHYDAKADLWSI 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 613 GVIFFQCLYGRKPFGHNqSQQDI---LQENTILkatevqfpvKPVVSSEAKAFIRR----CLAYRKEDRFDVHQLANDPY 685
Cdd:cd14201  200 GTVIYQCLVGKPPFQAN-SPQDLrmfYEKNKNL---------QPSIPRETSPYLADlllgLLQRNQKDRMDFEAFFSHPF 269

                 .
gi 211971036 686 L 686
Cdd:cd14201  270 L 270
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
419-686 1.38e-25

Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MARKs, also called Partitioning-defective 1 (Par1) proteins, function as regulators of diverse cellular processes in nematodes, Drosophila, yeast, and vertebrates. They are involved in embryogenesis, epithelial cell polarization, cell signaling, and neuronal differentiation. MARKs phosphorylate tau and related microtubule-associated proteins (MAPs), and regulates microtubule-based intracellular transport. Vertebrates contain four isoforms, namely MARK1 (or Par1c), MARK2 (or Par1b), MARK3 (Par1a), and MARK4 (or MARKL1). Known substrates of MARKs include the cell cycle-regulating phosphatase Cdc25, tyrosine phosphatase PTPH1, MAPK scaffolding protein KSR1, class IIa histone deacetylases, and plakophilin 2. The MARK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270974 [Multi-domain]  Cd Length: 253  Bit Score: 106.45  E-value: 1.38e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKI---HQLNKSWRDEkkenyhkhACREYRIHKELDHPRIVKLYDYFSLDTdTFCTVLEYCEG 495
Cdd:cd14072   13 FAKVKLARHVLTGREVAIKIidkTQLNPSSLQK--------LFREVRIMKILNHPNIVKLFEVIETEK-TLYLVMEYASG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 NDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvDGTAcgEIKITDFGLSKIMdddsygVDG 575
Cdd:cd14072   84 GEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKR--IVHRDLKAENLLL-DADM--NIKIADFGFSNEF------TPG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 MDLTSqGAGTYWYLPPECFvVGKE---PpkisnKVDVWSVGVIFFQCLYGRKPF-GHNQSQqdiLQENTILKATEVQFpv 651
Cdd:cd14072  153 NKLDT-FCGSPPYAAPELF-QGKKydgP-----EVDVWSLGVILYTLVSGSLPFdGQNLKE---LRERVLRGKYRIPF-- 220
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 211971036 652 kpVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14072  221 --YMSTDCENLLKKFLVLNPSKRGTLEQIMKDRWM 253
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
459-686 1.53e-25

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: 106.58  E-value: 1.53e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYD 538
Cdd:cd14116   54 REVEIQSHLRHPNILRLYGYFH-DATRVYLILEYAPLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKR--VIHRD 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLvdgTACGEIKITDFGLSKIMDDDSygvdgmdlTSQGAGTYWYLPPEcFVVGKEPpkiSNKVDVWSVGVIFFQ 618
Cdd:cd14116  131 IKPENLLL---GSAGELKIADFGWSVHAPSSR--------RTTLCGTLDYLPPE-MIEGRMH---DEKVDLWSLGVLCYE 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 619 CLYGRKPFGHNQSQQdilqenTILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14116  196 FLVGKPPFEANTYQE------TYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQRPMLREVLEHPWI 257
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
419-682 1.72e-25

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: 106.65  E-value: 1.72e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKswrdekkENYHKHACREYRIHKEL-DHPRIVKLYDYFSLDTDT---FCTVLEYCE 494
Cdd:cd13985   13 FSYVYLAHDVNTGRRYALKRMYFND-------EEQLRVAIKEIEIMKRLcGHPNIVQYYDSAILSSEGrkeVLLLMEYCP 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 GNDLDFYLKQHKL-MSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTACgeiKITDFGlSKIMDDDSYgv 573
Cdd:cd13985   86 GSLVDILEKSPPSpLSEEEVLRIFYQICQAVGHLHSQSPPIIHRDIKIENILFSNTGRF---KLCDFG-SATTEHYPL-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 574 dgmdLTSQGAGTY----------WYLPPECF-VVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFghnqsqqdilQENTIL 642
Cdd:cd13985  160 ----ERAEEVNIIeeeiqknttpMYRAPEMIdLYSKKP--IGEKADIWALGCLLYKLCFFKLPF----------DESSKL 223
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 211971036 643 KATEVQFPVK--PVVSSEAKAFIRRCLAYRKEDRFDVHQLAN 682
Cdd:cd13985  224 AIVAGKYSIPeqPRYSPELHDLIRHMLTPDPAERPDIFQVIN 265
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
433-686 1.81e-25

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK2, also called DAPK-related protein 1 (DRP-1), is a Ca2+/calmodulin (CaM)-regulated protein containing an N-terminal kinase domain, a CaM autoinhibitory site and a dimerization module. It lacks the cytoskeletal binding regions of DAPK1 and the exogenous protein has been shown to be soluble and cytoplasmic. FLAG-tagged DAPK2, however, accumulated within membrane-enclosed autophagic vesicles. It is unclear where endogenous DAPK2 is localized. DAPK2 participates in TNF-alpha and FAS-receptor induced cell death and enhances neutrophilic maturation in myeloid leukemic cells. It contributes to the induction of anoikis and its down-regulation is implicated in the beta-catenin induced resistance of malignant epithelial cells to anoikis. The DAPK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271098 [Multi-domain]  Cd Length: 269  Bit Score: 106.58  E-value: 1.81e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 433 YAA--VKIHQLNKSWRDEKKENYHkhacREYRIHKELDHPRIVKLYDYFSLDTDTfCTVLEYCEGNDLDFYLKQHKLMSE 510
Cdd:cd14196   33 YAAkfIKKRQSRASRRGVSREEIE----REVSILRQVLHPNIITLHDVYENRTDV-VLILELVSGGELFDFLAQKESLSE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 511 KEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTA-CGEIKITDFGLSKIMDDdsyGVDGMDLTsqgaGTYWYL 589
Cdd:cd14196  108 EEATSFIKQILDGVNYLHTKK--IAHFDLKPENIMLLDKNIpIPHIKLIDFGLAHEIED---GVEFKNIF----GTPEFV 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 590 PPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQENTilkATEVQFPVK--PVVSSEAKAFIRRCL 667
Cdd:cd14196  179 APE--IVNYEP--LGLEADMWSIGVITYILLSGASPF-LGDTKQETLANIT---AVSYDFDEEffSHTSELAKDFIRKLL 250
                        250
                 ....*....|....*....
gi 211971036 668 AYRKEDRFDVHQLANDPYL 686
Cdd:cd14196  251 VKETRKRLTIQEALRHPWI 269
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
419-686 2.36e-25

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: 105.78  E-value: 2.36e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKI--HQLNKSW------RDEKKENYHKHACReyrihkELDHPRIVKLYDYFSlDTDTFCTVL 490
Cdd:cd14005   13 FGTVYSGVRIRDGLPVAVKFvpKSRVTEWamingpVPVPLEIALLLKAS------KPGVPGVIRLLDWYE-RPDGFLLIM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 491 EYCEG-NDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacGEIKITDFGLSKIMDDD 569
Cdd:cd14005   86 ERPEPcQDLFDFITERGALSENLARIIFRQVVEAVRHCHQRG--VLHRDIKDENLLINLRT--GEVKLIDFGCGALLKDS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 570 SYGvdgmdlTSQGAGTYWylPPECFVVGKEPPkisNKVDVWSVGVIFFQCLYGRKPFgHNQSQqdilqentILKATeVQF 649
Cdd:cd14005  162 VYT------DFDGTRVYS--PPEWIRHGRYHG---RPATVWSLGILLYDMLCGDIPF-ENDEQ--------ILRGN-VLF 220
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 211971036 650 pvKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14005  221 --RPRLSKECCDLISRCLQFDPSKRPSLEQILSHPWF 255
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
433-629 2.91e-25

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: 106.38  E-value: 2.91e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 433 YAAVKIHQLNKSWRDEKKENYhkhaCREYRIHKELDHPRIVKLYD-----YFSLDTDTFCTVLEYCEGNDLDFYLKQHKL 507
Cdd:cd13989   20 YVAIKKCRQELSPSDKNRERW----CLEVQIMKKLNHPNVVSARDvppelEKLSPNDLPLLAMEYCSGGDLRKVLNQPEN 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 508 ---MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacGEI--KITDFGLSKIMDDDSygvdgmdLTSQG 582
Cdd:cd13989   96 ccgLKESEVRTLLSDISSAISYLHENR--IIHRDLKPENIVLQQGG--GRViyKLIDLGYAKELDQGS-------LCTSF 164
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 211971036 583 AGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFGHN 629
Cdd:cd13989  165 VGTLQYLAPELF----ESKKYTCTVDYWSFGTLAFECITGYRPFLPN 207
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
469-693 3.02e-25

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: 107.00  E-value: 3.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFSldtDTFCT--VLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILL 546
Cdd:cd14092   58 HPNIVKLHEVFQ---DELHTylVMELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKG--VVHRDLKPENLLF 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 547 VDGTACGEIKITDFGLSKIMDDdsygvdgMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd14092  133 TDEDDDAEIKIVDFGFARLKPE-------NQPLKTPCFTLPYAAPEVLKQALSTQGYDESCDLWSLGVILYTMLSGQVPF 205
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 627 ---GHNQSQQDILQEntiLKATEVQF--PVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLPHMRRS 693
Cdd:cd14092  206 qspSRNESAAEIMKR---IKSGDFSFdgEEWKNVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWLQGSSSPS 274
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
450-692 6.16e-25

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: 104.95  E-value: 6.16e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 450 KENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNE 529
Cdd:cd14117   46 KEGVEHQLRREIEIQSHLRHPNILRLYNYFHDRKRIY-LILEYAPRGELYKELQKHGRFDEQRTATFMEELADALHYCHE 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 530 IKppIIHYDLKPGNILLvdgTACGEIKITDFGLSkimdddsygVDGMDLTSQG-AGTYWYLPPECFvvgkEPPKISNKVD 608
Cdd:cd14117  125 KK--VIHRDIKPENLLM---GYKGELKIADFGWS---------VHAPSLRRRTmCGTLDYLPPEMI----EGRTHDEKVD 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 609 VWSVGVIFFQCLYGRKPF---GHNQSQQDILQentilkaTEVQFPvkPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14117  187 LWCIGVLCYELLVGMPPFesaSHTETYRRIVK-------VDLKFP--PFLSDGSRDLISKLLRYHPSERLPLKGVMEHPW 257

                 ....*..
gi 211971036 686 LLPHMRR 692
Cdd:cd14117  258 VKANSRR 264
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
419-626 6.84e-25

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: 106.25  E-value: 6.84e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKHACREYRIhKELDHPRIVKLYdyFSLDT-DTFCTVLEYCEGND 497
Cdd:cd05575    8 FGKVLLARHKAEGKLYAVKV--LQKKAILKRNEVKHIMAERNVLL-KNVKHPFLVGLH--YSFQTkDKLYFVLDYVNGGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddsYGVDGMD 577
Cdd:cd05575   83 LFFHLQRERHFPEPRARFYAAEIASALGYLHSLN--IIYRDLKPENILL---DSQGHVVLTDFGLCK------EGIEPSD 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 211971036 578 LTSQGAGTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd05575  152 TTSTFCGTPEYLAPE--VLRKQPYDRT--VDWWCLGAVLYEMLYGLPPF 196
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
419-686 9.04e-25

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: 104.31  E-value: 9.04e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSwrdekKENYHKHACREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDL 498
Cdd:cd06626   13 FGKVYTAVNLDTGELMAMKEIRFQDN-----DPKTIKEIADEMKVLEGLDHPNLVRYYG-VEVHREEVYIFMEYCQEGTL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSYGVDGMDL 578
Cdd:cd06626   87 EELLRHGRILDEAVIRVYTLQLLEGLAYLHENG--IVHRDIKPANIFLDSN---GLIKLGDFGSAVKLKNNTTTMAPGEV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQgAGTYWYLPPECFVVGKEPPKIsNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQEntiLKATEV-QFPVKPVVSS 657
Cdd:cd06626  162 NSL-VGTPAYMAPEVITGNKGEGHG-RAADIWSLGCVVLEMATGKRPWSELDNEWAIMYH---VGMGHKpPIPDSLQLSP 236
                        250       260
                 ....*....|....*....|....*....
gi 211971036 658 EAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06626  237 EGKDFLSRCLESDPKKRPTASELLDHPFI 265
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
419-686 1.10e-24

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: 104.93  E-value: 1.10e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNK-------SWRDEKkenyhkhacREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLE 491
Cdd:cd14094   16 FSVVRRCIHRETGQQFAVKIVDVAKftsspglSTEDLK---------REASICHMLKHPHIVELLETYSSDGMLY-MVFE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 492 YCEGNDLDFYLKQHK----LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMD 567
Cdd:cd14094   86 FMDGADLCFEIVKRAdagfVYSEAVASHYMRQILEALRYCHDNN--IIHRDVKPHCVLLASKENSAPVKLGGFGVAIQLG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 568 DdsygvdGMDLTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQqdiLQENTILKATEV 647
Cdd:cd14094  164 E------SGLVAGGRVGTPHFMAPE--VVKREP--YGKPVDVWGCGVILFILLSGCLPFYGTKER---LFEGIIKGKYKM 230
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 211971036 648 QFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14094  231 NPRQWSHISESAKDLVRRMLMLDPAERITVYEALNHPWI 269
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
419-633 1.41e-24

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: 104.57  E-value: 1.41e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihQLNKswrDEKKENYHKHACREYRIHKELDHPRIVKLYD------YFSLDTDTFcTVLEY 492
Cdd:cd07840   12 YGQVYKARNKKTGELVALK--KIRM---ENEKEGFPITAIREIKLLQKLDHPNVVRLKEivtskgSAKYKGSIY-MVFEY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 493 CEgNDLDFYLKQHKL-MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSY 571
Cdd:cd07840   86 MD-HDLTGLLDNPEVkFTESQIKCYMKQLLEGLQYLHSNG--ILHRDIKGSNILINND---GVLKLADFGLARPYTKENN 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 572 GvdgmDLTSqGAGTYWYLPPE----CFVVGKEppkisnkVDVWSVGVIFFQCLYGRKPF-GHNQSQQ 633
Cdd:cd07840  160 A----DYTN-RVITLWYRPPElllgATRYGPE-------VDMWSVGCILAELFTGKPIFqGKTELEQ 214
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
443-681 1.49e-24

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: 103.50  E-value: 1.49e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDE--KKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQI 520
Cdd:cd14161   33 KSIRKDriKDEQDLLHIRREIEIMSSLNHPHIISVYEVFE-NSSKIVIVMEYASRGDLYDYISERQRLSELEARHFFRQI 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 521 VNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYgvdgmdlTSQGAGTYWYLPPEcFVVGKep 600
Cdd:cd14161  112 VSAVHYCH--ANGIVHRDLKLENILL---DANGNIKIADFGLSNLYNQDKF-------LQTYCGSPLYASPE-IVNGR-- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 601 PKISNKVDVWSVGVIFFQCLYGRKPF-GHNqsQQDILQEntiLKATEVQFPVKPvvsSEAKAFIRRCLAYRKEDRFDVHQ 679
Cdd:cd14161  177 PYIGPEVDSWSLGVLLYILVHGTMPFdGHD--YKILVKQ---ISSGAYREPTKP---SDACGLIRWLLMVNPERRATLED 248

                 ..
gi 211971036 680 LA 681
Cdd:cd14161  249 VA 250
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
431-668 2.02e-24

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: 104.75  E-value: 2.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 431 QRYAAVKIhqLNKSWRDEKKENyhKHACREYRIHKELDHPRIVKLYdyFSLDT-DTFCTVLEYCEGNDLDFYLKQHKLMS 509
Cdd:cd05571   20 GELYAIKI--LKKEVIIAKDEV--AHTLTENRVLQNTRHPFLTSLK--YSFQTnDRLCFVMEYVNGGELFFHLSRERVFS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 510 EKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimDDDSYGvdgmDLTSQGAGTYWYL 589
Cdd:cd05571   94 EDRTRFYGAEIVLALGYLHSQG--IVYRDLKLENLLL---DKDGHIKITDFGLCK--EEISYG----ATTKTFCGTPEYL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 590 PPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPF---GHNQSQQDILQEntilkatEVQFPvkPVVSSEAKAFIRRC 666
Cdd:cd05571  163 APEVL----EDNDYGRAVDWWGLGVVMYEMMCGRLPFynrDHEVLFELILME-------EVRFP--STLSPEAKSLLAGL 229

                 ..
gi 211971036 667 LA 668
Cdd:cd05571  230 LK 231
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
419-686 2.03e-24

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: 104.66  E-value: 2.03e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKHACREYRIhKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL 498
Cdd:cd05604    9 FGKVLLAKRKRDGKYYAVKV--LQKKVILNRKEQKHIMAERNVLL-KNVKHPFLVGLHYSFQ-TTDKLYFVLDFVNGGEL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddsYGVDGMDL 578
Cdd:cd05604   85 FFHLQRERSFPEPRARFYAAEIASALGYLHSIN--IVYRDLKPENILL---DSQGHIVLTDFGLCK------EGISNSDT 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQdiLQENTILKatevQFPVKPVVSSE 658
Cdd:cd05604  154 TTTFCGTPEYLAPE--VIRKQP--YDNTVDWWCLGSVLYEMLYGLPPFYCRDTAE--MYENILHK----PLVLRPGISLT 223
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 659 AKAFIRRCLAYRKEDRF----DVHQLANDPYL 686
Cdd:cd05604  224 AWSILEELLEKDRQLRLgakeDFLEIKNHPFF 255
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
446-686 2.11e-24

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: 103.33  E-value: 2.11e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 446 RDEKKENYHKHAC-REYRIHKELDHPRIVKLYDYfsLDTDT-FCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNA 523
Cdd:cd14076   41 RDTQQENCQTSKImREINILKGLTHPNIVRLLDV--LKTKKyIGIVLEFVSGGELFDYILARRRLKDSVACRLFAQLISG 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 524 LRYLNeiKPPIIHYDLKPGNILLVDGTacgEIKITDFGLSkimddDSYGVDGMDLTSQGAGTYWYLPPECFVVGKepPKI 603
Cdd:cd14076  119 VAYLH--KKGVVHRDLKLENLLLDKNR---NLVITDFGFA-----NTFDHFNGDLMSTSCGSPCYAAPELVVSDS--MYA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 604 SNKVDVWSVGVIFFQCLYGRKPFG---HNQSQQDILQENTILKATEVQFPvkPVVSSEAKAFIRRCLAYRKEDRFDVHQL 680
Cdd:cd14076  187 GRKADIWSCGVILYAMLAGYLPFDddpHNPNGDNVPRLYRYICNTPLIFP--EYVTPKARDLLRRILVPNPRKRIRLSAI 264

                 ....*.
gi 211971036 681 ANDPYL 686
Cdd:cd14076  265 MRHAWL 270
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
419-685 4.20e-24

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: 102.37  E-value: 4.20e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfdlyeqRYAA----VKIHQLNKSWRDEKKenyhkhacREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCE 494
Cdd:cd14010   13 HSVVYKG------RRKGtiefVAIKCVDKSKRPEVL--------NEVRLTHELKHPNVLKFYEWYE-TSNHLWLVVEYCT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 GNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvDGTacGEIKITDFGLSKIMDD------ 568
Cdd:cd14010   78 GGDLETLLRQDGNLPESSVRKFGRDLVRGLHYIH--SKGIIYCDLKPSNILL-DGN--GTLKLSDFGLARREGEilkelf 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 569 ----DSYGVDGMDLTSQGAGTYWYLPPECFvvgKEPPkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQ---DILQENTi 641
Cdd:cd14010  153 gqfsDEGNVNKVSKKQAKRGTPYYMAPELF---QGGV-HSFASDLWALGCVLYEMFTGKPPFVAESFTElveKILNEDP- 227
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 211971036 642 lKATEVQFPVKPvvSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14010  228 -PPPPPKVSSKP--SPDFKSLLKGLLEKDPAKRLSWDELVKHPF 268
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
419-686 4.88e-24

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


Pssm-ID: 270811 [Multi-domain]  Cd Length: 283  Bit Score: 102.80  E-value: 4.88e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqlnkswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL 498
Cdd:cd06643   18 FGKVYKAQNKETGILAAAKV-------IDTKSEEELEDYMVEIDILASCDHPNIVKLLDAFYYENNLW-ILIEFCAGGAV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 D-FYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLS-----KIMDDDSYg 572
Cdd:cd06643   90 DaVMLELERPLTEPQIRVVCKQTLEALVYLHENK--IIHRDLKAGNILF---TLDGDIKLADFGVSakntrTLQRRDSF- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 573 vdgmdltsqgAGTYWYLPPECFV--VGKEPPkISNKVDVWSVGVIFFQcLYGRKPFGHNQSQQDILQEntILKATEVQFP 650
Cdd:cd06643  164 ----------IGTPYWMAPEVVMceTSKDRP-YDYKADVWSLGVTLIE-MAQIEPPHHELNPMRVLLK--IAKSEPPTLA 229
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 211971036 651 VKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06643  230 QPSRWSPEFKDFLRKCLEKNVDARWTTSQLLQHPFV 265
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
419-624 5.96e-24

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: 101.99  E-value: 5.96e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNkswrdEKKENYHKhACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd13996   19 FGSVYKVRNKVDGVTYAIKKIRLT-----EKSSASEK-VLREVKALAKLNHPNIVRYYTAW-VEEPPLYIQMELCEGGTL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQ---HKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtaCGEIKITDFGLSKIMDDDSYGVDG 575
Cdd:cd13996   92 RDWIDRrnsSSKNDRKLALELFKQILKGVSYIHSKG--IVHRDLKPSNIFLDND--DLQVKIGDFGLATSIGNQKRELNN 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 576 MDLT--------SQGAGTYWYLPPEcfvvGKEPPKISNKVDVWSVGVIFFQCLYGRK 624
Cdd:cd13996  168 LNNNnngntsnnSVGIGTPLYASPE----QLDGENYNEKADIYSLGIILFEMLHPFK 220
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
421-686 1.93e-23

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: 99.98  E-value: 1.93e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 421 EVYKAFDLYEQRYAAVKIHQLNKswrdEKKENyhkhACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDF 500
Cdd:cd06614   15 EVYKATDRATGKEVAIKKMRLRK----QNKEL----IINEILIMKECKHPNIVDYYDSY-LVGDELWVVMEYMDGGSLTD 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 501 YLKQHKL-MSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKImdddsygvdgmdLT 579
Cdd:cd06614   86 IITQNPVrMNESQIAYVCREVLQGLEYLH--SQNVIHRDIKSDNILL---SKDGSVKLADFGFAAQ------------LT 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 580 SQGA------GT-YWyLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFghnqsqqdiLQENTI----LKATEVQ 648
Cdd:cd06614  149 KEKSkrnsvvGTpYW-MAPE--VIKRKD--YGPKVDIWSLGIMCIEMAEGEPPY---------LEEPPLralfLITTKGI 214
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 211971036 649 FPVKP--VVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06614  215 PPLKNpeKWSPEFKDFLNKCLVKDPEKRPSAEELLQHPFL 254
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
419-667 1.95e-23

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: 100.25  E-value: 1.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKHAcrEYRI-HKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGND 497
Cdd:cd05611    9 FGSVYLAKKRSTGDYFAIKV--LKKSDMIAKNQVTNVKA--ERAImMIQGESPYVAKLYYSFQ-SKDYLYLVMEYLNGGD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNiLLVDGTacGEIKITDFGLSKIMDDDSYGVDGMd 577
Cdd:cd05611   84 CASLIKTLGGLPEDWAKQYIAEVVLGVEDLH--QRGIIHRDIKPEN-LLIDQT--GHLKLTDFGLSRNGLEKRHNKKFV- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 ltsqgaGTYWYLPPECfVVGKEPPKISnkvDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntiLKATEVQFP--VKPVV 655
Cdd:cd05611  158 ------GTPDYLAPET-ILGVGDDKMS---DWWSLGCVIFEFLFGYPPF-HAETPDAVFDN---ILSRRINWPeeVKEFC 223
                        250
                 ....*....|..
gi 211971036 656 SSEAKAFIRRCL 667
Cdd:cd05611  224 SPEAVDLINRLL 235
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
419-686 1.95e-23

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: 100.03  E-value: 1.95e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKenyhkhacrEYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGND- 497
Cdd:cd06612   16 YGSVYKAIHKETGQVVAIKVVPVEEDLQEIIK---------EISILKQCDSPYIVKYYGSYFKNTDLW-IVMEYCGAGSv 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMdddsygVDGMD 577
Cdd:cd06612   86 SDIMKITNKTLTEEEIAAILYQTLKGLEYLHSNK--KIHRDIKAGNILLNEE---GQAKLADFGVSGQL------TDTMA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQGAGTYWYLPPEcfVVGKepPKISNKVDVWSVGVIFFQCLYGRKPFGHnqsqqdilqentiLKATEVQF--PVKPV- 654
Cdd:cd06612  155 KRNTVIGTPFWMAPE--VIQE--IGYNNKADIWSLGITAIEMAEGKPPYSD-------------IHPMRAIFmiPNKPPp 217
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 211971036 655 -------VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06612  218 tlsdpekWSPEFNDFVKKCLVKDPEERPSAIQLLQHPFI 256
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
419-686 2.00e-23

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: 100.06  E-value: 2.00e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSWRDEkkENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFCTVLEYCEGNDL 498
Cdd:cd14163   13 YSKVKEAFSKKHQRKVAIKI--IDKSGGPE--EFIQRFLPRELQIVERLDHKNIIHVYEMLESADGKIYLVMELAEDGDV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacgeIKITDFGLSKIMDddsygVDGMDL 578
Cdd:cd14163   89 FDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCG--VAHRDLKCENALLQGFT----LKLTDFGFAKQLP-----KGGREL 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPEcfvVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENtilkaTEVQFPVKPVVSSE 658
Cdd:cd14163  158 SQTFCGSTAYAAPE---VLQGVPHDSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQ-----KGVSLPGHLGVSRT 229
                        250       260
                 ....*....|....*....|....*...
gi 211971036 659 AKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14163  230 CQDLLKRLLEPDMVLRPSIEEVSWHPWL 257
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
435-686 2.36e-23

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: 99.77  E-value: 2.36e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIhqLNKSWRDEkkENYHKhACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEAR 514
Cdd:cd14071   29 AIKI--IDKSQLDE--ENLKK-IYREVQIMKMLNHPHIIKLYQVME-TKDMLYLVTEYASNGEIFDYLAQHGRMSEKEAR 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 515 SIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvDGTacGEIKITDFGLSKIMDDDsygvdgmDLTSQGAGTYWYLPPECF 594
Cdd:cd14071  103 KKFWQILSAVEYCH--KRHIVHRDLKAENLLL-DAN--MNIKIADFGFSNFFKPG-------ELLKTWCGSPPYAAPEVF 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 595 vVGKE---PpkisnKVDVWSVGVIFFQCLYGRKPFGHNQSQqdILQEntilKATEVQFPVKPVVSSEAKAFIRRCLAYRK 671
Cdd:cd14071  171 -EGKEyegP-----QLDIWSLGVVLYVLVCGALPFDGSTLQ--TLRD----RVLSGRFRIPFFMSTDCEHLIRRMLVLDP 238
                        250
                 ....*....|....*
gi 211971036 672 EDRFDVHQLANDPYL 686
Cdd:cd14071  239 SKRLTIEQIKKHKWM 253
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
469-686 2.65e-23

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: 99.77  E-value: 2.65e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFSlDTDTFCTVLEyCEGNDLDF--YLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILL 546
Cdd:cd14004   67 HPNIVKLLDFFE-DDEFYYLVME-KHGSGMDLfdFIERKPNMDEKEAKYIFRQVADAVKHLHDQG--IVHRDIKDENVIL 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 547 vDGTacGEIKITDFGLSKIMDDDSYGVdgmdltsqGAGTYWYLPPEcfVVGKEPPKiSNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd14004  143 -DGN--GTIKLIDFGSAAYIKSGPFDT--------FVGTIDYAAPE--VLRGNPYG-GKEQDIWALGVLLYTLVFKENPF 208
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 627 ghnqsqQDILQentILKAtEVQFPVkpVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14004  209 ------YNIEE---ILEA-DLRIPY--AVSEDLIDLISRMLNRDVGDRPTIEELLTDPWL 256
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
470-685 2.88e-23

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: 100.16  E-value: 2.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 470 PRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvDG 549
Cdd:cd05583   59 PFLVTLHYAFQTDAKLH-LILDYVNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLG--IIYRDIKLENILL-DS 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 550 TacGEIKITDFGLSKIMDDDSygvdgMDLTSQGAGTYWYLPPEcfVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPF--- 626
Cdd:cd05583  135 E--GHVVLTDFGLSKEFLPGE-----NDRAYSFCGTIEYMAPE--VVRGGSDGHDKAVDWWSLGVLTYELLTGASPFtvd 205
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 211971036 627 GHNQSQQDILQEntILKAtevQFPVKPVVSSEAKAFIRRCLAYRKEDRF-----DVHQLANDPY 685
Cdd:cd05583  206 GERNSQSEISKR--ILKS---HPPIPKTFSAEAKDFILKLLEKDPKKRLgagprGAHEIKEHPF 264
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
460-686 3.43e-23

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: 99.62  E-value: 3.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDL 539
Cdd:cd14187   57 EIAIHRSLAHQHVVGFHGFFE-DNDFVYVVLELCRRRSLLELHKRRKALTEPEARYYLRQIILGCQYLHRNR--VIHRDL 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 540 KPGNILLVDGTacgEIKITDFGLSKIMDDDSygvdgmDLTSQGAGTYWYLPPEcfVVGKEPPkiSNKVDVWSVGVIFFQC 619
Cdd:cd14187  134 KLGNLFLNDDM---EVKIGDFGLATKVEYDG------ERKKTLCGTPNYIAPE--VLSKKGH--SFEVDIWSIGCIMYTL 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 620 LYGRKPFghnqsQQDILQENTI-LKATEVQFP--VKPVvsseAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14187  201 LVGKPPF-----ETSCLKETYLrIKKNEYSIPkhINPV----AASLIQKMLQTDPTARPTINELLNDEFF 261
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
433-686 3.46e-23

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK1 is the prototypical member of the subfamily and is also simply referred to as DAPK. DAPK2 is also called DAPK-related protein 1 (DRP-1), while DAPK3 has also been named DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk). These proteins are ubiquitously expressed in adult tissues, are capable of cross talk with each other, and may act synergistically in regulating cell death. The DAPK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271007 [Multi-domain]  Cd Length: 269  Bit Score: 99.87  E-value: 3.46e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 433 YAA--VKIHQLNKSWRDEKKENYHkhacREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSE 510
Cdd:cd14105   33 YAAkfIKKRRSKASRRGVSREDIE----REVSILRQVLHPNIITLHDVFENKTDVV-LILELVAGGELFDFLAEKESLSE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 511 KEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVD-GTACGEIKITDFGLSKIMDDdsyGVDGMDLtsqgAGTYWYL 589
Cdd:cd14105  108 EEATEFLKQILDGVNYLHTKN--IAHFDLKPENIMLLDkNVPIPRIKLIDFGLAHKIED---GNEFKNI----FGTPEFV 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 590 PPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFghnqsQQDILQEnTILKATEVQFPVKPVV----SSEAKAFIRR 665
Cdd:cd14105  179 APE--IVNYEP--LGLEADMWSIGVITYILLSGASPF-----LGDTKQE-TLANITAVNYDFDDEYfsntSELAKDFIRQ 248
                        250       260
                 ....*....|....*....|.
gi 211971036 666 CLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14105  249 LLVKDPRKRMTIQESLRHPWI 269
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
419-686 3.80e-23

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: 99.82  E-value: 3.80e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSwrdEKKENYhkhaCREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL 498
Cdd:cd06611   18 FGKVYKAQHKETGLFAAAKIIQIESE---EELEDF----MVEIDILSECKHPNIVGLYEAYFYENKLW-ILIEFCDGGAL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 D-FYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSkimdddSYGVDGMD 577
Cdd:cd06611   90 DsIMLELERGLTEPQIRYVCRQMLEALNFLHSHK--VIHRDLKAGNILL---TLDGDVKLADFGVS------AKNKSTLQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQGAGTYWYLPPEcfVVGKEPPK---ISNKVDVWSVGVIFFQcLYGRKPFGHNQSQQDILQEntILKATEVQFPVKPV 654
Cdd:cd06611  159 KRDTFIGTPYWMAPE--VVACETFKdnpYDYKADIWSLGITLIE-LAQMEPPHHELNPMRVLLK--ILKSEPPTLDQPSK 233
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 655 VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06611  234 WSSSFNDFLKSCLVKDPDDRPTAAELLKHPFV 265
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
435-686 3.88e-23

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: 100.05  E-value: 3.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIHQLN-KSWRDEKKENYHKHACREYRI-HKELDHPRIVKLYDyfSLDTDTFC-TVLEYCEGNDLDFYLKQHKLMSEK 511
Cdd:cd14181   39 AVKIIEVTaERLSPEQLEEVRSSTLKEIHIlRQVSGHPSIITLID--SYESSTFIfLVFDLMRRGELFDYLTEKVTLSEK 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 512 EARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDgtaCGEIKITDFGLSKIMDDDsygvdgmDLTSQGAGTYWYLPP 591
Cdd:cd14181  117 ETRSIMRSLLEAVSYLHANN--IVHRDLKPENILLDD---QLHIKLSDFGFSCHLEPG-------EKLRELCGTPGYLAP 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 592 ECFVVGKEP--PKISNKVDVWSVGVIFFQCLYGRKPFGHnqsQQDILQENTILKAtEVQF--PVKPVVSSEAKAFIRRCL 667
Cdd:cd14181  185 EILKCSMDEthPGYGKEVDLWACGVILFTLLAGSPPFWH---RRQMLMLRMIMEG-RYQFssPEWDDRSSTVKDLISRLL 260
                        250
                 ....*....|....*....
gi 211971036 668 AYRKEDRFDVHQLANDPYL 686
Cdd:cd14181  261 VVDPEIRLTAEQALQHPFF 279
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
419-686 3.98e-23

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: 99.96  E-value: 3.98e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVK-IHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFSLDTDTFCTvLEYCEGND 497
Cdd:cd14169   16 FSEVVLAQERGSQRLVALKcIPKKALRGKEAMVEN-------EIAVLRRINHENIVSLEDIYESPTHLYLA-MELVTGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDdsygvdgmD 577
Cdd:cd14169   88 LFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLG--IVHRDLKPENLLYATPFEDSKIMISDFGLSKIEAQ--------G 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILqeNTILKAT-EVQFPVKPVVS 656
Cdd:cd14169  158 MLSTACGTPGYVAPELL----EQKPYGKAVDVWAIGVISYILLCGYPPF-YDENDSELF--NQILKAEyEFDSPYWDDIS 230
                        250       260       270
                 ....*....|....*....|....*....|
gi 211971036 657 SEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14169  231 ESAKDFIRHLLERDPEKRFTCEQALQHPWI 260
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
419-674 4.76e-23

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: 98.93  E-value: 4.76e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKhacrEYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL 498
Cdd:cd14188   14 FAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQREKIDK----EIELHRILHHKHVVQFYHYFE-DKENIYILLEYCSRRSM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacgEIKITDFGLSKIMDDDSYGVDGMdl 578
Cdd:cd14188   89 AHILKARKVLTEPEVRYYLRQIVSGLKYLHEQE--ILHRDLKLGNFFINENM---ELKVGDFGLAARLEPLEHRRRTI-- 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 tsqgAGTYWYLPPEcfVVGKEPPKISNkvDVWSVGVIFFQCLYGRKPFghnqsqqdilqENTILKAT-----EVQFPVKP 653
Cdd:cd14188  162 ----CGTPNYLSPE--VLNKQGHGCES--DIWALGCVMYTMLLGRPPF-----------ETTNLKETyrcirEARYSLPS 222
                        250       260
                 ....*....|....*....|.
gi 211971036 654 VVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd14188  223 SLLAPAKHLIASMLSKNPEDR 243
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
435-686 4.88e-23

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: 100.77  E-value: 4.88e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIhqLNKSWRDEKKENYHKHACREyrIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEAR 514
Cdd:cd05599   30 AMKK--LRKSEMLEKEQVAHVRAERD--ILAEADNPWVVKLYYSFQ-DEENLYLIMEFLPGGDMMTLLMKKDTLTEEETR 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 515 SIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddsyGVDGMDLTSQGAGTYWYLPPECF 594
Cdd:cd05599  105 FYIAETVLAIESIHKLG--YIHRDIKPDNLLL---DARGHIKLSDFGLCT-------GLKKSHLAYSTVGTPDYIAPEVF 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 595 V---VGKEppkisnkVDVWSVGVIFFQCLYGRKPFGHNQSQ---QDILQENTILkatevQFPVKPVVSSEAKAFIRR--C 666
Cdd:cd05599  173 LqkgYGKE-------CDWWSLGVIMYEMLIGYPPFCSDDPQetcRKIMNWRETL-----VFPPEVPISPEAKDLIERllC 240
                        250       260
                 ....*....|....*....|
gi 211971036 667 LAYRKEDRFDVHQLANDPYL 686
Cdd:cd05599  241 DAEHRLGANGVEEIKSHPFF 260
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
468-667 5.69e-23

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: 100.37  E-value: 5.69e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 468 DHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLv 547
Cdd:cd05570   54 RHPFLTGLHACFQ-TEDRLYFVMEYVNGGDLMFHIQRARRFTEERARFYAAEICLALQFLHERG--IIYRDLKLDNVLL- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 548 dgTACGEIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFFQCLYGRKPFg 627
Cdd:cd05570  130 --DAEGHIKIADFGMCK------EGIWGGNTTSTFCGTPDYIAPE--ILREQDYGFS--VDWWALGVLLYEMLAGQSPF- 196
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 211971036 628 HNQSQQDILQEntiLKATEVQFPVKpvVSSEAKAFIRRCL 667
Cdd:cd05570  197 EGDDEDELFEA---ILNDEVLYPRW--LSREAVSILKGLL 231
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
459-686 7.28e-23

The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Caenorhabditis elegans and Aplysia californica Twitchin, Drosophila melanogaster Projectin, and similar proteins. These are very large muscle proteins containing multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains and a single kinase domain near the C-terminus. Twitchin and Projectin are both associated with thick filaments. Twitchin is localized in the outer parts of A-bands and is involved in regulating muscle contraction. It interacts with the myofibrillar proteins myosin and actin in a phosphorylation-dependent manner, and may be involved in regulating the myosin cross-bridge cycle. The kinase activity of Twitchen is activated by Ca2+ and the Ca2+ binding protein S100A1. Projectin is associated with the end of thick filaments and is a component of flight muscle connecting filaments. The kinase domain of Projectin may play roles in autophosphorylation and transphosphorylation, which impact the formation of myosin filaments. The Twitchin-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271016 [Multi-domain]  Cd Length: 259  Bit Score: 98.81  E-value: 7.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL-DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHY 537
Cdd:cd14114   48 KEIQIMNQLHHPKLINLHDAFE-DDNEMVLILEFLSGGELfERIAAEHYKMSEAEVINYMRQVCEGLCHMHENN--IVHL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLVDGTAcGEIKITDFGLSKIMDDDsygvdgmDLTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFF 617
Cdd:cd14114  125 DIKPENIMCTTKRS-NEVKLIDFGLATHLDPK-------ESVKVTTGTAEFAAPE--IVEREP--VGFYTDMWAVGVLSY 192
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 618 QCLYGRKPFGHNQSQQDILQentiLKATEVQFPVKPV--VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14114  193 VLLSGLSPFAGENDDETLRN----VKSCDWNFDDSAFsgISEEAKDFIRKLLLADPNKRMTIHQALEHPWL 259
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
420-686 9.15e-23

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: 99.13  E-value: 9.15e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 420 SEVYKAFDLYEQRYAAVKIHqlnkswrdeKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLD 499
Cdd:cd14085   17 SVVYRCRQKGTQKPYAVKKL---------KKTVDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEIS-LVLELVTGGELF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 500 FYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSygvdgmdLT 579
Cdd:cd14085   87 DRIVEKGYYSERDAADAVKQILEAVAYLHE--NGIVHRDLKPENLLYATPAPDAPLKIADFGLSKIVDQQV-------TM 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 580 SQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQEntILKAtEVQF--PVKPVVSS 657
Cdd:cd14085  158 KTVCGTPGYCAPE--ILRGCA--YGPEVDMWSVGVITYILLCGFEPFYDERGDQYMFKR--ILNC-DYDFvsPWWDDVSL 230
                        250       260
                 ....*....|....*....|....*....
gi 211971036 658 EAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14085  231 NAKDLVKKLIVLDPKKRLTTQQALQHPWV 259
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
419-685 9.54e-23

The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GSK3 is a mutifunctional kinase involved in many cellular processes including cell division, proliferation, differentiation, adhesion, and apoptosis. In plants, GSK3 plays a role in the response to osmotic stress. In Caenorhabditis elegans, it plays a role in regulating normal oocyte-to-embryo transition and response to oxidative stress. In Chlamydomonas reinhardtii, GSK3 regulates flagellar length and assembly. In mammals, there are two isoforms, GSK3alpha and GSK3beta, which show both distinct and redundant functions. The two isoforms differ mainly in their N-termini. They are both involved in axon formation and in Wnt signaling.They play distinct roles in cardiogenesis, with GSKalpha being essential in cardiomyocyte survival, and GSKbeta regulating heart positioning and left-right symmetry. GSK3beta was first identified as a regulator of glycogen synthesis, but has since been determined to play other roles. It regulates the degradation of beta-catenin and IkB. Beta-catenin is the main effector of Wnt, which is involved in normal haematopoiesis and stem cell function. IkB is a central inhibitor of NF-kB, which is critical in maintaining leukemic cell growth. GSK3beta is enriched in the brain and is involved in regulating neuronal signaling pathways. It is implicated in the pathogenesis of many diseases including Type II diabetes, obesity, mood disorders, Alzheimer's disease, osteoporosis, and some types of cancer, among others. The GSK3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271039 [Multi-domain]  Cd Length: 293  Bit Score: 99.11  E-value: 9.54e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENyhkhacREYRIHKELDHPRIVKLYDYF----SLDTDTF-CTVLEYC 493
Cdd:cd14137   17 FGVVYQAKLLETGEVVAIK-----KVLQDKRYKN------RELQIMRRLKHPNIVKLKYFFyssgEKKDEVYlNLVMEYM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 494 EGNDLDF---YLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacGEIKITDFGLSKIMDDD- 569
Cdd:cd14137   86 PETLYRVirhYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLG--ICHRDIKPQNLLVDPET--GVLKLCDFGSAKRLVPGe 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 570 ---SYgvdgmdltsqgAGTYWYLPPECFVVGKEppkISNKVDVWSVGVIFFQCLYGrKPFGHNQSQQDILQEntILK--- 643
Cdd:cd14137  162 pnvSY-----------ICSRYYRAPELIFGATD---YTTAIDIWSAGCVLAELLLG-QPLFPGESSVDQLVE--IIKvlg 224
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 211971036 644 -------------ATEVQFP-VKPV---------VSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14137  225 tptreqikamnpnYTEFKFPqIKPHpwekvfpkrTPPDAIDLLSKILVYNPSKRLTALEALAHPF 289
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
419-686 1.00e-22

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: 98.01  E-value: 1.00e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL 498
Cdd:cd14186   14 FACVYRARSLHTGLEVAIKM--IDK--KAMQKAGMVQRVRNEVEIHCQLKHPSILELYNYFE-DSNYVYLVLEMCHNGEM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKL-MSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLS---KIMDDDSYGVd 574
Cdd:cd14186   89 SRYLKNRKKpFTEDEARHFMHQIVTGMLYLH--SHGILHRDLTLSNLLL---TRNMNIKIADFGLAtqlKMPHEKHFTM- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 575 gmdltsqgAGTYWYLPPEcfVVGKEPPKISNkvDVWSVGVIFFQCLYGRKPFghnqsQQDILQeNTILKATEVQFPVKPV 654
Cdd:cd14186  163 --------CGTPNYISPE--IATRSAHGLES--DVWSLGCMFYTLLVGRPPF-----DTDTVK-NTLNKVVLADYEMPAF 224
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 655 VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14186  225 LSREAQDLIHQLLRKNPADRLSLSSVLDHPFM 256
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
448-694 1.01e-22

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: 99.05  E-value: 1.01e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 448 EKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYL 527
Cdd:cd06620   41 DAKSSVRKQILRELQILHECHSPYIVSFYGAFLNENNNIIICMEYMDCGSLDKILKKKGPFPEEVLGKIAVAVLEGLTYL 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 528 -NEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddsygvdgmDLTSQGA----GTYWYLPPECFVVGkeppK 602
Cdd:cd06620  121 yNVHR--IIHRDIKPSNILV---NSKGQIKLCDFGVSG------------ELINSIAdtfvGTSTYMSPERIQGG----K 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 603 ISNKVDVWSVGVIFFQCLYGRKPFG-HNQSQQ---------DILQEntILKATEVQFPVKPVVSSEAKAFIRRCLAYRKE 672
Cdd:cd06620  180 YSVKSDVWSLGLSIIELALGEFPFAgSNDDDDgyngpmgilDLLQR--IVNEPPPRLPKDRIFPKDLRDFVDRCLLKDPR 257
                        250       260
                 ....*....|....*....|..
gi 211971036 673 DRFDVHQLANDPYLLPHMRRSN 694
Cdd:cd06620  258 ERPSPQLLLDHDPFIQAVRASD 279
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
443-626 1.10e-22

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: 98.88  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFS-----LDTDTFCTVLEYCEGNDLDFYLKQHKL---MSEKEAR 514
Cdd:cd14038   25 KQCRQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEglqklAPNDLPLLAMEYCQGGDLRKYLNQFENccgLREGAIL 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 515 SIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSygvdgmdLTSQGAGTYWYLPPECF 594
Cdd:cd14038  105 TLLSDISSALRYLHENR--IIHRDLKPENIVLQQGEQRLIHKIIDLGYAKELDQGS-------LCTSFVGTLQYLAPELL 175
                        170       180       190
                 ....*....|....*....|....*....|..
gi 211971036 595 vvgkEPPKISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd14038  176 ----EQQKYTVTVDYWSFGTLAFECITGFRPF 203
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
419-686 1.30e-22

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: 98.54  E-value: 1.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL 498
Cdd:cd07833   14 YGVVLKCRNKATGEIVAIK-----KFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLY-LVFEYVERTLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSygvdGMDL 578
Cdd:cd07833   88 ELLEASPGGLPPDAVRSYIWQLLQAIAYCHSHN--IIHRDIKPENILV---SESGVLKLCDFGFARALTARP----ASPL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAgTYWYLPPECFVvgkEPPKISNKVDVWSVGVIFFQCLYGRKPF-GHN----------------QSQQDILQENTI 641
Cdd:cd07833  159 TDYVA-TRWYRAPELLV---GDTNYGKPVDVWAIGCIMAELLDGEPLFpGDSdidqlyliqkclgplpPSHQELFSSNPR 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 211971036 642 LkATEVQFPVKP----------VVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd07833  235 F-AGVAFPEPSQpeslerrypgKVSSPALDFLKACLRMDPKERLTCDELLQHPYF 288
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
419-686 1.49e-22

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: 97.72  E-value: 1.49e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYhkhacREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL 498
Cdd:cd08225   13 FGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASK-----KEVILLAKMKHPNIVTFFASFQENGRLF-IVMEYCDGGDL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHK--LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEI-KITDFGLSKIMDDDsygvdg 575
Cdd:cd08225   87 MKRINRQRgvLFSEDQILSWFVQISLGLKHIHDRK--ILHRDIKSQNIFL---SKNGMVaKLGDFGIARQLNDS------ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 MDLTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQdilqenTILKATEVQF-PVKPV 654
Cdd:cd08225  156 MELAYTCVGTPYYLSPE--ICQNRP--YNNKTDIWSLGCVLYELCTLKHPFEGNNLHQ------LVLKICQGYFaPISPN 225
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 655 VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd08225  226 FSRDLRSLISQLFKVSPRDRPSITSILKRPFL 257
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
419-686 1.72e-22

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: 97.72  E-value: 1.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSwrdekkenYHKHACREYRI------HKELDHPRIVKLYDYFSLDTDTfCTVLEY 492
Cdd:cd14133   12 FGQVVKCYDLLTGEEVALKIIKNNKD--------YLDQSLDEIRLlellnkKDKADKYHIVRLKDVFYFKNHL-CIVFEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 493 CEGNDLDFyLKQHKLM--SEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACgEIKITDFGLSkimdddS 570
Cdd:cd14133   83 LSQNLYEF-LKQNKFQylSLPRIRKIAQQILEALVFLHSLG--LIHCDLKPENILLASYSRC-QIKIIDFGSS------C 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 571 YgvdgmdlTSQGAGTY----WYLPPEcFVVGKeppKISNKVDVWSVGVIFFQcLYGRKPFGHNQSQQDILqeNTILkATE 646
Cdd:cd14133  153 F-------LTQRLYSYiqsrYYRAPE-VILGL---PYDEKIDMWSLGCILAE-LYTGEPLFPGASEVDQL--ARII-GTI 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 211971036 647 VQFPVKPVVSSEAK-----AFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14133  218 GIPPAHMLDQGKADdelfvDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
419-686 1.84e-22

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: 97.60  E-value: 1.84e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihQLNKSWRDEKKENYHKHAC----REYRIHKELDHPRIVKlYDYFSLDTDTFCTVLEYCE 494
Cdd:cd06628   13 FGSVYLGMNASSGELMAVK--QVELPSVSAENKDRKKSMLdalqREIALLRELQHENIVQ-YLGSSSDANHLNIFLEYVP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 GNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILlVDGTACgeIKITDFGLSKIMDDDSY--G 572
Cdd:cd06628   90 GGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRG--IIHRDIKGANIL-VDNKGG--IKISDFGISKKLEANSLstK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 573 VDGMDLTSQGAgTYWyLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFghnqsqQDILQENTILKATEVQFPVK 652
Cdd:cd06628  165 NNGARPSLQGS-VFW-MAPE--VVKQT--SYTRKADIWSLGCLVVEMLTGTHPF------PDCTQMQAIFKIGENASPTI 232
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 211971036 653 P-VVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06628  233 PsNISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
447-686 2.05e-22

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 101.25  E-value: 2.05e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 447 DEKKENYhkhACREYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCEGNDLDFYLKQ----HKLMSEKEARSIVMQIVN 522
Cdd:PTZ00267 105 DERQAAY---ARSELHCLAACDHFGIVKHFDDFKSD-DKLLLIMEYGSGGDLNKQIKQrlkeHLPFQEYEVGLLFYQIVL 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 523 ALRYLNEIKppIIHYDLKPGNILLVdgtACGEIKITDFGLSKIMDDDSygvdGMDLTSQGAGTYWYLPPECFvvgkEPPK 602
Cdd:PTZ00267 181 ALDEVHSRK--MMHRDLKSANIFLM---PTGIIKLGDFGFSKQYSDSV----SLDVASSFCGTPYYLAPELW----ERKR 247
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 603 ISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntILKATEVQFPVKpvVSSEAKAFIRRCLAYRKEDRFDVHQLAN 682
Cdd:PTZ00267 248 YSKKADMWSLGVILYELLTLHRPF-KGPSQREIMQQ--VLYGKYDPFPCP--VSSGMKALLDPLLSKNPALRPTTQQLLH 322

                 ....
gi 211971036 683 DPYL 686
Cdd:PTZ00267 323 TEFL 326
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
458-686 2.30e-22

Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related Apoptosis-inducing protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DRAKs were named based on their similarity (around 50% identity) to the kinase domain of DAPKs. They contain an N-terminal kinase domain and a C-terminal regulatory domain. Vertebrates contain two subfamily members, DRAK1 (also called STK17A) and DRAK2. Both DRAKs are localized to the nucleus, autophosphorylate themselves, and phosphorylate myosin light chain as a substrate. Rabbit DRAK1 has been shown to induce apoptosis in osteoclasts and overexpressio of human DRAK1 induces apoptosis in cultured fibroblast cells. DRAK1 may be involved in apoptotic signaling. The DRAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271099 [Multi-domain]  Cd Length: 271  Bit Score: 97.31  E-value: 2.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 458 CREYRIHK----EL--DHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL--DFYLKQHKLMSEKEARSIVMQIVNALRYLNE 529
Cdd:cd14197   51 CRMEIIHEiavlELaqANPWVINLHEVYETASEMI-LVLEYAAGGEIfnQCVADREEAFKEKDVKRLMKQILEGVSFLHN 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 530 IKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSYGVDGMdltsqgaGTYWYLPPEcfVVGKEPpkISNKVDV 609
Cdd:cd14197  130 NN--VVHLDLKPQNILLTSESPLGDIKIVDFGLSRILKNSEELREIM-------GTPEYVAPE--ILSYEP--ISTATDM 196
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 610 WSVGVIFFQCLYGRKPFGHNQSQQDILQENTI-LKATEVQFpvkPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14197  197 WSIGVLAYVMLTGISPFLGDDKQETFLNISQMnVSYSEEEF---EHLSESAIDFIKTLLIKKPENRATAEDCLKHPWL 271
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
432-663 2.37e-22

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: 98.54  E-value: 2.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 432 RYAAVKIhqLNKSWRDEKKENyhKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEK 511
Cdd:cd05595   21 RYYAMKI--LRKEVIIAKDEV--AHTVTESRVLQNTRHPFLTALKYAFQ-THDRLCFVMEYANGGELFFHLSRERVFTED 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 512 EARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPP 591
Cdd:cd05595   96 RARFYGAEIVSALEYLHSRD--VVYRDIKLENLMLDKD---GHIKITDFGLCK------EGITDGATMKTFCGTPEYLAP 164
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 592 ECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQentILKATEVQFPVKpvVSSEAKAFI 663
Cdd:cd05595  165 EVL----EDNDYGRAVDWWGLGVVMYEMMCGRLPF-YNQDHERLFE---LILMEEIRFPRT--LSPEAKSLL 226
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
419-677 2.38e-22

Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKDs are important regulators of many intracellular signaling pathways such as ERK and JNK, and cellular processes including the organization of the trans-Golgi network, membrane trafficking, cell proliferation, migration, and apoptosis. They contain N-terminal cysteine-rich zinc binding C1 (PKC conserved region 1), central PH (Pleckstrin Homology), and C-terminal catalytic kinase domains. Mammals harbor three types of PKDs: PKD1 (or PKCmu), PKD2, and PKD3 (or PKCnu). PKDs are activated in a PKC-dependent manner by many agents including diacylglycerol (DAG), PDGF, neuropeptides, oxidative stress, and tumor-promoting phorbol esters, among others. The PKD subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270984 [Multi-domain]  Cd Length: 260  Bit Score: 97.10  E-value: 2.38e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKHacrEYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL 498
Cdd:cd14082   16 FGIVYGGKHRKTGRDVAIKV--IDKLRFPTKQESQLRN---EVAILQQLSHPGVVNLECMFETPERVF-VVMEKLHGDML 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHK-LMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSYgvdgmd 577
Cdd:cd14082   90 EMILSSEKgRLPERITKFLVTQILVALRYLH--SKNIVHCDLKPENVLLASAEPFPQVKLCDFGFARIIGEKSF------ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 lTSQGAGTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILkatevqFPVKP--VV 655
Cdd:cd14082  162 -RRSVVGTPAYLAPE--VLRNKGYNRS--LDMWSVGVIIYVSLSGTFPFNEDEDINDQIQNAAFM------YPPNPwkEI 230
                        250       260
                 ....*....|....*....|..
gi 211971036 656 SSEAKAFIRRCLAYRKEDRFDV 677
Cdd:cd14082  231 SPDAIDLINNLLQVKMRKRYSV 252
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
419-681 2.42e-22

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


Pssm-ID: 270863 [Multi-domain]  Cd Length: 262  Bit Score: 97.34  E-value: 2.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnKSWRDEKKENyhkhAC-REYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGND 497
Cdd:cd08224   13 FSVVYRARCLLDGRLVALKKVQI-FEMMDAKARQ----DClKEIDLLQQLNHPNIIKYLASF-IENNELNIVLELADAGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLK----QHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGV 573
Cdd:cd08224   87 LSRLIKhfkkQKRLIPERTIWKYFVQLCSALEHMHSKR--IMHRDIKPANVFI---TANGVVKLGDLGLGRFFSSKTTAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 574 DGMdltsqgAGTYWYLPPECFvvgKEPPkISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQDILQentilKATEVQFPVK 652
Cdd:cd08224  162 HSL------VGTPYYMSPERI---REQG-YDFKSDIWSLGCLLYEMAALQSPFyGEKMNLYSLCK-----KIEKCEYPPL 226
                        250       260       270
                 ....*....|....*....|....*....|....
gi 211971036 653 P--VVSSEAKAFIRRCLAYRKEDRFD---VHQLA 681
Cdd:cd08224  227 PadLYSQELRDLVAACIQPDPEKRPDisyVLDVA 260
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
419-629 2.43e-22

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: 97.68  E-value: 2.43e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYkafdLYEQRYAAVKIHQlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYD----YFSLDTDTFCTVLEYCE 494
Cdd:cd14039    6 FGNVC----LYQNQETGEKIAI--KSCRLELSVKNKDRWCHEIQIMKKLNHPNVVKACDvpeeMNFLVNDVPLLAMEYCS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 GNDLDFYLKQHKL---MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSy 571
Cdd:cd14039   80 GGDLRKLLNKPENccgLKESQVLSLLSDIGSGIQYLHENK--IIHRDLKPENIVLQEINGKIVHKIIDLGYAKDLDQGS- 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 572 gvdgmdLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFGHN 629
Cdd:cd14039  157 ------LCTSFVGTLQYLAPELF----ENKSYTVTVDYWSFGTMVFECIAGFRPFLHN 204
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
453-692 3.34e-22

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: 97.49  E-value: 3.34e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 453 YHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFCTV-LEYCEGNDLDFYLKQHK----LMSEKEARSIVMQIVNALRYL 527
Cdd:cd06621   42 VQKQILRELEINKSCASPYIVKYYGAFLDEQDSSIGIaMEYCEGGSLDSIYKKVKkkggRIGEKVLGKIAESVLKGLSYL 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 528 NEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSkimdddsyGVDGMDLTSQGAGTYWYLPPEcfvvgkeppKISNK- 606
Cdd:cd06621  122 HSRK--IIHRDIKPSNILL---TRKGQVKLCDFGVS--------GELVNSLAGTFTGTSYYMAPE---------RIQGGp 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 607 ----VDVWSVGVIFFQCLYGRKPFGHNQSQQDILQE--NTILKATEVQFPVKPVV----SSEAKAFIRRCLAYRKEDRFD 676
Cdd:cd06621  180 ysitSDVWSLGLTLLEVAQNRFPFPPEGEPPLGPIEllSYIVNMPNPELKDEPENgikwSESFKDFIEKCLEKDGTRRPG 259
                        250
                 ....*....|....*.
gi 211971036 677 VHQLANDPYLLPHMRR 692
Cdd:cd06621  260 PWQMLAHPWIKAQEKK 275
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
419-702 3.52e-22

C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. They are activated by signaling inputs from extracellular regulated kinase (ERK) and phosphoinositide dependent kinase 1 (PDK1). ERK phosphorylates and activates the CTD of RSK, serving as a docking site for PDK1, which phosphorylates and activates the NTD, which in turn phosphorylates all known RSK substrates. RSKs act as downstream effectors of mitogen-activated protein kinase (MAPK) and play key roles in mitogen-activated cell growth, differentiation, and survival. Mammals possess four RSK isoforms (RSK1-4) from distinct genes. RSK proteins are also referred to as MAP kinase-activated protein kinases (MAPKAPKs), 90 kDa ribosomal protein S6 kinases (p90-RSKs), or p90S6Ks. The RSK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270993 [Multi-domain]  Cd Length: 291  Bit Score: 97.32  E-value: 3.52e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSWRDekkenyhkhaCREyrihkELD-------HPRIVKLYDYFslDTDTFC-TVL 490
Cdd:cd14091   13 YSVCKRCIHKATGKEYAVKI--IDKSKRD----------PSE-----EIEillrygqHPNIITLRDVY--DDGNSVyLVT 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 491 EYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACGE-IKITDFGLSKIMDDD 569
Cdd:cd14091   74 ELLRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLH--SQGVVHRDLKPSNILYADESGDPEsLRICDFGFAKQLRAE 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 570 sygvDGMDLTsqgagtywylPpeCFVVGKEPPKISNK------VDVWSVGVIFFQCLYGRKPF--GHNQSQQDILQenti 641
Cdd:cd14091  152 ----NGLLMT----------P--CYTANFVAPEVLKKqgydaaCDIWSLGVLLYTMLAGYTPFasGPNDTPEVILA---- 211
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 642 lKATEVQFPVK----PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLL--PHMRRSNSSGNLHMA 702
Cdd:cd14091  212 -RIGSGKIDLSggnwDHVSDSAKDLVRKMLHVDPSQRPTAAQVLQHPWIRnrDSLPQRQLTDPQDAA 277
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
419-686 3.60e-22

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: 96.70  E-value: 3.60e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSwrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCEGNDL 498
Cdd:cd06632   13 FGSVYEGFNGDTGDFFAVKEVSLVDD--DKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREE-DNLYIFLEYVPGGSI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNIlLVDGTacGEIKITDFGLSKImdddsygVDGMDL 578
Cdd:cd06632   90 HKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRN--TVHRDIKGANI-LVDTN--GVVKLADFGMAKH-------VEAFSF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPEcfVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQentILKATEVqfPVKP-VVSS 657
Cdd:cd06632  158 AKSFKGSPYWMAPE--VIMQKNSGYGLAVDIWSLGCTVLEMATGKPPWSQYEGVAAIFK---IGNSGEL--PPIPdHLSP 230
                        250       260
                 ....*....|....*....|....*....
gi 211971036 658 EAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06632  231 DAKDFIRLCLQRDPEDRPTASQLLEHPFV 259
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
419-686 4.72e-22

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: 96.25  E-value: 4.72e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSwRDEKKENYHKhacrEYRIHKELDHPRIVKLYDYfSLDTDTFCTVLEYCEGNDL 498
Cdd:cd14069   14 FGEVFLAVNRNTEEAVAVKFVDMKRA-PGDCPENIKK----EVCIQKMLSHKNVVRFYGH-RREGEFQYLFLEYASGGEL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvDGTacGEIKITDFGLSKImdddsYGVDGMDL 578
Cdd:cd14069   88 FDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCG--ITHRDIKPENLLL-DEN--DNLKISDFGLATV-----FRYKGKER 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGA-GTYWYLPPECFvvgKEPPKISNKVDVWSVGVIFFQCLYGRKPFGH-NQSQQDILQ--ENTILKATevqfPVKPv 654
Cdd:cd14069  158 LLNKMcGTLPYVAPELL---AKKKYRAEPVDVWSCGIVLFAMLAGELPWDQpSDSCQEYSDwkENKKTYLT----PWKK- 229
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 655 VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14069  230 IDTAALSLLRKILTENPNKRITIEDIKKHPWY 261
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
406-673 4.87e-22

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: 98.10  E-value: 4.87e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 406 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTD- 484
Cdd:cd07880   15 DRYRDLKQVGSGAYGTVCSALDRRTGAKVAIK-----KLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSl 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 485 ----TFCTVLEYCeGNDLDFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNilLVDGTACgEIKITDF 560
Cdd:cd07880   90 drfhDFYLVMPFM-GTDLGKLMKHEKL-SEDRIQFLVYQMLKGLKYIHAAG--IIHRDLKPGN--LAVNEDC-ELKILDF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 561 GLSKIMDDDSYGVdgmdltsqgAGTYWYLPPECFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQdiLQEN 639
Cdd:cd07880  163 GLARQTDSEMTGY---------VVTRWYRAPEVILNWM---HYTQTVDIWSVGCIMAEMLTGKPLFkGHDHLDQ--LMEI 228
                        250       260       270
                 ....*....|....*....|....*....|....
gi 211971036 640 TILKATEVQFPVKPVVSSEAKAFIRRCLAYRKED 673
Cdd:cd07880  229 MKVTGTPSKEFVQKLQSEDAKNYVKKLPRFRKKD 262
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
419-686 6.42e-22

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: 96.45  E-value: 6.42e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihqlnkswrDEKKENYHKHAC---REYRIHKEL-DHPRIVKLYDYFsLDTDTFCTVLEYCE 494
Cdd:cd07830   12 FGSVYLARNKETGELVAIK---------KMKKKFYSWEECmnlREVKSLRKLnEHPNIVKLKEVF-RENDELYFVFEYME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 GNDLDFYLKQ-HKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNIlLVDGTACgeIKITDFGLSK-IMDDDSYg 572
Cdd:cd07830   82 GNLYQLMKDRkGKPFSESVIRSIIYQILQGLAHIH--KHGFFHRDLKPENL-LVSGPEV--VKIADFGLAReIRSRPPY- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 573 vdgMDLTSqgagTYWYLPPECFVvgkEPPKISNKVDVWSVGVIFFQcLYGRKP-F-GHNQSQQ-----DIL---QENT-- 640
Cdd:cd07830  156 ---TDYVS----TRWYRAPEILL---RSTSYSSPVDIWALGCIMAE-LYTLRPlFpGSSEIDQlykicSVLgtpTKQDwp 224
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 641 ----ILKATEVQFP---------VKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd07830  225 egykLASKLGFRFPqfaptslhqLIPNASPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
455-689 8.78e-22

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: 97.16  E-value: 8.78e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 455 KHACREYRIHKELDHPRIVKLYDYFS-------------LDTDTFCTVLEYCEgNDLDFYLKQHKLmSEKEARSIVMQIV 521
Cdd:cd07854   47 KHALREIKIIRRLDHDNIVKVYEVLGpsgsdltedvgslTELNSVYIVQEYME-TDLANVLEQGPL-SEEHARLFMYQLL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 522 NALRYLNEIKppIIHYDLKPGNILLvdGTACGEIKITDFGLSKIMDDDsYGVDGMdlTSQGAGTYWYLPPECFVvgkEPP 601
Cdd:cd07854  125 RGLKYIHSAN--VLHRDLKPANVFI--NTEDLVLKIGDFGLARIVDPH-YSHKGY--LSEGLVTKWYRSPRLLL---SPN 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 602 KISNKVDVWSVGVIFFQCLYGRKPF--GHNQSQ-QDILQ---------ENTILKA---------TEVQFPVK---PVVSS 657
Cdd:cd07854  195 NYTKAIDMWAAGCIFAEMLTGKPLFagAHELEQmQLILEsvpvvreedRNELLNVipsfvrndgGEPRRPLRdllPGVNP 274
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 658 EAKAFIRRCLAYRKEDRFDVHQLANDPYLLPH 689
Cdd:cd07854  275 EALDFLEQILTFNPMDRLTAEEALMHPYMSCY 306
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
419-674 9.18e-22

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: 95.90  E-value: 9.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnkswRDEKKENyhKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd14046   19 FGQVVKVRNKLDGRYYAIKKIKL----RSESKNN--SRILREVMLLSRLNHQHVVRYYQAW-IERANLYIQMEYCEKSTL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMD----------- 567
Cdd:cd14046   92 RDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQG--IIHRDLKPVNIFL---DSNGNVKIGDFGLATSNKlnvelatqdin 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 568 --DDSYGVDGMDLTSQgAGTYWYLPPEcfVVGKEPPKISNKVDVWSVGVIFFQCLYgrkPFGHNQSQQDILqenTILKAT 645
Cdd:cd14046  167 ksTSAALGSSGDLTGN-VGTALYVAPE--VQSGTKSTYNEKVDMYSLGIIFFEMCY---PFSTGMERVQIL---TALRSV 237
                        250       260       270
                 ....*....|....*....|....*....|.
gi 211971036 646 EVQFPVKPVVSSEAKAF--IRRCLAYRKEDR 674
Cdd:cd14046  238 SIEFPPDFDDNKHSKQAklIRWLLNHDPAKR 268
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
443-685 9.35e-22

Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Syk-like subfamily is composed of Syk, ZAP-70, Shark, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. They are involved in the signaling downstream of activated receptors (including B-cell, T-cell, and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. Syk is important in B-cell receptor signaling, while Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor signaling. Syk also plays a central role in Fc receptor-mediated phagocytosis in the adaptive immune system. Shark is exclusively expressed in ectodermally derived epithelia, and is localized preferentially to the apical surface of the epithelial cells, it may play a role in a signaling pathway for epithelial cell polarity. The Syk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270650 [Multi-domain]  Cd Length: 257  Bit Score: 95.49  E-value: 9.35e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYfsLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVN 522
Cdd:cd05060   29 KTLKQEHEKAGKKEFLREASVMAQLDHPCIVRLIGV--CKGEPLMLVMELAPLGPLLKYLKKRREIPVSDLKELAHQVAM 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 523 ALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIM--DDDSYgvdgmdlTSQGAGTY---WYlPPECFVVG 597
Cdd:cd05060  107 GMAYLESKH--FVHRDLAARNVLLVNR---HQAKISDFGMSRALgaGSDYY-------RATTAGRWplkWY-APECINYG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 598 keppKISNKVDVWSVGVIFFQCL-YGRKPFGhNQSQQDILQentILKATEvQFPVKPVVSSEAKAFIRRCLAYRKEDRFD 676
Cdd:cd05060  174 ----KFSSKSDVWSYGVTLWEAFsYGAKPYG-EMKGPEVIA---MLESGE-RLPRPEECPQEIYSIMLSCWKYRPEDRPT 244
                        250
                 ....*....|...
gi 211971036 677 VHQL----ANDPY 685
Cdd:cd05060  245 FSELestfRRDPE 257
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
419-626 1.12e-21

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: 96.58  E-value: 1.12e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKHACREYRIhKELDHPRIVKLYdyFSLDT-DTFCTVLEYCEGND 497
Cdd:cd05603    8 FGKVLLAKRKCDGKFYAVKV--LQKKTILKKKEQNHIMAERNVLL-KNLKHPFLVGLH--YSFQTsEKLYFVLDYVNGGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddsYGVDGMD 577
Cdd:cd05603   83 LFFHLQRERCFLEPRARFYAAEVASAIGYLHSLN--IIYRDLKPENILL---DCQGHVVLTDFGLCK------EGMEPEE 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 211971036 578 LTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd05603  152 TTSTFCGTPEYLAPE--VLRKEP--YDRTVDWWCLGAVLYEMLYGLPPF 196
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
460-685 1.54e-21

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: 94.63  E-value: 1.54e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDL 539
Cdd:cd14185   48 EILIIKSLSHPNIVKLFEVYETEKEIY-LILEYVRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHS--KHIVHRDL 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 540 KPGNILL---VDGTAcgEIKITDFGLSKIMDDDSYGVdgmdltsqgAGTYWYLPPEcFVVGKeppKISNKVDVWSVGVIF 616
Cdd:cd14185  125 KPENLLVqhnPDKST--TLKLADFGLAKYVTGPIFTV---------CGTPTYVAPE-ILSEK---GYGLEVDMWAAGVIL 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 617 FQCLYGRKPFGHNQSQQDILQEntILKATEVQF--PVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14185  190 YILLCGFPPFRSPERDQEELFQ--IIQLGHYEFlpPYWDNISEAAKDLISRLLVVDPEKRYTAKQVLQHPW 258
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
419-682 2.06e-21

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: 96.21  E-value: 2.06e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDT--DTFCTVLEYCE-- 494
Cdd:cd07851   28 YGQVCSAFDTKTGRKVAIK-----KLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVFTPASslEDFQDVYLVTHlm 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 GNDLDFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtaCgEIKITDFGLSKIMDDDSYGVd 574
Cdd:cd07851  103 GADLNNIVKCQKL-SDDHIQFLVYQILRGLKYIHSAG--IIHRDLKPSNLAVNED--C-ELKILDFGLARHTDDEMTGY- 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 575 gmdltsqgAGTYWYLPPECfvvgkeppkISNK------VDVWSVGVIFFQCLYGRKPF-GHNQsqqdILQENTILKATEV 647
Cdd:cd07851  176 --------VATRWYRAPEI---------MLNWmhynqtVDIWSVGCIMAELLTGKTLFpGSDH----IDQLKRIMNLVGT 234
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 211971036 648 QFP--VKPVVSSEAKAFIRRCLAYRKEDRFDVHQLAN 682
Cdd:cd07851  235 PDEelLKKISSESARNYIQSLPQMPKKDFKEVFSGAN 271
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
463-681 2.75e-21

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: 94.11  E-value: 2.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 463 IHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEG---NDLDFYLKQ-HKLMSEKEARSIVMQIVNALRYLNEIKPpIIHYD 538
Cdd:cd08528   62 IKEQLRHPNIVRYYKTF-LENDRLYIVMELIEGaplGEHFSSLKEkNEHFTEDRIWNIFVQMVLALRYLHKEKQ-IVHRD 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLVDGTacgEIKITDFGLSKimdddSYGVDGMDLTSQgAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQ 618
Cdd:cd08528  140 LKPNNIMLGEDD---KVTITDFGLAK-----QKGPESSKMTSV-VGTILYSCPE--IVQNEP--YGEKADIWALGCILYQ 206
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 211971036 619 CLYGRKPFghnQSQQDILQENTILKAtevQF-PVKPVVSSEAKAF-IRRCLAYRKEDRFDVHQLA 681
Cdd:cd08528  207 MCTLQPPF---YSTNMLTLATKIVEA---EYePLPEGMYSDDITFvIRSCLTPDPEARPDIVEVS 265
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
419-686 2.85e-21

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: 94.15  E-value: 2.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNK----SWRDEKKEnyhkhacREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCE 494
Cdd:cd14097   14 FGVVIEATHKETQTKWAIKK--INRekagSSAVKLLE-------REVDILKHVNHAHIIHLEEVFETPKRMY-LVMELCE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 GNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNIL----LVDGTACGEIKITDFGLSKImdddS 570
Cdd:cd14097   84 DGELKELLLRKGFFSENETRHIIQSLASAVAYLH--KNDIVHRDLKLENILvkssIIDNNDKLNIKVTDFGLSVQ----K 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 571 YGVdGMDLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntiLKATEVQFP 650
Cdd:cd14097  158 YGL-GEDMLQETCGTPIYMAPEVI----SAHGYSQQCDIWSIGVIMYMLLCGEPPF-VAKSEEKLFEE---IRKGDLTFT 228
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 211971036 651 --VKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14097  229 qsVWQSVSDAAKNVLQQLLKVDPAHRMTASELLDNPWI 266
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
433-686 3.02e-21

Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DAPKs mediate cell death and act as tumor suppressors. They are necessary to induce cell death and their overexpression leads to death-associated changes including membrane blebbing, cell rounding, and formation of autophagic vesicles. Vertebrates contain three subfamily members with different domain architecture, localization, and function. DAPK3, also called DAP-like kinase (DLK) and zipper-interacting protein kinase (ZIPk), contains an N-terminal kinase domain and a C-terminal region with nuclear localization signals (NLS) and a leucine zipper motif that mediates homodimerization and interaction with other leucine zipper proteins. It interacts with Par-4, a protein that contains a death domain and interacts with actin filaments. DAPK3 is present in both the cytoplasm and nucleus. Its co-expression with Par-4 results in the co-localization of the two proteins to actin filaments. In addition to cell death, DAPK3 is also implicated in mediating cell motility and the contraction of smooth muscles. The DAPK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271097 [Multi-domain]  Cd Length: 271  Bit Score: 94.30  E-value: 3.02e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 433 YAA--VKIHQLNKSWRDEKKENYHkhacREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSE 510
Cdd:cd14195   33 YAAkfIKKRRLSSSRRGVSREEIE----REVNILREIQHPNIITLHDIFENKTDVV-LILELVSGGELFDFLAEKESLTE 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 511 KEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACG-EIKITDFGLskimdddSYGVDGMDLTSQGAGTYWYL 589
Cdd:cd14195  108 EEATQFLKQILDGVHYLHSKR--IAHFDLKPENIMLLDKNVPNpRIKLIDFGI-------AHKIEAGNEFKNIFGTPEFV 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 590 PPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDIlqenTILKATEVQFPVK--PVVSSEAKAFIRRCL 667
Cdd:cd14195  179 APE--IVNYEP--LGLEADMWSIGVITYILLSGASPFLGETKQETL----TNISAVNYDFDEEyfSNTSELAKDFIRRLL 250
                        250
                 ....*....|....*....
gi 211971036 668 AYRKEDRFDVHQLANDPYL 686
Cdd:cd14195  251 VKDPKKRMTIAQSLEHSWI 269
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
469-688 3.28e-21

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: 95.11  E-value: 3.28e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVD 548
Cdd:cd14179   61 HPNIVKLHEVYHDQLHTF-LVMELLKGGELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVG--VVHRDLKPENLLFTD 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 549 GTACGEIKITDFGLSKIMDDDSYgvdgmdltsqgagtywYLPPECFVVGKEPPKISNK------VDVWSVGVIFFQCLYG 622
Cdd:cd14179  138 ESDNSEIKIIDFGFARLKPPDNQ----------------PLKTPCFTLHYAAPELLNYngydesCDLWSLGVILYTMLSG 201
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 623 RKPF-GHNQSQQDILQENTILKATEVQFPVK----PVVSSEAKAFIRRCLAYRKEDRF------------DVHQLANDPY 685
Cdd:cd14179  202 QVPFqCHDKSLTCTSAEEIMKKIKQGDFSFEgeawKNVSQEAKDLIQGLLTVDPNKRIkmsglrynewlqDGSQLSSNPL 281

                 ...
gi 211971036 686 LLP 688
Cdd:cd14179  282 MTP 284
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
431-674 3.83e-21

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: 93.83  E-value: 3.83e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 431 QRYAAvKIHQLNKSWRDEKKENYHKHACREYrihkELDHPRIVKLYDYFSLDTDtFCTVLEYCEGNDLdFYL---KQHKL 507
Cdd:cd14198   34 QEYAA-KFLKKRRRGQDCRAEILHEIAVLEL----AKSNPRVVNLHEVYETTSE-IILILEYAAGGEI-FNLcvpDLAEM 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 508 MSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSYgvdgmdlTSQGAGTYW 587
Cdd:cd14198  107 VSENDIIRLIRQILEGVYYLHQ--NNIVHLDLKPQNILLSSIYPLGDIKIVDFGMSRKIGHACE-------LREIMGTPE 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 588 YLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTI-LKATEVQFpvkPVVSSEAKAFIRRC 666
Cdd:cd14198  178 YLAPE--ILNYDP--ITTATDMWNIGVIAYMLLTHESPFVGEDNQETFLNISQVnVDYSEETF---SSVSQLATDFIQKL 250

                 ....*...
gi 211971036 667 LAYRKEDR 674
Cdd:cd14198  251 LVKNPEKR 258
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
419-638 4.07e-21

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: 93.67  E-value: 4.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKEnyhkhACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL 498
Cdd:cd13978    6 FGTVSKARHVSWFGMVAIKCLHSSPNCIEERKA-----LLKEAEKMERARHSYVLPLLGVCV-ERRSLGLVMEYMENGSL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQhKLMSEKEARS--IVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTacgEIKITDFGLSKImDDDSYGVDGM 576
Cdd:cd13978   80 KSLLER-EIQDVPWSLRfrIIHEIALGMNFLHNMDPPLLHHDLKPENILLDNHF---HVKISDFGLSKL-GMKSISANRR 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 577 DLTSQGAGTYWYLPPECFVVGKEPPkiSNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQE 638
Cdd:cd13978  155 RGTENLGGTPIYMAPEAFDDFNKKP--TSKSDVYSFAIVIWAVLTRKEPFENAINPLLIMQI 214
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
459-686 6.16e-21

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: 92.83  E-value: 6.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL-DFYLKQHKLmSEKEARSIVMQIVNALRYLNEikPPIIHY 537
Cdd:cd14078   50 TEIEALKNLSHQHICRLYHVIETDNKIF-MVLEYCPGGELfDYIVAKDRL-SEDEARVFFRQIVSAVAYVHS--QGYAHR 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLVDGTacgEIKITDFGLSKIMDDdsyGVDGMDLTSQGAGTywYLPPEcFVVGKepPKISNKVDVWSVGVIFF 617
Cdd:cd14078  126 DLKPENLLLDEDQ---NLKLIDFGLCAKPKG---GMDHHLETCCGSPA--YAAPE-LIQGK--PYIGSEADVWSMGVLLY 194
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 618 QCLYGRKPFGHNqsqqdilqeNTIL---KATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14078  195 ALLCGFLPFDDD---------NVMAlyrKIQSGKYEEPEWLSPSSKLLLDQMLQVDPKKRITVKELLNHPWV 257
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
443-685 6.48e-21

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: 93.12  E-value: 6.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDEKKenyhkhACREYRIH-KELDHPRIVKLYD-YFSLDTDTFC--TVLEYCEGNDLDFYLKQHKL--MSEKEARSI 516
Cdd:cd14089   32 KVLRDNPK------ARREVELHwRASGCPHIVRIIDvYENTYQGRKCllVVMECMEGGELFSRIQERADsaFTEREAAEI 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 517 VMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKImdddsygVDGMDLTSQGAGTYWYLPPEcfVV 596
Cdd:cd14089  106 MRQIGSAVAHLHSMN--IAHRDLKPENLLYSSKGPNAILKLTDFGFAKE-------TTTKKSLQTPCYTPYYVAPE--VL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 597 GKEppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQFPVK--PVVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd14089  175 GPE--KYDKSCDMWSLGVIMYILLCGYPPFYSNHGLAISPGMKKRIRNGQYEFPNPewSNVSEEAKDLIRGLLKTDPSER 252
                        250
                 ....*....|.
gi 211971036 675 FDVHQLANDPY 685
Cdd:cd14089  253 LTIEEVMNHPW 263
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
419-674 6.79e-21

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: 92.80  E-value: 6.79e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENyhKHACREYRIHKELDHPRIVKlydYFSLDTD--TFCTVLEYCEGN 496
Cdd:cd06625   13 FGQVYLCYDADTGRELAVKQVEIDPINTEASKEV--KALECEIQLLKNLQHERIVQ---YYGCLQDekSLSIFMEYMPGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 497 DLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvDGTacGEIKITDFGLSKIMDDDSYGVDGM 576
Cdd:cd06625   88 SVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNM--IVHRDIKGANILR-DSN--GNVKLGDFGASKRLQTICSSTGMK 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 577 DLTsqgaGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTilKATEVQFPvkPVVS 656
Cdd:cd06625  163 SVT----GTPYWMSPE--VINGE--GYGRKADIWSVGCTVVEMLTTKPPWAEFEPMAAIFKIAT--QPTNPQLP--PHVS 230
                        250
                 ....*....|....*...
gi 211971036 657 SEAKAFIRRCLAYRKEDR 674
Cdd:cd06625  231 EDARDFLSLIFVRNKKQR 248
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
422-686 7.29e-21

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: 93.55  E-value: 7.29e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKIHQLNKswrdeKKENYHKHACREYRIHKEL-DHPRIVKLYDYFSLDTDtFCTVLEYCeGNDLDF 500
Cdd:cd07832   16 VFKAKDRETGETVALKKVALRK-----LEGGIPNQALREIKALQACqGHPYVVKLRDVFPHGTG-FVLVFEYM-LSSLSE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 501 YLK--QHKLmSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDsygvDGMDL 578
Cdd:cd07832   89 VLRdeERPL-TEAQVKRYMRMLLKGVAYMHANR--IMHRDLKPANLLISST---GVLKIADFGLARLFSEE----DPRLY 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQgAGTYWYLPPEcFVVGKepPKISNKVDVWSVGVIFFQCLYGRKPF-GHNqsqqDILQENTILK-------------- 643
Cdd:cd07832  159 SHQ-VATRWYRAPE-LLYGS--RKYDEGVDLWAVGCIFAELLNGSPLFpGEN----DIEQLAIVLRtlgtpnektwpelt 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036 644 ----ATEVQFP---------VKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd07832  231 slpdYNKITFPeskgirleeIFPDCSPEAIDLLKGLLVYNPKKRLSAEEALRHPYF 286
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
419-686 7.72e-21

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: 92.92  E-value: 7.72e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDekkeNYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFCTVLEYCEGNDL 498
Cdd:cd14165   14 YAKVKSAYSERLKCNVAIKIIDKKKAPDD----FVEKFLPRELEILARLNHKSIIKTYEIFETSDGKVYIVMELGVQGDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacgEIKITDFGLSKIMDDDSYGvdGMDL 578
Cdd:cd14165   90 LEFIKLRGALPEDVARKMFHQLSSAIKYCHELD--IVHRDLKCENLLLDKDF---NIKLTDFGFSKRCLRDENG--RIVL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPECFVVGKEPPKISnkvDVWSVGVIFFQCLYGRKPFghnqSQQDILQENTILKATEVQFPVKPVVSSE 658
Cdd:cd14165  163 SKTFCGSAAYAAPEVLQGIPYDPRIY---DIWSLGVILYIMVCGSMPY----DDSNVKKMLKIQKEHRVRFPRSKNLTSE 235
                        250       260
                 ....*....|....*....|....*...
gi 211971036 659 AKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14165  236 CKDLIYRLLQPDVSQRLCIDEVLSHPWL 263
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
422-685 8.48e-21

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: 92.72  E-value: 8.48e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFdlYEQRYAAVKihqlnKSWRDekkenYHKHACREYRIHKELD-HPRIVKlydYFSLDTD-TFC-TVLEYCEGNDL 498
Cdd:cd13982   18 VFRGT--FDGRPVAVK-----RLLPE-----FFDFADREVQLLRESDeHPNVIR---YFCTEKDrQFLyIALELCAASLQ 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHK----LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIK--ITDFGLSKIMDDDSYG 572
Cdd:cd13982   83 DLVESPREsklfLRPGLEPVRLLRQIASGLAHLHSLN--IVHRDLKPQNILISTPNAHGNVRamISDFGLCKKLDVGRSS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 573 VDGmdlTSQGAGTYWYLPPECFvVGKEPPKISNKVDVWSVGVIFFQCL-YGRKPFGHNQSQQ-DILQENTILKA--TEVQ 648
Cdd:cd13982  161 FSR---RSGVAGTSGWIAPEML-SGSTKRRQTRAVDIFSLGCVFYYVLsGGSHPFGDKLEREaNILKGKYSLDKllSLGE 236
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 211971036 649 FPVkpvvssEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd13982  237 HGP------EAQDLIERMIDFDPEKRPSAEEVLNHPF 267
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
459-667 9.92e-21

Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle preferentially expressed protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The Striated muscle preferentially expressed gene (SPEG) generates 4 different isoforms through alternative promoter use and splicing in a tissue-specific manner: SPEGalpha and SPEGbeta are expressed in cardiac and skeletal striated muscle; Aortic Preferentially Expressed Protein-1 (APEG-1) is expressed in vascular smooth muscle; and Brain preferentially expressed gene (BPEG) is found in the brain and aorta. SPEG proteins have mutliple immunoglobulin (Ig), 2 fibronectin type III (FN3), and two kinase domains. They are necessary for cardiac development and survival. The SPEG subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271013 [Multi-domain]  Cd Length: 257  Bit Score: 92.19  E-value: 9.92e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYD 538
Cdd:cd14111   48 QEYEILKSLHHERIMALHEAY-ITPRYLVLIAEFCSGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRR--VLHLD 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLVDGTAcgeIKITDFGLSKimdddSYGVDGMDLTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQ 618
Cdd:cd14111  125 IKPDNIMVTNLNA---IKIVDFGSAQ-----SFNPLSLRQLGRRTGTLEYMAPE--MVKGEP--VGPPADIWSIGVLTYI 192
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 211971036 619 CLYGRKPFghnQSQQDILQENTILKATEVQFPVKPVVSSEAKAFIRRCL 667
Cdd:cd14111  193 MLSGRSPF---EDQDPQETEAKILVAKFDAFKLYPNVSQSASLFLKKVL 238
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
446-686 1.23e-20

Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase (also called MAK-V); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HUNK/MAK-V was identified from a mammary tumor in an MMTV-neu transgenic mouse. It is required for the metastasis of c-myc-induced mammary tumors, but is not necessary for c-myc-induced primary tumor formation or normal development. It is required for HER2/neu-induced tumor formation and maintenance of the cells' tumorigenic phenotype. It is over-expressed in aggressive subsets of ovary, colon, and breast carcinomas. HUNK interacts with synaptopodin, and may also play a role in synaptic plasticity. The HUNK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270972 [Multi-domain]  Cd Length: 262  Bit Score: 92.19  E-value: 1.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 446 RDEKKENY-HKHACREYRIHKELDHPRIVKLYDyfSLDTD-TFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNA 523
Cdd:cd14070   38 KKAKKDSYvTKNLRREGRIQQMIRHPNITQLLD--ILETEnSYYLVMELCPGGNLMHRIYDKKRLEEREARRYIRQLVSA 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 524 LRYLNeiKPPIIHYDLKPGNILLVDGTacgEIKITDFGLSkimddDSYGVDGM-DLTSQGAGTYWYLPPECFVVGKEPPk 602
Cdd:cd14070  116 VEHLH--RAGVVHRDLKIENLLLDEND---NIKLIDFGLS-----NCAGILGYsDPFSTQCGSPAYAAPELLARKKYGP- 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 603 isnKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEvqfPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLAN 682
Cdd:cd14070  185 ---KVDVWSIGVNMYAMLTGTLPFTVEPFSLRALHQKMVDKEMN---PLPTDLSPGAISFLRSLLEPDPLKRPNIKQALA 258

                 ....
gi 211971036 683 DPYL 686
Cdd:cd14070  259 NRWL 262
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
460-685 1.32e-20

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called Doublecortin-like and CAM kinase-like 2); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL2 (or DCAMKL2) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL2 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL2 has been shown to interact with tubulin, JIP1/2, JNK, neurabin 2, and actin. It is associated with the terminal segments of axons and dendrites, and may function as a phosphorylation-dependent switch to control microtubule dynamics in neuronal growth cones. The DCKL2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271086 [Multi-domain]  Cd Length: 259  Bit Score: 92.02  E-value: 1.32e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDL 539
Cdd:cd14184   49 EVSILRRVKHPNIIMLIEEMDTPAELY-LVMELVKGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLC--IVHRDI 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 540 KPGNILLV---DGTAcgEIKITDFGLSKIMDDDSYGVdgmdltsqgAGTYWYLPPEcfVVGKEPPKIsnKVDVWSVGVIF 616
Cdd:cd14184  126 KPENLLVCeypDGTK--SLKLGDFGLATVVEGPLYTV---------CGTPTYVAPE--IIAETGYGL--KVDIWAAGVIT 190
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 617 FQCLYGRKPFGHNQSQQDILQENTILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14184  191 YILLCGFPPFRSENNLQEDLFDQILLGKLEFPSPYWDNITDSAKELISHMLQVNVEARYTAEQILSHPW 259
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
419-628 1.45e-20

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated Kinase-1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAK1 is also known as mitogen-activated protein kinase kinase kinase 7 (MAPKKK7 or MAP3K7), TAK, or MEKK7. As a MAPKKK, it is an important mediator of cellular responses to extracellular signals. It regulates both the c-Jun N-terminal kinase and p38 MAPK cascades by activating the MAPK kinases, MKK4 and MKK3/6. In addition, TAK1 plays diverse roles in immunity and development, in different biological contexts, through many signaling pathways including TGFbeta/BMP, Wnt/Fz, and NF-kB. It is also implicated in the activation of the tumor suppressor kinase, LKB1. The TAK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270960 [Multi-domain]  Cd Length: 253  Bit Score: 91.73  E-value: 1.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfdLYEQRYAAVKIHQLNKswrdEKKEnyhkhACREYRIHKELDHPRIVKLYDYFSLDTDTfCTVLEYCEGNDL 498
Cdd:cd14058    6 FGVVCKA--RWRNQIVAVKIIESES----EKKA-----FEVEVRQLSRVDHPNIIKLYGACSNQKPV-CLVMEYAEGGSL 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYL--KQHKLM-SEKEARSIVMQIVNALRYLNEIKP-PIIHYDLKPGNILLvdgTACGE-IKITDFGLSkimdddsygV 573
Cdd:cd14058   74 YNVLhgKEPKPIyTAAHAMSWALQCAKGVAYLHSMKPkALIHRDLKPPNLLL---TNGGTvLKICDFGTA---------C 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 211971036 574 DGMDLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFGH 628
Cdd:cd14058  142 DISTHMTNNKGSAAWMAPEVF----EGSKYSEKCDVFSWGIILWEVITRRKPFDH 192
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
459-686 1.67e-20

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: 92.32  E-value: 1.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYfsLD---TDTFCTVLEYCEGNDLdFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppII 535
Cdd:cd14200   72 QEIAILKKLDHVNIVKLIEV--LDdpaEDNLYMVFDLLRKGPV-MEVPSDKPFSEDQARLYFRDIVLGIEYLHYQK--IV 146
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 536 HYDLKPGNILLVDGtacGEIKITDFGLSKIMDddsyGVDGmdLTSQGAGTYWYLPPEcfVVGKEPPKISNK-VDVWSVGV 614
Cdd:cd14200  147 HRDIKPSNLLLGDD---GHVKIADFGVSNQFE----GNDA--LLSSTAGTPAFMAPE--TLSDSGQSFSGKaLDVWAMGV 215
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 615 IFFQCLYGRKPFghnqSQQDILQENTILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14200  216 TLYCFVYGKCPF----IDEFILALHNKIKNKPVEFPEEPEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
457-630 2.31e-20

Catalytic domain of Cyclin-Dependent protein Kinase 8-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 CDK8, CDC2L6, and similar proteins. CDK8 functions 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-dependent transcription. CDC2L6 also associates with Mediator in complexes lacking CDK8. In VP16-dependent transcriptional activation, CDK8 and CDC2L6 exerts opposing effects by positive and negative regulation, respectively, in similar conditions. 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-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: 270834 [Multi-domain]  Cd Length: 316  Bit Score: 92.73  E-value: 2.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 457 ACREYRIHKELDHPRIVKLYDYFsLDTDTFCT--VLEYCEgNDLDFYLKQH-----KLMSEKEARSIVMQIVNALRYLNE 529
Cdd:cd07842   49 ACREIALLRELKHENVVSLVEVF-LEHADKSVylLFDYAE-HDLWQIIKFHrqakrVSIPPSMVKSLLWQILNGIHYLHS 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 530 ikPPIIHYDLKPGNILLV-DGTACGEIKITDFGLSKIMDDDS---YGVDGMDLtsqgagTYWYLPPECFVVGKEPPKisn 605
Cdd:cd07842  127 --NWVLHRDLKPANILVMgEGPERGVVKIGDLGLARLFNAPLkplADLDPVVV------TIWYRAPELLLGARHYTK--- 195
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 211971036 606 KVDVWSVGVIF---------FQC----LYGRKPFGHNQ 630
Cdd:cd07842  196 AIDIWAIGCIFaelltlepiFKGreakIKKSNPFQRDQ 233
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
431-675 2.39e-20

Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The inactive PKA holoenzyme is a heterotetramer composed of two phosphorylated and active catalytic subunits with a dimer of regulatory (R) subunits. Activation is achieved through the binding of the important second messenger cAMP to the R subunits, which leads to the dissociation of PKA into the R dimer and two active subunits. PKA is present ubiquitously in cells and interacts with many different downstream targets. It plays a role in the regulation of diverse processes such as growth, development, memory, metabolism, gene expression, immunity, and lipolysis. The PKA subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271111 [Multi-domain]  Cd Length: 290  Bit Score: 92.08  E-value: 2.39e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 431 QRYAAVKIhqLNKswrdEK--KENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLM 508
Cdd:cd14209   26 GNYYAMKI--LDK----QKvvKLKQVEHTLNEKRILQAINFPFLVKLEYSFK-DNSNLYMVMEYVPGGEMFSHLRRIGRF 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 509 SEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvDGTacGEIKITDFGLSKIMDDDsygvdgmdlTSQGAGTYWY 588
Cdd:cd14209   99 SEPHARFYAAQIVLAFEYLHSLD--LIYRDLKPENLLI-DQQ--GYIKVTDFGFAKRVKGR---------TWTLCGTPEY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 589 LPPECFvvgkePPKISNK-VDVWSVGVIFFQCLYGRKPFGHNQSqqdILQENTILKAtEVQFPVKpvVSSEAKAFIRRCL 667
Cdd:cd14209  165 LAPEII-----LSKGYNKaVDWWALGVLIYEMAAGYPPFFADQP---IQIYEKIVSG-KVRFPSH--FSSDLKDLLRNLL 233

                 ....*...
gi 211971036 668 AYRKEDRF 675
Cdd:cd14209  234 QVDLTKRF 241
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
419-626 2.61e-20

Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of RIP4, ankyrin (ANK) repeat and kinase domain containing 1 (ANKK1), and similar proteins, all of which harbor C-terminal ANK repeats. RIP4, also called Protein Kinase C-associated kinase (PKK), regulates keratinocyte differentiation and cutaneous inflammation. It activates NF-kappaB and is important in the survival of diffuse large B-cell lymphoma cells. The ANKK1 protein, also called PKK2, has not been studied extensively. The ANKK1 gene, located less than 10kb downstream of the D2 dopamine receptor (DRD2) locus, is altered in the Taq1 A1 polymorphism, which is related to a reduced DRD2 binding affinity and consequently, to mental disorders. The RIP4-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: 270927 [Multi-domain]  Cd Length: 267  Bit Score: 91.40  E-value: 2.61e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSwrDEKKENYhkhACREYRIHKELDHPRIVKLYDYFSldtDTFCTVLEYCEGNDL 498
Cdd:cd14025    9 FGQVYKVRHKHWKTWLAIKCPPSLHV--DDSERME---LLEEAKKMEMAKFRHILPVYGICS---EPVGLVMEYMETGSL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARsIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTacgEIKITDFGLSKIMDddsyGVDGMDL 578
Cdd:cd14025   81 EKLLASEPLPWELRFR-IIHETAVGMNFLHCMKPPLLHLDLKPANILLDAHY---HVKISDFGLAKWNG----LSHSHDL 152
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 211971036 579 TSQGA-GTYWYLPPECFVVGKEPPkiSNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd14025  153 SRDGLrGTIAYLPPERFKEKNRCP--DTKHDVYSFAIVIWGILTQKKPF 199
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
403-686 2.68e-20

Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called Doublecortin-like and CAM kinase-like 1); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. DCKL1 (or DCAMKL1) belongs to the doublecortin (DCX) family of proteins which are involved in neuronal migration, neurogenesis, and eye receptor development, among others. Family members typically contain tandem doublecortin (DCX) domains at the N-terminus; DCX domains can bind microtubules and serve as protein-interaction platforms. In addition, DCKL1 contains a serine, threonine, and proline rich domain (SP) and a C-terminal kinase domain with similarity to CAMKs. DCKL1 interacts with tubulin, glucocorticoid receptor, dynein, JIP1/2, caspases (3 and 8), and calpain, among others. It plays roles in neurogenesis, neuronal migration, retrograde transport, and neuronal apoptosis. The DCKL1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271085 [Multi-domain]  Cd Length: 268  Bit Score: 91.21  E-value: 2.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 403 TLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIhqLNKSwRDEKKENYHKHacrEYRIHKELDHPRIVKLYDYFSLD 482
Cdd:cd14183    3 SISERYKVGRTIGDGNFAVVKECVERSTGREYALKI--INKS-KCRGKEHMIQN---EVSILRRVKHPNIVLLIEEMDMP 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 483 TDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLV---DGTAcgEIKITD 559
Cdd:cd14183   77 TELY-LVMELVKGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLN--IVHRDIKPENLLVYehqDGSK--SLKLGD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 560 FGLSKIMDDDSYGVdgmdltsqgAGTYWYLPPEcfVVGKEPPKIsnKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQEN 639
Cdd:cd14183  152 FGLATVVDGPLYTV---------CGTPTYVAPE--IIAETGYGL--KVDIWAAGVITYILLCGFPPFRGSGDDQEVLFDQ 218
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 211971036 640 TILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14183  219 ILMGQVDFPSPYWDNVSDSAKELITMMLQVDVDQRYSALQVLEHPWV 265
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
419-685 2.76e-20

Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase signal-integrating kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270992 [Multi-domain]  Cd Length: 289  Bit Score: 91.71  E-value: 2.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKswrdekkenyHKHACREyRIHKELD-------HPRIVKLYDYFSlDTDTFCTVLE 491
Cdd:cd14090   15 YASVQTCINLYTGKEYAVKI--IEK----------HPGHSRS-RVFREVEtlhqcqgHPNILQLIEYFE-DDERFYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 492 YCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACGEIKITDFGL-SKIMD--D 568
Cdd:cd14090   81 KMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLH--DKGIAHRDLKPENILCESMDKVSPVKICDFDLgSGIKLssT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 569 DSYGVDGMDLTSQgAGTYWYLPPE---CFVvgKEPPKISNKVDVWSVGVIFFQCLYGRKPF------------GHN-QSQ 632
Cdd:cd14090  159 SMTPVTTPELLTP-VGSAEYMAPEvvdAFV--GEALSYDKRCDLWSLGVILYIMLCGYPPFygrcgedcgwdrGEAcQDC 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 211971036 633 QDILQENtiLKATEVQFPVK--PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd14090  236 QELLFHS--IQEGEYEFPEKewSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
420-626 2.93e-20

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 95.25  E-value: 2.93e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 420 SEVYKAFDLYEQRYAAVKIHQLNKSwRDEkkeNYHKhacreyRIHKE------LDHPRIVKLYD--------YFsldtdt 485
Cdd:NF033483  21 AEVYLAKDTRLDRDVAVKVLRPDLA-RDP---EFVA------RFRREaqsaasLSHPNIVSVYDvgedggipYI------ 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 486 fctVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKI 565
Cdd:NF033483  85 ---VMEYVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNG--IVHRDIKPQNILI---TKDGRVKVTDFGIARA 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 566 MDDDSygvdgMDLTSQGAGTYWYLPPECfVVGKeppKISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:NF033483 157 LSSTT-----MTQTNSVLGTVHYLSPEQ-ARGG---TVDARSDIYSLGIVLYEMLTGRPPF 208
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
459-686 2.98e-20

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: 91.03  E-value: 2.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLDTDTFCTVLEYCEGNDL--DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIH 536
Cdd:cd14109   45 REVDIHNSLDHPNIVQMHDAYDDEKLAVTVIDNLASTIELvrDNLLPGKDYYTERQVAVFVRQLLLALKHMHDLG--IAH 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 537 YDLKPGNILLVDGtacgEIKITDFGLS-KIMDDDSYGVDgmdltsqgAGTYWYLPPEcfVVGKEPPKISNkvDVWSVGVI 615
Cdd:cd14109  123 LDLRPEDILLQDD----KLKLADFGQSrRLLRGKLTTLI--------YGSPEFVSPE--IVNSYPVTLAT--DMWSVGVL 186
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036 616 FFQCLYGRKPF-GHNQSQqdilqenTILKATEV--QFPVKPV--VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14109  187 TYVLLGGISPFlGDNDRE-------TLTNVRSGkwSFDSSPLgnISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
457-674 3.25e-20

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: 90.72  E-value: 3.25e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 457 ACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIH 536
Cdd:cd14107   45 AFQERDILARLSHRRLTCLLDQFE-TRKTLILILELCSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMN--ILH 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 537 YDLKPGNILLVDGTAcGEIKITDFGLSKimdddsyGVDGMDLTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIF 616
Cdd:cd14107  122 LDIKPDNILMVSPTR-EDIKICDFGFAQ-------EITPSEHQFSKYGSPEFVAPE--IVHQEP--VSAATDIWALGVIA 189
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211971036 617 FQCLYGRKPF-GHNqsqqdilQENTILKATEVQF----PVKPVVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd14107  190 YLSLTCHSPFaGEN-------DRATLLNVAEGVVswdtPEITHLSEDAKDFIKRVLQPDPEKR 245
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
419-686 4.44e-20

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: 90.55  E-value: 4.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVK-IhqlnkswrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCEGND 497
Cdd:cd06624   21 FGVVYAARDLSTQVRIAIKeI--------PERDSREVQPLHEEIALHSRLSHKNIVQYLGSVSED-GFFKIFMEQVPGGS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQH-KLMSEKEARSI--VMQIVNALRYLNEIKppIIHYDLKPGNILLvdGTACGEIKITDFGLSKIMDddsyGVD 574
Cdd:cd06624   92 LSALLRSKwGPLKDNENTIGyyTKQILEGLKYLHDNK--IVHRDIKGDNVLV--NTYSGVVKISDFGTSKRLA----GIN 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 575 GMdlTSQGAGTYWYLPPEcfVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKateVQFPVKPV 654
Cdd:cd06624  164 PC--TETFTGTLQYMAPE--VIDKGQRGYGPPADIWSLGCTIIEMATGKPPFIELGEPQAAMFKVGMFK---IHPEIPES 236
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 655 VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06624  237 LSEEAKSFILRCFEPDPDKRATASDLLQDPFL 268
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
419-675 4.75e-20

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: 92.00  E-value: 4.75e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKHACREYRIhKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL 498
Cdd:cd05602   20 FGKVLLARHKSDEKFYAVKV--LQKKAILKKKEEKHIMSERNVLL-KNVKHPFLVGLHFSFQ-TTDKLYFVLDYINGGEL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddsYGVDGMDL 578
Cdd:cd05602   96 FYHLQRERCFLEPRARFYAAEIASALGYLHSLN--IVYRDLKPENILL---DSQGHIVLTDFGLCK------ENIEPNGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQdiLQENTILKATEvqfpVKPVVSSE 658
Cdd:cd05602  165 TSTFCGTPEYLAPE--VLHKQP--YDRTVDWWCLGAVLYEMLYGLPPFYSRNTAE--MYDNILNKPLQ----LKPNITNS 234
                        250
                 ....*....|....*..
gi 211971036 659 AKAFIRRCLAYRKEDRF 675
Cdd:cd05602  235 ARHLLEGLLQKDRTKRL 251
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
431-686 5.30e-20

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


Pssm-ID: 270862 [Multi-domain]  Cd Length: 257  Bit Score: 90.19  E-value: 5.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 431 QRYAAVKIHQLNKSWRDEKKenyhkhACREYRIHKELDHPRIVKLYDYFSLDTDTFCTVLEYCEGNDLDFYLKQHK--LM 508
Cdd:cd08223   26 KQYVIKKLNLKNASKRERKA------AEQEAKLLSKLKHPNIVSYKESFEGEDGFLYIVMGFCEGGDLYTRLKEQKgvLL 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 509 SEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSygvdgmDLTSQGAGTYWY 588
Cdd:cd08223  100 EERQVVEWFVQIAMALQYMHERN--ILHRDLKTQNIFL---TKSNIIKVGDLGIARVLESSS------DMATTLIGTPYY 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 589 LPPECFvvGKEPpkISNKVDVWSVGViffqCLYGRKPFGHNQSQQDIlqENTILKATEVQFPVKPV-VSSEAKAFIRRCL 667
Cdd:cd08223  169 MSPELF--SNKP--YNHKSDVWALGC----CVYEMATLKHAFNAKDM--NSLVYKILEGKLPPMPKqYSPELGELIKAML 238
                        250
                 ....*....|....*....
gi 211971036 668 AYRKEDRFDVHQLANDPYL 686
Cdd:cd08223  239 HQDPEKRPSVKRILRQPYI 257
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
419-633 6.23e-20

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 91.75  E-value: 6.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENY-------HKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLE 491
Cdd:PTZ00024  22 YGKVEKAYDTLTGKIVAIKKVKIIEISNDVTKDRQlvgmcgiHFTTLRELKIMNEIKHENIMGLVDVY-VEGDFINLVMD 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 492 YCEGnDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGtacGEIKITDFGLSK------I 565
Cdd:PTZ00024 101 IMAS-DLKKVVDRKIRLTESQVKCILLQILNGLNVLH--KWYFMHRDLSPANIFINSK---GICKIADFGLARrygyppY 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 566 MD---DDSYGVDGMDLTSQGAgTYWYLPPEcFVVGKEppKISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQ 633
Cdd:PTZ00024 175 SDtlsKDETMQRREEMTSKVV-TLWYRAPE-LLMGAE--KYHFAVDMWSVGCIFAELLTGKPLFpGENEIDQ 242
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
455-686 7.03e-20

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: 90.60  E-value: 7.03e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 455 KHACREYRIHKEL-DHPRIVKLYDYFSLDTD---------TFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNAL 524
Cdd:cd14171   43 PKARTEVRLHMMCsGHPNIVQIYDVYANSVQfpgesspraRLLIVMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAV 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 525 RYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSygvdgmdLTSQGagTYWYLPPECF---------- 594
Cdd:cd14171  123 QHCHSLN--IAHRDLKPENLLLKDNSEDAPIKLCDFGFAKVDQGDL-------MTPQF--TPYYVAPQVLeaqrrhrker 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 595 --VVGKEPPKISNK-VDVWSVGVIFFQCLYGRKPF--GHNQSQQDILQENTILkATEVQFPVK--PVVSSEAKAFIRRCL 667
Cdd:cd14171  192 sgIPTSPTPYTYDKsCDMWSLGVIIYIMLCGYPPFysEHPSRTITKDMKRKIM-TGSYEFPEEewSQISEMAKDIVRKLL 270
                        250
                 ....*....|....*....
gi 211971036 668 AYRKEDRFDVHQLANDPYL 686
Cdd:cd14171  271 CVDPEERMTIEEVLHHPWL 289
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
424-686 9.71e-20

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: 89.68  E-value: 9.71e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 424 KAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKhacrEYRIHKELDHPRIVKLYDYFSLDTDtFCTVLEYCEGNDL-DFYL 502
Cdd:cd14191   17 QVFRLVEKKTKKVWAGKFFKAYSAKEKENIRQ----EISIMNCLHHPKLVQCVDAFEEKAN-IVMVLEMVSGGELfERII 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 503 KQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACgEIKITDFGLSKimdddsygvdgmDLTSQG 582
Cdd:cd14191   92 DEDFELTERECIKYMRQISEGVEYIH--KQGIVHLDLKPENIMCVNKTGT-KIKLIDFGLAR------------RLENAG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 583 A-----GTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDIlqENTILKATEVQFPVKPVVSS 657
Cdd:cd14191  157 SlkvlfGTPEFVAPE--VINYEP--IGYATDMWSIGVICYILVSGLSPFMGDNDNETL--ANVTSATWDFDDEAFDEISD 230
                        250       260
                 ....*....|....*....|....*....
gi 211971036 658 EAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14191  231 DAKDFISNLLKKDMKARLTCTQCLQHPWL 259
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
419-678 1.31e-19

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: 90.71  E-value: 1.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKENYHKHACREYRIHKELDH-PRIVKLYDYFSLDTDTFcTVLEYCEGND 497
Cdd:cd05586    6 FGQVYQVRKKDTRRIYAMKV--LSKKVIVAKKEVAHTIGERNILVRTALDEsPFIVGLKFSFQTPTDLY-LVTDYMSGGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSygvdgmD 577
Cdd:cd05586   83 LFWHLQKEGRFSEDRAKFYIAELVLALEHLH--KNDIVYRDLKPENILL---DANGHIALCDFGLSKADLTDN------K 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQGAGTYWYLPPECFVvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQdiLQENtiLKATEVQFPvKPVVSS 657
Cdd:cd05586  152 TTNTFCGTTEYLAPEVLL---DEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQ--MYRN--IAFGKVRFP-KDVLSD 223
                        250       260
                 ....*....|....*....|.
gi 211971036 658 EAKAFIRRCLAYRKEDRFDVH 678
Cdd:cd05586  224 EGRSFVKGLLNRNPKHRLGAH 244
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
419-686 1.85e-19

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK3 (or MYLK3) phosphorylates myosin regulatory light chain 2 and controls the contraction of cardiac muscles. It is expressed specifically in both the atrium and ventricle of the heart and its expression is regulated by the cardiac protein Nkx2-5. MLCK3 plays an important role in cardiogenesis by regulating the assembly of cardiac sarcomeres, the repeating contractile unit of striated muscle. MLCK3 contains a single kinase domain near the C-terminus and a unique N-terminal half, and unlike MLCK1/2, it does not appear to be regulated by Ca2+/calmodulin. The MLCK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271094 [Multi-domain]  Cd Length: 261  Bit Score: 88.87  E-value: 1.85e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFslDTDTFCT-VLEYCEGND 497
Cdd:cd14192   17 FGQVHKCTELSTGLTLAAKIIKVKGAKEREEVKN-------EINIMNQLNHVNLIQLYDAF--ESKTNLTlIMEYVDGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 L-DFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTAcGEIKITDFGLS-KIMDDDSYGVDg 575
Cdd:cd14192   88 LfDRITDESYQLTELDAILFTRQICEGVHYLHQ--HYILHLDLKPENILCVNSTG-NQIKIIDFGLArRYKPREKLKVN- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 mdltsqgAGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFghnQSQQDILQENTILKAT-EVQFPVKPV 654
Cdd:cd14192  164 -------FGTPEFLAPE--VVNYD--FVSFPTDMWSVGVITYMLLSGLSPF---LGETDAETMNNIVNCKwDFDAEAFEN 229
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 655 VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14192  230 LSEEAKDFISRLLVKEKSCRMSATQCLKHEWL 261
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
431-667 1.97e-19

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: 89.00  E-value: 1.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 431 QRYAAVKIHQLNKSWRdekkeNYHKHACREYRIHKELDHPRIVKLYdyFSLDTDT-FCTVLEYCEGNDLDFYLKQHKLMS 509
Cdd:cd05609   26 QRFAMKKINKQNLILR-----NQIQQVFVERDILTFAENPFVVSMY--CSFETKRhLCMVMEYVEGGDCATLLKNIGPLP 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 510 EKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKImdddsyGVdgMDLTS--------- 580
Cdd:cd05609   99 VDMARMYFAETVLALEYLHSYG--IVHRDLKPDNLLI---TSMGHIKLTDFGLSKI------GL--MSLTTnlyeghiek 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 581 --------QGAGTYWYLPPECFV---VGKEppkisnkVDVWSVGVIFFQCLYGRKPFGHNQSQQdiLQENTIlkATEVQF 649
Cdd:cd05609  166 dtrefldkQVCGTPEYIAPEVILrqgYGKP-------VDWWAMGIILYEFLVGCVPFFGDTPEE--LFGQVI--SDEIEW 234
                        250
                 ....*....|....*....
gi 211971036 650 PV-KPVVSSEAKAFIRRCL 667
Cdd:cd05609  235 PEgDDALPDDAQDLITRLL 253
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
465-686 2.86e-19

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: 88.43  E-value: 2.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 465 KELD-------HPRIVKLYDYFSLDTdTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHY 537
Cdd:cd14182   58 KEIDilrkvsgHPNIIQLKDTYETNT-FFFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLN--IVHR 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLVDGTacgEIKITDFGLSKIMDDdsygvdGMDLtSQGAGTYWYLPPECFVVGKEP--PKISNKVDVWSVGVI 615
Cdd:cd14182  135 DLKPENILLDDDM---NIKLTDFGFSCQLDP------GEKL-REVCGTPGYLAPEIIECSMDDnhPGYGKEVDMWSTGVI 204
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211971036 616 FFQCLYGRKPFGHnqsQQDILQENTILkATEVQF--PVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14182  205 MYTLLAGSPPFWH---RKQMLMLRMIM-SGNYQFgsPEWDDRSDTVKDLISRFLVVQPQKRYTAEEALAHPFF 273
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
456-663 2.94e-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: 89.76  E-value: 2.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 456 HACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppII 535
Cdd:cd05593   61 HTLTESRVLKNTRHPFLTSLKYSFQ-TKDRLCFVMEYVNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGK--IV 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 536 HYDLKPGNILLVDGtacGEIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVI 615
Cdd:cd05593  138 YRDLKLENLMLDKD---GHIKITDFGLCK------EGITDAATMKTFCGTPEYLAPEVL----EDNDYGRAVDWWGLGVV 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 211971036 616 FFQCLYGRKPFgHNQSQQDILQentILKATEVQFPvkPVVSSEAKAFI 663
Cdd:cd05593  205 MYEMMCGRLPF-YNQDHEKLFE---LILMEDIKFP--RTLSADAKSLL 246
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
460-686 3.44e-19

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK phosphorylates myosin regulatory light chain and controls the contraction of all muscle types. In vertebrates, different MLCKs function in smooth (MLCK1), skeletal (MLCK2), and cardiac (MLCK3) muscles. A fourth protein, MLCK4, has also been identified through comprehensive genome analysis although it has not been biochemically characterized. MLCK4 (or MYLK4 or SgK085) contains a single kinase domain near the C-terminus. The MLCK4 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271095 [Multi-domain]  Cd Length: 261  Bit Score: 88.05  E-value: 3.44e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL-DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYD 538
Cdd:cd14193   51 EIEVMNQLNHANLIQLYDAFESRNDIV-LVMEYVDGGELfDRIIDENYNLTELDTILFIKQICEGIQYMHQMY--ILHLD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLVDGTAcGEIKITDFGLSKIMDDdsygvdgMDLTSQGAGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQ 618
Cdd:cd14193  128 LKPENILCVSREA-NQVKIIDFGLARRYKP-------REKLRVNFGTPEFLAPE--VVNYE--FVSFPTDMWSLGVIAYM 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 619 CLYGRKPF---GHNQSQQDILQENTILKATEVQfpvkpVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14193  196 LLSGLSPFlgeDDNETLNNILACQWDFEDEEFA-----DISEEAKDFISKLLIKEKSWRMSASEALKHPWL 261
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
419-685 3.62e-19

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: 88.48  E-value: 3.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihQLNKSWRDEKKENyhkhACREYRIHKEL-DHPRIVKLYDY-FSLDTDTFCTVLEYCEGN 496
Cdd:cd07831   12 FSEVLKAQSRKTGKYYAIK--CMKKHFKSLEQVN----NLREIQALRRLsPHPNILRLIEVlFDRKTGRLALVFELMDMN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 497 DLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacgeIKITDFGLSKimdddsyGVDGM 576
Cdd:cd07831   86 LYELIKGRKRPLPEKRVKNYMYQLLKSLDHMHRNG--IFHRDIKPENILIKDDI----LKLADFGSCR-------GIYSK 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 577 DLTSQGAGTYWYLPPECFVV-GKEPPkisnKVDVWSVGVIFFQCLYGRKPF-GHNQSQQ-----DIL--QENTILK---- 643
Cdd:cd07831  153 PPYTEYISTRWYRAPECLLTdGYYGP----KMDIWAVGCVFFEILSLFPLFpGTNELDQiakihDVLgtPDAEVLKkfrk 228
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 211971036 644 --ATEVQFPVK---------PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd07831  229 srHMNYNFPSKkgtglrkllPNASAEGLDLLKKLLAYDPDERITAKQALRHPY 281
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
422-636 4.38e-19

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: 88.12  E-value: 4.38e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKIHQLnkswrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEgNDLDFY 501
Cdd:cd07835   15 VYKARDKLTGEIVALKKIRL-----ETEDEGVPSTAIREISLLKELNHPNIVRLLDVVHSENKLY-LVFEFLD-LDLKKY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 502 LKQHKLMSEKEA--RSIVMQIVNALRYLNEIKppIIHYDLKPGNiLLVDGTacGEIKITDFGLSKimdddSYGVDGMDLT 579
Cdd:cd07835   88 MDSSPLTGLDPPliKSYLYQLLQGIAFCHSHR--VLHRDLKPQN-LLIDTE--GALKLADFGLAR-----AFGVPVRTYT 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 580 SQGAgTYWYLPPECFVVGKEppkISNKVDVWSVGVIFFQcLYGRKPFGHNQSQQDIL 636
Cdd:cd07835  158 HEVV-TLWYRAPEILLGSKH---YSTPVDIWSVGCIFAE-MVTRRPLFPGDSEIDQL 209
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
448-685 4.65e-19

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: 88.20  E-value: 4.65e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 448 EKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYL 527
Cdd:cd07847   38 EDDPVIKKIALREIRMLKQLKHPNLVNLIEVFR-RKRKLHLVFEYCDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFC 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 528 NEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDdsygvDGMDLTSQGAgTYWYLPPEcFVVGKE---PPkis 604
Cdd:cd07847  117 HKHN--CIHRDVKPENILI---TKQGQIKLCDFGFARILTG-----PGDDYTDYVA-TRWYRAPE-LLVGDTqygPP--- 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 605 nkVDVWSVGVIFFQCLYG----------------RKPFG-----HNQsqqdILQENTILKATEVQFP--VKPV------V 655
Cdd:cd07847  182 --VDVWAIGCVFAELLTGqplwpgksdvdqlyliRKTLGdliprHQQ----IFSTNQFFKGLSIPEPetREPLeskfpnI 255
                        250       260       270
                 ....*....|....*....|....*....|
gi 211971036 656 SSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd07847  256 SSPALSFLKGCLQMDPTERLSCEELLEHPY 285
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
419-686 4.86e-19

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: 88.16  E-value: 4.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQlNKSwrDEKKENYhkhaCREYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCEGNDL 498
Cdd:cd06644   25 FGKVYKAKNKETGALAAAKVIE-TKS--EEELEDY----MVEIEILATCNHPYIVKLLGAFYWD-GKLWIMIEFCPGGAV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 D-FYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSkimdddSYGVDGMD 577
Cdd:cd06644   97 DaIMLELDRGLTEPQIQVICRQMLEALQYLHSMK--IIHRDLKAGNVLL---TLDGDIKLADFGVS------AKNVKTLQ 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQGAGTYWYLPPEcfVVGKEPPKISN---KVDVWSVGVIFFQcLYGRKPFGHNQSQQDILQEntILKATEVQFPVKPV 654
Cdd:cd06644  166 RRDSFIGTPYWMAPE--VVMCETMKDTPydyKADIWSLGITLIE-MAQIEPPHHELNPMRVLLK--IAKSEPPTLSQPSK 240
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 655 VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06644  241 WSMEFRDFLKTALDKHPETRPSAAQLLEHPFV 272
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
419-680 5.59e-19

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: 87.74  E-value: 5.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQR-YAAVKIHQLNKswRDEKKenyhkhACREYRIHKELDHPRIVKLYDY-FSLDTDTFCTV---LEYC 493
Cdd:cd13986   13 FSFVYLVEDLSTGRlYALKKILCHSK--EDVKE------AMREIENYRLFNHPNILRLLDSqIVKEAGGKKEVyllLPYY 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 494 EG----NDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKP-PIIHYDLKPGNILLVDGtacGEIKITDFG---LSKI 565
Cdd:cd13986   85 KRgslqDEIERRLVKGTFFPEDRILHIFLGICRGLKAMHEPELvPYAHRDIKPGNVLLSED---DEPILMDLGsmnPARI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 566 MDDDSYGVDGM-DLTSQgAGTYWYLPPECFVVgKEPPKISNKVDVWSVGVIFFQCLYGRKPF----GHNQS-QQDILQEN 639
Cdd:cd13986  162 EIEGRREALALqDWAAE-HCTMPYRAPELFDV-KSHCTIDEKTDIWSLGCTLYALMYGESPFerifQKGDSlALAVLSGN 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 211971036 640 TIlkatevqFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQL 680
Cdd:cd13986  240 YS-------FPDNSRYSEELHQLVKSMLVVNPAERPSIDDL 273
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
419-626 8.20e-19

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: 87.44  E-value: 8.20e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnkswrdEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTdTFCTVLEYCEgNDL 498
Cdd:cd07844   13 YATVYKGRSKLTGQLVALKEIRL------EHEEGAPFTAIREASLLKDLKHANIVTLHDIIHTKK-TLTLVFEYLD-TDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQH-KLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLS--KIMDDDSYgvdg 575
Cdd:cd07844   85 KQYMDDCgGGLSMHNVRLFLFQLLRGLAYCHQRR--VLHRDLKPQNLLI---SERGELKLADFGLAraKSVPSKTY---- 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 211971036 576 mdltSQGAGTYWYLPPECFVVGKEppkISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd07844  156 ----SNEVVTLWYRPPDVLLGSTE---YSTSLDMWGVGCIFYEMATGRPLF 199
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
460-686 8.97e-19

Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MLCK2 (or MYLK2) phosphorylates myosin regulatory light chain and controls the contraction of skeletal muscles. MLCK2 contains a single kinase domain near the C-terminus followed by a regulatory segment containing an autoinhibitory Ca2+/calmodulin binding site. The MLCK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271092 [Multi-domain]  Cd Length: 261  Bit Score: 86.90  E-value: 8.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL-DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYD 538
Cdd:cd14190   51 EIQVMNQLNHRNLIQLYEAIETPNEIV-LFMEYVEGGELfERIVDEDYHLTEVDAMVFVRQICEGIQFMHQMR--VLHLD 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLVDGTAcGEIKITDFGLSKIMDDDsygvdgmDLTSQGAGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQ 618
Cdd:cd14190  128 LKPENILCVNRTG-HQVKIIDFGLARRYNPR-------EKLKVNFGTPEFLSPE--VVNYD--QVSFPTDMWSMGVITYM 195
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 619 CLYGRKPF-GHNQSQ--QDILQENTILKATEVQfpvkpVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14190  196 LLSGLSPFlGDDDTEtlNNVLMGNWYFDEETFE-----HVSDEAKDFVSNLIIKERSARMSATQCLKHPWL 261
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
425-687 9.27e-19

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: 86.73  E-value: 9.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 425 AFDLYEQRYAAVKIHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYLKQ 504
Cdd:cd06648   26 ATDKSTGRQVAVKKMDLRKQQRRELLFN-------EVVIMRDYQHPNIVEMYSSY-LVGDELWVVMEFLEGGALTDIVTH 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 505 HKlMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsygvdgMDLTSQGAG 584
Cdd:cd06648   98 TR-MNEEQIATVCRAVLKALSFLHSQG--VIHRDIKSDSILL---TSDGRVKLSDFGFCAQVSKE------VPRRKSLVG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 585 TYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSqqdiLQENTILKATEVQFPVKPV-VSSEAKAFI 663
Cdd:cd06648  166 TPYWMAPE--VISRLP--YGTEVDIWSLGIMVIEMVDGEPPYFNEPP----LQAMKRIRDNEPPKLKNLHkVSPRLRSFL 237
                        250       260
                 ....*....|....*....|....
gi 211971036 664 RRCLAYRKEDRFDVHQLANDPYLL 687
Cdd:cd06648  238 DRMLVRDPAQRATAAELLNHPFLA 261
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
419-686 9.62e-19

Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIM1 is a widely-expressed kinase belonging to the AMP-activated protein kinase (AMPK) subfamily. Although present in most tissues, NIM1 kinase activity is only observed in the brain and testis. NIM1 is capable of autophosphorylating and activating itself, but may be present in other tissues in the inactive form. The physiological function of NIM1 has yet to be elucidated. The NIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270977 [Multi-domain]  Cd Length: 255  Bit Score: 86.62  E-value: 9.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKKEnyhKHACREYRIHKELDHPRIVKLYDYfsLDTDT-FCTVLEYCEGND 497
Cdd:cd14075   15 FSQVKLGIHQLTKEKVAIKI--LDKTKLDQKTQ---RLLSREISSMEKLHHPNIIRLYEV--VETLSkLHLVMEYASGGE 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsygvdgmD 577
Cdd:cd14075   88 LYTKISTEGKLSESEAKPLFAQIVSAVKHMHENN--IIHRDLKAENVFY---ASNNCVKVGDFGFSTHAKRG-------E 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQGAGTYWYLPPECFvvgKEPPKISNKVDVWSVGVIFFQCLYGRKPFghnqsqqdilQENTI--LKA--TEVQFPVKP 653
Cdd:cd14075  156 TLNTFCGSPPYAAPELF---KDEHYIGIYVDIWALGVLLYFMVTGVMPF----------RAETVakLKKciLEGTYTIPS 222
                        250       260       270
                 ....*....|....*....|....*....|...
gi 211971036 654 VVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14075  223 YVSEPCQELIRGILQPVPSDRYSIDEIKNSEWL 255
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
449-667 1.26e-18

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: 87.46  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 449 KKENYHKHAcrEYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLN 528
Cdd:cd05584   41 QKDTAHTKA--ERNILEAVKHPFIVDLHYAFQTGGKLY-LILEYLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLH 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 529 EIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPPECFVV---GKEppkisn 605
Cdd:cd05584  118 SLG--IIYRDLKPENILL---DAQGHVKLTDFGLCK------ESIHDGTVTHTFCGTIEYMAPEILTRsghGKA------ 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 606 kVDVWSVGVIFFQCLYGRKPFGHNQSQQDIlqeNTILKAtevQFPVKPVVSSEAKAFIRRCL 667
Cdd:cd05584  181 -VDWWSLGALMYDMLTGAPPFTAENRKKTI---DKILKG---KLNLPPYLTNEARDLLKKLL 235
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
458-712 1.46e-18

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 87.96  E-value: 1.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 458 CREYRIHKELDHPRIVKLYDYFSLDTDtFCTVLEYCEGNDLDfylkQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHY 537
Cdd:PLN00034 120 CREIEILRDVNHPNVVKCHDMFDHNGE-IQVLLEFMDGGSLE----GTHIADEQFLADVARQILSGIAYLHRRH--IVHR 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLVDGTacgEIKITDFGLSKIMDDDsygvdgMDLTSQGAGTYWYLPPEcfvvgkeppKISNKV---------- 607
Cdd:PLN00034 193 DIKPSNLLINSAK---NVKIADFGVSRILAQT------MDPCNSSVGTIAYMSPE---------RINTDLnhgaydgyag 254
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 608 DVWSVGVIFFQCLYGRKPFGHNQsQQDilQENTILKATEVQFPVKPV-VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:PLN00034 255 DIWSLGVSILEFYLGRFPFGVGR-QGD--WASLMCAICMSQPPEAPAtASREFRHFISCCLQREPAKRWSAMQLLQHPFI 331
                        250       260
                 ....*....|....*....|....*.
gi 211971036 687 LPHMRRSNSSGNlhmaGLTASPTPPS 712
Cdd:PLN00034 332 LRAQPGQGQGGP----NLHQLLPPPR 353
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
460-686 1.47e-18

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: 87.03  E-value: 1.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDL 539
Cdd:cd14168   58 EIAVLRKIKHENIVALEDIYE-SPNHLYLVMQLVSGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMG--IVHRDL 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 540 KPGNILLVDGTACGEIKITDFGLSKIMDDDsygvdgmDLTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQC 619
Cdd:cd14168  135 KPENLLYFSQDEESKIMISDFGLSKMEGKG-------DVMSTACGTPGYVAPE--VLAQKP--YSKAVDCWSIGVIAYIL 203
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 620 LYGRKPFgHNQSQQDILQEntILKAT-EVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14168  204 LCGYPPF-YDENDSKLFEQ--ILKADyEFDSPYWDDISDSAKDFIRNLMEKDPNKRYTCEQALRHPWI 268
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
419-683 1.54e-18

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: 85.90  E-value: 1.54e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihQLNKSWRDEKKENYHKhacREYRIHKEL-DHPRIVKLYDYFSLDtDTFCTVLEYCEGND 497
Cdd:cd13997   13 FSEVFKVRSKVDGCLYAVK--KSKKPFRGPKERARAL---REVEAHAALgQHPNIVRYYSSWEEG-GHLYIQMELCENGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLK---QHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDddsygVD 574
Cdd:cd13997   87 LQDALEelsPISKLSEAEVWDLLLQVALGLAFIHSKG--IVHLDIKPDNIFI---SNKGTCKIGDFGLATRLE-----TS 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 575 GMDLtsqgAGTYWYLPPEcfvVGKEPPKISNKVDVWSVGVIFFQCLYGRK-PFGHNQSQQdilqentiLKATEVQFPVKP 653
Cdd:cd13997  157 GDVE----EGDSRYLAPE---LLNENYTHLPKADIFSLGVTVYEAATGEPlPRNGQQWQQ--------LRQGKLPLPPGL 221
                        250       260       270
                 ....*....|....*....|....*....|.
gi 211971036 654 VVSSEAKAFIRRCLAYRKEDRFDVHQ-LAND 683
Cdd:cd13997  222 VLSQELTRLLKVMLDPDPTRRPTADQlLAHD 252
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
432-663 1.57e-18

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: 87.78  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 432 RYAAVKIhqLNKSWRDEKKENyhKHACREYRIHKELDHPRIVKLYdyFSLDT-DTFCTVLEYCEGNDLDFYLKQHKLMSE 510
Cdd:cd05594   51 RYYAMKI--LKKEVIVAKDEV--AHTLTENRVLQNSRHPFLTALK--YSFQThDRLCFVMEYANGGELFFHLSRERVFSE 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 511 KEARSIVMQIVNALRYLNEIKpPIIHYDLKPGNILLVDGtacGEIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLP 590
Cdd:cd05594  125 DRARFYGAEIVSALDYLHSEK-NVVYRDLKLENLMLDKD---GHIKITDFGLCK------EGIKDGATMKTFCGTPEYLA 194
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211971036 591 PECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQentILKATEVQFPvkPVVSSEAKAFI 663
Cdd:cd05594  195 PEVL----EDNDYGRAVDWWGLGVVMYEMMCGRLPF-YNQDHEKLFE---LILMEEIRFP--RTLSPEAKSLL 257
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
419-626 1.57e-18

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: 86.72  E-value: 1.57e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKhacrEYRIHKELDHPRIVKLYdYFSLDTDTFCTVLEYCEGNDL 498
Cdd:cd05612   14 FGRVHLVRDRISEHYYALKVMAIPEVIRLKQEQHVHN----EKRVLKEVSHPFIIRLF-WTEHDQRFLYMLMEYVPGGEL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGVdgmdl 578
Cdd:cd05612   89 FSYLRNSGRFSNSTGLFYASEIVCALEYLHSKE--IVYRDLKPENILL---DKEGHIKLTDFGFAKKLRDRTWTL----- 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 211971036 579 tsqgAGTYWYLPPEcfVVGKeppKISNK-VDVWSVGVIFFQCLYGRKPF 626
Cdd:cd05612  159 ----CGTPEYLAPE--VIQS---KGHNKaVDWWALGILIYEMLVGYPPF 198
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
406-686 1.59e-18

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


Pssm-ID: 270990 [Multi-domain]  Cd Length: 265  Bit Score: 86.23  E-value: 1.59e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 406 ERYLLLHLLGRGGFSEVYKAFDlyeqrYAAVKIHQLNKSW-RDEKKenYHKHACREYRIHKELDHPRIVKLYDYFSLDTD 484
Cdd:cd14088    1 DRYDLGQVIKTEEFCEIFRAKD-----KTTGKLYTCKKFLkRDGRK--VRKAAKNEINILKMVKHPNILQLVDVFETRKE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 485 TFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSK 564
Cdd:cd14088   74 YF-IFLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLK--IVHRNLKLENLVYYNRLKNSKIVISDFHLAK 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 565 IMDDdsygvdgmdLTSQGAGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQEN----- 639
Cdd:cd14088  151 LENG---------LIKEPCGTPEYLAPE--VVGRQ--RYGRPVDCWAIGVIMYILLSGNPPFYDEAEEDDYENHDknlfr 217
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 211971036 640 TILKAT-EVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14088  218 KILAGDyEFDSPYWDDISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
419-626 1.68e-18

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: 85.91  E-value: 1.68e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFdlYEQRYAAVKIHQLNKswrDEKKENYHKHACREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDL 498
Cdd:cd14061    7 FGKVYRGI--WRGEEVAVKAARQDP---DEDISVTLENVRQEARLFWMLRHPNIIALRG-VCLQPPNLCLVMEYARGGAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVmQIVNALRYLNEIKP-PIIHYDLKPGNILLVDGTACGEI-----KITDFGLSKIMdddsYG 572
Cdd:cd14061   81 NRVLAGRKIPPHVLVDWAI-QIARGMNYLHNEAPvPIIHRDLKSSNILILEAIENEDLenktlKITDFGLAREW----HK 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 211971036 573 VDGMDltsqGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd14061  156 TTRMS----AAGTYAWMAPEVIKSS----TFSKASDVWSYGVLLWELLTGEVPY 201
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
419-686 1.76e-18

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK3 shows a restricted expression pattern; it is found at high levels in the pituary glands and is also expressed in the kidney and brain. It has been shown to regulate many ion transporters including members of the SLC12A family of cation-chloride cotransporters such as NCC and NKCC2, the renal potassium channel ROMK, and the epithelial calcium channels TRPV5 and TRPV6. WNK3 appears to sense low-chloride hypotonic stress and under these conditions, it activates SPAK, which directly interacts and phosphorylates cation-chloride cotransporters. WNK3 has also been shown to promote cell survival, possibly through interaction with procaspase-3 and HSP70. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK3 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270933 [Multi-domain]  Cd Length: 275  Bit Score: 86.31  E-value: 1.76e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDL---YEQRYAAVKIHQLNKSWRDEKKEnyhkhacrEYRIHKELDHPRIVKLYDYF-SLDTDTFCTVL--EY 492
Cdd:cd14031   23 FKTVYKGLDTetwVEVAWCELQDRKLTKAEQQRFKE--------EAEMLKGLQHPNIVRFYDSWeSVLKGKKCIVLvtEL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 493 CEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTacGEIKITDFGLSKIMDddsyg 572
Cdd:cd14031   95 MTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPT--GSVKIGDLGLATLMR----- 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 573 vdgMDLTSQGAGTYWYLPPECFvvgkePPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQentilkatEVQFPVK 652
Cdd:cd14031  168 ---TSFAKSVIGTPEFMAPEMY-----EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYR--------KVTSGIK 231
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 211971036 653 P-----VVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14031  232 PasfnkVTDPEVKEIIEGCIRQNKSERLSIKDLLNHAFF 270
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
422-626 1.81e-18

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: 86.65  E-value: 1.81e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDT-DTFCTVLEYCEgNDLDF 500
Cdd:cd07845   23 VYRARDTTSGEIVALK-----KVRMDNERDGIPISSLREITLLLNLRHPNIVELKEVVVGKHlDSIFLVMEYCE-QDLAS 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 501 YLKQHKL-MSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGtacGEIKITDFGLSKimdddSYGVDGMDLT 579
Cdd:cd07845   97 LLDNMPTpFSESQVKCLMLQLLRGLQYLHE--NFIIHRDLKVSNLLLTDK---GCLKIADFGLAR-----TYGLPAKPMT 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 211971036 580 SQGAgTYWYLPPEcFVVGKEppKISNKVDVWSVGVIFFQcLYGRKPF 626
Cdd:cd07845  167 PKVV-TLWYRAPE-LLLGCT--TYTTAIDMWAVGCILAE-LLAHKPL 208
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
459-686 2.79e-18

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: 85.79  E-value: 2.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYfsLD---TDTFCTVLEYC-EGNDLDfyLKQHKLMSEKEARSIVMQIVNALRYLNEIKppI 534
Cdd:cd14199   74 QEIAILKKLDHPNVVKLVEV--LDdpsEDHLYMVFELVkQGPVME--VPTLKPLSEDQARFYFQDLIKGIEYLHYQK--I 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 535 IHYDLKPGNILLVDGtacGEIKITDFGLSKIMDddsyGVDGmdLTSQGAGTYWYLPPECFvvgKEPPKI--SNKVDVWSV 612
Cdd:cd14199  148 IHRDVKPSNLLVGED---GHIKIADFGVSNEFE----GSDA--LLTNTVGTPAFMAPETL---SETRKIfsGKALDVWAM 215
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 211971036 613 GVIFFQCLYGRKPFghnqSQQDILQENTILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14199  216 GVTLYCFVFGQCPF----MDERILSLHSKIKTQPLEFPDQPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
443-626 2.87e-18

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: 85.83  E-value: 2.87e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTdTFCTVLEYCEgNDLDFYLKQ-HKLMSEKEARSIVMQIV 521
Cdd:cd07871   36 KEIRLEHEEGAPCTAIREVSLLKNLKHANIVTLHDIIHTER-CLTLVFEYLD-SDLKQYLDNcGNLMSMHNVKIFMFQLL 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 522 NALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGL--SKIMDDDSYgvdgmdltSQGAGTYWYLPPECFVVGKE 599
Cdd:cd07871  114 RGLSYCHKRK--ILHRDLKPQNLLINEK---GELKLADFGLarAKSVPTKTY--------SNEVVTLWYRPPDVLLGSTE 180
                        170       180
                 ....*....|....*....|....*..
gi 211971036 600 ppkISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd07871  181 ---YSTPIDMWGVGCILYEMATGRPMF 204
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
419-682 3.12e-18

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


Pssm-ID: 270634 [Multi-domain]  Cd Length: 284  Bit Score: 85.51  E-value: 3.12e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKA-FD-LYEQRYAAVKIHQLNKSWRDEKKENYHkhacREYRIHKELDHPRIVKL-YDYFSLDTDTFCTVLEYCEG 495
Cdd:cd05038   17 FGSVELCrYDpLGDNTGEQVAVKSLQPSGEEQHMSDFK----REIEILRTLDHEYIVKYkGVCESPGRRSLRLIMEYLPS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 NDLDFYLKQHK-LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILlVDGTACgeIKITDFGLSKIM--DDDSYG 572
Cdd:cd05038   93 GSLRDYLQRHRdQIDLKRLLLFASQICKGMEYLGSQR--YIHRDLAARNIL-VESEDL--VKISDFGLAKVLpeDKEYYY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 573 VDGMDLTSqgagTYWYlPPECFvvgkEPPKISNKVDVWSVGVIFFQCL-YGRK----------PFGHNQSQQDILQENTI 641
Cdd:cd05038  168 VKEPGESP----IFWY-APECL----RESRFSSASDVWSFGVTLYELFtYGDPsqsppalflrMIGIAQGQMIVTRLLEL 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 211971036 642 LKATEvQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLAN 682
Cdd:cd05038  239 LKSGE-RLPRPPSCPDEVYDLMKECWEYEPQDRPSFSDLIL 278
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
419-685 3.51e-18

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: 85.61  E-value: 3.51e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnkswrdEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCEgNDL 498
Cdd:cd07836   13 YATVYKGRNRTTGEIVALKEIHL------DAEEGTPSTAIREISLMKELKHENIVRLHDVIHTE-NKLMLVFEYMD-KDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKL---MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddSYGVDg 575
Cdd:cd07836   85 KKYMDTHGVrgaLDPNTVKSFTYQLLKGIAFCHENR--VLHRDLKPQNLLI---NKRGELKLADFGLAR-----AFGIP- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 MDLTSQGAGTYWYLPPECFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQ-----DIL---QENT---ILK 643
Cdd:cd07836  154 VNTFSNEVVTLWYRAPDVLLGSR---TYSTSIDIWSVGCIMAEMITGRPLFpGTNNEDQllkifRIMgtpTESTwpgISQ 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 211971036 644 ATEVQ--FPVKPVVSSE---------AKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd07836  231 LPEYKptFPRYPPQDLQqlfphadplGIDLLHRLLQLNPELRISAHDALQHPW 283
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
469-686 4.01e-18

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: 84.90  E-value: 4.01e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFSLdTDTFCTVLE---YCEgnDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNIL 545
Cdd:cd14101   66 HRGVIRLLDWFEI-PEGFLLVLErpqHCQ--DLFDYITERGALDESLARRFFKQVVEAVQHCHS--KGVVHRDIKDENIL 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 546 lVDgTACGEIKITDFGLSKIMDDDSYgvdgmdltSQGAGTYWYLPPECFVVGKEPpkiSNKVDVWSVGVIFFQCLYGRKP 625
Cdd:cd14101  141 -VD-LRTGDIKLIDFGSGATLKDSMY--------TDFDGTRVYSPPEWILYHQYH---ALPATVWSLGILLYDMVCGDIP 207
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 626 FghnQSQQDILqentilkATEVQFPVKpvVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14101  208 F---ERDTDIL-------KAKPSFNKR--VSNDCRSLIRSCLAYNPSDRPSLEQILLHPWM 256
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
419-643 4.97e-18

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: 85.24  E-value: 4.97e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnkswrDEKKENYHKHACREYRIHKELDHPRIVKLYDY---------FSLDTDTFCTV 489
Cdd:cd07864   20 YGQVYKAKDKDTGELVALKKVRL-----DNEKEGFPITAIREIKILRQLNHRSVVNLKEIvtdkqdaldFKKDKGAFYLV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 490 LEYCEgNDLdFYLKQHKLM--SEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGtacGEIKITDFGLSKImd 567
Cdd:cd07864   95 FEYMD-HDL-MGLLESGLVhfSEDHIKSFMKQLLEGLNYCH--KKNFLHRDIKCSNILLNNK---GQIKLADFGLARL-- 165
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036 568 ddsYGVDGMDLTSQGAGTYWYLPPEcFVVGKEppKISNKVDVWSVGVIFFQcLYGRKPFghNQSQQDILQENTILK 643
Cdd:cd07864  166 ---YNSEESRPYTNKVITLWYRPPE-LLLGEE--RYGPAIDVWSCGCILGE-LFTKKPI--FQANQELAQLELISR 232
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
460-664 5.27e-18

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: 85.53  E-value: 5.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDL 539
Cdd:cd05582   47 ERDILADVNHPFIVKLHYAFQTEGKLY-LILDFLRGGDLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLG--IIYRDL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 540 KPGNILLvdgTACGEIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFFQC 619
Cdd:cd05582  124 KPENILL---DEDGHIKLTDFGLSK------ESIDHEKKAYSFCGTVEYMAPE--VVNRRGHTQS--ADWWSFGVLMFEM 190
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 211971036 620 LYGRKPFgHNQSQQDILqeNTILKA--TEVQFpvkpvVSSEAKAFIR 664
Cdd:cd05582  191 LTGSLPF-QGKDRKETM--TMILKAklGMPQF-----LSPEAQSLLR 229
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
443-626 5.77e-18

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: 83.70  E-value: 5.77e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDEKkENYHKHAcreyrihKELDHPRIVKlYDYFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVN 522
Cdd:cd14059   22 KKVRDEK-ETDIKHL-------RKLNHPNIIK-FKGVCTQAPCYCILMEYCPYGQLYEVLRAGREITPSLLVDWSKQIAS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 523 ALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSKIMDDDSygvDGMDLtsqgAGTYWYLPPEcfVVGKEPpk 602
Cdd:cd14059   93 GMNYLHLHK--IIHRDLKSPNVLVTYNDV---LKISDFGTSKELSEKS---TKMSF----AGTVAWMAPE--VIRNEP-- 156
                        170       180
                 ....*....|....*....|....
gi 211971036 603 ISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd14059  157 CSEKVDIWSFGVVLWELLTGEIPY 180
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
448-685 5.85e-18

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2, group 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271135 [Multi-domain]  Cd Length: 257  Bit Score: 84.27  E-value: 5.85e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 448 EKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYL 527
Cdd:cd14665   34 ERGEKIDENVQREIINHRSLRHPNIVRFKEVI-LTPTHLAIVMEYAAGGELFERICNAGRFSEDEARFFFQQLISGVSYC 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 528 NEIKppIIHYDLKPGNILLvDGTACGEIKITDFGLSKimdddsygvdGMDLTSQ---GAGTYWYLPPECFVVGKEPPKIS 604
Cdd:cd14665  113 HSMQ--ICHRDLKLENTLL-DGSPAPRLKICDFGYSK----------SSVLHSQpksTVGTPAYIAPEVLLKKEYDGKIA 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 605 nkvDVWSVGVIFFQCLYGRKPFGHNQSQQDIlqENTILKATEVQFPVKPVV--SSEAKAFIRRCLAYRKEDRFDVHQLAN 682
Cdd:cd14665  180 ---DVWSCGVTLYVMLVGAYPFEDPEEPRNF--RKTIQRILSVQYSIPDYVhiSPECRHLISRIFVADPATRITIPEIRN 254

                 ...
gi 211971036 683 DPY 685
Cdd:cd14665  255 HEW 257
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
419-614 6.61e-18

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: 84.28  E-value: 6.61e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKswrDEKKENYHkhacrEYRIHKEL-DHPRIVKLYDYF-----SLDTDTFCTVLEY 492
Cdd:cd06608   19 YGKVYKARHKKTGQLAAIKIMDIIE---DEEEEIKL-----EINILRKFsNHPNIATFYGAFikkdpPGGDDQLWLVMEY 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 493 CEGN---DL-DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDd 568
Cdd:cd06608   91 CGGGsvtDLvKGLRKKGKRLKEEWIAYILRETLRGLAYLHENK--VIHRDIKGQNILLTEE---AEVKLVDFGVSAQLD- 164
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 211971036 569 dsygvdgmdlTSQGA-----GTYWYLPPECFVVGKEP-PKISNKVDVWSVGV 614
Cdd:cd06608  165 ----------STLGRrntfiGTPYWMAPEVIACDQQPdASYDARCDVWSLGI 206
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
419-625 7.31e-18

Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), Bypass UAS Requirement 1, and similar proteins; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BUR1, also called SGV1, is a yeast CDK that is functionally equivalent to mammalian CDK9. It associates with the cyclin BUR2. BUR genes were orginally identified in a genetic screen as factors involved in general transcription. The BUR1/BUR2 complex phosphorylates the C-terminal domain of RNA polymerase II. In addition, this complex regulates histone modification by phosporylating Rad6 and mediating the association of the Paf1 complex with chromatin. 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 BUR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270849 [Multi-domain]  Cd Length: 311  Bit Score: 85.06  E-value: 7.31e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVK-IHQLNKswrdekKENYHKHACREYRIHKELDHPRIVKL----YDYFSLDTDT---FCTVL 490
Cdd:cd07866   21 FGEVYKARQIKTGRVVALKkILMHNE------KDGFPITALREIKILKKLKHPNVVPLidmaVERPDKSKRKrgsVYMVT 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 491 EYCEgNDLDFYLKQHKL-MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNIlLVDGTacGEIKITDFGLSKIMDDD 569
Cdd:cd07866   95 PYMD-HDLSGLLENPSVkLTESQIKCYMLQLLEGINYLHENH--ILHRDIKAANI-LIDNQ--GILKIADFGLARPYDGP 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 570 SY------GVDGMDLTSQgAGTYWYLPPEcFVVGKEppKISNKVDVWSVGVIFFQcLYGRKP 625
Cdd:cd07866  169 PPnpkgggGGGTRKYTNL-VVTRWYRPPE-LLLGER--RYTTAVDIWGIGCVFAE-MFTRRP 225
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
460-686 7.43e-18

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: 84.12  E-value: 7.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDL 539
Cdd:cd14087   47 ELNVLRRVRHTNIIQLIEVFETKERVY-MVMELATGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLG--ITHRDL 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 540 KPGNILLVDGTACGEIKITDFGLS---KIMDDdsygvdgmDLTSQGAGTYWYLPPECFVvgKEPpkISNKVDVWSVGVIF 616
Cdd:cd14087  124 KPENLLYYHPGPDSKIMITDFGLAstrKKGPN--------CLMKTTCGTPEYIAPEILL--RKP--YTQSVDMWAVGVIA 191
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 617 FQCLYGRKPFGHNQSQQDILQentILKATEVQFPVK-PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14087  192 YILLSGTMPFDDDNRTRLYRQ---ILRAKYSYSGEPwPSVSNLAKDFIDRLLTVNPGERLSATQALKHPWI 259
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
431-674 9.00e-18

Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Syk is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Syk was first cloned from the spleen, and its function in hematopoietic cells is well-established. It is involved in the signaling downstream of activated receptors (including B-cell and Fc receptors) that contain ITAMs (immunoreceptor tyr activation motifs), leading to processes such as cell proliferation, differentiation, survival, adhesion, migration, and phagocytosis. More recently, Syk expression has been detected in other cell types (including epithelial cells, vascular endothelial cells, neurons, hepatocytes, and melanocytes), suggesting a variety of biological functions in non-immune cells. Syk plays a critical role in maintaining vascular integrity and in wound healing during embryogenesis. It also regulates Vav3, which is important in osteoclast function including bone development. In breast epithelial cells, where Syk acts as a negative regulator for EGFR signaling, loss of Syk expression is associated with abnormal proliferation during cancer development suggesting a potential role as a tumor suppressor. In mice, Syk has been shown to inhibit malignant transformation of mammary epithelial cells induced with murine mammary tumor virus (MMTV). The Syk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133247 [Multi-domain]  Cd Length: 257  Bit Score: 83.86  E-value: 9.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 431 QRYAAVKIHQlnkswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYfsLDTDTFCTVLEYCEGNDLDFYLKQHKLMSE 510
Cdd:cd05116   22 VKTVAVKILK-----NEANDPALKDELLREANVMQQLDNPYIVRMIGI--CEAESWMLVMEMAELGPLNKFLQKNRHVTE 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 511 KEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACgeiKITDFGLSKIM-DDDSYgvdgmdLTSQGAGTY--- 586
Cdd:cd05116   95 KNITELVHQVSMGMKYLEESN--FVHRDLAARNVLLVTQHYA---KISDFGLSKALrADENY------YKAQTHGKWpvk 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 587 WYlPPECFvvgkEPPKISNKVDVWSVGVIFFQCL-YGRKPFgHNQSQQDILQenTILKATEVQFPvkPVVSSEAKAFIRR 665
Cdd:cd05116  164 WY-APECM----NYYKFSSKSDVWSFGVLMWEAFsYGQKPY-KGMKGNEVTQ--MIEKGERMECP--AGCPPEMYDLMKL 233

                 ....*....
gi 211971036 666 CLAYRKEDR 674
Cdd:cd05116  234 CWTYDVDER 242
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
459-674 9.90e-18

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: 83.53  E-value: 9.90e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKEL-DHPRIVKLYDYFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHY 537
Cdd:cd13987   38 REYNISLELsVHPHIIKTYDVAFETEDYYVFAQEYAPYGDLFSIIPPQVGLPEERVKRCAAQLASALDFMHSKN--LVHR 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLVDgTACGEIKITDFGLSKIMDDdsygvdgmdLTSQGAGTYWYLPPE-CFVVGKEPPKISNKVDVWSVGVIF 616
Cdd:cd13987  116 DIKPENVLLFD-KDCRRVKLCDFGLTRRVGS---------TVKRVSGTIPYTAPEvCEAKKNEGFVVDPSIDVWAFGVLL 185
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211971036 617 FQCLYGRKPF----GHNQSQQDILQ-ENTILKATEVQFpvKPvVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd13987  186 FCCLTGNFPWekadSDDQFYEEFVRwQKRKNTAVPSQW--RR-FTPKALRMFKKLLAPEPERR 245
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
419-626 1.02e-17

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: 83.50  E-value: 1.02e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfdLYEQRYAAVKIHQLNKswrDEKKENYHKHACREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDL 498
Cdd:cd14148    7 FGKVYKG--LWRGEEVAVKAARQDP---DEDIAVTAENVRQEARLFWMLQHPNIIALRG-VCLNPPHLCLVMEYARGGAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLmsekEARSIV---MQIVNALRYL-NEIKPPIIHYDLKPGNILLV-----DGTACGEIKITDFGLSKimddD 569
Cdd:cd14148   81 NRALAGKKV----PPHVLVnwaVQIARGMNYLhNEAIVPIIHRDLKSSNILILepienDDLSGKTLKITDFGLAR----E 152
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 570 SYGVDGMdltsQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd14148  153 WHKTTKM----SAAGTYAWMAPEVIRLS----LFSKSSDVWSFGVLLWELLTGEVPY 201
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
419-680 1.15e-17

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: 83.44  E-value: 1.15e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKI---HQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEG 495
Cdd:cd14189   14 FARCYEMTDLATNKTYAVKViphSRVAKPHQREKIVN-------EIELHRDLHHKHVVKFSHHFE-DAENIYIFLELCSR 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 NDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTacgEIKITDFGLSKIMDddsyGVDG 575
Cdd:cd14189   86 KSLAHIWKARHTLLEPEVRYYLKQIISGLKYLHL--KGILHRDLKLGNFFINENM---ELKVGDFGLAARLE----PPEQ 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 MDLTSqgAGTYWYLPPECFVVGKEPPkisnKVDVWSVGVIFFQCLYGRKPFghnqsqqdilqENTILKAT-----EVQFP 650
Cdd:cd14189  157 RKKTI--CGTPNYLAPEVLLRQGHGP----ESDVWSLGCVMYTLLCGNPPF-----------ETLDLKETyrcikQVKYT 219
                        250       260       270
                 ....*....|....*....|....*....|
gi 211971036 651 VKPVVSSEAKAFIRRCLAYRKEDRFDVHQL 680
Cdd:cd14189  220 LPASLSLPARHLLAGILKRNPGDRLTLDQI 249
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
455-686 1.41e-17

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: 84.38  E-value: 1.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 455 KHACREYRIHKEL-DHPRIVKLYDYFSLDTDTFCTVLEYCE--GNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIK 531
Cdd:cd07857   46 KRALRELKLLRHFrGHKNITCLYDMDIVFPGNFNELYLYEElmEADLHQIIRSGQPLTDAHFQSFIYQILCGLKYIHSAN 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 532 ppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGVDGMdLTSQGAgTYWYLPPECFVVGKEppkISNKVDVWS 611
Cdd:cd07857  126 --VLHRDLKPGNLLV---NADCELKICDFGLARGFSENPGENAGF-MTEYVA-TRWYRAPEIMLSFQS---YTKAIDVWS 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 612 VGVIFFQcLYGRKPF--GHNQSQQ-------------DILQENTILKATEV--QFPVKPVV---------SSEAKAFIRR 665
Cdd:cd07857  196 VGCILAE-LLGRKPVfkGKDYVDQlnqilqvlgtpdeETLSRIGSPKAQNYirSLPNIPKKpfesifpnaNPLALDLLEK 274
                        250       260
                 ....*....|....*....|.
gi 211971036 666 CLAYRKEDRFDVHQLANDPYL 686
Cdd:cd07857  275 LLAFDPTKRISVEEALEHPYL 295
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
471-686 1.41e-17

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: 83.50  E-value: 1.41e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 471 RIVKLYDYFSLDTDTFCTVLEYCEGNDLDFYLKQH--KLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVD 548
Cdd:cd14172   61 HILDVYENMHHGKRCLLIIMECMEGGELFSRIQERgdQAFTEREASEIMRDIGTAIQYLHSMN--IAHRDVKPENLLYTS 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 549 GTACGEIKITDFGLSKimdddsygvdgmDLTSQGA-----GTYWYLPPEcfVVGkePPKISNKVDVWSVGVIFFQCLYGR 623
Cdd:cd14172  139 KEKDAVLKLTDFGFAK------------ETTVQNAlqtpcYTPYYVAPE--VLG--PEKYDKSCDMWSLGVIMYILLCGF 202
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 211971036 624 KPFGHNQSQQDILQENTILKATEVQFPVK--PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14172  203 PPFYSNTGQAISPGMKRRIRMGQYGFPNPewAEVSEEAKQLIRHLLKTDPTERMTITQFMNHPWI 267
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
419-614 1.70e-17

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


Pssm-ID: 270788 [Multi-domain]  Cd Length: 259  Bit Score: 82.74  E-value: 1.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnkswrdEKKENYhKHACREYRIHKELDHPRIVKLY-DYFSLdtDTFCTVLEYCEGND 497
Cdd:cd06613   13 YGDVYKARNIATGELAAVKVIKL------EPGDDF-EIIQQEISMLKECRHPNIVAYFgSYLRR--DKLWIVMEYCGGGS 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKimdddsygvdgmD 577
Cdd:cd06613   84 LQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTG--KIHRDIKGANILLTED---GDVKLADFGVSA------------Q 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 211971036 578 LTSQGA------GT-YWyLPPECFVVGKEPPkISNKVDVWSVGV 614
Cdd:cd06613  147 LTATIAkrksfiGTpYW-MAPEVAAVERKGG-YDGKCDIWALGI 188
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
459-686 1.81e-17

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: 84.15  E-value: 1.81e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKEL-DHPRIVKLYDYFSLDTDT-FCTVLEYCEgNDLDFYLKqHKLMSEKEARSIVMQIVNALRYLNEIKppIIH 536
Cdd:cd07852   55 REIMFLQELnDHPNIIKLLNVIRAENDKdIYLVFEYME-TDLHAVIR-ANILEDIHKQYIMYQLLKALKYLHSGG--VIH 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 537 YDLKPGNILLvdGTACgEIKITDFGLSKIMDDDSYGVDGMDLTSQGAgTYWYLPPEcFVVGKepPKISNKVDVWSVGVIF 616
Cdd:cd07852  131 RDLKPSNILL--NSDC-RVKLADFGLARSLSQLEEDDENPVLTDYVA-TRWYRAPE-ILLGS--TRYTKGVDMWSVGCIL 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 617 FQCLYGRKPF-GH---NQ-----------SQQDILQEN-----TILKATEVQFPVK-----PVVSSEAKAFIRRCLAYRK 671
Cdd:cd07852  204 GEMLLGKPLFpGTstlNQlekiievigrpSAEDIESIQspfaaTMLESLPPSRPKSldelfPKASPDALDLLKKLLVFNP 283
                        250
                 ....*....|....*
gi 211971036 672 EDRFDVHQLANDPYL 686
Cdd:cd07852  284 NKRLTAEEALRHPYV 298
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
422-643 2.16e-17

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: 83.43  E-value: 2.16e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDY-FSLDTDTFCTVLEYCEgNDLDF 500
Cdd:cd07843   21 VYRARDKKTGEIVALK-----KLKMEKEKEGFPITSLREINILLKLQHPNIVTVKEVvVGSNLDKIYMVMEYVE-HDLKS 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 501 YLKQHK-LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddSYGVDGMDLT 579
Cdd:cd07843   95 LMETMKqPFLQSEVKCLMLQLLSGVAHLHDNW--ILHRDLKTSNLLL---NNRGILKICDFGLAR-----EYGSPLKPYT 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 211971036 580 sQGAGTYWYLPPECFVvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFghnQSQQDILQENTILK 643
Cdd:cd07843  165 -QLVVTLWYRAPELLL---GAKEYSTAIDMWSVGCIFAELLTKKPLF---PGKSEIDQLNKIFK 221
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
469-663 2.51e-17

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: 83.59  E-value: 2.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvD 548
Cdd:cd05592   55 HPFLTHLFCTFQTESHLF-FVMEYLNGGDLMFHIQQSGRFDEDRARFYGAEIICGLQFLH--SRGIIYRDLKLDNVLL-D 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 549 GTacGEIKITDFGLSKImdddsyGVDGMDLTSQGAGTYWYLPPEcFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPFgH 628
Cdd:cd05592  131 RE--GHIKIADFGMCKE------NIYGENKASTFCGTPDYIAPE-ILKGQ---KYNQSVDWWSFGVLLYEMLIGQSPF-H 197
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 211971036 629 NQSQQDILQenTILKaTEVQFPVkpVVSSEAKAFI 663
Cdd:cd05592  198 GEDEDELFW--SICN-DTPHYPR--WLTKEAASCL 227
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
451-686 2.66e-17

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: 82.09  E-value: 2.66e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 451 ENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYLKQHK--LMSEKEARSIVMQIVNALRYLN 528
Cdd:cd08221   40 EKERRDALNEIDILSLLNHDNIITYYNHF-LDGESLFIEMEYCNGGNLHDKIAQQKnqLFPEEVVLWYLYQIVSAVSHIH 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 529 EIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGVDGMdltsqgAGTYWYLPPEcFVVGKeppKISNKVD 608
Cdd:cd08221  119 KAG--ILHRDIKTLNIFL---TKADLVKLGDFGISKVLDSESSMAESI------VGTPYYMSPE-LVQGV---KYNFKSD 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 609 VWSVGVIFFQCLYGRKPF-GHNQSQ--QDILQENTILkatevqfpVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPY 685
Cdd:cd08221  184 IWAVGCVLYELLTLKRTFdATNPLRlaVKIVQGEYED--------IDEQYSEEIIQLVHDCLHQDPEDRPTAEELLERPL 255

                 .
gi 211971036 686 L 686
Cdd:cd08221  256 L 256
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
419-681 3.11e-17

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


Pssm-ID: 270865 [Multi-domain]  Cd Length: 268  Bit Score: 82.38  E-value: 3.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENyhkhACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd08228   15 FSEVYRATCLLDRKPVALKKVQIFEMMDAKARQD----CVKEIDLLKQLNHPNVIKYLDSF-IEDNELNIVLELADAGDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 D----FYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGVD 574
Cdd:cd08228   90 SqmikYFKKQKRLIPERTVWKYFVQLCSAVEHMHSRR--VMHRDIKPANVFI---TATGVVKLGDLGLGRFFSSKTTAAH 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 575 GMdltsqgAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQDILQentilKATEVQFPVKP 653
Cdd:cd08228  165 SL------VGTPYYMSPERI----HENGYNFKSDIWSLGCLLYEMAALQSPFyGDKMNLFSLCQ-----KIEQCDYPPLP 229
                        250       260       270
                 ....*....|....*....|....*....|...
gi 211971036 654 V--VSSEAKAFIRRCLAYRKEDRFD---VHQLA 681
Cdd:cd08228  230 TehYSEKLRELVSMCIYPDPDQRPDigyVHQIA 262
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
463-703 3.23e-17

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: 82.59  E-value: 3.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 463 IHKELD------HPRIVKLYDYFSLDTDTF-CtvLEYCEGNDLD-FY--LKQHKLMSEKEARSIVMQIVNALRYLNEiKP 532
Cdd:cd06622   46 IIMELDilhkavSPYIVDFYGAFFIEGAVYmC--MEYMDAGSLDkLYagGVATEGIPEDVLRRITYAVVKGLKFLKE-EH 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 533 PIIHYDLKPGNILLvdgTACGEIKITDFGLSkimdddsyGVDGMDLTSQGAGTYWYLPPECFVVG--KEPPKISNKVDVW 610
Cdd:cd06622  123 NIIHRDVKPTNVLV---NGNGQVKLCDFGVS--------GNLVASLAKTNIGCQSYMAPERIKSGgpNQNPTYTVQSDVW 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 611 SVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQFPvkPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLphm 690
Cdd:cd06622  192 SLGLSILEMALGRYPYPPETYANIFAQLSAIVDGDPPTLP--SGYSDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLV--- 266
                        250
                 ....*....|...
gi 211971036 691 rrSNSSGNLHMAG 703
Cdd:cd06622  267 --KYKNADVDMAE 277
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
468-674 3.29e-17

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 82.21  E-value: 3.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 468 DHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLV 547
Cdd:PHA03390  67 DNPNFIKLYYSVTTLKGHV-LIMDYIKDGDLFDLLKKEGKLSEAEVKKIIRQLVEALNDLHKHN--IIHNDIKLENVLYD 143
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 548 DgtACGEIKITDFGLSKIMDDDSYgvdgMDltsqgaGTYWYLPPEcfvvgkeppKISNK-----VDVWSVGVIFFQCLYG 622
Cdd:PHA03390 144 R--AKDRIYLCDYGLCKIIGTPSC----YD------GTLDYFSPE---------KIKGHnydvsFDWWAVGVLTYELLTG 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 211971036 623 RKPFghNQSQQDILQENTILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDR 674
Cdd:PHA03390 203 KHPF--KEDEDEELDLESLLKRQQKKLPFIKNVSKNANDFVQSMLKYNINYR 252
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
419-633 3.37e-17

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CDK9, together with a cyclin partner (cyclin T1, T2a, T2b, or K), is the main component of distinct positive transcription elongation factors (P-TEFb), which function as Ser2 C-terminal domain kinases of RNA polymerase II. P-TEFb participates in multiple steps of gene expression including transcription elongation, mRNA synthesis, processing, export, and translation. It also plays a role in mediating cytokine induced transcription networks such as IL6-induced STAT3 signaling. In addition, the CDK9/cyclin T2a complex promotes muscle differentiation and enhances the function of some myogenic regulatory factors. 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 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: 270848 [Multi-domain]  Cd Length: 310  Bit Score: 83.19  E-value: 3.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDY-------FSLDTDTFCTVLE 491
Cdd:cd07865   25 FGEVFKARHRKTGQIVALK-----KVLMENEKEGFPITALREIKILQLLKHENVVNLIEIcrtkatpYNRYKGSIYLVFE 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 492 YCEgNDLDFYLKQHKL-MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGL------SK 564
Cdd:cd07865  100 FCE-HDLAGLLSNKNVkFTLSEIKKVMKMLLNGLYYIHRNK--ILHRDMKAANILI---TKDGVLKLADFGLarafslAK 173
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211971036 565 IMDDDSYgvdgmdltSQGAGTYWYLPPECFVVGKE--PPkisnkVDVWSVGVIFFQcLYGRKPF--GHNQSQQ 633
Cdd:cd07865  174 NSQPNRY--------TNRVVTLWYRPPELLLGERDygPP-----IDMWGAGCIMAE-MWTRSPImqGNTEQHQ 232
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
419-665 3.53e-17

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


Pssm-ID: 270818 [Multi-domain]  Cd Length: 264  Bit Score: 82.01  E-value: 3.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKEnYHKHACrEYRIHKELDHPRIVKLYDYFSLDTD-TFCTVLEYCEGND 497
Cdd:cd06652   15 FGRVYLCYDADTGRELAVKQVQFDPESPETSKE-VNALEC-EIQLLKNLLHERIVQYYGCLRDPQErTLSIFMEYMPGGS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGVDGMD 577
Cdd:cd06652   93 IKDQLKSYGALTENVTRKYTRQILEGVHYLH--SNMIVHRDIKGANILR---DSVGNVKLGDFGASKRLQTICLSGTGMK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSqgaGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTilKATEVQFPvkPVVSS 657
Cdd:cd06652  168 SVT---GTPYWMSPE--VISGE--GYGRKADIWSVGCTVVEMLTEKPPWAEFEAMAAIFKIAT--QPTNPQLP--AHVSD 236

                 ....*...
gi 211971036 658 EAKAFIRR 665
Cdd:cd06652  237 HCRDFLKR 244
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
419-686 4.27e-17

Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK2 is widely expressed and has been shown to be epigenetically silenced in gliomas. It inhibits cell growth by acting as a negative regulator of MEK1-ERK1/2 signaling. WNK2 modulates growth factor-induced cancer cell proliferation, suggesting that it may be a tumor suppressor gene. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. They are critical in regulating ion balance and are thus, important components in the control of blood pressure. The WNK2-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: 270934 [Multi-domain]  Cd Length: 266  Bit Score: 82.05  E-value: 4.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDL---YEQRYAAVKIHQLNKSWRDEKKEnyhkhacrEYRIHKELDHPRIVKLYDYF-SLDTDTFCTVL--EY 492
Cdd:cd14032   14 FKTVYKGLDTetwVEVAWCELQDRKLTKVERQRFKE--------EAEMLKGLQHPNIVRFYDFWeSCAKGKRCIVLvtEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 493 CEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTacGEIKITDFGLSKIMDddsyg 572
Cdd:cd14032   86 MTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTPPIIHRDLKCDNIFITGPT--GSVKIGDLGLATLKR----- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 573 vdgMDLTSQGAGTYWYLPPECFvvgkePPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQentilkatEVQFPVK 652
Cdd:cd14032  159 ---ASFAKSVIGTPEFMAPEMY-----EEHYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYR--------KVTCGIK 222
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 211971036 653 P-----VVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14032  223 PasfekVTDPEIKEIIGECICKNKEERYEIKDLLSHAFF 261
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
457-667 4.29e-17

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: 81.49  E-value: 4.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 457 ACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMsEKEARSIVMQIVNALRYLNEIKppIIH 536
Cdd:cd14108   45 ARRELALLAELDHKSIVRFHDAFE-KRRVVIIVTELCHEELLERITKRPTVC-ESEVRSYMRQLLEGIEYLHQND--VLH 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 537 YDLKPGNILLVDGTAcGEIKITDFGLSKIM--DDDSYGvdgmdltsqGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGV 614
Cdd:cd14108  121 LDLKPENLLMADQKT-DQVRICDFGNAQELtpNEPQYC---------KYGTPEFVAPE--IVNQSP--VSKVTDIWPVGV 186
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 211971036 615 IFFQCLYGRKPF-GHNQSQQDILQENTILKATEVQFpvkPVVSSEAKAFIRRCL 667
Cdd:cd14108  187 IAYLCLTGISPFvGENDRTTLMNIRNYNVAFEESMF---KDLCREAKGFIIKVL 237
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
406-682 4.30e-17

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: 83.17  E-value: 4.30e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 406 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYF----SL 481
Cdd:cd07877   17 ERYQNLSPVGSGAYGSVCAAFDTKTGLRVAVK-----KLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVFtparSL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 482 DTDTFCTVLEYCEGNDLDFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtaCgEIKITDFG 561
Cdd:cd07877   92 EEFNDVYLVTHLMGADLNNIVKCQKL-TDDHVQFLIYQILRGLKYIHSAD--IIHRDLKPSNLAVNED--C-ELKILDFG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 562 LSKIMDDDSYGVdgmdltsqgAGTYWYLPPECFVVGKEppkISNKVDVWSVGVIFFQCLYGRKPFghnQSQQDILQENTI 641
Cdd:cd07877  166 LARHTDDEMTGY---------VATRWYRAPEIMLNWMH---YNQTVDIWSVGCIMAELLTGRTLF---PGTDHIDQLKLI 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 211971036 642 LKATEVQFP--VKPVVSSEAKAFIRRCLAYRKEDRFDVHQLAN 682
Cdd:cd07877  231 LRLVGTPGAelLKKISSESARNYIQSLTQMPKMNFANVFIGAN 273
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
419-626 4.37e-17

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: 82.01  E-value: 4.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFdlYEQRYAAVKIHQLNKswrDEKKENYHKHACREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDL 498
Cdd:cd14145   19 FGKVYRAI--WIGDEVAVKAARHDP---DEDISQTIENVRQEAKLFAMLKHPNIIALRG-VCLKEPNLCLVMEFARGGPL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVmQIVNALRYL-NEIKPPIIHYDLKPGNILLVDGTACGEI-----KITDFGLSKimddDSYG 572
Cdd:cd14145   93 NRVLSGKRIPPDILVNWAV-QIARGMNYLhCEAIVPVIHRDLKSSNILILEKVENGDLsnkilKITDFGLAR----EWHR 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 211971036 573 VDGMdltsQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd14145  168 TTKM----SAAGTYAWMAPEVI----RSSMFSKGSDVWSYGVLLWELLTGEVPF 213
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
470-667 4.49e-17

N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK1 plays a role in the regulation of translational control and transcriptional activation. It phosphorylates the transcription factors, CREB and NFkB. It also phosphorylates the nucleosomal proteins H3 and HMG-14. Increased phosphorylation of MSK1 is associated with the development of cerebral ischemic/hypoxic preconditioning. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family. MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270764 [Multi-domain]  Cd Length: 290  Bit Score: 82.36  E-value: 4.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 470 PRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdg 549
Cdd:cd05613   65 PFLVTLHYAFQTDTKLH-LILDYINGGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLG--IIYRDIKLENILL--- 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 550 TACGEIKITDFGLSKimdddSYGVDGMDLTSQGAGTYWYLPPEcFVVGKEPPKiSNKVDVWSVGVIFFQCLYGRKPF--- 626
Cdd:cd05613  139 DSSGHVVLTDFGLSK-----EFLLDENERAYSFCGTIEYMAPE-IVRGGDSGH-DKAVDWWSLGVLMYELLTGASPFtvd 211
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 211971036 627 GHNQSQQDILQEntILKaTEVQFPVKpvVSSEAKAFIRRCL 667
Cdd:cd05613  212 GEKNSQAEISRR--ILK-SEPPYPQE--MSALAKDIIQRLL 247
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
469-687 6.28e-17

C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MSK2 and MSK1 play nonredundant roles in activating histone H3 kinases, which play pivotal roles in compaction of the chromatin fiber. MSK2 is the required H3 kinase in response to stress stimuli and activation of the p38 MAPK pathway. MSK2 also plays a role in the pathogenesis of psoriasis. MSKs contain an N-terminal kinase domain (NTD) from the AGC family and a C-terminal kinase domain (CTD) from the CAMK family, similar to 90 kDa ribosomal protein S6 kinases (RSKs). MSKs are activated by two major signaling cascades, the Ras-MAPK and p38 stress kinase pathways, which trigger phosphorylation in the activation loop (A-loop) of the CTD of MSK. The active CTD phosphorylates the hydrophobic motif (HM) of NTD, which facilitates the phosphorylation of the A-loop and activates the NTD, which in turn phosphorylates downstream targets. The MSK2 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271082 [Multi-domain]  Cd Length: 309  Bit Score: 82.23  E-value: 6.28e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVD 548
Cdd:cd14180   60 HPNIVALHEVLHDQYHTY-LVMELLRGGELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAG--VVHRDLKPENILYAD 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 549 GTACGEIKITDFGLSKIMDDDSYGVDGMDLTSQgagtywYLPPECFVVGkeppKISNKVDVWSVGVIFFQCLYGRKPFgh 628
Cdd:cd14180  137 ESDGAVLKVIDFGFARLRPQGSRPLQTPCFTLQ------YAAPELFSNQ----GYDESCDLWSLGVILYTMLSGQVPF-- 204
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 629 nQSQQDILQEN----TILKATEVQFPVK----PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLL 687
Cdd:cd14180  205 -QSKRGKMFHNhaadIMHKIKEGDFSLEgeawKGVSEEAKDLVRGLLTVDPAKRLKLSELRESDWLQ 270
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
436-686 8.12e-17

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: 81.01  E-value: 8.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 436 VKIHQLNKSWRDEKKenyhkhacREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHK--LMSEKEA 513
Cdd:cd08218   33 INISKMSPKEREESR--------KEVAVLSKMKHPNIVQYQESFE-ENGNLYIVMDYCDGGDLYKRINAQRgvLFPEDQI 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 514 RSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsygvdgMDLTSQGAGTYWYLPPEc 593
Cdd:cd08218  104 LDWFVQLCLALKHVHDRK--ILHRDIKSQNIFL---TKDGIIKLGDFGIARVLNST------VELARTCIGTPYYLSPE- 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 594 fVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQsqqdilQENTILKATEVQF-PVKPVVSSEAKAFIRRCLAYRKE 672
Cdd:cd08218  172 -ICENKP--YNNKSDIWALGCVLYEMCTLKHAFEAGN------MKNLVLKIIRGSYpPVPSRYSYDLRSLVSQLFKRNPR 242
                        250
                 ....*....|....
gi 211971036 673 DRFDVHQLANDPYL 686
Cdd:cd08218  243 DRPSINSILEKPFI 256
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
422-689 8.52e-17

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: 81.65  E-value: 8.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKihQLNKSwrDEKKENyhKHACREYRI-HKELDHPRIVKLYDYFSLDTDTF-CT-VLEYCegndL 498
Cdd:cd06618   31 VYKMRHKKTGHVMAVK--QMRRS--GNKEEN--KRILMDLDVvLKSHDCPYIVKCYGYFITDSDVFiCMeLMSTC----L 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQ-HKLMSEKEARSIVMQIVNALRYLNEiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMdddsygVDGMD 577
Cdd:cd06618  101 DKLLKRiQGPIPEDILGKMTVSIVKALHYLKE-KHGVIHRDVKPSNILL---DESGNVKLCDFGISGRL------VDSKA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTsQGAGTYWYLPPECFvvgkEPPKISN---KVDVWSVGVIFFQCLYGRKPFGHNQSQQD----ILQENTILKATEVQFp 650
Cdd:cd06618  171 KT-RSAGCAAYMAPERI----DPPDNPKydiRADVWSLGISLVELATGQFPYRNCKTEFEvltkILNEEPPSLPPNEGF- 244
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 211971036 651 vkpvvSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLPH 689
Cdd:cd06618  245 -----SPDFCSFVDLCLTKDHRYRPKYRELLQHPFIRRY 278
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
464-689 9.17e-17

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: 80.48  E-value: 9.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 464 HKELDHPRIVKLYDY-FSLDTDTF----CTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYD 538
Cdd:cd14012   52 LKKLRHPNLVSYLAFsIERRGRSDgwkvYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYLH--RNGVVHKS 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLVDGTACGEIKITDFGLSKIMdDDSYGVDGMDLTSQgagTYWyLPPEcfvVGKEPPKISNKVDVWSVGVIFFQ 618
Cdd:cd14012  130 LHAGNVLLDRDAGTGIVKLTDYSLGKTL-LDMCSRGSLDEFKQ---TYW-LPPE---LAQGSKSPTRKTDVWDLGLLFLQ 201
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 619 CLYGrkpfghnqsqQDILQENTilkaTEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQlandpyLLPH 689
Cdd:cd14012  202 MLFG----------LDVLEKYT----SPNPVLVSLDLSASLQDFLSKCLSLDPKKRPTALE------LLPH 252
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
419-687 1.02e-16

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: 80.57  E-value: 1.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKI-----HQLNKSWRDEKKEnyhkhacreYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYC 493
Cdd:cd06607   14 FGAVYYARNKRTSEVVAIKKmsysgKQSTEKWQDIIKE---------VKFLRQLRHPNTIEYKGCY-LREHTAWLVMEYC 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 494 EGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPpiIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGV 573
Cdd:cd06607   84 LGSASDIVEVHKKPLQEVEIAAICHGALQGLAYLHSHNR--IHRDVKAGNILL---TEPGTVKLADFGSASLVCPANSFV 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 574 dgmdltsqgaGTYWYLPPECFVVGKEPPkISNKVDVWSVGVIFFQcLYGRKP--FGHN---------QSQQDILQENTIl 642
Cdd:cd06607  159 ----------GTPYWMAPEVILAMDEGQ-YDGKVDVWSLGITCIE-LAERKPplFNMNamsalyhiaQNDSPTLSSGEW- 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 211971036 643 katevqfpvkpvvSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLL 687
Cdd:cd06607  226 -------------SDDFRNFVDSCLQKIPQDRPSAEDLLKHPFVT 257
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
422-686 1.42e-16

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: 80.36  E-value: 1.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKihQLNKSwRDEKKEnyhkHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFY 501
Cdd:cd06647   23 VYTAIDVATGQEVAIK--QMNLQ-QQPKKE----LIINEILVMRENKNPNIVNYLDSY-LVGDELWVVMEYLAGGSLTDV 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 502 LKQhKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILL-VDGTacgeIKITDFGL-SKIMDDDSYgvdgmdlT 579
Cdd:cd06647   95 VTE-TCMDEGQIAAVCRECLQALEFLHSNQ--VIHRDIKSDNILLgMDGS----VKLTDFGFcAQITPEQSK-------R 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 580 SQGAGTYWYLPPECFVVGKEPPKisnkVDVWSVGVIFFQCLYGRKPFghnqsqqdiLQENTI----LKAT----EVQFPV 651
Cdd:cd06647  161 STMVGTPYWMAPEVVTRKAYGPK----VDIWSLGIMAIEMVEGEPPY---------LNENPLralyLIATngtpELQNPE 227
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 211971036 652 KpvVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06647  228 K--LSAIFRDFLNRCLEMDVEKRGSAKELLQHPFL 260
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
459-647 1.44e-16

Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TBK1 is also called T2K and NF-kB-activating kinase. It is widely expressed in most cell types and acts as an IkappaB kinase (IKK)-activating kinase responsible for NF-kB activation in response to growth factors. It plays a role in modulating inflammatory responses through the NF-kB pathway. TKB1 is also a major player in innate immune responses since it functions as a virus-activated kinase necessary for establishing an antiviral state. It phosphorylates IRF-3 and IRF-7, which are important transcription factors for inducing type I interferon during viral infection. In addition, TBK1 may also play roles in cell transformation and oncogenesis. The TBK1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270890 [Multi-domain]  Cd Length: 316  Bit Score: 81.38  E-value: 1.44e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLydyFSLDTDTF----CTVLEYCEGNDLdFYLKQHKL----MSEKEARSIVMQIVNALRYLNEI 530
Cdd:cd13988   40 REFEVLKKLNHKNIVKL---FAIEEELTtrhkVLVMELCPCGSL-YTVLEEPSnaygLPESEFLIVLRDVVAGMNHLREN 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 531 KppIIHYDLKPGNILLV---DGTACgeIKITDFGLSK-IMDDDSYgvdgMDLTsqgaGTYWYLPPECF---VVGKEPPK- 602
Cdd:cd13988  116 G--IVHRDIKPGNIMRVigeDGQSV--YKLTDFGAAReLEDDEQF----VSLY----GTEEYLHPDMYeraVLRKDHQKk 183
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 211971036 603 ISNKVDVWSVGVIFFQCLYGR---KPFGHNQSQQDILQENTILKATEV 647
Cdd:cd13988  184 YGATVDLWSIGVTFYHAATGSlpfRPFEGPRRNKEVMYKIITGKPSGA 231
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
419-626 1.57e-16

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: 80.47  E-value: 1.57e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfdLYEQRYAAVKIHQLNKswrDEKKENYHKHACREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDL 498
Cdd:cd14146    7 FGKVYRA--TWKGQEVAVKAARQDP---DEDIKATAESVRQEAKLFSMLRHPNIIKLEG-VCLEEPNLCLVMEFARGGTL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLK-QHKLMSEKEARSI--------VMQIVNALRYLN-EIKPPIIHYDLKPGNILLVDGTACGEI-----KITDFGLS 563
Cdd:cd14146   81 NRALAaANAAPGPRRARRIpphilvnwAVQIARGMLYLHeEAVVPILHRDLKSSNILLLEKIEHDDIcnktlKITDFGLA 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211971036 564 KimddDSYGVDGMdltsQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd14146  161 R----EWHRTTKM----SAAGTYAWMAPEVI----KSSLFSKGSDIWSYGVLLWELLTGEVPY 211
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
432-626 1.67e-16

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 81.40  E-value: 1.67e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 432 RYAAVKIhqLNKswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEK 511
Cdd:PTZ00263  44 EYYAIKC--LKK--REILKMKQVQHVAQEKSILMELSHPFIVNMMCSF-QDENRVYFLLEFVVGGELFTHLRKAGRFPND 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 512 EARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvDGTacGEIKITDFGLSKIMDDDSYGVdgmdltsqgAGTYWYLPP 591
Cdd:PTZ00263 119 VAKFYHAELVLAFEYLHSKD--IIYRDLKPENLLL-DNK--GHVKVTDFGFAKKVPDRTFTL---------CGTPEYLAP 184
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 211971036 592 ECFvvgkePPKISNK-VDVWSVGVIFFQCLYGRKPF 626
Cdd:PTZ00263 185 EVI-----QSKGHGKaVDWWTMGVLLYEFIAGYPPF 215
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
419-636 1.68e-16

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: 80.78  E-value: 1.68e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihqlnkSWRDEKKEN-YHKHACREYRIHKEL---DHPRIVKLYDYFS---LDTDTFCT-VL 490
Cdd:cd07863   13 YGTVYKARDPHSGHFVALK------SVRVQTNEDgLPLSTVREVALLKRLeafDHPNIVRLMDVCAtsrTDRETKVTlVF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 491 EYCEgNDLDFYLKQHK---LMSEKeARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMd 567
Cdd:cd07863   87 EHVD-QDLRTYLDKVPppgLPAET-IKDLMRQFLRGLDFLHANC--IVHRDLKPENILVTSG---GQVKLADFGLARIY- 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 568 ddSYgvdGMDLTSQgAGTYWYLPPECFVvgkePPKISNKVDVWSVGVIFFQcLYGRKPFGHNQSQQDIL 636
Cdd:cd07863  159 --SC---QMALTPV-VVTLWYRAPEVLL----QSTYATPVDMWSVGCIFAE-MFRRKPLFCGNSEADQL 216
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
430-637 1.88e-16

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: 79.63  E-value: 1.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 430 EQRYAAVKIhQLNKSWRDekKENYHKHACreyrIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQH--KL 507
Cdd:cd08219   25 DQKYAMKEI-RLPKSSSA--VEDSRKEAV----LLAKMKHPNIVAFKESFEADGHLY-IVMEYCDGGDLMQKIKLQrgKL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 508 MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsygvdgMDLTSQGAGTYW 587
Cdd:cd08219   97 FPEDTILQWFVQMCLGVQHIHEKR--VLHRDIKSKNIFL---TQNGKVKLGDFGSARLLTSP------GAYACTYVGTPY 165
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 211971036 588 YLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQ 637
Cdd:cd08219  166 YVPPEIW----ENMPYNNKSDIWSLGCILYELCTLKHPFQANSWKNLILK 211
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
458-680 1.90e-16

Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of Drosophila melanogaster NAK, human BMP-2-inducible protein kinase (BMP2K or BIKe) and similar vertebrate proteins, as well as the Saccharomyces cerevisiae proteins Prk1, Actin-regulating kinase 1 (Ark1), and Akl1. NAK was the first characterized member of this subfamily. It plays a role in asymmetric cell division through its association with Numb. It also regulates the localization of Dlg, a protein essential for septate junction formation. BMP2K contains a nuclear localization signal and a kinase domain that is capable of phosphorylating itself and myelin basic protein. The expression of the BMP2K gene is increase during BMP-2-induced osteoblast differentiation. It may function to control the rate of differentiation. Prk1, Ark1, and Akl1 comprise a subfamily of yeast proteins that are important regulators of the actin cytoskeleton and endocytosis. They share an N-terminal kinase domain but no significant homology in other regions of their sequences. The NAK-like subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270939 [Multi-domain]  Cd Length: 277  Bit Score: 80.02  E-value: 1.90e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 458 CREYRIHKEL-DHPRIVKLYDYFSLDT-DTFCTVL---EYCE-GNDLDFYLK--QHKLmSEKEARSIVMQIVNALRYLNE 529
Cdd:cd14037   48 KREIEIMKRLsGHKNIVGYIDSSANRSgNGVYEVLllmEYCKgGGVIDLMNQrlQTGL-TESEILKIFCDVCEAVAAMHY 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 530 IKPPIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSYGVDGMDLTSQGAGTY---WYLPPECFVVGKEPPkISNK 606
Cdd:cd14037  127 LKPPLIHRDLKVENVLISDS---GNYKLCDFGSATTKILPPQTKQGVTYVEEDIKKYttlQYRAPEMIDLYRGKP-ITEK 202
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 211971036 607 VDVWSVGVIFFQCLYGRKPFGHNQSQqdilqenTILKATeVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQL 680
Cdd:cd14037  203 SDIWALGCLLYKLCFYTTPFEESGQL-------AILNGN-FTFPDNSRYSKRLHKLIRYMLEEDPEKRPNIYQV 268
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
419-626 2.05e-16

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: 80.39  E-value: 2.05e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKswrdekKENYHKHACREYRIHKELDHPRIVKLYDYF-SLDTDTFctVLEYCEgND 497
Cdd:cd07870   13 YATVYKGISRINGQLVALKVISMKT------EEGVPFTAIREASLLKGLKHANIVLLHDIIhTKETLTF--VFEYMH-TD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKL-MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGL--SKIMDDDSYgvd 574
Cdd:cd07870   84 LAQYMIQHPGgLHPYNVRLFMFQLLRGLAYIHGQH--ILHRDLKPQNLLI---SYLGELKLADFGLarAKSIPSQTY--- 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 211971036 575 gmdltSQGAGTYWYLPPECFVVGKEppkISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd07870  156 -----SSEVVTLWYRPPDVLLGATD---YSSALDIWGAGCIFIEMLQGQPAF 199
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
472-686 2.55e-16

Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase signal-integrating kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAPK signal-integrating kinases (Mnks) are MAPK-activated protein kinases and is comprised by a group of four proteins, produced by alternative splicing from two genes (Mnk1 and Mnk2). The isoforms of Mnk1 (1a/1b) and Mnk2 (2a/2b) differ at their C-termini, with the a-form having a longer C-terminus containing a MAPK-binding region. All Mnks contain a catalytic kinase domain and a polybasic region at the N-terminus which binds importin and the eukaryotic initiation factor eIF4G. The best characterized Mnk substrate is eIF4G, whose phosphorylation may promote the export of certain mRNAs from the nucleus. Mnk also phosphorylate substrates that bind to AU-rich elements that regulate mRNA stability and translation. Mnks have also been implicated in tyrosine kinase receptor signaling, inflammation, and cell prolieration or survival. The Mnk subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271076 [Multi-domain]  Cd Length: 289  Bit Score: 80.07  E-value: 2.55e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 472 IVKLYDYFSLDTdTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTA 551
Cdd:cd14174   62 ILELIEFFEDDT-RFYLVFEKLRGGSILAHIQKRKHFNEREASRVVRDIASALDFLH--TKGIAHRDLKPENILCESPDK 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 552 CGEIKITDFGLSKIMDDDS--YGVDGMDLTSQgAGTYWYLPPECFVVGKEPPKISNK-VDVWSVGVIFFQCLYGRKPF-G 627
Cdd:cd14174  139 VSPVKICDFDLGSGVKLNSacTPITTPELTTP-CGSAEYMAPEVVEVFTDEATFYDKrCDLWSLGVILYIMLSGYPPFvG 217
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211971036 628 H------------NQSQQDILQENtiLKATEVQFPVK--PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14174  218 HcgtdcgwdrgevCRVCQNKLFES--IQEGKYEFPDKdwSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
406-682 2.87e-16

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: 80.86  E-value: 2.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 406 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDT-- 483
Cdd:cd07878   15 ERYQNLTPVGSGAYGSVCSAYDTRLRQKVAVK-----KLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVFTPATsi 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 484 DTFCTV--LEYCEGNDLDFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtaCgEIKITDFG 561
Cdd:cd07878   90 ENFNEVylVTNLMGADLNNIVKCQKL-SDEHVQFLIYQLLRGLKYIHSAG--IIHRDLKPSNVAVNED--C-ELRILDFG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 562 LSKIMDDDSYGVdgmdltsqgAGTYWYLPPECFVVGKEppkISNKVDVWSVGVIFFQCLYGRKPFGHNQSqqdILQENTI 641
Cdd:cd07878  164 LARQADDEMTGY---------VATRWYRAPEIMLNWMH---YNQTVDIWSVGCIMAELLKGKALFPGNDY---IDQLKRI 228
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 211971036 642 LKATEVQFP--VKPVVSSEAKAFIRRCLAYRKEDRFDVHQLAN 682
Cdd:cd07878  229 MEVVGTPSPevLKKISSEHARKYIQSLPHMPQQDLKKIFRGAN 271
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
422-636 3.17e-16

Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher eukaryotes; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. 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. CDK1/cyclin A2 has also been implicated as an important regulator of S phase events. The CDK1/cyclin B complex is critical for G2 to M phase transition. It induces mitosis by activating nuclear enzymes that regulate chromatin condensation, nuclear membrane degradation, mitosis-specific microtubule and cytoskeletal reorganization. CDK1 also associates with cyclin E and plays a role in the entry into S phase. CDK1 transcription is stable throughout the cell cycle but is modulated in some pathological conditions. It may play a role in regulating apoptosis under these conditions. In breast cancer cells, HER2 can mediate apoptosis by inactivating CDK1. Activation of CDK1 may contribute to HIV-1 induced apoptosis as well as neuronal apoptosis in neurodegenerative diseases. 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: 270845 [Multi-domain]  Cd Length: 285  Bit Score: 79.77  E-value: 3.17e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKIHQLnkswrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYcegndLDFY 501
Cdd:cd07861   16 VYKGRNKKTGQIVAMKKIRL-----ESEEEGVPSTAIREISLLKELQHPNIVCLEDVLMQENRLY-LVFEF-----LSMD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 502 LKQH-------KLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNiLLVDGTacGEIKITDFGLSKimdddSYGVD 574
Cdd:cd07861   85 LKKYldslpkgKYMDAELVKSYLYQILQGILFCHSRR--VLHRDLKPQN-LLIDNK--GVIKLADFGLAR-----AFGIP 154
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 575 GMDLTSQGAgTYWYLPPECFVVGkepPKISNKVDVWSVGVIFFQcLYGRKPFGHNQSQQDIL 636
Cdd:cd07861  155 VRVYTHEVV-TLWYRAPEVLLGS---PRYSTPVDIWSIGTIFAE-MATKKPLFHGDSEIDQL 211
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
419-628 3.54e-16

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: 79.11  E-value: 3.54e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFdlYEQRYAAVKIHQLN----KSWRDekkenyhkHACREYRIHKELDHPRIVKLYDYFSLDTDTFCTVLEYCE 494
Cdd:cd14064    6 FGKVYKGR--CRNKIVAIKRYRANtycsKSDVD--------MFCREVSILCRLNHPCVIQFVGACLDDPSQFAIVTQYVS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 GNDLdFYL--KQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILL-VDGTAcgeiKITDFGLSKI---MDD 568
Cdd:cd14064   76 GGSL-FSLlhEQKRVIDLQSKLIIAVDVAKGMEYLHNLTQPIIHRDLNSHNILLyEDGHA----VVADFGESRFlqsLDE 150
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 569 DsygvdgmDLTSQGAGTYWyLPPECFvvgKEPPKISNKVDVWSVGVIFFQCLYGRKPFGH 628
Cdd:cd14064  151 D-------NMTKQPGNLRW-MAPEVF---TQCTRYSIKADVFSYALCLWELLTGEIPFAH 199
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
419-680 3.87e-16

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK4 shows a restricted expression pattern and is usually found in epithelial cells. It is expressed in nephrons and in extrarenal tissues including intestine, eye, mammary glands, and prostate. WNK4 regulates a variety of ion transport proteins including apical or basolateral ion transporters, ion channels in the transcellular pathway, and claudins in the paracellular pathway. Mutations in WNK4 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK4 inhibits the activity of the thiazide-sensitive Na-Cl cotransporter (NCC), which is responsible for about 15% of NaCl reabsorption in the kidney. It also inhibits the renal outer medullary potassium channel (ROMK) and decreases its surface expression. Hypertension and hyperkalemia in PHAII patients with WNK4 mutations may be partly due to increased NaCl reabsorption through NCC and impaired renal potassium secretion by ROMK, respectively. The WNK4 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: 270935 [Multi-domain]  Cd Length: 261  Bit Score: 78.89  E-value: 3.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDL---YEQRYAAVKIHQLNKSWRDEKKEnyhkhacrEYRIHKELDHPRIVKLYDYF-SLDTDTFCTVL--EY 492
Cdd:cd14033   14 FKTVYRGLDTettVEVAWCELQTRKLSKGERQRFSE--------EVEMLKGLQHPNIVRFYDSWkSTVRGHKCIILvtEL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 493 CEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTacGEIKITDFGLSKImdddsyg 572
Cdd:cd14033   86 MTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRCPPILHRDLKCDNIFITGPT--GSVKIGDLGLATL------- 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 573 vDGMDLTSQGAGTYWYLPPECFvvgkePPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQFPVK 652
Cdd:cd14033  157 -KRASFAKSVIGTPEFMAPEMY-----EEKYDEAVDVYAFGMCILEMATSEYPYSECQNAAQIYRKVTSGIKPDSFYKVK 230
                        250       260
                 ....*....|....*....|....*...
gi 211971036 653 pvvSSEAKAFIRRCLAYRKEDRFDVHQL 680
Cdd:cd14033  231 ---VPELKEIIEGCIRTDKDERFTIQDL 255
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
469-654 4.14e-16

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: 80.45  E-value: 4.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLvd 548
Cdd:cd05617   75 NPFLVGLHSCFQTTSRLF-LVIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHE--RGIIYRDLKLDNVLL-- 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 549 gTACGEIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPPEcFVVGKEppkISNKVDVWSVGVIFFQCLYGRKPFgh 628
Cdd:cd05617  150 -DADGHIKLTDYGMCK------EGLGPGDTTSTFCGTPNYIAPE-ILRGEE---YGFSVDWWALGVLMFEMMAGRSPF-- 216
                        170       180
                 ....*....|....*....|....*....
gi 211971036 629 nqsqqDILQENTILKATEVQFPV---KPV 654
Cdd:cd05617  217 -----DIITDNPDMNTEDYLFQVileKPI 240
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
469-686 4.25e-16

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: 79.30  E-value: 4.25e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVD 548
Cdd:cd14173   59 HRNVLELIEFFE-EEDKFYLVFEKMRGGSILSHIHRRRHFNELEASVVVQDIASALDFLH--NKGIAHRDLKPENILCEH 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 549 GTACGEIKITDFGL-SKI-MDDDSYGVDGMDLTSQgAGTYWYLPPECFVVGKEPPKISNK-VDVWSVGVIFFQCLYGRKP 625
Cdd:cd14173  136 PNQVSPVKICDFDLgSGIkLNSDCSPISTPELLTP-CGSAEYMAPEVVEAFNEEASIYDKrCDLWSLGVILYIMLSGYPP 214
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036 626 F-GHNQSQ------------QDILQENtiLKATEVQFPVK--PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14173  215 FvGRCGSDcgwdrgeacpacQNMLFES--IQEGKYEFPEKdwAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
449-674 4.26e-16

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: 79.11  E-value: 4.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 449 KKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDtFCTVLEYCEGNDLDFYLKQHKLMSEKEARSI--VMQIVNALRY 526
Cdd:cd05577   32 KKKKGETMALNEKIILEKVSSPFIVSLAYAFETKDK-LCLVLTLMNGGDLKYHIYNVGTRGFSEARAIfyAAEIICGLEH 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 527 LNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLskimdddSYGVDGMDLTSQGAGTYWYLPPEcfvVGKEPPKISNK 606
Cdd:cd05577  111 LHNRF--IVYRDLKPENILLDDH---GHVRISDLGL-------AVEFKGGKKIKGRVGTHGYMAPE---VLQKEVAYDFS 175
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 607 VDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQFPVKpvVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd05577  176 VDWFALGCMLYEMIAGRSPFRQRKEKVDKEELKRRTLEMAVEYPDS--FSPEARSLCEGLLQKDPERR 241
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
465-696 4.65e-16

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: 79.06  E-value: 4.65e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 465 KELDHPRIVKLYDYFSLDTdTFCTVLEYCEGNDLDFYLKQHKLmSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNI 544
Cdd:cd06917   57 KLGQPKNIIKYYGSYLKGP-SLWIIMDYCEGGSIRTLMRAGPI-AERYIAVIMREVLVALKFIH--KDGIIHRDIKAANI 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 545 LLvdgTACGEIKITDFGLSKIMDDDSYGVDGMdltsqgAGTYWYLPPECFVVGKEppkISNKVDVWSVGVIFFQCLYGRK 624
Cdd:cd06917  133 LV---TNTGNVKLCDFGVAASLNQNSSKRSTF------VGTPYWMAPEVITEGKY---YDTKADIWSLGITTYEMATGNP 200
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 211971036 625 PFghnqSQQDILQENTILKATevQFPVKP--VVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLPHMRRSNSS 696
Cdd:cd06917  201 PY----SDVDALRAVMLIPKS--KPPRLEgnGYSPLLKEFVAACLDEEPKDRLSADELLKSKWIKQHSKTPTSV 268
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
419-686 5.02e-16

Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. WNK1 is widely expressed and is most abundant in the testis. In hyperosmotic or hypotonic low-chloride stress conditions, WNK1 is activated and it phosphorylates its substrates including SPAK and OSR1 kinases, which regulate the activity of cation-chloride cotransporters through direct interaction and phosphorylation. Mutations in WNK1 cause PseudoHypoAldosteronism type II (PHAII), characterized by hypertension and hyperkalemia. WNK1 negates WNK4-mediated inhibition of the sodium-chloride cotransporter NCC and activates the epithelial sodium channel ENaC by activating SGK1. WNK1 also decreases the surface expression of renal outer medullary potassium channel (ROMK) by stimulating their endocytosis. Hypertension and hyperkalemia in PHAII patients with WNK1 mutations may be due partly to increased activity of NCC and ENaC, and impaired renal potassium secretion by ROMK, respectively. In addition, WNK1 interacts with MEKK2/3 and acts as an activator of extracellular signal-regulated kinase (ERK) 5. It also negatively regulates TGFbeta signaling. WNKs comprise a subfamily of STKs with an unusual placement of the catalytic lysine relative to all other protein kinases. The WNK1 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: 270932 [Multi-domain]  Cd Length: 289  Bit Score: 79.32  E-value: 5.02e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDL---YEQRYAAVKIHQLNKSWRDEKKEnyhkhacrEYRIHKELDHPRIVKLYDYF-SLDTDTFCTVL--EY 492
Cdd:cd14030   38 FKTVYKGLDTettVEVAWCELQDRKLSKSERQRFKE--------EAGMLKGLQHPNIVRFYDSWeSTVKGKKCIVLvtEL 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 493 CEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDGTacGEIKITDFGLSKIMDddsyg 572
Cdd:cd14030  110 MTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTPPIIHRDLKCDNIFITGPT--GSVKIGDLGLATLKR----- 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 573 vdgMDLTSQGAGTYWYLPPECFvvgkePPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQentilkatEVQFPVK 652
Cdd:cd14030  183 ---ASFAKSVIGTPEFMAPEMY-----EEKYDESVDVYAFGMCMLEMATSEYPYSECQNAAQIYR--------RVTSGVK 246
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 211971036 653 P-----VVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14030  247 PasfdkVAIPEVKEIIEGCIRQNKDERYAIKDLLNHAFF 285
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
448-685 5.14e-16

Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein kinase subfamily 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The SnRKs form three different subfamilies designated SnRK1-3. SnRK2 is represented in this cd. SnRK2s are involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development. The SnRK2s subfamily is in turn classed into three subgroups, all 3 of which are represented in this CD. Group 1 comprises kinases not activated by ABA, group 2 - kinases not activated or activated very weakly by ABA (depending on plant species), and group 3 - kinases strongly activated by ABA. The SnRKs belong to a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271132 [Multi-domain]  Cd Length: 257  Bit Score: 78.66  E-value: 5.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 448 EKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYL 527
Cdd:cd14662   34 ERGLKIDENVQREIINHRSLRHPNIIRFKEVV-LTPTHLAIVMEYAAGGELFERICNAGRFSEDEARYFFQQLISGVSYC 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 528 NEIKppIIHYDLKPGNILLvDGTACGEIKITDFGLSKimdddsygvdGMDLTSQ---GAGTYWYLPPECFVVGKEPPKIs 604
Cdd:cd14662  113 HSMQ--ICHRDLKLENTLL-DGSPAPRLKICDFGYSK----------SSVLHSQpksTVGTPAYIAPEVLSRKEYDGKV- 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 605 nkVDVWSVGVIFFQCLYGRKPFGHNQSQQDIlqENTILKATEVQFPVKPVV--SSEAKAFIRRCLAYRKEDRFDVHQLAN 682
Cdd:cd14662  179 --ADVWSCGVTLYVMLVGAYPFEDPDDPKNF--RKTIQRIMSVQYKIPDYVrvSQDCRHLLSRIFVANPAKRITIPEIKN 254

                 ...
gi 211971036 683 DPY 685
Cdd:cd14662  255 HPW 257
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
431-667 5.52e-16

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: 80.28  E-value: 5.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 431 QRYAAVKIHQLnKSWRdeKKENYHK----HACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHK 506
Cdd:cd05629   21 QKKDTGKIYAM-KTLL--KSEMFKKdqlaHVKAERDVLAESDSPWVVSLYYSFQ-DAQYLYLIMEFLPGGDLMTMLIKYD 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 507 LMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLS----KIMDDDSY----------- 571
Cdd:cd05629   97 TFSEDVTRFYMAECVLAIEAVH--KLGFIHRDIKPDNILI---DRGGHIKLSDFGLStgfhKQHDSAYYqkllqgksnkn 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 572 --------GVDGMDLTSQG------------------AGTYWYLPPECFVvgkePPKISNKVDVWSVGVIFFQCLYGRKP 625
Cdd:cd05629  172 ridnrnsvAVDSINLTMSSkdqiatwkknrrlmaystVGTPDYIAPEIFL----QQGYGQECDWWSLGAIMFECLIGWPP 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 211971036 626 FGHNQSQQDILQentILKATE-VQFPVKPVVSSEAKAFIRRCL 667
Cdd:cd05629  248 FCSENSHETYRK---IINWREtLYFPDDIHLSVEAEDLIRRLI 287
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
422-686 5.88e-16

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: 78.77  E-value: 5.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKIHQLNKSwrdekkENYHKHACREYRIHKELDHPRIVKLYDYFSLDTD-TFCTvlEYCEGNDLDF 500
Cdd:cd06619   17 VYKAYHLLTRRILAVKVIPLDIT------VELQKQIMSELEILYKCDSPYIIGFYGAFFVENRiSICT--EFMDGGSLDV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 501 YLKqhklMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMdddsygVDGMDLTS 580
Cdd:cd06619   89 YRK----IPEHVLGRIAVAVVKGLTYLWSLK--ILHRDVKPSNMLV---NTRGQVKLCDFGVSTQL------VNSIAKTY 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 581 qgAGTYWYLPPEcFVVGKEPPKISnkvDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKA-TEVQFPVKPV--VSS 657
Cdd:cd06619  154 --VGTNAYMAPE-RISGEQYGIHS---DVWSLGISFMELALGRFPYPQIQKNQGSLMPLQLLQCiVDEDPPVLPVgqFSE 227
                        250       260
                 ....*....|....*....|....*....
gi 211971036 658 EAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06619  228 KFVHFITQCMRKQPKERPAPENLMDHPFI 256
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
472-686 6.51e-16

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: 78.07  E-value: 6.51e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 472 IVKLYDYFSlDTDTFCTVLEYCE-GNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNiLLVDgT 550
Cdd:cd14102   66 VIKLLDWYE-RPDGFLIVMERPEpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCG--VVHRDIKDEN-LLVD-L 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 551 ACGEIKITDFGLSKIMDDDSYgvdgmdltSQGAGTYWYLPPECFVVGKEPPKISNkvdVWSVGVIFFQCLYGRKPFghnQ 630
Cdd:cd14102  141 RTGELKLIDFGSGALLKDTVY--------TDFDGTRVYSPPEWIRYHRYHGRSAT---VWSLGVLLYDMVCGDIPF---E 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036 631 SQQDILQentilkateVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14102  207 QDEEILR---------GRLYFRRRVSPECQQLIKWCLSLRPSDRPTLEQIFDHPWM 253
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
419-637 6.76e-16

Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of most class EphA receptors including EphA3, EphA4, EphA5, and EphA7, but excluding EphA1, EphA2 and EphA10. Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. One exception is EphA4, which also binds ephrins-B2/B3. EphA receptors and ephrin-A ligands are expressed in multiple areas of the developing brain, especially in the retina and tectum. They are part of a system controlling retinotectal mapping. EphRs comprise the largest subfamily of receptor PTKs (RTKs). EphRs contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270651 [Multi-domain]  Cd Length: 267  Bit Score: 78.37  E-value: 6.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEV-YKAFDLYEQRYAAVKIHQLNKSWRDEKKENYhkhaCREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGND 497
Cdd:cd05066   17 FGEVcSGRLKLPGKREIPVAIKTLKAGYTEKQRRDF----LSEASIMGQFDHPNIIHLEGVVT-RSKPVMIVTEYMENGS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHklmsekEARSIVMQIVNALR-------YLNEIKppIIHYDLKPGNILLVDGTACgeiKITDFGLSKIMDDDS 570
Cdd:cd05066   92 LDAFLRKH------DGQFTVIQLVGMLRgiasgmkYLSDMG--YVHRDLAARNILVNSNLVC---KVSDFGLSRVLEDDP 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 571 ygvDGMDLTSQGAGTYWYLPPECFVVgkepPKISNKVDVWSVGVIFFQCL-YGRKPFgHNQSQQDILQ 637
Cdd:cd05066  161 ---EAAYTTRGGKIPIRWTAPEAIAY----RKFTSASDVWSYGIVMWEVMsYGERPY-WEMSNQDVIK 220
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
422-626 8.53e-16

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: 78.32  E-value: 8.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKIHQLnkswrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEgNDLDFY 501
Cdd:cd07860   16 VYKARNKLTGEVVALKKIRL-----DTETEGVPSTAIREISLLKELNHPNIVKLLDVIHTENKLY-LVFEFLH-QDLKKF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 502 LKQHKL--MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddSYGVDGMDLT 579
Cdd:cd07860   89 MDASALtgIPLPLIKSYLFQLLQGLAFCHSHR--VLHRDLKPQNLLI---NTEGAIKLADFGLAR-----AFGVPVRTYT 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 211971036 580 SQgAGTYWYLPPECFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd07860  159 HE-VVTLWYRAPEILLGCK---YYSTAVDIWSLGCIFAEMVTRRALF 201
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
468-626 8.87e-16

Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. aPKCs only require phosphatidylserine (PS) for activation. They contain a C2-like region, instead of a calcium-binding (C2) region found in classical PKCs, in their regulatory domain. There are two aPKC isoforms, zeta and iota. aPKCs are involved in many cellular functions including proliferation, migration, apoptosis, polarity maintenance and cytoskeletal regulation. They also play a critical role in the regulation of glucose metabolism and in the pathogenesis of type 2 diabetes. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. The aPKC subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270740 [Multi-domain]  Cd Length: 328  Bit Score: 79.00  E-value: 8.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 468 DHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLv 547
Cdd:cd05588   54 NHPFLVGLHSCFQTESRLF-FVIEFVNGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHE--KGIIYRDLKLDNVLL- 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 548 dgTACGEIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPPEcFVVGKEppkISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd05588  130 --DSEGHIKLTDYGMCK------EGLRPGDTTSTFCGTPNYIAPE-ILRGED---YGFSVDWWALGVLMFEMLAGRSPF 196
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
419-686 8.98e-16

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: 78.74  E-value: 8.98e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqlnksWRDEKKenYHKHACREYRI------HKELDHPRIVKLYDYFSLdTDTFCTVLEY 492
Cdd:cd14210   26 FGQVVKCLDHKTGQLVAIKI------IRNKKR--FHQQALVEVKIlkhlndNDPDDKHNIVRYKDSFIF-RGHLCIVFEL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 493 CEGNDLDFyLKQHKL--MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGeIKITDFGLSKIMDDDS 570
Cdd:cd14210   97 LSINLYEL-LKSNNFqgLSLSLIRKFAKQILQALQFLHKLN--IIHCDLKPENILLKQPSKSS-IKVIDFGSSCFEGEKV 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 571 YgvdgmdltsqgagTY----WYLPPECFVVGKEPPKIsnkvDVWSVGVIFFQCLYGRKPF-GHNQSQQ-----DIL---Q 637
Cdd:cd14210  173 Y-------------TYiqsrFYRAPEVILGLPYDTAI----DMWSLGCILAELYTGYPLFpGENEEEQlacimEVLgvpP 235
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036 638 ENTILKAT------EVQFPVKPVVSSEAK---------------------AFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14210  236 KSLIDKASrrkkffDSNGKPRPTTNSKGKkrrpgskslaqvlkcddpsflDFLKKCLRWDPSERMTPEEALQHPWI 311
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
449-684 9.21e-16

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: 78.41  E-value: 9.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 449 KKENYHKHACREYRIHKELDHPRIVKLYdyFSLDTDT-FCTVLEYCEGNDLDFYLKQHKLMSEKEARSI--VMQIVNALR 525
Cdd:cd05607   41 KKKSGEKMALLEKEILEKVNSPFIVSLA--YAFETKThLCLVMSLMNGGDLKYHIYNVGERGIEMERVIfySAQITCGIL 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 526 YLNEIKppIIHYDLKPGNILLVDGTACgeiKITDFGLSKIMDDDSygvdgmdLTSQGAGTYWYLPPEcfVVGKEPpkISN 605
Cdd:cd05607  119 HLHSLK--IVYRDMKPENVLLDDNGNC---RLSDLGLAVEVKEGK-------PITQRAGTNGYMAPE--ILKEES--YSY 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 606 KVDVWSVGVIFFQCLYGRKPFGHNQSQ--QDILQENTIlkATEVQFPvKPVVSSEAKAFIRRCLAYRKEDRFDVHQLAND 683
Cdd:cd05607  183 PVDWFAMGCSIYEMVAGRTPFRDHKEKvsKEELKRRTL--EDEVKFE-HQNFTEEAKDICRLFLAKKPENRLGSRTNDDD 259

                 .
gi 211971036 684 P 684
Cdd:cd05607  260 P 260
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
443-626 9.23e-16

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: 78.51  E-value: 9.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTdTFCTVLEYCEgNDLDFYLKQ-HKLMSEKEARSIVMQIV 521
Cdd:cd07873   33 KEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIIHTEK-SLTLVFEYLD-KDLKQYLDDcGNSINMHNVKLFLFQLL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 522 NALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLS--KIMDDDSYgvdgmdltSQGAGTYWYLPPECFVVGKE 599
Cdd:cd07873  111 RGLAYCHRRK--VLHRDLKPQNLLINER---GELKLADFGLAraKSIPTKTY--------SNEVVTLWYRPPDILLGSTD 177
                        170       180
                 ....*....|....*....|....*..
gi 211971036 600 ppkISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd07873  178 ---YSTQIDMWGVGCIFYEMSTGRPLF 201
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
422-637 9.48e-16

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: 78.24  E-value: 9.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKIHQLnkswrDEKKENYHKHACREYRIHKELDHPRIVKLYDYfsLDTDTFCT-VLEYCEgNDLDF 500
Cdd:cd07839   16 VFKAKNRETHEIVALKRVRL-----DDDDEGVPSSALREICLLKELKHKNIVRLYDV--LHSDKKLTlVFEYCD-QDLKK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 501 YLKQ-HKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKimdddSYGVDgMDLT 579
Cdd:cd07839   88 YFDScNGDIDPEIVKSFMFQLLKGLAFCHSHN--VLHRDLKPQNLLINKN---GELKLADFGLAR-----AFGIP-VRCY 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 580 SQGAGTYWYLPPECFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQ 637
Cdd:cd07839  157 SAEVVTLWYRPPDVLFGAK---LYSTSIDMWSAGCIFAELANAGRPLFPGNDVDDQLK 211
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
443-626 9.93e-16

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: 78.50  E-value: 9.93e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTdTFCTVLEYcegndLDFYLKQH-----KLMSEKEARSIV 517
Cdd:cd07872   37 KEIRLEHEEGAPCTAIREVSLLKDLKHANIVTLHDIVHTDK-SLTLVFEY-----LDKDLKQYmddcgNIMSMHNVKIFL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 518 MQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLS--KIMDDDSYgvdgmdltSQGAGTYWYLPPECFV 595
Cdd:cd07872  111 YQILRGLAYCHRRK--VLHRDLKPQNLLINER---GELKLADFGLAraKSVPTKTY--------SNEVVTLWYRPPDVLL 177
                        170       180       190
                 ....*....|....*....|....*....|.
gi 211971036 596 VGKEppkISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd07872  178 GSSE---YSTQIDMWGVGCIFFEMASGRPLF 205
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
431-665 1.04e-15

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: 78.90  E-value: 1.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 431 QRYAAVKIhqLNKSwrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSE 510
Cdd:cd05598   26 NALYAMKT--LRKK--DVLKRNQVAHVKAERDILAEADNEWVVKLYYSFQ-DKENLYFVMDYIPGGDLMSLLIKKGIFEE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 511 KEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSK----IMDDDSYgvdgmdLTSQGAGTY 586
Cdd:cd05598  101 DLARFYIAELVCAIESVHKMG--FIHRDIKPDNILI---DRDGHIKLTDFGLCTgfrwTHDSKYY------LAHSLVGTP 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 587 WYLPPECF-VVGkeppkISNKVDVWSVGVIFFQCLYGRKPFGHN---QSQQDILQENTILkatevQFPVKPVVSSEAKAF 662
Cdd:cd05598  170 NYIAPEVLlRTG-----YTQLCDWWSVGVILYEMLVGQPPFLAQtpaETQLKVINWRTTL-----KIPHEANLSPEAKDL 239

                 ...
gi 211971036 663 IRR 665
Cdd:cd05598  240 ILR 242
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
398-674 1.18e-15

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO3 is also known as JIK (c-Jun N-terminal kinase inhibitory kinase) or KFC (kinase from chicken). It specifically activates JNK, presumably by phosphorylating and activating MKK4/MKK7. In Saccharomyces cerevisiae, TAO3 is a component of the RAM (regulation of Ace2p activity and cellular morphogenesis) signaling pathway. TAO3 is upregulated in retinal ganglion cells after axotomy, and may play a role in apoptosis. TAO proteins possess mitogen-activated protein kinase (MAPK) kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270803 [Multi-domain]  Cd Length: 313  Bit Score: 78.54  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 398 FKDHPtlNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKI-----HQLNKSWRDekkenyhkhACREYRIHKELDHPRI 472
Cdd:cd06633   15 YKDDP--EEIFVDLHEIGHGSFGAVYFATNSHTNEVVAIKKmsysgKQTNEKWQD---------IIKEVKFLQQLKHPNT 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 473 VKlYDYFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLvdgTAC 552
Cdd:cd06633   84 IE-YKGCYLKDHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHS--HNMIHRDIKAGNILL---TEP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 553 GEIKITDFGLSKIMDDDSYGVdgmdltsqgaGTYWYLPPECfVVGKEPPKISNKVDVWSVGVIFFQcLYGRKPFGHNQSQ 632
Cdd:cd06633  158 GQVKLADFGSASIASPANSFV----------GTPYWMAPEV-ILAMDEGQYDGKVDIWSLGITCIE-LAERKPPLFNMNA 225
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 211971036 633 QDIL-----QENTILKATEvqfpvkpvVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd06633  226 MSALyhiaqNDSPTLQSNE--------WTDSFRGFVDYCLQKIPQER 264
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
404-673 1.24e-15

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: 78.79  E-value: 1.24e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 404 LNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSL-- 481
Cdd:cd07879   13 LPERYTSLKQVGSGAYGSVCSAIDKRTGEKVAIK-----KLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSav 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 482 ---DTDTFCTVLEYCEgNDLDFYLKQHklMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNilLVDGTACgEIKIT 558
Cdd:cd07879   88 sgdEFQDFYLVMPYMQ-TDLQKIMGHP--LSEDKVQYLVYQMLCGLKYIH--SAGIIHRDLKPGN--LAVNEDC-ELKIL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 559 DFGLSKIMDDDSYGVdgmdltsqgAGTYWYLPPECFVVGKEppkISNKVDVWSVGVIFFQCLYGRKPFghnqSQQDILQE 638
Cdd:cd07879  160 DFGLARHADAEMTGY---------VVTRWYRAPEVILNWMH---YNQTVDIWSVGCIMAEMLTGKTLF----KGKDYLDQ 223
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 211971036 639 NT-ILKATEVQFP--VKPVVSSEAKAFIRRCLAYRKED 673
Cdd:cd07879  224 LTqILKVTGVPGPefVQKLEDKAAKSYIKSLPKYPRKD 261
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
419-588 1.25e-15

Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK1 phosphorylates a variety of substrates including enzymes, transcription and splice factors, cytoskeletal proteins, viral oncogenes, receptors, and membrane-associated proteins. There are mutliple isoforms of CK1 and in mammals, seven isoforms (alpha, beta, gamma1-3, delta, and epsilon) have been characterized. These isoforms differ mainly in the length and structure of their C-terminal non-catalytic region. Some isoforms have several splice variants such as the long (L) and short (S) variants of CK1alpha. CK1 proteins are involved in the regulation of many cellular processes including membrane transport processes, circadian rhythm, cell division, apoptosis, and the development of cancer and neurodegenerative diseases. The CK1 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: 270918 [Multi-domain]  Cd Length: 266  Bit Score: 77.50  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqlnkswrdEKKENYHKHACREYRIHKEL-DHPRIVKLYDYFSLDTDTFCtVLEYCeGND 497
Cdd:cd14016   13 FGEVYLGIDLKTGEEVAIKI---------EKKDSKHPQLEYEAKVYKLLqGGPGIPRLYWFGQEGDYNVM-VMDLL-GPS 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 L-DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSYG---- 572
Cdd:cd14016   82 LeDLFNKCGRKFSLKTVLMLADQMISRLEYLHSKG--YIHRDIKPENFLMGLGKNSNKVYLIDFGLAKKYRDPRTGkhip 159
                        170
                 ....*....|....*..
gi 211971036 573 -VDGMDLTsqgaGTYWY 588
Cdd:cd14016  160 yREGKSLT----GTARY 172
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
468-678 1.25e-15

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: 79.31  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 468 DHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLv 547
Cdd:cd05618   79 NHPFLVGLHSCFQTESRLF-FVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHE--RGIIYRDLKLDNVLL- 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 548 dgTACGEIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFFQCLYGRKPF- 626
Cdd:cd05618  155 --DSEGHIKLTDYGMCK------EGLRPGDTTSTFCGTPNYIAPE--ILRGEDYGFS--VDWWALGVLMFEMMAGRSPFd 222
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 627 ------GHNQSQQDILQENTIlkatEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVH 678
Cdd:cd05618  223 ivgssdNPDQNTEDYLFQVIL----EKQIRIPRSLSVKAASVLKSFLNKDPKERLGCH 276
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
457-684 1.25e-15

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: 77.47  E-value: 1.25e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 457 ACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYLKQHK--LMSEKEARSIVMQIVNALRYLNeiKPPI 534
Cdd:cd08220   46 ALNEVKVLSMLHHPNIIEYYESF-LEDKALMIVMEYAPGGTLFEYIQQRKgsLLSEEEILHFFVQILLALHHVH--SKQI 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 535 IHYDLKPGNILLVDGTACgeIKITDFGLSKIMDDDSygvdgmdLTSQGAGTYWYLPPEcfVVGKEPPkiSNKVDVWSVGV 614
Cdd:cd08220  123 LHRDLKTQNILLNKKRTV--VKIGDFGISKILSSKS-------KAYTVVGTPCYISPE--LCEGKPY--NQKSDIWALGC 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 615 IFFQCLYGRKPFGHNQSQQDILQentILKATEVqfPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDP 684
Cdd:cd08220  190 VLYELASLKRAFEAANLPALVLK---IMRGTFA--PISDRYSEELRHLILSMLHLDPNKRPTLSEIMAQP 254
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
419-684 1.55e-15

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: 77.47  E-value: 1.55e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVK-IHQLNKSWRDEKK--ENYHKhacrEYRIHKELDHPRIVKLYDYfSLDTDTFCTVLEYCEG 495
Cdd:cd06630   13 FSSCYQARDVKTGTLMAVKqVSFCRNSSSEQEEvvEAIRE----EIRMMARLNHPNIVRMLGA-TQHKSHFNIFVEWMAG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 NDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNiLLVDGTAcGEIKITDFGLSKIMDDDSYGVDg 575
Cdd:cd06630   88 GSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQ--IIHRDLKGAN-LLVDSTG-QRLRIADFGAAARLASKGTGAG- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 mDLTSQGAGTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQfPVKPVV 655
Cdd:cd06630  163 -EFQGQLLGTIAFMAPE--VLRGEQYGRS--CDVWSVGCVIIEMATAKPPWNAEKISNHLALIFKIASATTPP-PIPEHL 236
                        250       260
                 ....*....|....*....|....*....
gi 211971036 656 SSEAKAFIRRCLAYRKEDRFDVHQLANDP 684
Cdd:cd06630  237 SPGLRDVTLRCLELQPEDRPPARELLKHP 265
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
435-711 1.92e-15

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: 78.92  E-value: 1.92e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIhqLNKS---WRDEKKenyhkHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEK 511
Cdd:cd05600   40 ALKI--MKKKvlfKLNEVN-----HVLTERDILTTTNSPWLVKLLYAFQ-DPENVYLAMEYVPGGDFRTLLNNSGILSEE 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 512 EARSIVMQIVNALRYLNEIKppIIHYDLKPGNiLLVDGTacGEIKITDFGLSK--------------------------I 565
Cdd:cd05600  112 HARFYIAEMFAAISSLHQLG--YIHRDLKPEN-FLIDSS--GHIKLTDFGLASgtlspkkiesmkirleevkntaflelT 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 566 MDDDSYGVDGMDLTSQG-----AGTYWYLPPEcFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQ---DILQ 637
Cdd:cd05600  187 AKERRNIYRAMRKEDQNyansvVGSPDYMAPE-VLRGE---GYDLTVDYWSLGCILFECLVGFPPFSGSTPNEtwaNLYH 262
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036 638 ENTILKATEVQFPVK-PVVSSEAKAFIRRCLAYRkEDRF-DVHQLANDPYLlphmrrsnssGNLHMAGLTASPTPP 711
Cdd:cd05600  263 WKKTLQRPVYTDPDLeFNLSDEAWDLITKLITDP-QDRLqSPEQIKNHPFF----------KNIDWDRLREGSKPP 327
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
419-671 2.01e-15

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: 76.99  E-value: 2.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKEnYHKHACrEYRIHKELDHPRIVKLYDYFSLDTDTFCTV-LEYCEGND 497
Cdd:cd06653   15 FGEVYLCYDADTGRELAVKQVPFDPDSQETSKE-VNALEC-EIQLLKNLRHDRIVQYYGCLRDPEEKKLSIfVEYMPGGS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGVDGMD 577
Cdd:cd06653   93 VKDQLKAYGALTENVTRRYTRQILQGVSYLH--SNMIVHRDIKGANILR---DSAGNVKLGDFGASKRIQTICMSGTGIK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSqgaGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTilKATEVQFPvkPVVSS 657
Cdd:cd06653  168 SVT---GTPYWMSPE--VISGE--GYGRKADVWSVACTVVEMLTEKPPWAEYEAMAAIFKIAT--QPTKPQLP--DGVSD 236
                        250
                 ....*....|....
gi 211971036 658 EAKAFIRRCLAYRK 671
Cdd:cd06653  237 ACRDFLRQIFVEEK 250
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
419-636 3.02e-15

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: 77.00  E-value: 3.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQ-RYAAVKIHQLNKSwrdekKENYHKHACREYRIHKELD---HPRIVKLYDYFSL---DTDTFCT-VL 490
Cdd:cd07862   14 YGKVFKARDLKNGgRFVALKRVRVQTG-----EEGMPLSTIREVAVLRHLEtfeHPNVVRLFDVCTVsrtDRETKLTlVF 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 491 EYCEgNDLDFYLKQ--HKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKImdd 568
Cdd:cd07862   89 EHVD-QDLTTYLDKvpEPGVPTETIKDMMFQLLRGLDFLHSHR--VVHRDLKPQNILV---TSSGQIKLADFGLARI--- 159
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 569 dsYGVDgMDLTSQgAGTYWYLPPECFVvgkePPKISNKVDVWSVGVIFFQcLYGRKPFGHNQSQQDIL 636
Cdd:cd07862  160 --YSFQ-MALTSV-VVTLWYRAPEVLL----QSSYATPVDLWSVGCIFAE-MFRRKPLFRGSSDVDQL 218
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
460-681 3.03e-15

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


Pssm-ID: 133243 [Multi-domain]  Cd Length: 256  Bit Score: 76.14  E-value: 3.03e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDLDFYLKQHK-LMSEKEARSIVMQIVNALRYLNEikPPIIHYD 538
Cdd:cd05112   49 EAEVMMKLSHPKLVQLYG-VCLEQAPICLVFEFMEHGCLSDYLRTQRgLFSAETLLGMCLDVCEGMAYLEE--ASVIHRD 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLVDGTAcgeIKITDFGLSKIMDDDSYgvdgmdltSQGAGTYW---YLPPECFVVGkeppKISNKVDVWSVGVI 615
Cdd:cd05112  126 LAARNCLVGENQV---VKVSDFGMTRFVLDDQY--------TSSTGTKFpvkWSSPEVFSFS----RYSSKSDVWSFGVL 190
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211971036 616 FFQCLY-GRKPFgHNQSQQDILQE-NTILKAtevqfpVKPVVSSEA-KAFIRRCLAYRKEDR--FD--VHQLA 681
Cdd:cd05112  191 MWEVFSeGKIPY-ENRSNSEVVEDiNAGFRL------YKPRLASTHvYEIMNHCWKERPEDRpsFSllLRQLA 256
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
419-672 3.63e-15

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Triple functional domain protein; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Triple functional domain protein (Trio), also called PTPRF-interacting protein, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. Trio plays important roles in neuronal cell migration and axon guidance. It was originally identified as an interacting partner of the of the receptor-like tyrosine phosphatase (RPTP) LAR (leukocyte-antigen-related protein), a family of receptors that function in the signaling to the actin cytoskeleton during development. Trio functions as a GEF for Rac1, RhoG, and RhoA, and is involved in the regulation of lamellipodia formation, mediating Rac1-dependent cell spreading and migration. The Trio subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271015 [Multi-domain]  Cd Length: 263  Bit Score: 76.17  E-value: 3.63e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKSW--RDEkkenyhkhACREYRIHKELDHPRIVKLYDYFSLDTdTFCTVLEYCEGN 496
Cdd:cd14113   20 FSVVKKCDQRGTKRAVATKF--VNKKLmkRDQ--------VTHELGVLQSLQHPQLVGLLDTFETPT-SYILVLEMADQG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 497 DLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGlskimddDSYGVDGM 576
Cdd:cd14113   89 RLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCR--IAHLDLKPENILVDQSLSKPTIKLADFG-------DAVQLNTT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 577 DLTSQGAGTYWYLPPEcFVVGkEPPKISNkvDVWSVGVIFFQCLYGRKPFghnqsqQDILQENTILKATEVQFPVK---- 652
Cdd:cd14113  160 YYIHQLLGSPEFAAPE-IILG-NPVSLTS--DLWSIGVLTYVLLSGVSPF------LDESVEETCLNICRLDFSFPddyf 229
                        250       260
                 ....*....|....*....|
gi 211971036 653 PVVSSEAKAFIrrCLAYRKE 672
Cdd:cd14113  230 KGVSQKAKDFV--CFLLQMD 247
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
435-686 3.70e-15

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: 76.60  E-value: 3.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIhqLNKSWRDEKKEnyhKHACREYRihkelDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL-DFYLKQhKLMSEKEA 513
Cdd:cd14175   30 AVKV--IDKSKRDPSEE---IEILLRYG-----QHPNIITLKDVYD-DGKHVYLVTELMRGGELlDKILRQ-KFFSEREA 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 514 RSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTACGE-IKITDFGLSKIMDDDsygvDGMDLTSqgagtywylppe 592
Cdd:cd14175   98 SSVLHTICKTVEYLHS--QGVVHRDLKPSNILYVDESGNPEsLRICDFGFAKQLRAE----NGLLMTP------------ 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 593 CFVVGKEPPKISNK------VDVWSVGVIFFQCLYGRKPFGHNQSQQdilQENTILKATEVQFPVK----PVVSSEAKAF 662
Cdd:cd14175  160 CYTANFVAPEVLKRqgydegCDIWSLGILLYTMLAGYTPFANGPSDT---PEEILTRIGSGKFTLSggnwNTVSDAAKDL 236
                        250       260
                 ....*....|....*....|....
gi 211971036 663 IRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14175  237 VSKMLHVDPHQRLTAKQVLQHPWI 260
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
449-667 3.70e-15

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: 77.27  E-value: 3.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 449 KKENYHKHACREYRIhkeLDH----PRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNAL 524
Cdd:cd05614   43 QKAKTVEHTRTERNV---LEHvrqsPFLVTLHYAFQTDAKLH-LILDYVSGGELFTHLYQRDHFSEDEVRFYSGEIILAL 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 525 RYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdddSYGVDGMDLTSQGAGTYWYLPPEcFVVGKEPPkiS 604
Cdd:cd05614  119 EHLHKLG--IVYRDIKLENILL---DSEGHVVLTDFGLSK-----EFLTEEKERTYSFCGTIEYMAPE-IIRGKSGH--G 185
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036 605 NKVDVWSVGVIFFQCLYGRKPF---GHNQSQQDILQEntILKATEvqfPVKPVVSSEAKAFIRRCL 667
Cdd:cd05614  186 KAVDWWSLGILMFELLTGASPFtleGEKNTQSEVSRR--ILKCDP---PFPSFIGPVARDLLQKLL 246
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
420-680 3.89e-15

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: 76.24  E-value: 3.89e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 420 SEVYKAFDLYEQRYAAVKIHQLnkswrdEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCEGNDLD 499
Cdd:cd06610   15 AVVYAAYCLPKKEKVAIKRIDL------EKCQTSMDELRKEIQAMSQCNHPNVVSYYTSFVVG-DELWLVMPLLSGGSLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 500 FYLKQ---HKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMdddsygVDGM 576
Cdd:cd06610   88 DIMKSsypRGGLDEAIIATVLKEVLKGLEYLH--SNGQIHRDVKAGNILLGED---GSVKIADFGVSASL------ATGG 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 577 DLTSQG----AGTYWYLPPEcfvVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHN----------QSQQDILQENTIL 642
Cdd:cd06610  157 DRTRKVrktfVGTPCWMAPE---VMEQVRGYDFKADIWSFGITAIELATGAAPYSKYppmkvlmltlQNDPPSLETGADY 233
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 211971036 643 KAtevqfpvkpvVSSEAKAFIRRCLAYRKEDRFDVHQL 680
Cdd:cd06610  234 KK----------YSKSFRKMISLCLQKDPSKRPTAEEL 261
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
455-686 4.29e-15

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: 77.02  E-value: 4.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 455 KHACREYRIHKELDHPRIVKLYDYF------SLDTDTFcTVLEYCEgNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLN 528
Cdd:cd07855   49 KRTLRELKILRHFKHDNIIAIRDILrpkvpyADFKDVY-VVLDLME-SDLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIH 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 529 EIKppIIHYDLKPGNiLLVDGTacGEIKITDFGLSKIMDDDSygVDGMDLTSQGAGTYWYLPPECFVVgkePPKISNKVD 608
Cdd:cd07855  127 SAN--VIHRDLKPSN-LLVNEN--CELKIGDFGMARGLCTSP--EEHKYFMTEYVATRWYRAPELMLS---LPEYTQAID 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 609 VWSVGVIFFQCLyGRKPF--GHNQSQQ-------------DILQE--NTILKATEVQFPVKPVV---------SSEAKAF 662
Cdd:cd07855  197 MWSVGCIFAEML-GRRQLfpGKNYVHQlqliltvlgtpsqAVINAigADRVRRYIQNLPNKQPVpwetlypkaDQQALDL 275
                        250       260
                 ....*....|....*....|....
gi 211971036 663 IRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd07855  276 LSQMLRFDPSERITVAEALQHPFL 299
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
419-638 5.62e-15

Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They can be classified into two classes (EphA and EphB), according to their extracellular sequences, which largely correspond to binding preferences for either GPI-anchored ephrin-A ligands or transmembrane ephrin-B ligands. Vertebrates have ten EphA and six EphB receptors, which display promiscuous ligand interactions within each class. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. This allows ephrin/EphR dimers to form, leading to the activation of the intracellular tyr kinase domain. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The main effect of ephrin/EphR interaction is cell-cell repulsion or adhesion. Ephrin/EphR signaling is important in neural development and plasticity, cell morphogenesis and proliferation, cell-fate determination, embryonic development, tissue patterning, and angiogenesis.The EphR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270629 [Multi-domain]  Cd Length: 266  Bit Score: 75.49  E-value: 5.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKA-FDLYEQRYAAVKIHQLNKSWRDEKKENYhkhaCREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGND 497
Cdd:cd05033   17 FGEVCSGsLKLPGKKEIDVAIKTLKSGYSDKQRLDF----LTEASIMGQFDHPNVIRLEGVVT-KSRPVMIVTEYMENGS 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHklmsekEARSIVMQIVNALR-------YLNEIKppIIHYDLKPGNILLVDGTACgeiKITDFGLSKIMDDds 570
Cdd:cd05033   92 LDKFLREN------DGKFTVTQLVGMLRgiasgmkYLSEMN--YVHRDLAARNILVNSDLVC---KVSDFGLSRRLED-- 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 571 ygVDGMDLTSQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQ-CLYGRKPFGhNQSQQDILQE 638
Cdd:cd05033  159 --SEATYTTKGGKIPIRWTAPEAIAYR----KFTSASDVWSFGIVMWEvMSYGERPYW-DMSNQDVIKA 220
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
419-630 5.70e-15

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: 75.50  E-value: 5.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfdLYEQRYAAVKIHQLNKSWRDEKKE-NYHKHACReyrihkeLDHPRIVKLYDYFS-LDTDTFCTVL-EYCEG 495
Cdd:cd13979   16 FGSVYKA--TYKGETVAVKIVRRRRKNRASRQSfWAELNAAR-------LRHENIVRVLAAETgTDFASLGLIImEYCGN 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 NDLdfylkQHKL------MSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACgeiKITDFGLSKIMDDD 569
Cdd:cd13979   87 GTL-----QQLIyegsepLPLAHRILISLDIARALRFCH--SHGIVHLDVKPANILISEQGVC---KLCDFGCSVKLGEG 156
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 570 SYGVDGMdltSQGAGTYWYLPPEcfVVGKEPPkiSNKVDVWSVGVIFFQCLYGRKPF-GHNQ 630
Cdd:cd13979  157 NEVGTPR---SHIGGTYTYRAPE--LLKGERV--TPKADIYSFGITLWQMLTRELPYaGLRQ 211
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
455-689 5.86e-15

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: 76.46  E-value: 5.86e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 455 KHACREYRIHKELDHPRIVKLYDYF--SLDTDTFCTVLEyceGNDLDFYLKQHKLmsEKE-ARSIVMQIVNALRYLNEIK 531
Cdd:cd07856   54 KRTYRELKLLKHLRHENIISLSDIFisPLEDIYFVTELL---GTDLHRLLTSRPL--EKQfIQYFLYQILRGLKYVHSAG 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 532 ppIIHYDLKPGNILLVDGtaCgEIKITDFGLSKIMDDDSYGVdgmdltsqgAGTYWYLPPECFVVGKeppKISNKVDVWS 611
Cdd:cd07856  129 --VIHRDLKPSNILVNEN--C-DLKICDFGLARIQDPQMTGY---------VSTRYYRAPEIMLTWQ---KYDVEVDIWS 191
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 612 VGVIFFQCLYGRKPF-GHNQSQQ-----------------DILQENTIL------KATEVQFPVK-PVVSSEAKAFIRRC 666
Cdd:cd07856  192 AGCIFAEMLEGKPLFpGKDHVNQfsiitellgtppddvinTICSENTLRfvqslpKRERVPFSEKfKNADPDAIDLLEKM 271
                        250       260
                 ....*....|....*....|...
gi 211971036 667 LAYRKEDRFDVHQLANDPYLLPH 689
Cdd:cd07856  272 LVFDPKKRISAAEALAHPYLAPY 294
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
469-674 7.45e-15

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: 76.19  E-value: 7.45e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFSLDtDTFCTVLEYCEGNDLDFYLKQhKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvd 548
Cdd:cd05589   61 HPFLVNLFACFQTP-EHVCFVMEYAAGGDLMMHIHE-DVFSEPRAVFYAACVVLGLQFLHEHK--IVYRDLKLDNLLL-- 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 549 gTACGEIKITDFGLSKimdddsygvDGM---DLTSQGAGTYWYLPPEcfvVGKEPpKISNKVDVWSVGVIFFQCLYGRKP 625
Cdd:cd05589  135 -DTEGYVKIADFGLCK---------EGMgfgDRTSTFCGTPEFLAPE---VLTDT-SYTRAVDWWGLGVLIYEMLVGESP 200
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 211971036 626 F-GHNQSQ--QDILQEntilkatEVQFPvkPVVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd05589  201 FpGDDEEEvfDSIVND-------EVRYP--RFLSTEAISIMRRLLRKNPERR 243
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
419-674 7.71e-15

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: 75.46  E-value: 7.71e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfdlyeQRYAAVKIHQLNKSWRDEKKENYHKhacREYRIHKELDHPRIVKLYDYfSLDTDTFCTVLEYCEGNDL 498
Cdd:cd14063   13 FGRVHRG-----RWHGDVAIKLLNIDYLNEEQLEAFK---EEVAAYKNTRHDNLVLFMGA-CMDPPHLAIVTSLCKGRTL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKL-MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvDGtacGEIKITDFGLskimdddsYGVDGMD 577
Cdd:cd14063   84 YSLIHERKEkFDFNKTVQIAQQICQGMGYLHAKG--IIHKDLKSKNIFL-EN---GRVVITDFGL--------FSLSGLL 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSQGAGT-----YW--YLPPEcfVVGK-EPPK-------ISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTIL 642
Cdd:cd14063  150 QPGRREDTlvipnGWlcYLAPE--IIRAlSPDLdfeeslpFTKASDVYAFGTVWYELLAGRWPFKEQPAESIIWQVGCGK 227
                        250       260       270
                 ....*....|....*....|....*....|....
gi 211971036 643 KA--TEVQFPVkpvvssEAKAFIRRCLAYRKEDR 674
Cdd:cd14063  228 KQslSQLDIGR------EVKDILMQCWAYDPEKR 255
PK_IRAK3 cd14160
Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain ...
419-624 7.93e-15

Pseudokinase domain of Interleukin-1 Receptor Associated Kinase 3; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain (a pseudokinase in the case of IRAK3), and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK3 (or IRAK-M) is the only IRAK that does not show kinase activity. It is found only in monocytes and macrophages in humans, and functions as a negative regulator of TLR signaling including TLR-2 induced p38 activation. It also negatively regulates the alternative NFkB pathway in a TLR-2 specific manner. IRAK3 is downregulated in the monocytes of obese people, and is associated with high SOD2, a marker of mitochondrial oxidative stress. It is an important inhibitor of inflammation in association with obesity and metabolic syndrome. The IRAK3 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: 271062 [Multi-domain]  Cd Length: 276  Bit Score: 75.31  E-value: 7.93e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfDLYEQRYAAvkihqlnKSWRDEKKENYHKHACR---EYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEG 495
Cdd:cd14160    6 IFEVYRV-RIGNRSYAV-------KLFKQEKKMQWKKHWKRflsELEVLLLFQHPNILELAAYFT-ETEKFCLVYPYMQN 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 NDLDFYLKQH---KLMSEKEARSIVMQIVNALRYLNEIKP-PIIHYDLKPGNILLVDGTacgEIKITDFGLSKIMDDDSY 571
Cdd:cd14160   77 GTLFDRLQCHgvtKPLSWHERINILIGIAKAIHYLHNSQPcTVICGNISSANILLDDQM---QPKLTDFALAHFRPHLED 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 211971036 572 GVDGMDLTSQGAGTYWYLPPECFVVGKeppkISNKVDVWSVGVIFFQCLYGRK 624
Cdd:cd14160  154 QSCTINMTTALHKHLWYMPEEYIRQGK----LSVKTDVYSFGIVIMEVLTGCK 202
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
419-680 8.20e-15

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: 75.43  E-value: 8.20e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKI----HQLnkswrDEKKEnyhkhacREYRIHKEL-DHPRIVKLYD-YFSLDT---DTFCTV 489
Cdd:cd06638   31 YGKVFKVLNKKNGSKAAVKIldpiHDI-----DEEIE-------AEYNILKALsDHPNVVKFYGmYYKKDVkngDQLWLV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 490 LEYCEGNDL-DF---YLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKI 565
Cdd:cd06638   99 LELCNGGSVtDLvkgFLKRGERMEEPIIAYILHEALMGLQHLHVNK--TIHRDVKGNNILLTTE---GGVKLVDFGVSAQ 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 566 MDDDSYgvdgmdLTSQGAGTYWYLPPECFVVGKE-PPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQentILKA 644
Cdd:cd06638  174 LTSTRL------RRNTSVGTPFWMAPEVIACEQQlDSTYDARCDVWSLGITAIELGDGDPPLADLHPMRALFK---IPRN 244
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 211971036 645 TEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQL 680
Cdd:cd06638  245 PPPTLHQPELWSNEFNDFIRKCLTKDYEKRPTVSDL 280
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
443-676 8.66e-15

Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Zap-70 is a cytoplasmic (or nonreceptor) PTK containing two Src homology 2 (SH2) domains N-terminal to the catalytic tyr kinase domain. Zap-70 is primarily expressed in T-cells and NK cells, and is a crucial component in T-cell receptor (TCR) signaling. Zap-70 binds the phosphorylated ITAM (immunoreceptor tyr activation motif) sequences of the activated TCR zeta-chain through its SH2 domains, leading to its phosphorylation and activation. It then phosphorylates target proteins, which propagate the signals to downstream pathways. Zap-70 is hardly detected in normal peripheral B-cells, but is present in some B-cell malignancies. It is used as a diagnostic marker for chronic lymphocytic leukemia (CLL) as it is associated with the more aggressive subtype of the disease. The Zap-70 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270686 [Multi-domain]  Cd Length: 269  Bit Score: 74.98  E-value: 8.66e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYfsLDTDTFCTVLEYCEGNDLDFYLKQHKlmSEKEARSIVM---Q 519
Cdd:cd05115   37 KVLKQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGV--CEAEALMLVMEMASGGPLNKFLSGKK--DEITVSNVVElmhQ 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 520 IVNALRYLNEIKppIIHYDLKPGNILLVDGTACgeiKITDFGLSKIMD-DDSYgvdgmdLTSQGAGTY---WYlPPECFV 595
Cdd:cd05115  113 VSMGMKYLEEKN--FVHRDLAARNVLLVNQHYA---KISDFGLSKALGaDDSY------YKARSAGKWplkWY-APECIN 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 596 VgkepPKISNKVDVWSVGVIFFQCL-YGRKPFGHNQSQQDIlqeNTILKATEVQFPvkPVVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd05115  181 F----RKFSSRSDVWSYGVTMWEAFsYGQKPYKKMKGPEVM---SFIEQGKRMDCP--AECPPEMYALMSDCWIYKWEDR 251

                 ..
gi 211971036 675 FD 676
Cdd:cd05115  252 PN 253
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
419-592 8.83e-15

Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as ACVR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. ACVR2 acts primarily as the receptors for activins, nodal, myostatin, GDF11, and a subset of BMPs. ACVR2 signaling impacts many cellular and physiological processes including reproductive and gonadal functions, myogenesis, bone remodeling and tooth development, kidney organogenesis, apoptosis, fibrosis, inflammation, and neurogenesis. Vertebrates contain two ACVR2 proteins, ACVR2a (or ActRIIA) and ACVR2b (or ActRIIB). The ACVR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270955 [Multi-domain]  Cd Length: 290  Bit Score: 75.44  E-value: 8.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfdLYEQRYAAVKI--HQLNKSWrdekkENyhkhacrEYRIHKE--LDHPRIVKLYD----YFSLDTDtFCTVL 490
Cdd:cd14053    8 FGAVWKA--QYLNRLVAVKIfpLQEKQSW-----LT-------EREIYSLpgMKHENILQFIGaekhGESLEAE-YWLIT 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 491 EYCEGNDLDFYLKQHkLMSEKEARSIVMQIVNALRYLNE--------IKPPIIHYDLKPGNILLV-DGTACgeikITDFG 561
Cdd:cd14053   73 EFHERGSLCDYLKGN-VISWNELCKIAESMARGLAYLHEdipatnggHKPSIAHRDFKSKNVLLKsDLTAC----IADFG 147
                        170       180       190
                 ....*....|....*....|....*....|.
gi 211971036 562 LSKIMDddsYGVDGMDLTSQgAGTYWYLPPE 592
Cdd:cd14053  148 LALKFE---PGKSCGDTHGQ-VGTRRYMAPE 174
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
499-692 1.03e-14

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: 75.15  E-value: 1.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFY---LKQHKLMSEKEARSIVMQIVNALRYLNEiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSkimdddSYGVDG 575
Cdd:cd06617   88 KFYkkvYDKGLTIPEDILGKIAVSIVKALEYLHS-KLSVIHRDVKPSNVLI---NRNGQVKLCDFGIS------GYLVDS 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 MDLTSQgAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFG--HNQSQQdILQentILKATEVQFPVKP 653
Cdd:cd06617  158 VAKTID-AGCKPYMAPERINPELNQKGYDVKSDVWSLGITMIELATGRFPYDswKTPFQQ-LKQ---VVEEPSPQLPAEK 232
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 211971036 654 vVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLPHMRR 692
Cdd:cd06617  233 -FSPEFQDFVNKCLKKNYKERPNYPELLQHPFFELHLSK 270
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
459-626 1.04e-14

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: 75.80  E-value: 1.04e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYfsLDTDTFCT------VLEYCEgNDLDFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKp 532
Cdd:cd07849   52 REIKILLRFKHENIIGILDI--QRPPTFESfkdvyiVQELME-TDLYKLIKTQHL-SNDHIQYFLYQILRGLKYIHSAN- 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 533 pIIHYDLKPGNILLvdGTACgEIKITDFGLSKIMDDDSyGVDGMdLTSQGAgTYWYLPPECFVVGKEppkISNKVDVWSV 612
Cdd:cd07849  127 -VLHRDLKPSNLLL--NTNC-DLKICDFGLARIADPEH-DHTGF-LTEYVA-TRWYRAPEIMLNSKG---YTKAIDIWSV 196
                        170
                 ....*....|....
gi 211971036 613 GVIFFQCLYGRKPF 626
Cdd:cd07849  197 GCILAEMLSNRPLF 210
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
470-672 1.15e-14

Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ROCK is also referred to as Rho-associated kinase or simply as Rho kinase. It contains an N-terminal extension, a catalytic kinase domain, and a long C-terminal extension, which contains a coiled-coil region encompassing a Rho-binding domain (RBD) and a pleckstrin homology (PH) domain. ROCK is auto-inhibited by the RBD and PH domain interacting with the catalytic domain. It is activated via interaction with Rho GTPases and is involved in many cellular functions including contraction, adhesion, migration, motility, proliferation, and apoptosis. The ROCK subfamily consists of two isoforms, ROCK1 and ROCK2, which may be functionally redundant in some systems, but exhibit different tissue distributions. Both isoforms are ubiquitously expressed in most tissues, but ROCK2 is more prominent in brain and skeletal muscle while ROCK1 is more pronounced in the liver, testes, and kidney. Studies in knockout mice result in different phenotypes, suggesting that the two isoforms do not compensate for each other during embryonic development. The ROCK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270747 [Multi-domain]  Cd Length: 352  Bit Score: 75.88  E-value: 1.15e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 470 PRIVKLYDYFSlDTDTFCTVLEYCEGNDLdfylkqHKLMS-----EKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNI 544
Cdd:cd05596   86 EWIVQLHYAFQ-DDKYLYMVMDYMPGGDL------VNLMSnydvpEKWARFYTAEVVLALDAIHSMG--FVHRDVKPDNM 156
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 545 LLvdgTACGEIKITDFGLSKIMDDDsygvdGMDLTSQGAGTYWYLPPECF-------VVGKEppkisnkVDVWSVGVIFF 617
Cdd:cd05596  157 LL---DASGHLKLADFGTCMKMDKD-----GLVRSDTAVGTPDYISPEVLksqggdgVYGRE-------CDWWSVGVFLY 221
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 618 QCLYGRKPFGHNQ---SQQDILQENTILkatevQFPVKPVVSSEAKAFIRRCLAYRKE 672
Cdd:cd05596  222 EMLVGDTPFYADSlvgTYGKIMNHKNSL-----QFPDDVEISKDAKSLICAFLTDREV 274
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
435-636 1.85e-14

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: 74.67  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIhqLNKSWRD--EKKENYHKHAcreyrihkelDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL-DFYLKQhKLMSEK 511
Cdd:cd14177   33 AVKI--IDKSKRDpsEEIEILMRYG----------QHPNIITLKDVYD-DGRYVYLVTELMKGGELlDRILRQ-KFFSER 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 512 EARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACGE-IKITDFGLSKIMDDDsygvDGMDLTSqgAGTYWYLP 590
Cdd:cd14177   99 EASAVLYTITKTVDYLH--CQGVVHRDLKPSNILYMDDSANADsIRICDFGFAKQLRGE----NGLLLTP--CYTANFVA 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 211971036 591 PECFVvgkePPKISNKVDVWSVGVIFFQCLYGRKPF--GHNQSQQDIL 636
Cdd:cd14177  171 PEVLM----RQGYDAACDIWSLGVLLYTMLAGYTPFanGPNDTPEEIL 214
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
422-686 2.19e-14

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: 74.38  E-value: 2.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKIHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFY 501
Cdd:cd06655   35 VFTAIDVATGQEVAIKQINLQKQPKKELIIN-------EILVMKELKNPNIVNFLDSFLVGDELF-VVMEYLAGGSLTDV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 502 LKQhKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGL-SKIMDDDSYgvdgmdlTS 580
Cdd:cd06655  107 VTE-TCMDEAQIAAVCRECLQALEFLHANQ--VIHRDIKSDNVLL---GMDGSVKLTDFGFcAQITPEQSK-------RS 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 581 QGAGTYWYLPPECFVVGKEPPKisnkVDVWSVGVIFFQCLYGRKPFghnqsqqdiLQENTI----LKAT----EVQFPVK 652
Cdd:cd06655  174 TMVGTPYWMAPEVVTRKAYGPK----VDIWSLGIMAIEMVEGEPPY---------LNENPLralyLIATngtpELQNPEK 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 211971036 653 pvVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06655  241 --LSPIFRDFLNRCLEMDVEKRGSAKELLQHPFL 272
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
457-691 2.23e-14

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: 74.69  E-value: 2.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 457 ACREYRIH-KELDHPRIVKLYD-YFSLDTDTFC--TVLEYCEGNDLDFYLKQH--KLMSEKEARSIVMQIVNALRYLNEI 530
Cdd:cd14170   41 ARREVELHwRASQCPHIVRIVDvYENLYAGRKCllIVMECLDGGELFSRIQDRgdQAFTEREASEIMKSIGEAIQYLHSI 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 531 KppIIHYDLKPGNILLVDGTACGEIKITDFGLSKimdddsyGVDGMDLTSQGAGTYWYLPPEcfVVGkePPKISNKVDVW 610
Cdd:cd14170  121 N--IAHRDVKPENLLYTSKRPNAILKLTDFGFAK-------ETTSHNSLTTPCYTPYYVAPE--VLG--PEKYDKSCDMW 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 611 SVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEVQFPVK--PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLP 688
Cdd:cd14170  188 SLGVIMYILLCGYPPFYSNHGLAISPGMKTRIRMGQYEFPNPewSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMQ 267

                 ...
gi 211971036 689 HMR 691
Cdd:cd14170  268 STK 270
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
404-633 2.26e-14

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: 75.05  E-value: 2.26e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 404 LNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQlnkswrdeKKENYHKHACREYRIHKELD-HPR-----IVKLYD 477
Cdd:cd14226   11 WMDRYEIDSLIGKGSFGQVVKAYDHVEQEWVAIKIIK--------NKKAFLNQAQIEVRLLELMNkHDTenkyyIVRLKR 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 478 YFSLdTDTFCTVLEYCEGNDLDFYLKQH-KLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLVDG--TAcge 554
Cdd:cd14226   83 HFMF-RNHLCLVFELLSYNLYDLLRNTNfRGVSLNLTRKFAQQLCTALLFLSTPELSIIHCDLKPENILLCNPkrSA--- 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 555 IKITDFGLSKIMDDDSYgvdgmdltsQGAGTYWYLPPEcFVVGKEppkISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQ 633
Cdd:cd14226  159 IKIIDFGSSCQLGQRIY---------QYIQSRFYRSPE-VLLGLP---YDLAIDMWSLGCILVEMHTGEPLFsGANEVDQ 225
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
459-680 2.37e-14

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: 74.71  E-value: 2.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLDTD-TFCtvLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEiKPPIIHY 537
Cdd:cd06650   52 RELQVLHECNSPYIVGFYGAFYSDGEiSIC--MEHMDGGSLDQVLKKAGRIPEQILGKVSIAVIKGLTYLRE-KHKIMHR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLvdgTACGEIKITDFGLSKIMDDdsygvdgmDLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFF 617
Cdd:cd06650  129 DVKPSNILV---NSRGEIKLCDFGVSGQLID--------SMANSFVGTRSYMSPERL----QGTHYSVQSDIWSMGLSLV 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 618 QCLYGRKPFGHNQSQQDILQENTILKATEVQFPVKP--------------------------------------VVSSEA 659
Cdd:cd06650  194 EMAVGRYPIPPPDAKELELMFGCQVEGDAAETPPRPrtpgrplssygmdsrppmaifelldyivnepppklpsgVFSLEF 273
                        250       260
                 ....*....|....*....|.
gi 211971036 660 KAFIRRCLAYRKEDRFDVHQL 680
Cdd:cd06650  274 QDFVNKCLIKNPAERADLKQL 294
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
469-627 3.23e-14

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: 73.30  E-value: 3.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEK---EAR-SIVMQIVNALRYL-NEIKPPIIHYDLKPGN 543
Cdd:cd14664   49 HRNIVRLRGYCS-NPTTNLLVYEYMPNGSLGELLHSRPESQPPldwETRqRIALGSARGLAYLhHDCSPLIIHRDVKSNN 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 544 ILLvDGTAcgEIKITDFGLSKIMDDDsygvdGMDLTSQGAGTYWYLPPECFVVGKeppkISNKVDVWSVGVIFFQCLYGR 623
Cdd:cd14664  128 ILL-DEEF--EAHVADFGLAKLMDDK-----DSHVMSSVAGSYGYIAPEYAYTGK----VSEKSDVYSYGVVLLELITGK 195

                 ....
gi 211971036 624 KPFG 627
Cdd:cd14664  196 RPFD 199
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
419-637 4.78e-14

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: 73.57  E-value: 4.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnkswrdEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEgNDL 498
Cdd:cd07869   18 YATVYKGKSKVNGKLVALKVIRL------QEEEGTPFTAIREASLLKGLKHANIVLLHDIIH-TKETLTLVFEYVH-TDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKL-MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDgtaCGEIKITDFGLSKIMDDDSYGVdgmd 577
Cdd:cd07869   90 CQYMDKHPGgLHPENVKLFLFQLLRGLSYIHQRY--ILHRDLKPQNLLISD---TGELKLADFGLARAKSVPSHTY---- 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 ltSQGAGTYWYLPPECFVVGKEppkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQ 637
Cdd:cd07869  161 --SNEVVTLWYRPPDVLLGSTE---YSTCLDMWGVGCIFVEMIQGVAAFPGMKDIQDQLE 215
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
419-626 5.85e-14

Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER, ErbB) subfamily members include EGFR (HER1, ErbB1), HER2 (ErbB2), HER3 (ErbB3), HER4 (ErbB4), and similar proteins. They are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, resulting in the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Collectively, they can recognize a variety of ligands including EGF, TGFalpha, and neuregulins, among others. All four subfamily members can form homo- or heterodimers. HER3 contains an impaired kinase domain and depends on its heterodimerization partner for activation. EGFR subfamily members are involved in signaling pathways leading to a broad range of cellular responses including cell proliferation, differentiation, migration, growth inhibition, and apoptosis. Gain of function alterations, through their overexpression, deletions, or point mutations in their kinase domains, have been implicated in various cancers. These receptors are targets of many small molecule inhibitors and monoclonal antibodies used in cancer therapy. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270648 [Multi-domain]  Cd Length: 279  Bit Score: 72.83  E-value: 5.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRyaAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDyFSLdTDTFCTVLEYCEGNDL 498
Cdd:cd05057   20 FGTVYKGVWIPEGE--KVKIPVAIKVLREETGPKANEEILDEAYVMASVDHPHLVRLLG-ICL-SSQVQLITQLMPLGCL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKlmSEKEARSIV---MQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIM--DDDSYGV 573
Cdd:cd05057   96 LDYVRNHR--DNIGSQLLLnwcVQIAKGMSYLEEKR--LVHRDLAARNVLV---KTPNHVKITDFGLAKLLdvDEKEYHA 168
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 211971036 574 DGmdltsqGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQCL-YGRKPF 626
Cdd:cd05057  169 EG------GKVPIKWMALESIQYR----IYTHKSDVWSYGVTVWELMtFGAKPY 212
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
459-626 6.17e-14

Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src subfamily members include Src, Lck, Hck, Blk, Lyn, Fgr, Fyn, Yrk, and Yes. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Src kinases are overexpressed in a variety of human cancers, making them attractive targets for therapy. They are also implicated in acute inflammatory responses and osteoclast function. Src, Fyn, Yes, and Yrk are widely expressed, while Blk, Lck, Hck, Fgr, and Lyn show a limited expression pattern. The Src-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270630 [Multi-domain]  Cd Length: 248  Bit Score: 72.32  E-value: 6.17e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEY-CEGNDLDfYLKQHKLMSEKEARSIVM--QIVNALRYLNEIKppII 535
Cdd:cd05034   39 QEAQIMKKLRHDKLVQLYAVCS-DEEPIYIVTELmSKGSLLD-YLRTGEGRALRLPQLIDMaaQIASGMAYLESRN--YI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 536 HYDLKPGNILLVDGTACgeiKITDFGLSKIMDDDSYgvdgmdLTSQGAGtywyLP-----PECFVVGkeppKISNKVDVW 610
Cdd:cd05034  115 HRDLAARNILVGENNVC---KVADFGLARLIEDDEY------TAREGAK----FPikwtaPEAALYG----RFTIKSDVW 177
                        170
                 ....*....|....*..
gi 211971036 611 SVGVIFFQCL-YGRKPF 626
Cdd:cd05034  178 SFGILLYEIVtYGRVPY 194
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
419-637 7.76e-14

Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily contains c-ros, Sevenless, and similar proteins. The proto-oncogene c-ros encodes an orphan receptor PTK (RTK) with an unknown ligand. RTKs contain an extracellular ligand-binding domain, a transmembrane region, 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. C-ros is expressed in embryonic cells of the kidney, intestine and lung, but disappears soon after birth. It persists only in the adult epididymis. Male mice bearing inactive mutations of c-ros lack the initial segment of the epididymis and are infertile. The Drosophila protein, Sevenless, is required for the specification of the R7 photoreceptor cell during eye development. The c-ros subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270640 [Multi-domain]  Cd Length: 268  Bit Score: 72.45  E-value: 7.76e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYK--AFDL-----YEQRyAAVKihQLNKSWRDEKKENYHKHAcreyRIHKELDHPRIVKLYDyFSLDTDTFCTVLE 491
Cdd:cd05044    8 FGEVFEgtAKDIlgdgsGETK-VAVK--TLRKGATDQEKAEFLKEA----HLMSNFKHPNILKLLG-VCLDNDPQYIILE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 492 YCEGNDLDFYLKQHK-------LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEI-KITDFGLS 563
Cdd:cd05044   80 LMEGGDLLSYLRAARptaftppLLTLKDLLSICVDVAKGCVYLEDMH--FVHRDLAARNCLVSSKDYRERVvKIGDFGLA 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036 564 K-IMDDDSYGVDGmdltsQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQCL-YGRKPFGhNQSQQDILQ 637
Cdd:cd05044  158 RdIYKNDYYRKEG-----EGLLPVRWMAPESLVDG----VFTTQSDVWAFGVLMWEILtLGQQPYP-ARNNLEVLH 223
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
459-667 9.20e-14

Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Obscurin, approximately 800 kDa in size, is one of three giant proteins expressed in vetebrate striated muscle, together with titin and nebulin. It is a multidomain protein composed of tandem adhesion and signaling domains, including 49 immunoglobulin (Ig) and 2 fibronectin type III (FN3) domains at the N-terminus followed by a more complex region containing more Ig domains, a conserved SH3 domain near a RhoGEF and PH domains, non-modular regions, as well as IQ and phosphorylation motifs. The obscurin gene also encode two kinase domains, which are not expressed as part of the 800 kDa protein, but as a smaller, alternatively spliced product present mainly in the heart muscle, also called obscurin-MLCK. Obscurin is localized at the peripheries of Z-disks and M-lines, where it is able to communicate with the surrounding myoplasm. It interacts with diverse proteins including sAnk1, myosin, titin, and MyBP-C. It may act as a scaffold for the assembly of elements of the contractile apparatus. The obscurin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271012 [Multi-domain]  Cd Length: 257  Bit Score: 71.87  E-value: 9.20e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYD 538
Cdd:cd14110   48 REYQVLRRLSHPRIAQLHSAY-LSPRHLVLIEELCSGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRR--ILHLD 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLvdgTACGEIKITDFGLSK--------IMDDDSYGVDGMD---LTSQGAGtywylpPEcfvvgkeppkisnkV 607
Cdd:cd14110  125 LRSENMII---TEKNLLKIVDLGNAQpfnqgkvlMTDKKGDYVETMApelLEGQGAG------PQ--------------T 181
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 608 DVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntiLKATEVQFP-VKPVVSSEAKAFIRRCL 667
Cdd:cd14110  182 DIWAIGVTAFIMLSADYPV-SSDLNWERDRN---IRKGKVQLSrCYAGLSGGAVNFLKSTL 238
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
419-681 1.43e-13

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


Pssm-ID: 133187 [Multi-domain]  Cd Length: 270  Bit Score: 71.68  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKA-FDLYEQRYAAVKIHQLNKSWRDEKKENYhkhaCREYRIHKELDHPRIVKLYDYFSldTDTFCTVLEYCEGND 497
Cdd:cd05056   19 FGDVYQGvYMSPENEKIAVAVKTCKNCTSPSVREKF----LQEAYIMRQFDHPHIVKLIGVIT--ENPVWIVMELAPLGE 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKlmSEKEARSIVM---QIVNALRYLNEIKppIIHYDLKPGNILLVDGTaCgeIKITDFGLSKIMDDDSYGVd 574
Cdd:cd05056   93 LRSYLQVNK--YSLDLASLILyayQLSTALAYLESKR--FVHRDIAARNVLVSSPD-C--VKLGDFGLSRYMEDESYYK- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 575 gmdlTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCL-YGRKPFghnqsqQDILQENTILKATEVQFPVKP 653
Cdd:cd05056  165 ----ASKGKLPIKWMAPESI----NFRRFTSASDVWMFGVCMWEILmLGVKPF------QGVKNNDVIGRIENGERLPMP 230
                        250       260
                 ....*....|....*....|....*....
gi 211971036 654 VVSSEA-KAFIRRCLAYRKEDRFDVHQLA 681
Cdd:cd05056  231 PNCPPTlYSLMTKCWAYDPSKRPRFTELK 259
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
422-686 1.52e-13

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: 72.06  E-value: 1.52e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKIHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFY 501
Cdd:cd06656   35 VYTAIDIATGQEVAIKQMNLQQQPKKELIIN-------EILVMRENKNPNIVNYLDSY-LVGDELWVVMEYLAGGSLTDV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 502 LKQhKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILL-VDGTacgeIKITDFGL-SKIMDDDSYgvdgmdlT 579
Cdd:cd06656  107 VTE-TCMDEGQIAAVCRECLQALDFLHSNQ--VIHRDIKSDNILLgMDGS----VKLTDFGFcAQITPEQSK-------R 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 580 SQGAGTYWYLPPECFVVGKEPPKisnkVDVWSVGVIFFQCLYGRKPFghnqsqqdiLQENTI----LKAT----EVQFPV 651
Cdd:cd06656  173 STMVGTPYWMAPEVVTRKAYGPK----VDIWSLGIMAIEMVEGEPPY---------LNENPLralyLIATngtpELQNPE 239
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 211971036 652 KpvVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06656  240 R--LSAVFRDFLNRCLEMDVDRRGSAKELLQHPFL 272
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
470-685 1.64e-13

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: 72.34  E-value: 1.64e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 470 PRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHK-LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvd 548
Cdd:cd05601   61 PWITKLQYAFQ-DSENLYLVMEYHPGGDLLSLLSRYDdIFEESMARFYLAELVLAIHSLHSMG--YVHRDIKPENILI-- 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 549 gTACGEIKITDFGLSKIMDDDSYGVDGMDLtsqgaGTYWYLPPECFVVGKEPPKISNKV--DVWSVGVIFFQCLYGRKPF 626
Cdd:cd05601  136 -DRTGHIKLADFGSAAKLSSDKTVTSKMPV-----GTPDYIAPEVLTSMNGGSKGTYGVecDWWSLGIVAYEMLYGKTPF 209
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 627 GHNQSQQDIlqeNTILKATE-VQFPVKPVVSSEAKAFIRRCLAyRKEDRFDVHQLANDPY 685
Cdd:cd05601  210 TEDTVIKTY---SNIMNFKKfLKFPEDPKVSESAVDLIKGLLT-DAKERLGYEGLCCHPF 265
STKc_IRAK1 cd14159
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; ...
469-661 1.84e-13

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK1 plays a role in the activation of IRF3/7, STAT, and NFkB. It mediates IL-6 and IFN-gamma responses following IL-1 and IL-18 stimulation, respectively. It also plays an essential role in IFN-alpha induction downstream of TLR7 and TLR9. The IRAK1 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: 271061 [Multi-domain]  Cd Length: 296  Bit Score: 71.78  E-value: 1.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYfSLDTDTFCTVLEYCEGNDLDFYLKQHK---LMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNIL 545
Cdd:cd14159   51 HPNIVDLAGY-SAQQGNYCLIYVYLPNGSLEDRLHCQVscpCLSWSQRLHVLLGTARAIQYLHSDSPSLIHGDVKSSNIL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 546 LVDGTacgEIKITDFGLSKIMDDDSYGVDGMDL--TSQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQCLYGR 623
Cdd:cd14159  130 LDAAL---NPKLGDFGLARFSRRPKQPGMSSTLarTQTVRGTLAYLPEEYVKTG----TLSVEIDVYSFGVVLLELLTGR 202
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 211971036 624 KPF-----GHNQSQQDILQEntilKATEVQFPVKPVVSSEAKA 661
Cdd:cd14159  203 RAMevdscSPTKYLKDLVKE----EEEAQHTPTTMTHSAEAQA 241
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
459-627 2.08e-13

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: 71.06  E-value: 2.08e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYF----------SLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKE---ARSIVMQIVNALR 525
Cdd:cd14048   53 REVRALAKLDHPGIVRYFNAWlerppegwqeKMDEVYLYIQMQLCRKENLKDWMNRRCTMESRElfvCLNIFKQIASAVE 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 526 YLNEikPPIIHYDLKPGNILL-VDGTacgeIKITDFGLSKIMDDDSYGV------DGMDLTSQGAGTYWYLPPECFvvgk 598
Cdd:cd14048  133 YLHS--KGLIHRDLKPSNVFFsLDDV----VKVGDFGLVTAMDQGEPEQtvltpmPAYAKHTGQVGTRLYMSPEQI---- 202
                        170       180
                 ....*....|....*....|....*....
gi 211971036 599 EPPKISNKVDVWSVGVIFFQCLYgrkPFG 627
Cdd:cd14048  203 HGNQYSEKVDIFALGLILFELIY---SFS 228
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
468-650 2.22e-13

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: 71.86  E-value: 2.22e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 468 DHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLV 547
Cdd:cd05590   54 NHPFLTQLYCCFQ-TPDRLFFVMEFVNGGDLMFHIQKSRRFDEARARFYAAEITSALMFLHD--KGIIYRDLKLDNVLLD 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 548 DGTACgeiKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPPECFVVGKEPPKisnkVDVWSVGVIFFQCLYGRKPFg 627
Cdd:cd05590  131 HEGHC---KLADFGMCK------EGIFNGKTTSTFCGTPDYIAPEILQEMLYGPS----VDWWAMGVLLYEMLCGHAPF- 196
                        170       180
                 ....*....|....*....|...
gi 211971036 628 HNQSQQDILQenTILKaTEVQFP 650
Cdd:cd05590  197 EAENEDDLFE--AILN-DEVVYP 216
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
469-687 2.31e-13

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: 71.98  E-value: 2.31e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFSlDTDTFCTVLEYCEGNDL-DFYLKQhKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLV 547
Cdd:cd14176   72 HPNIITLKDVYD-DGKYVYVVTELMKGGELlDKILRQ-KFFSEREASAVLFTITKTVEYLH--AQGVVHRDLKPSNILYV 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 548 DGTACGE-IKITDFGLSKIMDDDsygvDGMDLTSqgAGTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd14176  148 DESGNPEsIRICDFGFAKQLRAE----NGLLMTP--CYTANFVAPE--VLERQGYDAA--CDIWSLGVLLYTMLTGYTPF 217
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 211971036 627 GHNqsqQDILQENTILKATEVQFPVK----PVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLL 687
Cdd:cd14176  218 ANG---PDDTPEEILARIGSGKFSLSggywNSVSDTAKDLVSKMLHVDPHQRLTAALVLRHPWIV 279
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
406-636 2.36e-13

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 71.39  E-value: 2.36e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 406 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLnkswrDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDT 485
Cdd:PLN00009   2 DQYEKVEKIGEGTYGVVYKARDRVTNETIALKKIRL-----EQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 486 FcTVLEYcegndLDFYLKQHKLMSEKEARSIVM------QIVNALRYLNEIKppIIHYDLKPGNILLVDGTacGEIKITD 559
Cdd:PLN00009  77 Y-LVFEY-----LDLDLKKHMDSSPDFAKNPRLiktylyQILRGIAYCHSHR--VLHRDLKPQNLLIDRRT--NALKLAD 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 560 FGLSKimdddSYGVDGMDLTSQgAGTYWYLPPECFVVGKEppkISNKVDVWSVGVIFFQcLYGRKPFGHNQSQQDIL 636
Cdd:PLN00009 147 FGLAR-----AFGIPVRTFTHE-VVTLWYRAPEILLGSRH---YSTPVDIWSVGCIFAE-MVNQKPLFPGDSEIDEL 213
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
459-626 2.53e-13

Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal regulatory tyrosine and N-terminal myristylation sites (Srm) and Breast tumor kinase (Brk); PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Srm and Brk (also called protein tyrosine kinase 6) are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Brk has been found to be overexpressed in a majority of breast tumors. Src kinases in general contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr; they are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Srm and Brk however, lack the N-terminal myristylation sites. Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. The Srm/Brk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133248 [Multi-domain]  Cd Length: 261  Bit Score: 70.54  E-value: 2.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVM--QIVNALRYLNEIKppIIH 536
Cdd:cd05148   51 KEVQALKRLRHKHLISLFAVCSVG-EPVYIITELMEKGSLLAFLRSPEGQVLPVASLIDMacQVAEGMAYLEEQN--SIH 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 537 YDLKPGNILLVDGTACgeiKITDFGLSKIMDDDSYgvdgmdLTSQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIF 616
Cdd:cd05148  128 RDLAARNILVGEDLVC---KVADFGLARLIKEDVY------LSSDKKIPYKWTAPEAASHG----TFSTKSDVWSFGILL 194
                        170
                 ....*....|.
gi 211971036 617 FQCL-YGRKPF 626
Cdd:cd05148  195 YEMFtYGQVPY 205
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
469-636 2.73e-13

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: 71.20  E-value: 2.73e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFSlDTDTFCTVLEYCEGNDL-DFYLKQhKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLV 547
Cdd:cd14178   56 HPNIITLKDVYD-DGKFVYLVMELMRGGELlDRILRQ-KCFSEREASAVLCTITKTVEYLHS--QGVVHRDLKPSNILYM 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 548 DGTACGE-IKITDFGLSKIMDDDsygvDGMDLTSqgagtywylppeCFVVGKEPPKISNK------VDVWSVGVIFFQCL 620
Cdd:cd14178  132 DESGNPEsIRICDFGFAKQLRAE----NGLLMTP------------CYTANFVAPEVLKRqgydaaCDIWSLGILLYTML 195
                        170
                 ....*....|....*...
gi 211971036 621 YGRKPF--GHNQSQQDIL 636
Cdd:cd14178  196 AGFTPFanGPDDTPEEIL 213
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
468-637 2.80e-13

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: 71.49  E-value: 2.80e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 468 DHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLV 547
Cdd:cd05619   64 EHPFLTHLFCTFQTKENLF-FVMEYLNGGDLMFHIQSCHKFDLPRATFYAAEIICGLQFLHS--KGIVYRDLKLDNILLD 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 548 DGtacGEIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPPEcFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPFg 627
Cdd:cd05619  141 KD---GHIKIADFGMCK------ENMLGDAKTSTFCGTPDYIAPE-ILLGQ---KYNTSVDWWSFGVLLYEMLIGQSPF- 206
                        170
                 ....*....|
gi 211971036 628 HNQSQQDILQ 637
Cdd:cd05619  207 HGQDEEELFQ 216
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
398-639 2.83e-13

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Human TAO2 is also known as prostate-derived Ste20-like kinase (PSK) and was identified in a screen for overexpressed RNAs in prostate cancer. TAO2 possesses mitogen-activated protein kinase (MAPK) kinase kinase activity and activates both p38 and c-Jun N-terminal kinase (JNK), by phosphorylating and activating their respective MAP/ERK kinases, MEK3/MEK6 and MKK4/MKK7. It contains a long C-terminal extension with autoinhibitory segments, and is activated by the release of this inhibition and the phosphorylation of its activation loop serine. TAO2 functions as a regulator of actin cytoskeletal and microtubule organization. In addition, it regulates the transforming growth factor-activated kinase 1 (TAK1), which is a MAPKKK that plays an essential role in the signaling pathways of tumor necrosis factor, interleukin 1, and Toll-like receptor. The TAO2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270804 [Multi-domain]  Cd Length: 308  Bit Score: 71.21  E-value: 2.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 398 FKDHPtlNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKI-----HQLNKSWRDekkenyhkhACREYRIHKELDHPRI 472
Cdd:cd06634    9 FKDDP--EKLFSDLREIGHGSFGAVYFARDVRNNEVVAIKKmsysgKQSNEKWQD---------IIKEVKFLQKLRHPNT 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 473 VKlYDYFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTAC 552
Cdd:cd06634   78 IE-YRGCYLREHTAWLVMEYCLGSASDLLEVHKKPLQEVEIAAITHGALQGLAYLHSHN--MIHRDVKAGNILL---TEP 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 553 GEIKITDFGLSKIMDDDSYGVdgmdltsqgaGTYWYLPPECfVVGKEPPKISNKVDVWSVGVIFFQcLYGRKP--FGHN- 629
Cdd:cd06634  152 GLVKLGDFGSASIMAPANSFV----------GTPYWMAPEV-ILAMDEGQYDGKVDVWSLGITCIE-LAERKPplFNMNa 219
                        250
                 ....*....|....*...
gi 211971036 630 --------QSQQDILQEN 639
Cdd:cd06634  220 msalyhiaQNESPALQSG 237
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
459-686 2.88e-13

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: 71.31  E-value: 2.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLDTDtFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEiKPPIIHYD 538
Cdd:cd06615   48 RELKVLHECNSPYIVGFYGAFYSDGE-ISICMEHMDGGSLDQVLKKAGRIPENILGKISIAVLRGLTYLRE-KHKIMHRD 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLvdgTACGEIKITDFGLSKIMdddsygVDGMdlTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQ 618
Cdd:cd06615  126 VKPSNILV---NSRGEIKLCDFGVSGQL------IDSM--ANSFVGTRSYMSPERL----QGTHYTVQSDIWSLGLSLVE 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 619 CLYGRKPFGHNQSQQDILQENTILKATEVQFPVKPVV--------------------------------SSEAKAFIRRC 666
Cdd:cd06615  191 MAIGRYPIPPPDAKELEAMFGRPVSEGEAKESHRPVSghppdsprpmaifelldyivnepppklpsgafSDEFQDFVDKC 270
                        250       260
                 ....*....|....*....|
gi 211971036 667 LAYRKEDRFDVHQLANDPYL 686
Cdd:cd06615  271 LKKNPKERADLKELTKHPFI 290
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
455-625 3.03e-13

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: 71.63  E-value: 3.03e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 455 KHACREYRIHKELDHPRIVKLYDYFSL-DTDTFCTVLEYCEGNDLDFY--LKQHKLMSEKEARSIVMQIVNALRYLNEIK 531
Cdd:cd07858   49 KRTLREIKLLRHLDHENVIAIKDIMPPpHREAFNDVYIVYELMDTDLHqiIRSSQTLSDDHCQYFLYQLLRGLKYIHSAN 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 532 ppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSygvdgmDLTSQGAGTYWYLPPECFVVGKEppkISNKVDVWS 611
Cdd:cd07858  129 --VLHRDLKPSNLLL---NANCDLKICDFGLARTTSEKG------DFMTEYVVTRWYRAPELLLNCSE---YTTAIDVWS 194
                        170
                 ....*....|....
gi 211971036 612 VGVIFFQcLYGRKP 625
Cdd:cd07858  195 VGCIFAE-LLGRKP 207
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
419-681 3.20e-13

Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GAK, also called auxilin-2, contains an N-terminal kinase domain that phosphorylates the mu subunits of adaptor protein (AP) 1 and AP2. In addition, it contains an auxilin-1-like domain structure consisting of PTEN-like, clathrin-binding, and J domains. Like auxilin-1, GAK facilitates Hsc70-mediated dissociation of clathrin from clathrin-coated vesicles. GAK is expressed ubiquitously and is enriched in the Golgi, unlike auxilin-1 which is nerve-specific. GAK also plays regulatory roles outside of clathrin-mediated membrane traffic including the maintenance of centrosome integrity and chromosome congression, neural patterning, survival of neurons, and immune responses through interaction with the interleukin 12 receptor. It also interacts with the androgen receptor, acting as a transcriptional coactivator, and its expression is significantly increased with the progression of prostate cancer. The GAK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270938 [Multi-domain]  Cd Length: 282  Bit Score: 70.62  E-value: 3.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKswrDEKKenyhKHACREYRIHKELD-HPRIVKLYDYFSL---DTDTFCT----VL 490
Cdd:cd14036   13 FAFVYEAQDVGTGKEYALKRLLSNE---EEKN----KAIIQEINFMKKLSgHPNIVQFCSAASIgkeESDQGQAeyllLT 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 491 EYCEGNDLDFY--LKQHKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIM-- 566
Cdd:cd14036   86 ELCKGQLVDFVkkVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSPPIIHRDLKIENLLI---GNQGQIKLCDFGSATTEah 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 567 -DDDSYGVDGMDLTS---QGAGTYWYLPPECFVVGKEPPkISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQENTIL 642
Cdd:cd14036  163 yPDYSWSAQKRSLVEdeiTRNTTPMYRTPEMIDLYSNYP-IGEKQDIWALGCILYLLCFRKHPF-EDGAKLRIINAKYTI 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 211971036 643 KATEVQFPVkpvvsseAKAFIRRCLAYRKEDRFD----VHQLA 681
Cdd:cd14036  241 PPNDTQYTV-------FHDLIRSTLKVNPEERLSiteiVEQLQ 276
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
460-680 3.44e-13

Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. IRAKs are involved in Toll-like receptor (TLR) and interleukin-1 (IL-1) signalling pathways, and are thus critical in regulating innate immune responses and inflammation. IRAKs contain an N-terminal Death domain (DD), a proST region (rich in serines, prolines, and threonines), a central kinase domain, and a C-terminal domain; IRAK-4 lacks the C-terminal domain. Vertebrates contain four IRAKs (IRAK-1, -2, -3 (or -M), and -4) that display distinct functions and patterns of expression and subcellular distribution, and can differentially mediate TLR signaling. IRAK4 plays a critical role in NFkB activation by its interaction with MyD88, which acts as a scaffold that enables IRAK4 to phosphorylate and activate IRAK1 and/or IRAK2. It also plays an important role in type I IFN production induced by TLR7/8/9. The IRAK4 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: 271060 [Multi-domain]  Cd Length: 288  Bit Score: 70.61  E-value: 3.44e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYfSLDTDTFCTVLEYCEGNDLdfyLKQHKLMSEKEARSIVMQI------VNALRYLNEikPP 533
Cdd:cd14158   64 EIQVMAKCQHENLVELLGY-SCDGPQLCLVYTYMPNGSL---LDRLACLNDTPPLSWHMRCkiaqgtANGINYLHE--NN 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 534 IIHYDLKPGNILLVDGTACgeiKITDFGLSKIMDDDSYGVdgmdLTSQGAGTYWYLPPECFvvgkePPKISNKVDVWSVG 613
Cdd:cd14158  138 HIHRDIKSANILLDETFVP---KISDFGLARASEKFSQTI----MTERIVGTTAYMAPEAL-----RGEITPKSDIFSFG 205
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036 614 VIFFQCLYGRKPFGHNQSQQDIL--------QENTILKATEVQFPVKPVVSSEAKAFI-RRCLAYRKEDRFDVHQL 680
Cdd:cd14158  206 VVLLEIITGLPPVDENRDPQLLLdikeeiedEEKTIEDYVDKKMGDWDSTSIEAMYSVaSQCLNDKKNRRPDIAKV 281
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
419-637 3.59e-13

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The EphA2 receptor is overexpressed in tumor cells and tumor blood vessels in a variety of cancers including breast, prostate, lung, and colon. As a result, it is an attractive target for drug design since its inhibition could affect several aspects of tumor progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). Class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. The EphA2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 133194 [Multi-domain]  Cd Length: 268  Bit Score: 70.39  E-value: 3.59e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKA-FDLYEQRYAAVKIHQLNKSWRDEKKENYhkhaCREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGND 497
Cdd:cd05063   18 FGEVFRGiLKMPGRKEVAVAIKTLKPGYTEKQRQDF----LSEASIMGQFSHHNIIRLEGVVTKFKPAM-IITEYMENGA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHK-LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACgeiKITDFGLSKIMDDDSygvDGM 576
Cdd:cd05063   93 LDKYLRDHDgEFSSYQLVGMLRGIAAGMKYLSDMN--YVHRDLAARNILVNSNLEC---KVSDFGLSRVLEDDP---EGT 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 577 DLTSQGAGTYWYLPPECFVVgkepPKISNKVDVWSVGVIFFQCL-YGRKPFgHNQSQQDILQ 637
Cdd:cd05063  165 YTTSGGKIPIRWTAPEAIAY----RKFTSASDVWSFGIVMWEVMsFGERPY-WDMSNHEVMK 221
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
434-674 4.02e-13

Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The DDR subfamily consists of homologs of mammalian DDR1, DDR2, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270644 [Multi-domain]  Cd Length: 297  Bit Score: 70.44  E-value: 4.02e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 434 AAVKIhqLNKSWRDEKKENYHKhacrEYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEA 513
Cdd:cd05051   49 VAVKM--LRPDASKNAREDFLK----EVKIMSQLKDPNIVRLLG-VCTRDEPLCMIVEYMENGDLNQFLQKHEAETQGAS 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 514 RS------------IVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgtacGE---IKITDFGLSKIM-DDDSYGVDGMD 577
Cdd:cd05051  122 ATnsktlsygtllyMATQIASGMKYLESLN--FVHRDLATRNCLV------GPnytIKIADFGMSRNLySGDYYRIEGRA 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LtsqgagtywyLPP-----ECFVVGkeppKISNKVDVWSVGV----IFFQClyGRKPFGHNQSQQDIlqENTILK----A 644
Cdd:cd05051  194 V----------LPIrwmawESILLG----KFTTKSDVWAFGVtlweILTLC--KEQPYEHLTDEQVI--ENAGEFfrddG 255
                        250       260       270
                 ....*....|....*....|....*....|
gi 211971036 645 TEVQFPVKPVVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd05051  256 MEVYLSRPPNCPKEIYELMLECWRRDEEDR 285
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
431-671 4.18e-13

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: 71.96  E-value: 4.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 431 QRYAAVKIhqLNKsWRDEKKEnyhKHAC-REYR-IHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYL-KQHKL 507
Cdd:cd05624   97 ERIYAMKI--LNK-WEMLKRA---ETACfREERnVLVNGDCQWITTLHYAFQ-DENYLYLVMDYYVGGDLLTLLsKFEDK 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 508 MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsygvdGMDLTSQGAGTYW 587
Cdd:cd05624  170 LPEDMARFYIGEMVLAIHSIHQLH--YVHRDIKPDNVLL---DMNGHIRLADFGSCLKMNDD-----GTVQSSVAVGTPD 239
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 588 YLPPECFV-----VGKEPPKisnkVDVWSVGVIFFQCLYGRKPFghnQSQQDILQENTILKATE-VQFPVKPV-VSSEAK 660
Cdd:cd05624  240 YISPEILQamedgMGKYGPE----CDWWSLGVCMYEMLYGETPF---YAESLVETYGKIMNHEErFQFPSHVTdVSEEAK 312
                        250
                 ....*....|.
gi 211971036 661 AFIRRCLAYRK 671
Cdd:cd05624  313 DLIQRLICSRE 323
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
419-615 5.74e-13

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: 70.74  E-value: 5.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHqlnKSwrdekKENYHKHACREYRIHKEL-------DHPRIVKLYDYFSLdTDTFCTVLE 491
Cdd:cd14212   12 FGQVVKCQDLKTNKLVAVKVL---KN-----KPAYFRQAMLEIAILTLLntkydpeDKHHIVRLLDHFMH-HGHLCIVFE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 492 yCEGNDLDFYLKQHKL--MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcGEIKITDFGlSKIMDDd 569
Cdd:cd14212   83 -LLGVNLYELLKQNQFrgLSLQLIRKFLQQLLDALSVLKDAR--IIHCDLKPENILLVNLDS-PEIKLIDFG-SACFEN- 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 211971036 570 sygvdgmdltsQGAGTY----WYLPPEcFVVGKeppKISNKVDVWSVGVI 615
Cdd:cd14212  157 -----------YTLYTYiqsrFYRSPE-VLLGL---PYSTAIDMWSLGCI 191
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
422-686 6.90e-13

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: 69.75  E-value: 6.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKIHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFY 501
Cdd:cd06654   36 VYTAMDVATGQEVAIRQMNLQQQPKKELIIN-------EILVMRENKNPNIVNYLDSY-LVGDELWVVMEYLAGGSLTDV 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 502 LKQhKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILL-VDGTacgeIKITDFGL-SKIMDDDSYgvdgmdlT 579
Cdd:cd06654  108 VTE-TCMDEGQIAAVCRECLQALEFLHSNQ--VIHRDIKSDNILLgMDGS----VKLTDFGFcAQITPEQSK-------R 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 580 SQGAGTYWYLPPECFVVGKEPPKisnkVDVWSVGVIFFQCLYGRKPFghnqsqqdiLQENTI----LKAT----EVQFPV 651
Cdd:cd06654  174 STMVGTPYWMAPEVVTRKAYGPK----VDIWSLGIMAIEMIEGEPPY---------LNENPLralyLIATngtpELQNPE 240
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 211971036 652 KpvVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06654  241 K--LSAIFRDFLNRCLEMDVEKRGSAKELLQHQFL 273
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
457-639 6.93e-13

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: 70.10  E-value: 6.93e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 457 ACREYRIHKELDHPRIVKLYDYFSLDTDTFCTVL-EYCEgNDLDFYLKQHKL---------MSEKEARSIVMQIVNALRY 526
Cdd:cd07867   46 ACREIALLRELKHPNVIALQKVFLSHSDRKVWLLfDYAE-HDLWHIIKFHRAskankkpmqLPRSMVKSLLYQILDGIHY 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 527 LNeiKPPIIHYDLKPGNILLV-DGTACGEIKITDFGLSKIMDDDSYGVDGMDLTsqgAGTYWYLPPECFVVGKEPPKisn 605
Cdd:cd07867  125 LH--ANWVLHRDLKPANILVMgEGPERGRVKIADMGFARLFNSPLKPLADLDPV---VVTFWYRAPELLLGARHYTK--- 196
                        170       180       190
                 ....*....|....*....|....*....|....
gi 211971036 606 KVDVWSVGVIFFQCLYGrKPFGHNQsQQDILQEN 639
Cdd:cd07867  197 AIDIWAIGCIFAELLTS-EPIFHCR-QEDIKTSN 228
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
419-614 9.88e-13

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: 69.20  E-value: 9.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSwRDEKKEnyhkhACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd06609   14 FGEVYKGIDKRTNQVVAIKVIDLEEA-EDEIED-----IQQEIQFLSQCDSPYITKYYGSF-LKGSKLWIIMEYCGGGSV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKPpiIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGVDGMdl 578
Cdd:cd06609   87 LDLLKPGPL-DETYIAFILREVLLGLEYLHSEGK--IHRDIKAANILL---SEEGDVKLADFGVSGQLTSTMSKRNTF-- 158
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 211971036 579 tsqgAGTYWYLPPEcfVVGKEppKISNKVDVWSVGV 614
Cdd:cd06609  159 ----VGTPFWMAPE--VIKQS--GYDEKADIWSLGI 186
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
419-672 1.07e-12

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: 69.18  E-value: 1.07e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfdLYEQRYAAVKIHQLNKSWRDEK-------KENYHKHACREYRIHKE-------LDHPRIVKLydyFSLDTD 484
Cdd:cd14000    7 FGSVYRA--SYKGEPVAVKIFNKHTSSNFANvpadtmlRHLRATDAMKNFRLLRQeltvlshLHHPSIVYL---LGIGIH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 485 TFCTVLEYCEGNDLDFYLKQHKL----MSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILL--VDGTACGEIKIT 558
Cdd:cd14000   82 PLMLVLELAPLGSLDHLLQQDSRsfasLGRTLQQRIALQVADGLRYLH--SAMIIYRDLKSHNVLVwtLYPNSAIIIKIA 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 559 DFGLSKimdddsYGVDGMDLTSQGagTYWYLPPEcfvVGKEPPKISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQDIlq 637
Cdd:cd14000  160 DYGISR------QCCRMGAKGSEG--TPGFRAPE---IARGNVIYNEKVDVFSFGMLLYEILSGGAPMvGHLKFPNEF-- 226
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 211971036 638 enTILKAtevqfpVKPVVSSEAKAFIRRCLAYRKE 672
Cdd:cd14000  227 --DIHGG------LRPPLKQYECAPWPEVEVLMKK 253
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
449-675 1.09e-12

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: 69.28  E-value: 1.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 449 KKENYHKHACREYRIHKELDHPRIVKL-YDYFSldTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSI--VMQIVNALR 525
Cdd:cd05630   39 KKRKGEAMALNEKQILEKVNSRFVVSLaYAYET--KDALCLVLTLMNGGDLKFHIYHMGQAGFPEARAVfyAAEICCGLE 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 526 YLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSygvdgmdlTSQG-AGTYWYLPPEcfVVGKEppKIS 604
Cdd:cd05630  117 DLHRER--IVYRDLKPENILLDDH---GHIRISDLGLAVHVPEGQ--------TIKGrVGTVGYMAPE--VVKNE--RYT 179
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 605 NKVDVWSVGVIFFQCLYGRKPFghNQSQQDILQENTILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRF 675
Cdd:cd05630  180 FSPDWWALGCLLYEMIAGQSPF--QQRKKKIKREEVERLVKEVPEEYSEKFSPQARSLCSMLLCKDPAERL 248
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
459-625 1.13e-12

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: 69.69  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLDTD-TFCtvLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEiKPPIIHY 537
Cdd:cd06649   52 RELQVLHECNSPYIVGFYGAFYSDGEiSIC--MEHMDGGSLDQVLKEAKRIPEEILGKVSIAVLRGLAYLRE-KHQIMHR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLvdgTACGEIKITDFGLSKIMDDdsygvdgmDLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFF 617
Cdd:cd06649  129 DVKPSNILV---NSRGEIKLCDFGVSGQLID--------SMANSFVGTRSYMSPERL----QGTHYSVQSDIWSMGLSLV 193

                 ....*...
gi 211971036 618 QCLYGRKP 625
Cdd:cd06649  194 ELAIGRYP 201
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
419-677 1.23e-12

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


Pssm-ID: 270866 [Multi-domain]  Cd Length: 292  Bit Score: 69.29  E-value: 1.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnkswRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd08229   37 FSEVYRATCLLDGVPVALKKVQI----FDLMDAKARADCIKEIDLLKQLNHPNVIKYYASF-IEDNELNIVLELADAGDL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 D----FYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGVD 574
Cdd:cd08229  112 SrmikHFKKQKRLIPEKTVWKYFVQLCSALEHMHSRR--VMHRDIKPANVFI---TATGVVKLGDLGLGRFFSSKTTAAH 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 575 GMdltsqgAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQEntilKATEVQFPVKPV 654
Cdd:cd08229  187 SL------VGTPYYMSPERI----HENGYNFKSDIWSLGCLLYEMAALQSPFYGDKMNLYSLCK----KIEQCDYPPLPS 252
                        250       260
                 ....*....|....*....|....*
gi 211971036 655 --VSSEAKAFIRRCLAYRKEDRFDV 677
Cdd:cd08229  253 dhYSEELRQLVNMCINPDPEKRPDI 277
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
419-687 1.55e-12

Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TAO1 is sometimes referred to as prostate-derived sterile 20-like kinase 2 (PSK2). TAO1 activates the p38 MAPK through direct interaction with and activation of MEK3. TAO1 is highly expressed in the brain and may play a role in neuronal apoptosis. TAO1 interacts with the checkpoint proteins BubR1 and Mad2, and plays an important role in regulating mitotic progression, which is required for both chromosome congression and checkpoint-induced anaphase delay. TAO1 may play a role in protecting genomic stability. TAO proteins possess MAPK kinase kinase activity. MAPK signaling cascades are important in mediating cellular responses to extracellular signals. The TAO1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270805 [Multi-domain]  Cd Length: 317  Bit Score: 69.31  E-value: 1.55e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKI-----HQLNKSWRDekkenyhkhACREYRIHKELDHPRIVKlYDYFSLDTDTFCTVLEYC 493
Cdd:cd06635   38 FGAVYFARDVRTSEVVAIKKmsysgKQSNEKWQD---------IIKEVKFLQRIKHPNSIE-YKGCYLREHTAWLVMEYC 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 494 EGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGV 573
Cdd:cd06635  108 LGSASDLLEVHKKPLQEIEIAAITHGALQGLAYLHSHN--MIHRDIKAGNILL---TEPGQVKLADFGSASIASPANSFV 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 574 dgmdltsqgaGTYWYLPPECfVVGKEPPKISNKVDVWSVGVIFFQcLYGRKPFGHNQSQQDIL-----QENTILKATEvq 648
Cdd:cd06635  183 ----------GTPYWMAPEV-ILAMDEGQYDGKVDVWSLGITCIE-LAERKPPLFNMNAMSALyhiaqNESPTLQSNE-- 248
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 211971036 649 fpvkpvVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLL 687
Cdd:cd06635  249 ------WSDYFRNFVDSCLQKIPQDRPTSEELLKHMFVL 281
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
419-632 1.56e-12

Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; Fes subfamily; catalytic (c) domain. Fes subfamily members include Fes (or Fps), Fer, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes subfamily proteins are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated tyr kinase activity. Fes and Fer kinases play roles in haematopoiesis, inflammation and immunity, growth factor signaling, cytoskeletal regulation, cell migration and adhesion, and the regulation of cell-cell interactions. Fes and Fer show redundancy in their biological functions.


Pssm-ID: 270637 [Multi-domain]  Cd Length: 251  Bit Score: 68.24  E-value: 1.56e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihqlnkSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGND- 497
Cdd:cd05041    8 FGDVYRGVLKPDNTEVAVK------TCRETLPPDLKRKFLQEARILKQYDHPNIVKLIG-VCVQKQPIMIVMELVPGGSl 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLnEIKpPIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSYGV-DGM 576
Cdd:cd05041   81 LTFLRKKGARLTVKQLLQMCLDAAAGMEYL-ESK-NCIHRDLAARNCLVGEN---NVLKISDFGMSREEEDGEYTVsDGL 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 577 dltsQGAGTYWyLPPECFVVGkeppKISNKVDVWSVGVIFFQCL-YGRKPF-GHNQSQ 632
Cdd:cd05041  156 ----KQIPIKW-TAPEALNYG----RYTSESDVWSFGILLWEIFsLGATPYpGMSNQQ 204
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
443-632 1.59e-12

Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Trk subfamily consists of TrkA, TrkB, TrkC, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, the nerve growth factor (NGF) family of neutrotrophins, leads to Trk receptor oligomerization and activation of the catalytic domain. Trk receptors are mainly expressed in the peripheral and central nervous systems. They play important roles in cell fate determination, neuronal survival and differentiation, as well as in the regulation of synaptic plasticity. Altered expression of Trk receptors is associated with many human diseases. The Trk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270643 [Multi-domain]  Cd Length: 280  Bit Score: 68.65  E-value: 1.59e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDLDFYLKQH-------KLMSEKEAR- 514
Cdd:cd05049   41 KTLKDASSPDARKDFEREAELLTNLQHENIVKFYG-VCTEGDPLLMVFEYMEHGDLNKFLRSHgpdaaflASEDSAPGEl 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 515 ------SIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSK-IMDDDSYGVDGMDLTSqgagTYW 587
Cdd:cd05049  120 tlsqllHIAVQIASGMVYLASQH--FVHRDLATRNCLVGTNLV---VKIGDFGMSRdIYSTDYYRVGGHTMLP----IRW 190
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 211971036 588 yLPPECFVVGkeppKISNKVDVWSVGVIFFQCL-YGRKP-FGHNQSQ 632
Cdd:cd05049  191 -MPPESILYR----KFTTESDVWSFGVVLWEIFtYGKQPwFQLSNTE 232
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
465-679 1.74e-12

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


Pssm-ID: 270894 [Multi-domain]  Cd Length: 268  Bit Score: 68.19  E-value: 1.74e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 465 KELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDL-DFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPII-HYDLKPG 542
Cdd:cd13992   51 KELVHDNLNKFIG-ICINPPNIAVVTEYCTRGSLqDVLLNREIKMDWMFKSSFIKDIVKGMNYLH--SSSIGyHGRLKSS 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 543 NILlVDGTAcgEIKITDFGLSKIMDDDsyGVDGMDLTSQGAGTYWyLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYG 622
Cdd:cd13992  128 NCL-VDSRW--VVKLTDFGLRNLLEEQ--TNHQLDEDAQHKKLLW-TAPELLRGSLLEVRGTQKGDVYSFAIILYEILFR 201
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 623 RKPFghnqsqqDILQENTILKatEVQ----FPVKPVVSSEAK-------AFIRRCLAYRKEDRFDVHQ 679
Cdd:cd13992  202 SDPF-------ALEREVAIVE--KVIsggnKPFRPELAVLLDefpprlvLLVKQCWAENPEKRPSFKQ 260
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
419-685 1.81e-12

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: 68.19  E-value: 1.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKEnYHKHACrEYRIHKELDHPRIVKLYDYFSLDTDTFCTV-LEYCEGND 497
Cdd:cd06651   20 FGRVYLCYDVDTGRELAAKQVQFDPESPETSKE-VSALEC-EIQLLKNLQHERIVQYYGCLRDRAEKTLTIfMEYMPGGS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGVDGMD 577
Cdd:cd06651   98 VKDQLKAYGALTESVTRKYTRQILEGMSYLH--SNMIVHRDIKGANILR---DSAGNVKLGDFGASKRLQTICMSGTGIR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 LTSqgaGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTilKATEVQFPVKpvVSS 657
Cdd:cd06651  173 SVT---GTPYWMSPE--VISGE--GYGRKADVWSLGCTVVEMLTEKPPWAEYEAMAAIFKIAT--QPTNPQLPSH--ISE 241
                        250       260
                 ....*....|....*....|....*...
gi 211971036 658 EAKAFIRRCLAYRKEdRFDVHQLANDPY 685
Cdd:cd06651  242 HARDFLGCIFVEARH-RPSAEELLRHPF 268
PKc_TOPK cd14001
Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer ...
435-620 2.15e-12

Catalytic domain of the Dual-specificity protein kinase, Lymphokine-activated killer T-cell-originated protein 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. TOPK, also called PDZ-binding kinase (PBK), is activated at the early stage of mitosis and plays a critical role in cytokinesis. It partly functions as a mitogen-activated protein kinase (MAPK) kinase and is capable of phosphorylating p38, JNK1, and ERK2. TOPK also plays a role in DNA damage sensing and repair through its phosphorylation of histone H2AX. It contributes to cancer development and progression by downregulating the function of tumor suppressor p53 and reducing cell-cycle regulatory proteins. TOPK is found highly expressed in breast and skin cancer cells. The TOPK 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: 270903 [Multi-domain]  Cd Length: 292  Bit Score: 68.19  E-value: 2.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKihQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFCTVLEYCegndldfylkQHKLMSEKEAR 514
Cdd:cd14001   32 AVK--KINSKCDKGQRSLYQERLKEEAKILKSLNHPNIVGFRAFTKSEDGSLCLAMEYG----------GKSLNDLIEER 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 515 S--------------IVMQIVNALRYL-NEIKppIIHYDLKPGNIlLVDGTAcGEIKITDFGLSKIMDDDSYGVDgmDLT 579
Cdd:cd14001  100 YeaglgpfpaatilkVALSIARALEYLhNEKK--ILHGDIKSGNV-LIKGDF-ESVKLCDFGVSLPLTENLEVDS--DPK 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 211971036 580 SQGAGTYWYLPPEcfvVGKEPPKISNKVDVWSVGVIFFQCL 620
Cdd:cd14001  174 AQYVGTEPWKAKE---ALEEGGVITDKADIFAYGLVLWEMM 211
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
460-627 2.17e-12

Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Tec-like subfamily is composed of Tec, Btk, Bmx (Etk), Itk (Tsk, Emt), Rlk (Txk), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, some members contain the Tec homology (TH) domain, which contains proline-rich and zinc-binding regions. Tec kinases form the second largest subfamily of nonreceptor PTKs and are expressed mainly by haematopoietic cells, although Tec and Bmx are also found in endothelial cells. B-cells express Btk and Tec, while T-cells express Itk, Txk, and Tec. Collectively, Tec kinases are expressed in a variety of myeloid cells such as mast cells, platelets, macrophages, and dendritic cells. Each Tec kinase shows a distinct cell-type pattern of expression. Tec kinases play important roles in the development, differentiation, maturation, regulation, survival, and function of B-cells and T-cells. Mutations in Btk cause the severe B-cell immunodeficiency, X-linked agammaglobulinaemia (XLA). The Tec-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173637 [Multi-domain]  Cd Length: 256  Bit Score: 67.86  E-value: 2.17e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDLDFYLKQHKlmsEKEARSIVM----QIVNALRYLNEIKppII 535
Cdd:cd05059   49 EAKVMMKLSHPKLVQLYG-VCTKQRPIFIVTEYMANGCLLNYLRERR---GKFQTEQLLemckDVCEAMEYLESNG--FI 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 536 HYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSYgvdgmdLTSQGAG--TYWYlPPECFVVGkeppKISNKVDVWSVG 613
Cdd:cd05059  123 HRDLAARNCLVGEQ---NVVKVSDFGLARYVLDDEY------TSSVGTKfpVKWS-PPEVFMYS----KFSSKSDVWSFG 188
                        170
                 ....*....|....*
gi 211971036 614 VIFFQCLY-GRKPFG 627
Cdd:cd05059  189 VLMWEVFSeGKMPYE 203
STKc_CDK8 cd07868
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 8; STKs ...
457-639 2.22e-12

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: 68.93  E-value: 2.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 457 ACREYRIHKELDHPRIVKLYDYFSLDTDTFCTVL-EYCEgNDLDFYLKQHKLMSEKE---------ARSIVMQIVNALRY 526
Cdd:cd07868   61 ACREIALLRELKHPNVISLQKVFLSHADRKVWLLfDYAE-HDLWHIIKFHRASKANKkpvqlprgmVKSLLYQILDGIHY 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 527 LNeiKPPIIHYDLKPGNILLV-DGTACGEIKITDFGLSKIMDDDSYGVDGMDLTsqgAGTYWYLPPECFVVGKEPPKisn 605
Cdd:cd07868  140 LH--ANWVLHRDLKPANILVMgEGPERGRVKIADMGFARLFNSPLKPLADLDPV---VVTFWYRAPELLLGARHYTK--- 211
                        170       180       190
                 ....*....|....*....|....*....|....
gi 211971036 606 KVDVWSVGVIFFQCLYGrKPFGHNQsQQDILQEN 639
Cdd:cd07868  212 AIDIWAIGCIFAELLTS-EPIFHCR-QEDIKTSN 243
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
470-664 2.25e-12

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: 68.57  E-value: 2.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 470 PRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdg 549
Cdd:cd05587   57 PFLTQLHSCFQ-TMDRLYFVMEYVNGGDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLH--SKGIIYRDLKLDNVML--- 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 550 TACGEIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPPEcfVVGKEPPKISnkVDVWSVGVIFFQCLYGRKPF-GH 628
Cdd:cd05587  131 DAEGHIKIADFGMCK------EGIFGGKTTRTFCGTPDYIAPE--IIAYQPYGKS--VDWWAYGVLLYEMLAGQPPFdGE 200
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 211971036 629 NQSQ--QDILQENtilkateVQFPvkPVVSSEAKAFIR 664
Cdd:cd05587  201 DEDElfQSIMEHN-------VSYP--KSLSKEAVSICK 229
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
443-680 2.36e-12

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak1 is widely expressed in many tissues. Many cytokines are dependent on Jak1 for signaling, including those that use the shared receptor subunits common gamma chain (IL-2, IL-4, IL-7, IL-9, IL-15, IL-21) and gp130 (IL-6, IL-11, oncostatin M, G-CSF, and IFNs, among others). The many varied interactions of Jak1 and its ubiquitous expression suggest many biological roles. Jak1 is important in neurological development, as well as in lymphoid development and function. It also plays a role in the pathophysiology of cardiac hypertrophy and heart failure. A mutation in the ATP-binding site of Jak1 was identified in a human uterine leiomyosarcoma cell line, resulting in defective cytokine induction and antigen presentation, thus allowing the tumor to evade the immune system. Jak1 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Jak1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173644 [Multi-domain]  Cd Length: 284  Bit Score: 68.03  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDT-FCTVLEYCEGNDLDFYLKQHK-LMSEKEARSIVMQI 520
Cdd:cd05079   39 KSLKPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDGGNgIKLIMEFLPSGSLKEYLPRNKnKINLKQQLKYAVQI 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 521 VNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSK-IMDDDSYGVDGMDLTSQgagTYWYlPPECFVvgke 599
Cdd:cd05079  119 CKGMDYLGSRQ--YVHRDLAARNVLVESE---HQVKIGDFGLTKaIETDKEYYTVKDDLDSP---VFWY-APECLI---- 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 600 PPKISNKVDVWSVGVIFFQCL-YGR----------KPFGHNQSQQDILQENTILKaTEVQFPVKPVVSSEAKAFIRRCLA 668
Cdd:cd05079  186 QSKFYIASDVWSFGVTLYELLtYCDsesspmtlflKMIGPTHGQMTVTRLVRVLE-EGKRLPRPPNCPEEVYQLMRKCWE 264
                        250
                 ....*....|..
gi 211971036 669 YRKEDRFDVHQL 680
Cdd:cd05079  265 FQPSKRTTFQNL 276
PK_NRBP1_like cd13984
Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The ...
466-686 2.88e-12

Pseudokinase domain of Nuclear Receptor Binding Protein 1 and similar proteins; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. This subfamily is composed of NRBP1, also called MLF1-adaptor molecule (MADM), and MADML. NRBP1 was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking. MADML (for MADM-Like) has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. The NRBP1-like 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: 270886 [Multi-domain]  Cd Length: 256  Bit Score: 67.56  E-value: 2.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 466 ELDHPRIVKLYDYFsldTDT--------FCTvlEYCEGNDLDFYLKQ----HKLMSEKEARSIVMQIVNALRYLNEIKPP 533
Cdd:cd13984   51 QLDHPNIVKFHRYW---TDVqeekarviFIT--EYMSSGSLKQFLKKtkknHKTMNEKSWKRWCTQILSALSYLHSCDPP 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 534 IIHydlkpGNIllvdgtACGEIKITDFGLSKI----MDDDSYGVdgmDLTSQGAGTYWYLPPECfvvgKEPPKISNKVDV 609
Cdd:cd13984  126 IIH-----GNL------TCDTIFIQHNGLIKIgsvaPDAIHNHV---KTCREEHRNLHFFAPEY----GYLEDVTTAVDI 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 610 WSVGViffqC-LYGRKPFGHNQSQQDILQENTILKAtevqfpVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd13984  188 YSFGM----CaLEMAALEIQSNGEKVSANEEAIIRA------IFSLEDPLQKDFIRKCLSVAPQDRPSARDLLFHPVL 255
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
450-632 3.44e-12

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 70.15  E-value: 3.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036  450 KENYHKHACREYRIHKELDHPRIVKLYDYF-SLDTDTFCTVLEYCEGNDLDFYLKQ-HKLMSEKEARSIV---MQIVNAL 524
Cdd:PTZ00266   52 KEREKSQLVIEVNVMRELKHKNIVRYIDRFlNKANQKLYILMEFCDAGDLSRNIQKcYKMFGKIEEHAIVditRQLLHAL 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036  525 RYLNEIK-----PPIIHYDLKPGNILLVDGTA-CGEI-------------KITDFGLSKimdddSYGVDGMDLTSQGAGT 585
Cdd:PTZ00266  132 AYCHNLKdgpngERVLHRDLKPQNIFLSTGIRhIGKItaqannlngrpiaKIGDFGLSK-----NIGIESMAHSCVGTPY 206
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 211971036  586 YWylPPECFVvgKEPPKISNKVDVWSVGVIFFQCLYGRKPF--GHNQSQ 632
Cdd:PTZ00266  207 YW--SPELLL--HETKSYDDKSDMWALGCIIYELCSGKTPFhkANNFSQ 251
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
460-626 3.52e-12

Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes a subset of Src-like PTKs including Src, Fyn, Yrk, and Yes, which are all widely expressed. Yrk has been detected only in chickens. It is primarily found in neuronal and epithelial cells and in macrophages. It may play a role in inflammation and in response to injury. Src (or c-Src) proteins are cytoplasmic (or non-receptor) PTKs which are anchored to the plasma membrane. They contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). Src proteins are involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. They were identified as the first proto-oncogene products, and they regulate cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. They are also implicated in acute inflammatory responses and osteoclast function. The Src/Fyn-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271105 [Multi-domain]  Cd Length: 248  Bit Score: 66.86  E-value: 3.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSldTDTFCTVLEY-CEGNDLDF-------YLKQHKLMSekearsIVMQIVNALRYLNEIK 531
Cdd:cd14203   40 EAQIMKKLRHDKLVQLYAVVS--EEPIYIVTEFmSKGSLLDFlkdgegkYLKLPQLVD------MAAQIASGMAYIERMN 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 532 ppIIHYDLKPGNILLVDGTACgeiKITDFGLSKIMDDDSYGvdgmdlTSQGAG--TYWyLPPECFVVGkeppKISNKVDV 609
Cdd:cd14203  112 --YIHRDLRAANILVGDNLVC---KIADFGLARLIEDNEYT------ARQGAKfpIKW-TAPEAALYG----RFTIKSDV 175
                        170
                 ....*....|....*...
gi 211971036 610 WSVGVIFFQCLY-GRKPF 626
Cdd:cd14203  176 WSFGILLTELVTkGRVPY 193
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
419-625 4.15e-12

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: 67.40  E-value: 4.15e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnkswrdEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGND- 497
Cdd:cd06641   17 FGEVFKGIDNRTQKVVAIKIIDL------EEAEDEIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLW-IIMEYLGGGSa 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDfyLKQHKLMSEKEARSIVMQIVNALRYLNEIKPpiIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSYGVDGMd 577
Cdd:cd06641   90 LD--LLEPGPLDETQIATILREILKGLDYLHSEKK--IHRDIKAANVLLSEH---GEVKLADFGVAGQLTDTQIKRN*F- 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 211971036 578 ltsqgAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKP 625
Cdd:cd06641  162 -----VGTPFWMAPEVI----KQSAYDSKADIWSLGITAIELARGEPP 200
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
435-686 4.22e-12

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


Pssm-ID: 270801 [Multi-domain]  Cd Length: 266  Bit Score: 67.08  E-value: 4.22e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIHQLNKSWRDEKKENYHKHAcREYRIHKELDHPRIVKlYDYFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEAR 514
Cdd:cd06631   29 AVKQVELDTSDKEKAEKEYEKLQ-EEVDLLKTLKHVNIVG-YLGTCLEDNVVSIFMEFVPGGSIASILARFGALEEPVFC 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 515 SIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSYGVDGMDLTSQGAGTYWYLPPEcf 594
Cdd:cd06631  107 RYTKQILEGVAYLHNNN--VIHRDIKGNNIMLMPN---GVIKLIDFGCAKRLCINLSSGSQSQLLKSMRGTPYWMAPE-- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 595 VVGKEppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEvQFPVKpvVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd06631  180 VINET--GHGRKSDIWSIGCTVFEMATGKPPWADMNPMAAIFAIGSGRKPVP-RLPDK--FSPEARDFVHACLTRDQDER 254
                        250
                 ....*....|..
gi 211971036 675 FDVHQLANDPYL 686
Cdd:cd06631  255 PSAEQLLKHPFI 266
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
419-636 4.33e-12

Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Class EphB receptors bind to transmembrane ephrin-B ligands. There are six vertebrate EphB receptors (EphB1-6), which display promiscuous interactions with three ephrin-B ligands. One exception is EphB2, which also interacts with ephrin A5. EphB receptors play important roles in synapse formation and plasticity, spine morphogenesis, axon guidance, and angiogenesis. In the intestinal epithelium, EphBs are Wnt signaling target genes that control cell compartmentalization. They function as suppressors of colon cancer progression. EphRs comprise the largest subfamily of receptor PTKs (RTKs). They contain an ephrin-binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion. The EphB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173638 [Multi-domain]  Cd Length: 269  Bit Score: 67.20  E-value: 4.33e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKA-FDLYEQRYAAVKIHQLNKSWRDEKKENYhkhaCREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGND 497
Cdd:cd05065   17 FGEVCRGrLKLPGKREIFVAIKTLKSGYTEKQRRDF----LSEASIMGQFDHPNIIHLEGVVTKSRPVM-IITEFMENGA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQhklmseKEARSIVMQIVNALR-------YLNEIKppIIHYDLKPGNILLVDGTACgeiKITDFGLSKIMDDDS 570
Cdd:cd05065   92 LDSFLRQ------NDGQFTVIQLVGMLRgiaagmkYLSEMN--YVHRDLAARNILVNSNLVC---KVSDFGLSRFLEDDT 160
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 571 ygVDGMDLTSQGAGT-YWYLPPECFVVgkepPKISNKVDVWSVGVIFFQCL-YGRKPFgHNQSQQDIL 636
Cdd:cd05065  161 --SDPTYTSSLGGKIpIRWTAPEAIAY----RKFTSASDVWSYGIVMWEVMsYGERPY-WDMSNQDVI 221
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
489-680 4.40e-12

Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PDIK1L is also called STK35 or CLIK-1. It is predominantly a nuclear protein which is capable of autophosphorylation. Through its interaction with the PDZ-LIM protein CLP-36, it is localized to actin stress fibers. The PDIK1L 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: 270879 [Multi-domain]  Cd Length: 322  Bit Score: 67.97  E-value: 4.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 489 VLEYCEGNDLDFYLKQHKlMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMdd 568
Cdd:cd13977  113 VMEFCDGGDMNEYLLSRR-PDRQTNTSFMLQLSSALAFLH--RNQIVHRDLKPDNILISHKRGEPILKVADFGLSKVC-- 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 569 DSYGVDGMDLT-------SQGAGTYWYLPPECFvvgkePPKISNKVDVWSVGVIFFQCLYgRKPFGHNQSQQDILQ---- 637
Cdd:cd13977  188 SGSGLNPEEPAnvnkhflSSACGSDFYMAPEVW-----EGHYTAKADIFALGIIIWAMVE-RITFRDGETKKELLGtyiq 261
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 638 -------------ENTILkatEVQFPVKPVVSSEA--KAFIRRCLAYRKEDRFDVHQL 680
Cdd:cd13977  262 qgkeivplgeallENPKL---ELQIPLKKKKSMNDdmKQLLRDMLAANPQERPDAFQL 316
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
460-682 4.61e-12

Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. PKC-alpha is expressed in many tissues and is associated with cell proliferation, apoptosis, and cell motility. It plays a role in the signaling of the growth factors PDGF, VEGF, EGF, and FGF. Abnormal levels of PKC-alpha have been detected in many transformed cell lines and several human tumors. In addition, PKC-alpha is required for HER2 dependent breast cancer invasion. PKCs are classified into three groups (classical, atypical, and novel) depending on their mode of activation and the structural characteristics of their regulatory domain. PKCs undergo three phosphorylations in order to take mature forms. In addition, cPKCs depend on calcium, DAG (1,2-diacylglycerol), and in most cases, phosphatidylserine (PS) for activation. The cPKC-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270766 [Multi-domain]  Cd Length: 341  Bit Score: 68.10  E-value: 4.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPR-IVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYD 538
Cdd:cd05615   60 EKRVLALQDKPPfLTQLHSCFQ-TVDRLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLH--KKGIIYRD 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLvdgTACGEIKITDFGLSKimdddSYGVDGMDlTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQ 618
Cdd:cd05615  137 LKLDNVML---DSEGHIKIADFGMCK-----EHMVEGVT-TRTFCGTPDYIAPE--IIAYQP--YGRSVDWWAYGVLLYE 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 619 CLYGRKPF-GHNQSQ--QDILQEN------------TILKATEVQFPVKPV-VSSEAKAFIRRCLAYRkedRFDVHQLAN 682
Cdd:cd05615  204 MLAGQPPFdGEDEDElfQSIMEHNvsypkslskeavSICKGLMTKHPAKRLgCGPEGERDIREHAFFR---RIDWDKLEN 280
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
459-626 4.81e-12

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: 66.98  E-value: 4.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLyDYFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVmQIVNALRYLN-EIKPPIIHY 537
Cdd:cd14147   51 QEARLFAMLAHPNIIAL-KAVCLEEPNLCLVMEYAAGGPLSRALAGRRVPPHVLVNWAV-QIARGMHYLHcEALVPVIHR 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLVDGTA--CGE---IKITDFGLSKimddDSYGVDGMdltsQGAGTYWYLPPECFvvgkEPPKISNKVDVWSV 612
Cdd:cd14147  129 DLKSNNILLLQPIEndDMEhktLKITDFGLAR----EWHKTTQM----SAAGTYAWMAPEVI----KASTFSKGSDVWSF 196
                        170
                 ....*....|....
gi 211971036 613 GVIFFQCLYGRKPF 626
Cdd:cd14147  197 GVLLWELLTGEVPY 210
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
419-618 5.28e-12

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: 67.06  E-value: 5.28e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYA-AVKIHQLNKSWRDEKKENYhkhacREYRIHKELD---HPRIVKLYDYFSlDTDTFCTVLEYCE 494
Cdd:cd14052   13 FSQVYKVSERVPTGKVyAVKKLKPNYAGAKDRLRRL-----EEVSILRELTldgHDNIVQLIDSWE-YHGHLYIQTELCE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 GNDLDFYLK---QHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSy 571
Cdd:cd14052   87 NGSLDVFLSelgLLGRLDEFRVWKILVELSLGLRFIHDHH--FVHLDLKPANVLI---TFEGTLKIGDFGMATVWPLIR- 160
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 211971036 572 gvdGMDltsqGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQ 618
Cdd:cd14052  161 ---GIE----REGDREYIAPEILSEH----MYDKPADIFSLGLILLE 196
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
432-687 6.12e-12

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: 66.93  E-value: 6.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 432 RYAAVKIHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEK 511
Cdd:cd06659   47 RQVAVKMMDLRKQQRRELLFN-------EVVIMRDYQHPNVVEMYKSY-LVGEELWVLMEYLQGGALTDIVSQTRLNEEQ 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 512 EArSIVMQIVNALRYLNEikPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGVDGMdltsqgAGTYWYLPP 591
Cdd:cd06659  119 IA-TVCEAVLQALAYLHS--QGVIHRDIKSDSILL---TLDGRVKLSDFGFCAQISKDVPKRKSL------VGTPYWMAP 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 592 EcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDI--LQENTILKATEVQfPVKPVVsseaKAFIRRCLAY 669
Cdd:cd06659  187 E--VISRCP--YGTEVDIWSLGIMVIEMVDGEPPYFSDSPVQAMkrLRDSPPPKLKNSH-KASPVL----RDFLERMLVR 257
                        250
                 ....*....|....*...
gi 211971036 670 RKEDRFDVHQLANDPYLL 687
Cdd:cd06659  258 DPQERATAQELLDHPFLL 275
PTKc_ALK_LTK cd05036
Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte ...
419-637 8.88e-12

Catalytic domain of the Protein Tyrosine Kinases, Anaplastic Lymphoma Kinase and Leukocyte Tyrosine Kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyr residues in protein substrates. ALK and LTK are orphan receptor PTKs (RTKs) whose ligands are not yet well-defined. ALK appears to play an important role in mammalian neural development as well as visceral muscle differentiation in Drosophila. ALK is aberrantly expressed as fusion proteins, due to chromosomal translocations, in about 60% of anaplastic large cell lymphomas (ALCLs). ALK fusion proteins are also found in rare cases of diffuse large B cell lymphomas (DLBCLs). LTK is mainly expressed in B lymphocytes and neuronal tissues. It is important in cell proliferation and survival. Transgenic mice expressing TLK display retarded growth and high mortality rate. In addition, a polymorphism in mouse and human LTK is implicated in the pathogenesis of systemic lupus erythematosus. RTKs contain an extracellular ligand-binding domain, a transmembrane region, and an intracellular tyr kinase domain. They are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The ALK/LTK subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270632 [Multi-domain]  Cd Length: 277  Bit Score: 66.26  E-value: 8.88e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAA---VKIHQLNKSWRDEKKENYHKHACreyrIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEG 495
Cdd:cd05036   19 FGEVYEGTVSGMPGDPSplqVAVKTLPELCSEQDEMDFLMEAL----IMSKFNHPNIVRCIG-VCFQRLPRFILLELMAG 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 NDLDFYLKQHKLMSEKEArSIVM--------QIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSK-IM 566
Cdd:cd05036   94 GDLKSFLRENRPRPEQPS-SLTMldllqlaqDVAKGCRYLEENH--FIHRDIAARNCLLTCKGPGRVAKIGDFGMARdIY 170
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 567 DDDSYGVDGMDLTSqgagTYWyLPPECFVVGkeppKISNKVDVWSVGVIFFQCL-YGRKPFGhNQSQQDILQ 637
Cdd:cd05036  171 RADYYRKGGKAMLP----VKW-MPPEAFLDG----IFTSKTDVWSFGVLLWEIFsLGYMPYP-GKSNQEVME 232
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
419-626 9.11e-12

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: 65.75  E-value: 9.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihQLNKSwrdEKkenyhkhacrEYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd14060    6 FGSVYRAIWVSQDKEVAVK--KLLKI---EK----------EAEILSVLSHRNIIQFYGAI-LEAPNYGIVTEYASYGSL 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYL--KQHKLMSEKEARSIVMQIVNALRYLNEIKP-PIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYgvdg 575
Cdd:cd14060   70 FDYLnsNESEEMDMDQIMTWATDIAKGMHYLHMEAPvKVIHRDLKSRNVVI---AADGVLKICDFGASRFHSHTTH---- 142
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 211971036 576 MDLTsqgaGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd14060  143 MSLV----GTFPWMAPE--VIQSLP--VSETCDTYSYGVVLWEMLTREVPF 185
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
432-667 9.37e-12

C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide Exchange Factor, Kalirin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Kalirin, also called Duo or Duet, is a large multidomain protein containing a series of spectrin-like repeats, two each of RhoGEF and SH3 domains, an immunoglobulin-like (Ig) domain and a C-terminal kinase. As a GEF, it activates Rac1, RhoA, and RhoG. It is highly expressed in neurons and is required for spine formation. The kalirin gene produces at least 10 isoforms from alternative promoter use and splicing. Of the major isoforms (Kalirin-7, -9, and -12), only kalirin-12 contains the C-terminal kinase domain. Kalirin-12 is highly expressed during embryonic development and it plays an important role in axon outgrowth. The Kalirin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271017 [Multi-domain]  Cd Length: 248  Bit Score: 65.75  E-value: 9.37e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 432 RYAAVKiHQLNKSWRDE-------KKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTdTFCTVLEYCE-GNDLDFYLK 503
Cdd:cd14115    5 RFSIVK-KCLHKATRKDvavkfvsKKMKKKEQAAHEAALLQHLQHPQYITLHDTYESPT-SYILVLELMDdGRLLDYLMN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 504 QHKLMSEKEARSIvMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGlskimddDSYGVDGMDLTSQGA 583
Cdd:cd14115   83 HDELMEEKVAFYI-RDIMEALQYLHNCR--VAHLDIKPENLLIDLRIPVPRVKLIDLE-------DAVQISGHRHVHHLL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 584 GTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFghnqsqQDILQENTILKATEVQFPVKPV----VSSEA 659
Cdd:cd14115  153 GNPEFAAPE--VIQGTP--VSLATDIWSIGVLTYVMLSGVSPF------LDESKEETCINVCRVDFSFPDEyfgdVSQAA 222

                 ....*...
gi 211971036 660 KAFIRRCL 667
Cdd:cd14115  223 RDFINVIL 230
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
419-621 9.61e-12

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: 66.82  E-value: 9.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqlnksWRDEKKenYHKHACREYRIHKEL------DHPRIVKLYDYFSLDtDTFCTVLEY 492
Cdd:cd14134   25 FGKVLECWDRKRKRYVAVKI------IRNVEK--YREAAKIEIDVLETLaekdpnGKSHCVQLRDWFDYR-GHMCIVFEL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 493 CEGNDLDFyLKQHKLMS--EKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGT----------------ACGE 554
Cdd:cd14134   96 LGPSLYDF-LKKNNYGPfpLEHVQHIAKQLLEAVAFLHDLK--LTHTDLKPENILLVDSDyvkvynpkkkrqirvpKSTD 172
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 555 IKITDFGlSKIMDDDSYGvdgmDLTSqgagTYWYLPPEcfVV---GKEPPkisnkVDVWSVGVIFFQcLY 621
Cdd:cd14134  173 IKLIDFG-SATFDDEYHS----SIVS----TRHYRAPE--VIlglGWSYP-----CDVWSIGCILVE-LY 225
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
425-686 9.70e-12

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: 66.60  E-value: 9.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 425 AFDLYEQRYAAVKIHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDfYLKQ 504
Cdd:cd06658   41 ATEKHTGKQVAVKKMDLRKQQRRELLFN-------EVVIMRDYHHENVVDMYNSY-LVGDELWVVMEFLEGGALT-DIVT 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 505 HKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDSYGVDGMdltsqgAG 584
Cdd:cd06658  112 HTRMNEEQIATVCLSVLRALSYLH--NQGVIHRDIKSDSILL---TSDGRIKLSDFGFCAQVSKEVPKRKSL------VG 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 585 TYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDI--LQENTILKATEVQfpvkpVVSSEAKAF 662
Cdd:cd06658  181 TPYWMAPE--VISRLP--YGTEVDIWSLGIMVIEMIDGEPPYFNEPPLQAMrrIRDNLPPRVKDSH-----KVSSVLRGF 251
                        250       260
                 ....*....|....*....|....
gi 211971036 663 IRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06658  252 LDLMLVREPSQRATAQELLQHPFL 275
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
497-675 1.09e-11

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: 66.28  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 497 DLDFYLKQHKLMSEKEARSI---VMQIVNALRYLNeikppIIHYDLKPGNILLVDGTAcgEIKITDFGLSKIMDDDSygv 573
Cdd:cd13974  118 NLQHYVIREKRLSEREALVIfydVVRVVEALHKKN-----IVHRDLKLGNMVLNKRTR--KITITNFCLGKHLVSED--- 187
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 574 dgmDLTSQGAGTYWYLPPECfVVGKepPKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQEntiLKATEVQFPVKP 653
Cdd:cd13974  188 ---DLLKDQRGSPAYISPDV-LSGK--PYLGKPSDMWALGVVLFTMLYGQFPF-YDSIPQELFRK---IKAAEYTIPEDG 257
                        170       180
                 ....*....|....*....|..
gi 211971036 654 VVSSEAKAFIRRCLAYRKEDRF 675
Cdd:cd13974  258 RVSENTVCLIRKLLVLNPQKRL 279
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
456-638 1.12e-11

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: 66.44  E-value: 1.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 456 HACREYRIHKELDHPRIVKLYdyFSLDT-DTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppI 534
Cdd:cd05585   40 HTLAERTVLAQVDCPFIVPLK--FSFQSpEKLYLVLAFINGGELFHHLQREGRFDLSRARFYTAELLCALECLHKFN--V 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 535 IHYDLKPGNILLvDGTacGEIKITDFGLSKI-MDDDsygvdgmDLTSQGAGTYWYLPPEcFVVGKEPPKIsnkVDVWSVG 613
Cdd:cd05585  116 IYRDLKPENILL-DYT--GHIALCDFGLCKLnMKDD-------DKTNTFCGTPEYLAPE-LLLGHGYTKA---VDWWTLG 181
                        170       180
                 ....*....|....*....|....*...
gi 211971036 614 VIFFQCLYGRKPF---GHNQSQQDILQE 638
Cdd:cd05585  182 VLLYEMLTGLPPFydeNTNEMYRKILQE 209
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
419-621 1.13e-11

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: 65.98  E-value: 1.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSwrdekkenyhkHACREYRIHKELDHPRIVKLY------DYFS---------LDT 483
Cdd:cd14047   19 FGQVFKAKHRIDGKTYAIKRVKLNNE-----------KAEREVKALAKLDHPNIVRYNgcwdgfDYDPetsssnssrSKT 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 484 DTFCTVLEYCEGNDLDFYL-KQHKLMSEK-EARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFG 561
Cdd:cd14047   88 KCLFIQMEFCEKGTLESWIeKRNGEKLDKvLALEIFEQITKGVEYIHSKK--LIHRDLKPSNIFLVDT---GKVKIGDFG 162
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 562 LSKIMDDDSYgvdgmdlTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLY 621
Cdd:cd14047  163 LVTSLKNDGK-------RTKSKGTLSYMSPEQI----SSQDYGKEVDIYALGLILFELLH 211
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
419-674 1.16e-11

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: 66.23  E-value: 1.16e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKkenyhkhacreyRIHKELDH-------PRIVKLYDyfSLDTDTFCTVle 491
Cdd:cd06616   19 FGTVNKMLHKPSGTIMAVKRIRSTVDEKEQK------------RLLMDLDVvmrssdcPYIVKFYG--ALFREGDCWI-- 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 492 yC-EGNDLDF-------YLKQHKLMSEKEARSIVMQIVNALRYL-NEIKppIIHYDLKPGNILLVDGtacGEIKITDFGL 562
Cdd:cd06616   83 -CmELMDISLdkfykyvYEVLDSVIPEEILGKIAVATVKALNYLkEELK--IIHRDVKPSNILLDRN---GNIKLCDFGI 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 563 SkimdddSYGVDGMDLTsQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFGH-----NQSQQDILQ 637
Cdd:cd06616  157 S------GQLVDSIAKT-RDAGCRPYMAPERIDPSASRDGYDVRSDVWSLGITLYEVATGKFPYPKwnsvfDQLTQVVKG 229
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 211971036 638 ENTILKATEvqfpvKPVVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd06616  230 DPPILSNSE-----EREFSPSFVNFVNLCLIKDESKR 261
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
469-670 1.20e-11

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: 66.36  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvd 548
Cdd:cd05591   55 HPFLTALHSCFQ-TKDRLFFVMEYVNGGDLMFQIQRARKFDEPRARFYAAEVTLALMFLH--RHGVIYRDLKLDNILL-- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 549 gTACGEIKITDFGLSK--IMDDDsygvdgmdLTSQGAGTYWYLPPECFvvgKEPPkISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd05591  130 -DAEGHCKLADFGMCKegILNGK--------TTTTFCGTPDYIAPEIL---QELE-YGPSVDWWALGVLMYEMMAGQPPF 196
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 211971036 627 ghNQSQQDILQEnTILKaTEVQFPVkpVVSSEA----KAFIRRCLAYR 670
Cdd:cd05591  197 --EADNEDDLFE-SILH-DDVLYPV--WLSKEAvsilKAFMTKNPAKR 238
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
449-675 1.23e-11

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: 66.17  E-value: 1.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 449 KKENYHKHACREYRIHKELDHPRIVKL-YDYFSldTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSI--VMQIVNALR 525
Cdd:cd05631   39 KKRKGEAMALNEKRILEKVNSRFVVSLaYAYET--KDALCLVLTIMNGGDLKFHIYNMGNPGFDEQRAIfyAAELCCGLE 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 526 YLNeiKPPIIHYDLKPGNILLVDgtaCGEIKITDFGLSKIMDDDSygvdgmdlTSQG-AGTYWYLPPEcfVVGKEppKIS 604
Cdd:cd05631  117 DLQ--RERIVYRDLKPENILLDD---RGHIRISDLGLAVQIPEGE--------TVRGrVGTVGYMAPE--VINNE--KYT 179
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 605 NKVDVWSVGVIFFQCLYGRKPFghNQSQQDILQENTILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRF 675
Cdd:cd05631  180 FSPDWWGLGCLIYEMIQGQSPF--RKRKERVKREEVDRRVKEDQEEYSEKFSEDAKSICRMLLTKNPKERL 248
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
470-639 1.48e-11

Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like kinase (also called greatwall kinase); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The MASTL kinases in this group carry only a catalytic domain, which contains a long insertion relative to MAST kinases. MASTL, also called greatwall kinase (Gwl), is involved in the regulation of mitotic entry, which is controlled by the coordinated activities of protein kinases and opposing protein phosphatases (PPs). The cyclin B/CDK1 complex induces entry into M-phase while PP2A-B55 shows anti-mitotic activity. MASTL/Gwl is activated downstream of cyclin B/CDK1 and indirectly inhibits PP2A-B55 by phosphorylating the small protein alpha-endosulfine (Ensa) or the cAMP-regulated phosphoprotein 19 (Arpp19), resulting in M-phase progression. Gwl kinase may also play roles in mRNA stabilization and DNA checkpoint recovery. The human MASTL gene has also been named FLJ14813; a missense mutation in FLJ14813 is associated with autosomal dominant thrombocytopenia. The MASTL kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270761 [Multi-domain]  Cd Length: 349  Bit Score: 66.44  E-value: 1.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 470 PRIVKLYdyFSLDTDTFC-TVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvd 548
Cdd:cd05610   64 PFIVHLY--YSLQSANNVyLVMEYLIGGDVKSLLHIYGYFDEEMAVKYISEVALALDYLH--RHGIIHRDLKPDNMLI-- 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 549 gTACGEIKITDFGLSKI--------MD-----------DDSYGVDG--MDLTS-----------------QGA------- 583
Cdd:cd05610  138 -SNEGHIKLTDFGLSKVtlnrelnmMDilttpsmakpkNDYSRTPGqvLSLISslgfntptpyrtpksvrRGAarveger 216
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 584 --GTYWYLPPECFVVGKEPPkisnKVDVWSVGVIFFQCLYGRKPFGHNQSQ---QDILQEN 639
Cdd:cd05610  217 ilGTPDYLAPELLLGKPHGP----AVDWWALGVCLFEFLTGIPPFNDETPQqvfQNILNRD 273
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
419-646 1.57e-11

Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The Ror subfamily consists of Ror1, Ror2, and similar proteins. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. Ror kinases are expressed in many tissues during development. They play important roles in bone and heart formation. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Drosophila Ror is expressed only in the developing nervous system during neurite outgrowth and neuronal differentiation, suggesting a role for Drosophila Ror in neural development. More recently, mouse Ror1 and Ror2 have also been found to play an important role in regulating neurite growth in central neurons. Ror1 and Ror2 are believed to have some overlapping and redundant functions. The Ror subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270642 [Multi-domain]  Cd Length: 283  Bit Score: 65.47  E-value: 1.57e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKA--FDLYEQRYA-AVKIHQLNKSWRDEKKENYHkhacREYRIHKELDHPRIVKLYDYFSLDTDTfCTVLEYCEG 495
Cdd:cd05048   18 FGKVYKGelLGPSSEESAiSVAIKTLKENASPKTQQDFR----REAELMSDLQHPNIVCLLGVCTKEQPQ-CMLFEYMAH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 496 NDLDFYLKQHKLMSEKEARS----------------IVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITD 559
Cdd:cd05048   93 GDLHEFLVRHSPHSDVGVSSdddgtassldqsdflhIAIQIAAGMEYLSSHH--YVHRDLAARNCLVGDGLT---VKISD 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 560 FGLSKimddDSYGVDGMDLTSQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQCL-YGRKP-FGH-NQSQQDIL 636
Cdd:cd05048  168 FGLSR----DIYSSDYYRVQSKSLLPVRWMPPEAILYG----KFTTESDVWSFGVVLWEIFsYGLQPyYGYsNQEVIEMI 239
                        250
                 ....*....|
gi 211971036 637 QENTILKATE 646
Cdd:cd05048  240 RSRQLLPCPE 249
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
484-670 1.84e-11

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: 66.24  E-value: 1.84e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 484 DTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGtacGEIKITDFGLS 563
Cdd:cd05633   81 DKLCFILDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMH--NRFVVYRDLKPANILLDEH---GHVRISDLGLA 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 564 kimdddsygvdgMDLTSQ----GAGTYWYLPPECFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQDILQE 638
Cdd:cd05633  156 ------------CDFSKKkphaSVGTHGYMAPEVLQKGT---AYDSSADWFSLGCMLFKLLRGHSPFrQHKTKDKHEIDR 220
                        170       180       190
                 ....*....|....*....|....*....|..
gi 211971036 639 NTILKATEVQFPVKPVVSSEAKAFIRRCLAYR 670
Cdd:cd05633  221 MTLTVNVELPDSFSPELKSLLEGLLQRDVSKR 252
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
460-626 1.91e-11

Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Lck and Blk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Lck is expressed in T-cells and natural killer cells. It plays a critical role in T-cell maturation, activation, and T-cell receptor (TCR) signaling. Lck phosphorylates ITAM (immunoreceptor tyr activation motif) sequences on several subunits of TCRs, leading to the activation of different second messenger cascades. Phosphorylated ITAMs serve as binding sites for other signaling factor such as Syk and ZAP-70, leading to their activation and propagation of downstream events. In addition, Lck regulates drug-induced apoptosis by interfering with the mitochondrial death pathway. The apototic role of Lck is independent of its primary function in T-cell signaling. Blk is expressed specifically in B-cells. It is involved in pre-BCR (B-cell receptor) signaling. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Lck/Blk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270652 [Multi-domain]  Cd Length: 264  Bit Score: 64.91  E-value: 1.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSldTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVM--QIVNALRYLNEIKppIIHY 537
Cdd:cd05067   52 EANLMKQLQHQRLVRLYAVVT--QEPIYIITEYMENGSLVDFLKTPSGIKLTINKLLDMaaQIAEGMAFIEERN--YIHR 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLVDGTACgeiKITDFGLSKIMDDDSYgvdgmdlTSQGAGTY---WyLPPECFVVGkeppKISNKVDVWSVGV 614
Cdd:cd05067  128 DLRAANILVSDTLSC---KIADFGLARLIEDNEY-------TAREGAKFpikW-TAPEAINYG----TFTIKSDVWSFGI 192
                        170
                 ....*....|...
gi 211971036 615 IFFQCL-YGRKPF 626
Cdd:cd05067  193 LLTEIVtHGRIPY 205
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
468-675 2.04e-11

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: 65.83  E-value: 2.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 468 DHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHK-LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILL 546
Cdd:cd05597   59 DRRWITKLHYAFQ-DENYLYLVMDYYCGGDLLTLLSKFEdRLPEEMARFYLAEMVLAIDSIHQLG--YVHRDIKPDNVLL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 547 vdgTACGEIKITDFGLSKIMDDDsygvdGMDLTSQGAGTYWYLPPECF--------VVGKEppkisnkVDVWSVGVIFFQ 618
Cdd:cd05597  136 ---DRNGHIRLADFGSCLKLRED-----GTVQSSVAVGTPDYISPEILqamedgkgRYGPE-------CDWWSLGVCMYE 200
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 619 CLYGRKPFghnqsQQDILQEN--TILKATE-VQFP-VKPVVSSEAKAFIRRcLAYRKEDRF 675
Cdd:cd05597  201 MLYGETPF-----YAESLVETygKIMNHKEhFSFPdDEDDVSEEAKDLIRR-LICSRERRL 255
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
519-641 2.08e-11

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: 66.31  E-value: 2.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 519 QIVNALRYLNEIKppIIHYDLKPGNILLvdGTACgEIKITDFGLSKIMDDDsygvDGMDLTsQGAGTYWYLPPEcFVVGK 598
Cdd:cd07853  111 QILRGLKYLHSAG--ILHRDIKPGNLLV--NSNC-VLKICDFGLARVEEPD----ESKHMT-QEVVTQYYRAPE-ILMGS 179
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 211971036 599 epPKISNKVDVWSVGVIFFQCLYGRKPFghnQSQQDILQENTI 641
Cdd:cd07853  180 --RHYTSAVDIWSVGCIFAELLGRRILF---QAQSPIQQLDLI 217
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
419-683 2.47e-11

Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; Fer kinase; catalytic (c) domain. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fer kinase is a member of the Fes subfamily of proteins which are cytoplasmic (or nonreceptor) tyr kinases containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. Fer kinase is expressed in a wide variety of tissues, and is found to reside in both the cytoplasm and the nucleus. It plays important roles in neuronal polarization and neurite development, cytoskeletal reorganization, cell migration, growth factor signaling, and the regulation of cell-cell interactions mediated by adherens junctions and focal adhesions. Fer kinase also regulates cell cycle progression in malignant cells.


Pssm-ID: 270668 [Multi-domain]  Cd Length: 251  Bit Score: 64.64  E-value: 2.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfDLYEQRYAAVKihqlnkSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL 498
Cdd:cd05085    9 FGEVYKG-TLKDKTPVAVK------TCKEDLPQELKIKFLSEARILKQYDHPNIVKLIGVCTQRQPIY-IVMELVPGGDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKlmSEKEARSIVMQIVNA---LRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSKIMDDDSYGVDG 575
Cdd:cd05085   81 LSFLRKKK--DELKTKQLVKFSLDAaagMAYLESKN--CIHRDLAARNCLVGENNA---LKISDFGMSRQEDDGVYSSSG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 MdltsQGAGTYWyLPPECFVVGkeppKISNKVDVWSVGVIFFQCL-YGRKPFGHNQSQQdilQENTILKATEVQFPVKpv 654
Cdd:cd05085  154 L----KQIPIKW-TAPEALNYG----RYSSESDVWSFGILLWETFsLGVCPYPGMTNQQ---AREQVEKGYRMSAPQR-- 219
                        250       260
                 ....*....|....*....|....*....
gi 211971036 655 VSSEAKAFIRRCLAYRKEDRFDVHQLAND 683
Cdd:cd05085  220 CPEDIYKIMQRCWDYNPENRPKFSELQKE 248
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
468-717 2.69e-11

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: 65.79  E-value: 2.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 468 DHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLv 547
Cdd:cd05621  110 NSPWVVQLFCAFQ-DDKYLYMVMEYMPGGDLVNLMSNYDV-PEKWAKFYTAEVVLALDAIHSMG--LIHRDVKPDNMLL- 184
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 548 dgTACGEIKITDFGLSKIMDDDsygvdGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFG 627
Cdd:cd05621  185 --DKYGHLKLADFGTCMKMDET-----GMVHCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLFEMLVGDTPFY 257
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 628 HNQ---SQQDILQENTILkatevQFPVKPVVSSEAKAFIRRCLAYR--KEDRFDVHQLANDPYLlphmrrSNSSGNLHMA 702
Cdd:cd05621  258 ADSlvgTYSKIMDHKNSL-----NFPDDVEISKHAKNLICAFLTDRevRLGRNGVEEIKQHPFF------RNDQWNWDNI 326
                        250
                 ....*....|....*..
gi 211971036 703 GLTASPTPP--SSSIIT 717
Cdd:cd05621  327 RETAAPVVPelSSDIDT 343
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
467-626 2.74e-11

Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of Csk, Chk, and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Chk inhibit Src kinases using a noncatalytic mechanism by simply binding to them. As negative regulators of Src kinases, Csk and Chk play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. The Csk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270635 [Multi-domain]  Cd Length: 256  Bit Score: 64.29  E-value: 2.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 467 LDHPRIVKLYDyFSLDTDTFCTVLEYCE-GNDLDfYLKQ--HKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGN 543
Cdd:cd05039   57 LRHPNLVQLLG-VVLEGNGLYIVTEYMAkGSLVD-YLRSrgRAVITRKDQLGFALDVCEGMEYLESKK--FVHRDLAARN 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 544 ILLV-DGTAcgeiKITDFGLSKimdDDSYGVDGMDLTSQgagtyWyLPPECFVVGKeppkISNKVDVWSVGVIFFQCL-Y 621
Cdd:cd05039  133 VLVSeDNVA----KVSDFGLAK---EASSNQDGGKLPIK-----W-TAPEALREKK----FSTKSDVWSFGILLWEIYsF 195

                 ....*
gi 211971036 622 GRKPF 626
Cdd:cd05039  196 GRVPY 200
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
419-592 2.83e-11

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type I Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. This subfamily is composed of type I receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation through trans-phosphorylation by type II receptors, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. They are inhibited by the immunophilin FKBP12, which is thought to control leaky signaling caused by receptor oligomerization in the absence of ligand. The TGFbR-I subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270958 [Multi-domain]  Cd Length: 287  Bit Score: 64.99  E-value: 2.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfdLYEQRYAAVKIHqlnkSWRDEKKENyhkhacREYRIH--KELDHPRIVKLY--DYFSLDTDT-FCTVLEYC 493
Cdd:cd14056    8 YGEVWLG--KYRGEKVAVKIF----SSRDEDSWF------RETEIYqtVMLRHENILGFIaaDIKSTGSWTqLWLITEYH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 494 EGNDLDFYLKQHKLmSEKEARSIVMQIVNALRYL-NEI-----KPPIIHYDLKPGNILLV-DGTACgeikITDFGLSKIM 566
Cdd:cd14056   76 EHGSLYDYLQRNTL-DTEEALRLAYSAASGLAHLhTEIvgtqgKPAIAHRDLKSKNILVKrDGTCC----IADLGLAVRY 150
                        170       180
                 ....*....|....*....|....*.
gi 211971036 567 DDDSYGVDgMDLTSQgAGTYWYLPPE 592
Cdd:cd14056  151 DSDTNTID-IPPNPR-VGTKRYMAPE 174
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
448-678 2.88e-11

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkA is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkA to its ligand, nerve growth factor (NGF), results in receptor oligomerization and activation of the catalytic domain. TrkA is expressed mainly in neural-crest-derived sensory and sympathetic neurons of the peripheral nervous system, and in basal forebrain cholinergic neurons of the central nervous system. It is critical for neuronal growth, differentiation and survival. Alternative TrkA splicing has been implicated as a pivotal regulator of neuroblastoma (NB) behavior. Normal TrkA expression is associated with better NB prognosis, while the hypoxia-regulated TrkAIII splice variant promotes NB pathogenesis and progression. Aberrant TrkA expression has also been demonstrated in non-neural tumors including prostate, breast, lung, and pancreatic cancers. The TrkA subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270674 [Multi-domain]  Cd Length: 280  Bit Score: 64.99  E-value: 2.88e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 448 EKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQH----KLMSEKEARS-------- 515
Cdd:cd05092   45 EATESARQDFQREAELLTVLQHQHIVRFYGVCT-EGEPLIMVFEYMRHGDLNRFLRSHgpdaKILDGGEGQApgqltlgq 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 516 ---IVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSK-IMDDDSYGVDGMDLTSqgagTYWyLPP 591
Cdd:cd05092  124 mlqIASQIASGMVYLASLH--FVHRDLATRNCLVGQGLV---VKIGDFGMSRdIYSTDYYRVGGRTMLP----IRW-MPP 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 592 ECFVVgkepPKISNKVDVWSVGVIFFQCL-YGRKPFGHNQSQQDIlqeNTILKATEVQFPvkPVVSSEAKAFIRRCLAYR 670
Cdd:cd05092  194 ESILY----RKFTTESDIWSFGVVLWEIFtYGKQPWYQLSNTEAI---ECITQGRELERP--RTCPPEVYAIMQGCWQRE 264
                        250
                 ....*....|.
gi 211971036 671 KEDRF---DVH 678
Cdd:cd05092  265 PQQRHsikDIH 275
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
460-626 3.05e-11

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


Pssm-ID: 270657 [Multi-domain]  Cd Length: 272  Bit Score: 64.68  E-value: 3.05e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEY-CEGNDLDFYLKQH--KLMSEKEArSIVMQIVNALRYLNeiKPPIIH 536
Cdd:cd05072   52 EANLMKTLQHDKLVRLYAVVT-KEEPIYIITEYmAKGSLLDFLKSDEggKVLLPKLI-DFSAQIAEGMAYIE--RKNYIH 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 537 YDLKPGNILLVDGTACgeiKITDFGLSKIMDDDSYgvdgmdLTSQGAG--TYWYLPPE----CFVVgkeppkisnKVDVW 610
Cdd:cd05072  128 RDLRAANVLVSESLMC---KIADFGLARVIEDNEY------TAREGAKfpIKWTAPEAinfgSFTI---------KSDVW 189
                        170
                 ....*....|....*..
gi 211971036 611 SVGVIFFQCL-YGRKPF 626
Cdd:cd05072  190 SFGILLYEIVtYGKIPY 206
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
484-626 3.11e-11

Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. RIP2, also called RICK or CARDIAK, harbors a C-terminal Caspase Activation and Recruitment domain (CARD) belonging to the Death domain (DD) superfamily. It functions as an effector kinase downstream of the pattern recognition receptors from the Nod-like (NLR) family, Nod1 and Nod2, which recognizes bacterial peptidoglycans released upon infection. RIP2 may also be involved in regulating wound healing and keratinocyte proliferation. RIP kinases serve as essential sensors of cellular stress. The RIP2 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: 270928 [Multi-domain]  Cd Length: 284  Bit Score: 64.94  E-value: 3.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 484 DTFCTVLEYCEGNDLDfylkqhKLMSEKEAR---------SIVMQIVNALRYLNEIKPPIIHYDLKPGNILLvDGTAcgE 554
Cdd:cd14026   70 EFLGIVTEYMTNGSLN------ELLHEKDIYpdvawplrlRILYEIALGVNYLHNMSPPLLHHDLKTQNILL-DGEF--H 140
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 555 IKITDFGLSKIMDDDSYGVDGMDLTSQGaGTYWYLPPECFVVGKEpPKISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd14026  141 VKIADFGLSKWRQLSISQSRSSKSAPEG-GTIIYMPPEEYEPSQK-RRASVKHDIYSYAIIMWEVLSRKIPF 210
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
443-626 3.14e-11

Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Musk is a receptor PTK (RTK) containing an extracellular region with four immunoglobulin-like domains and a cysteine-rich cluster, a transmembrane segment, and an intracellular catalytic domain. Musk is expressed and concentrated in the postsynaptic membrane in skeletal muscle. It is essential for the establishment of the neuromuscular junction (NMJ), a peripheral synapse that conveys signals from motor neurons to muscle cells. Agrin, a large proteoglycan released from motor neurons, stimulates Musk autophosphorylation and activation, leading to the clustering of acetylcholine receptors (AChRs). To date, there is no evidence to suggest that agrin binds directly to Musk. Mutations in AChR, Musk and other partners are responsible for diseases of the NMJ, such as the autoimmune syndrome myasthenia gravis. The Musk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133181 [Multi-domain]  Cd Length: 288  Bit Score: 64.85  E-value: 3.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCEGNDLDFYLK------QHKL--------- 507
Cdd:cd05050   41 KMLKEEASADMQADFQREAALMAEFDHPNIVKLLGVCAVG-KPMCLLFEYMAYGDLNEFLRhrspraQCSLshstssark 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 508 -------MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLS-KIMDDDSYGVDGMDLT 579
Cdd:cd05050  120 cglnplpLSCTEQLCIAKQVAAGMAYLSERK--FVHRDLATRNCLVGENMV---VKIADFGLSrNIYSADYYKASENDAI 194
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 211971036 580 SqgagTYWyLPPECFVVGkeppKISNKVDVWSVGVIFFQCL-YGRKPF 626
Cdd:cd05050  195 P----IRW-MPPESIFYN----RYTTESDVWAYGVVLWEIFsYGMQPY 233
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
433-630 3.40e-11

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 65.39  E-value: 3.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 433 YAAVKIHQLNKSWRDEKKENyhKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKE 512
Cdd:PTZ00426  56 FPPVAIKRFEKSKIIKQKQV--DHVFSERKILNYINHPFCVNLYGSFK-DESYLYLVLEFVIGGEFFTFLRRNKRFPNDV 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 513 ARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSYGVdgmdltsqgAGTYWYLPPE 592
Cdd:PTZ00426 133 GCFYAAQIVLIFEYLQSLN--IVYRDLKPENLLLDKD---GFIKMTDFGFAKVVDTRTYTL---------CGTPEYIAPE 198
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 211971036 593 CFV-VGKeppkiSNKVDVWSVGVIFFQCLYGRKPFGHNQ 630
Cdd:PTZ00426 199 ILLnVGH-----GKAADWWTLGIFIYEILVGCPPFYANE 232
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
468-674 3.63e-11

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: 64.38  E-value: 3.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 468 DHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLV 547
Cdd:cd05606   56 DCPFIVCMTYAFQ-TPDKLCFILDLMNGGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHN--RFIVYRDLKPANILLD 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 548 DGtacGEIKITDFGLSKIMDDdsygvdgmDLTSQGAGTYWYLPPECFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPFG 627
Cdd:cd05606  133 EH---GHVRISDLGLACDFSK--------KKPHASVGTHGYMAPEVLQKGV---AYDSSADWFSLGCMLYKLLKGHSPFR 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 211971036 628 HNQSqQDILQENTILKATEVQFPVKpvVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd05606  199 QHKT-KDKHEIDRMTLTMNVELPDS--FSPELKSLLEGLLQRDVSKR 242
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
435-671 4.00e-11

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: 65.42  E-value: 4.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIhqLNKsWRDEKKEnyhKHAC-REYR-IHKELDHPRIVKLYDYFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKE 512
Cdd:cd05623  101 AMKI--LNK-WEMLKRA---ETACfREERdVLVNGDSQWITTLHYAFQDDNNLYLVMDYYVGGDLLTLLSKFEDRLPEDM 174
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 513 ARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLS-KIMDDdsygvdGMDLTSQGAGTYWYLPP 591
Cdd:cd05623  175 ARFYLAEMVLAIDSVHQLH--YVHRDIKPDNILM---DMNGHIRLADFGSClKLMED------GTVQSSVAVGTPDYISP 243
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 592 ECFVV-----GKEPPKisnkVDVWSVGVIFFQCLYGRKPFghnQSQQDILQENTILKATE-VQFPVKPV-VSSEAKAFIR 664
Cdd:cd05623  244 EILQAmedgkGKYGPE----CDWWSLGVCMYEMLYGETPF---YAESLVETYGKIMNHKErFQFPTQVTdVSENAKDLIR 316

                 ....*..
gi 211971036 665 RCLAYRK 671
Cdd:cd05623  317 RLICSRE 323
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
419-626 4.87e-11

Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Cdc7 kinase (or Hsk1 in fission yeast) is a critical regulator in the initiation of DNA replication. It forms a complex with a Dbf4-related regulatory subunit, a cyclin-like molecule that activates the kinase in late G1 phase, and is also referred to as Dbf4-dependent kinase (DDK). Its main targets are mini-chromosome maintenance (MCM) proteins. Cdc7 kinase may also have additional roles in meiosis, checkpoint responses, the maintenance and repair of chromosome structures, and cancer progression. The Cdc7 kinase subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270921 [Multi-domain]  Cd Length: 252  Bit Score: 63.78  E-value: 4.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDL-------YEQRYAAVKIHQLNKSwrdekkenyHKHACREYRIHKELD-HPRIVKLYDYFSlDTDTFCTVL 490
Cdd:cd14019   14 FSSVYKAEDKlhdlydrNKGRLVALKHIYPTSS---------PSRILNELECLERLGgSNNVSGLITAFR-NEDQVVAVL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 491 EYCEGNDL-DFYLKqhklMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGeiKITDFGLSKIMDDD 569
Cdd:cd14019   84 PYIEHDDFrDFYRK----MSLTDIRIYLRNLFKALKHVHSFG--IIHRDVKPGNFLYNRETGKG--VLVDFGLAQREEDR 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 570 SYGVdgmdltSQGAGTYWYLPPEcfVVGKePPKISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd14019  156 PEQR------APRAGTRGFRAPE--VLFK-CPHQTTAIDIWSAGVILLSILSGRFPF 203
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
453-635 6.34e-11

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: 63.67  E-value: 6.34e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 453 YHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARsIVMQIVNALRYLNEIKp 532
Cdd:cd14027   34 HNEALLEEGKMMNRLRHSRVVKLLGVI-LEEGKYSLVMEYMEKGNLMHVLKKVSVPLSVKGR-IILEIIEGMAYLHGKG- 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 533 pIIHYDLKPGNIlLVDGTAcgEIKITDFGL------SKIMDDDSYGVDGMDLTSQ-GAGTYWYLPPECFVVGKEPPkiSN 605
Cdd:cd14027  111 -VIHKDLKPENI-LVDNDF--HIKIADLGLasfkmwSKLTKEEHNEQREVDGTAKkNAGTLYYMAPEHLNDVNAKP--TE 184
                        170       180       190
                 ....*....|....*....|....*....|
gi 211971036 606 KVDVWSVGVIFFQCLYGRKPFGHNQSQQDI 635
Cdd:cd14027  185 KSDVYSFAIVLWAIFANKEPYENAINEDQI 214
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
446-675 6.61e-11

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: 64.65  E-value: 6.61e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 446 RDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALR 525
Cdd:cd05626   37 KDVLNRNQVAHVKAERDILAEADNEWVVKLYYSFQ-DKDNLYFVMDYIPGGDMMSLLIRMEVFPEVLARFYIAELTLAIE 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 526 YLNEIKppIIHYDLKPGNILL-VDgtacGEIKITDFGL----------------SKIMDDDSYGVDGMD----------- 577
Cdd:cd05626  116 SVHKMG--FIHRDIKPDNILIdLD----GHIKLTDFGLctgfrwthnskyyqkgSHIRQDSMEPSDLWDdvsncrcgdrl 189
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 578 --------------LTSQGAGTYWYLPPECFVvgkePPKISNKVDVWSVGVIFFQCLYGRKPF---GHNQSQQDILQ-EN 639
Cdd:cd05626  190 ktleqratkqhqrcLAHSLVGTPNYIAPEVLL----RKGYTQLCDWWSVGVILFEMLVGQPPFlapTPTETQLKVINwEN 265
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 211971036 640 TIlkatevQFPVKPVVSSEAKAFIRRcLAYRKEDRF 675
Cdd:cd05626  266 TL------HIPPQVKLSPEAVDLITK-LCCSAEERL 294
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
431-626 6.92e-11

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: 63.75  E-value: 6.92e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 431 QRYAAVKIH---QLNKSwRDEKKENYhKHACREYRIHKELDHPRIVKLYDYFSLDTDtFCTVLEYCEGNDLDFYL----K 503
Cdd:cd05608   21 QMRATGKLYackKLNKK-RLKKRKGY-EGAMVEKRILAKVHSRFIVSLAYAFQTKTD-LCLVMTIMNGGDLRYHIynvdE 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 504 QHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDddsygvDGMDLTSQGA 583
Cdd:cd05608   98 ENPGFQEPRACFYTAQIISGLEHLHQRR--IIYRDLKPENVLLDDD---GNVRISDLGLAVELK------DGQTKTKGYA 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 211971036 584 GTYWYLPPEcFVVGKEppkISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd05608  167 GTPGFMAPE-LLLGEE---YDYSVDYFTLGVTLYEMIAARGPF 205
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
468-637 7.69e-11

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: 63.81  E-value: 7.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 468 DHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLv 547
Cdd:cd05620   54 ENPFLTHLYCTFQTKEHLF-FVMEFLNGGDLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHS--KGIIYRDLKLDNVML- 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 548 DGTacGEIKITDFGLSKimdddsYGVDGMDLTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPFg 627
Cdd:cd05620  130 DRD--GHIKIADFGMCK------ENVFGDNRASTFCGTPDYIAPEIL----QGLKYTFSVDWWSFGVLLYEMLIGQSPF- 196
                        170
                 ....*....|
gi 211971036 628 HNQSQQDILQ 637
Cdd:cd05620  197 HGDDEDELFE 206
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
435-635 7.85e-11

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR1 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR1 results in a slow but sustained receptor activation. DDR1 binds to all collagens tested to date (types I-IV). It is widely expressed in many tissues. It is abundant in the brain and is also found in keratinocytes, colonic mucosa epithelium, lung epithelium, thyroid follicles, and the islets of Langerhans. During embryonic development, it is found in the developing neuroectoderm. DDR1 is a key regulator of cell morphogenesis, differentiation and proliferation. It is important in the development of the mammary gland, the vasculator and the kidney. DDR1 is also found in human leukocytes, where it facilitates cell adhesion, migration, maturation, and cytokine production. The DDR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133227 [Multi-domain]  Cd Length: 304  Bit Score: 63.80  E-value: 7.85e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIhqlnksWRDEKKENYHKHACREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMsEKEAR 514
Cdd:cd05096   50 AVKI------LRPDANKNARNDFLKEVKILSRLKDPNIIRLLG-VCVDEDPLCMITEYMENGDLNQFLSSHHLD-DKEEN 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 515 S--------------------IVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgtacGE---IKITDFGLSK-IMDDDS 570
Cdd:cd05096  122 GndavppahclpaisyssllhVALQIASGMKYLSSLN--FVHRDLATRNCLV------GEnltIKIADFGMSRnLYAGDY 193
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 571 YGVDGmdltsQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQCLY--GRKPFGHNQSQQDI 635
Cdd:cd05096  194 YRIQG-----RAVLPIRWMAWECILMG----KFTTASDVWAFGVTLWEILMlcKEQPYGELTDEQVI 251
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
470-639 8.42e-11

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: 63.86  E-value: 8.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 470 PRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLvdg 549
Cdd:cd05616   61 PFLTQLHSCFQ-TMDRLYFVMEYVNGGDLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQS--KGIIYRDLKLDNVML--- 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 550 TACGEIKITDFGLSK--IMDddsyGVDgmdlTSQGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPF- 626
Cdd:cd05616  135 DSEGHIKIADFGMCKenIWD----GVT----TKTFCGTPDYIAPE--IIAYQP--YGKSVDWWAFGVLLYEMLAGQAPFe 202
                        170
                 ....*....|....*
gi 211971036 627 GHNQSQ--QDILQEN 639
Cdd:cd05616  203 GEDEDElfQSIMEHN 217
PTK_CCK4 cd05046
Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also ...
419-682 1.09e-10

Pseudokinase domain of the Protein Tyrosine Kinase, Colon Carcinoma Kinase 4; CCK4, also called protein tyrosine kinase 7 (PTK7), is an orphan receptor PTK (RTK) containing an extracellular region with seven immunoglobulin domains, a transmembrane segment, and an intracellular inactive pseudokinase domain, which shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. Studies in mice reveal that CCK4 is essential for neural development. Mouse embryos containing a truncated CCK4 die perinatally and display craniorachischisis, a severe form of neural tube defect. The mechanism of action of the CCK4 pseudokinase is still unknown. Other pseudokinases such as HER3 rely on the activity of partner RTKs. The CCK4 subfamily is part of a larger superfamily that includes other pseudokinases and the catalytic domains of active kinases including PTKs, protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133178 [Multi-domain]  Cd Length: 275  Bit Score: 62.87  E-value: 1.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAF---DLYEQRYAAVKIHQLNKswrdeKKENyhkHACREYRihKELD------HPRIVKLYDyFSLDTDTFCTV 489
Cdd:cd05046   18 FGEVFLAKakgIEEEGGETLVLVKALQK-----TKDE---NLQSEFR--RELDmfrklsHKNVVRLLG-LCREAEPHYMI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 490 LEYCEGNDLDFYLKQHKL---------MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDF 560
Cdd:cd05046   87 LEYTDLGDLKQFLRATKSkdeklkpppLSTKQKVALCTQIALGMDHLSNAR--FVHRDLAARNCLV---SSQREVKVSLL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 561 GLSKimddDSYGVDGMDLTSQGAGTYWyLPPECFVVGkeppKISNKVDVWSVGVIFFQCL-YGRKPFGhNQSQQDILQEn 639
Cdd:cd05046  162 SLSK----DVYNSEYYKLRNALIPLRW-LAPEAVQED----DFSTKSDVWSFGVLMWEVFtQGELPFY-GLSDEEVLNR- 230
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 211971036 640 tiLKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLAN 682
Cdd:cd05046  231 --LQAGKLELPVPEGCPSRLYKLMTRCWAVNPKDRPSFSELVS 271
pknD PRK13184
serine/threonine-protein kinase PknD;
419-647 1.22e-10

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 65.18  E-value: 1.22e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVkihqlnKSWRDEKKEN--YHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGN 496
Cdd:PRK13184  15 MGEVYLAYDPVCSRRVAL------KKIREDLSENplLKKRFLREAKIAADLIHPGIVPVYSICS-DGDPVYYTMPYIEGY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 497 DLDFYLKQ-------HKLMSEKEA----RSIVMQIVNALRYLNEikPPIIHYDLKPGNILLvdgTACGEIKITDFG--LS 563
Cdd:PRK13184  88 TLKSLLKSvwqkeslSKELAEKTSvgafLSIFHKICATIEYVHS--KGVLHRDLKPDNILL---GLFGEVVILDWGaaIF 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 564 KIMDDD-----SYGVDGM---DLTSQG--AGTYWYLPPECfVVGKEPpkiSNKVDVWSVGVIFFQCLYGRKPFgHNQSQQ 633
Cdd:PRK13184 163 KKLEEEdlldiDVDERNIcysSMTIPGkiVGTPDYMAPER-LLGVPA---SESTDIYALGVILYQMLTLSFPY-RRKKGR 237
                        250
                 ....*....|....
gi 211971036 634 DILQENTILKATEV 647
Cdd:PRK13184 238 KISYRDVILSPIEV 251
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
449-626 1.64e-10

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: 62.76  E-value: 1.64e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 449 KKENYHKHACREYRIHKELDHPRIVKL-YDYFSldTDTFCTVLEYCEGNDLDFYLkqHKLM----SEKEARSIVMQIVNA 523
Cdd:cd05605   39 KKRKGEAMALNEKQILEKVNSRFVVSLaYAYET--KDALCLVLTIMNGGDLKFHI--YNMGnpgfEEERAVFYAAEITCG 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 524 LRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLS-KIMDDDSygVDGMdltsqgAGTYWYLPPEcfVVGKEppK 602
Cdd:cd05605  115 LEHLHSER--IVYRDLKPENILLDDH---GHVRISDLGLAvEIPEGET--IRGR------VGTVGYMAPE--VVKNE--R 177
                        170       180
                 ....*....|....*....|....
gi 211971036 603 ISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd05605  178 YTFSPDWWGLGCLIYEMIEGQAPF 201
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
459-696 2.09e-10

Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Plant MAPKs are typed based on the conserved phosphorylation motif present in the activation loop, TEY and TDY. This subfamily represents the TDY subtype and is composed of Group D plant MAPKs including Arabidopsis thaliana MPK18 (AtMPK18), Oryza sativa Blast- and Wound-induced MAPK1 (OsBWMK1), OsWJUMK1 (Wound- and JA-Uninducible MAPK1), Zea mays MPK6, and the Medicago sativa TDY1 gene product. OsBWMK1 enhances resistance to pathogenic infections. It mediates stress-activated defense responses by activating a transcription factor that affects the expression of stress-related genes. AtMPK18 is involved in microtubule-related functions. In plants, MAPKs are associated with physiological, developmental, hormonal, and stress responses. Some plants show numerous gene duplications of MAPKs; Arabidopsis thaliana harbors at least 20 MAPKs, named AtMPK1-20 while Oryza sativa contains at least 17 MAPKs. Arabidopsis thaliana contains more TEY-type MAPKs than TDY-type, whereas the reverse is true for Oryza sativa. The TDY MAPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 143364 [Multi-domain]  Cd Length: 338  Bit Score: 62.88  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKL-YDYFSLDTDTF---CTVLEYCEgNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppI 534
Cdd:cd07859   48 REIKLLRLLRHPDIVEIkHIMLPPSRREFkdiYVVFELME-SDLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTAN--V 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 535 IHYDLKPGNILlvdGTACGEIKITDFGLSKIMDDDSygvDGMDLTSQGAGTYWYLPPEcfVVGKEPPKISNKVDVWSVGV 614
Cdd:cd07859  125 FHRDLKPKNIL---ANADCKLKICDFGLARVAFNDT---PTAIFWTDYVATRWYRAPE--LCGSFFSKYTPAIDIWSIGC 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 615 IFFQCLYGRKPF-GHNQSQQ-DILQE----------------------NTILKATEVQFPVK-PVVSSEAKAFIRRCLAY 669
Cdd:cd07859  197 IFAEVLTGKPLFpGKNVVHQlDLITDllgtpspetisrvrnekarrylSSMRKKQPVPFSQKfPNADPLALRLLERLLAF 276
                        250       260
                 ....*....|....*....|....*....
gi 211971036 670 RKEDRFDVHQLANDPYL--LPHMRRSNSS 696
Cdd:cd07859  277 DPKDRPTAEEALADPYFkgLAKVEREPSA 305
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
468-663 2.10e-10

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: 63.49  E-value: 2.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 468 DHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLv 547
Cdd:cd05622  131 NSPWVVQLFYAFQDDRYLY-MVMEYMPGGDLVNLMSNYDV-PEKWARFYTAEVVLALDAIHSMG--FIHRDVKPDNMLL- 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 548 dgTACGEIKITDFGLSKIMDDDsygvdGMDLTSQGAGTYWYLPPECFVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFG 627
Cdd:cd05622  206 --DKSGHLKLADFGTCMKMNKE-----GMVRCDTAVGTPDYISPEVLKSQGGDGYYGRECDWWSVGVFLYEMLVGDTPFY 278
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 211971036 628 HNQ---SQQDILQENTILkatevQFPVKPVVSSEAKAFI 663
Cdd:cd05622  279 ADSlvgTYSKIMNHKNSL-----TFPDDNDISKEAKNLI 312
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
422-626 2.14e-10

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: 62.82  E-value: 2.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDT--DTFCT---VLEYCEGN 496
Cdd:cd07850   16 VCAAYDTVTGQNVAIK-----KLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVFTPQKslEEFQDvylVMELMDAN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 497 -------DLDfylkqHKLMSekearSIVMQIVNALRYLNEikPPIIHYDLKPGNIllVDGTACgEIKITDFGLSKIMDDD 569
Cdd:cd07850   91 lcqviqmDLD-----HERMS-----YLLYQMLCGIKHLHS--AGIIHRDLKPSNI--VVKSDC-TLKILDFGLARTAGTS 155
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 211971036 570 ----SYGVdgmdltsqgagTYWYLPPEcFVVG---KEppkisnKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd07850  156 fmmtPYVV-----------TRYYRAPE-VILGmgyKE------NVDIWSVGCIMGEMIRGTVLF 201
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
459-695 2.57e-10

Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. Titin, also called connectin, is a muscle-specific elastic protein and is the largest known protein to date. It contains multiple immunoglobulin (Ig)-like and fibronectin type III (FN3) domains, and a single kinase domain near the C-terminus. It spans half of the sarcomere, the repeating contractile unit of striated muscle, and performs mechanical and catalytic functions. Titin contributes to the passive force generated when muscle is stretched during relaxation. Its kinase domain phosphorylates and regulates the muscle protein telethonin, which is required for sarcomere formation in differentiating myocytes. In addition, titin binds many sarcomere proteins and acts as a molecular scaffold for filament formation during myofibrillogenesis. The Titin subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271006 [Multi-domain]  Cd Length: 277  Bit Score: 61.80  E-value: 2.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKL-MSEKEARSIVMQIVNALRYLNeiKPPIIHY 537
Cdd:cd14104   45 KEISILNIARHRNILRLHESFE-SHEELVMIFEFISGVDIFERITTARFeLNEREIVSYVRQVCEALEFLH--SKNIGHF 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLVdgTACGE-IKITDFGLSK-IMDDDSYGvdgMDLTSQGagtywYLPPECFvvgkEPPKISNKVDVWSVGVI 615
Cdd:cd14104  122 DIRPENIIYC--TRRGSyIKIIEFGQSRqLKPGDKFR---LQYTSAE-----FYAPEVH----QHESVSTATDMWSLGCL 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 616 FFQCLYGRKPFgHNQSQQDILQenTILKAtEVQFPVKPV--VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYLLPHMRRS 693
Cdd:cd14104  188 VYVLLSGINPF-EAETNQQTIE--NIRNA-EYAFDDEAFknISIEALDFVDRLLVKERKSRMTAQEALNHPWLKQGMETV 263

                 ..
gi 211971036 694 NS 695
Cdd:cd14104  264 SS 265
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
419-618 5.10e-10

Catalytic domain of Transforming Growth Factor beta Receptor-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 receptors for the TGFbeta family of secreted signaling molecules including TGFbeta, bone morphogenetic proteins (BMPs), activins, growth and differentiation factors (GDFs), and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. There are two types of TGFbeta receptors included in this subfamily, I and II, that play different roles in signaling. For signaling to occur, the ligand first binds to the high-affinity type II receptor, which is followed by the recruitment of the low-affinity type I receptor to the complex and its activation through trans-phosphorylation by the type II receptor. The active type I receptor kinase starts intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. Different ligands interact with various combinations of types I and II receptors to elicit a specific signaling pathway. Activins primarily signal through combinations of ACVR1b/ALK7 and ACVR2a/b; myostatin and GDF11 through TGFbR1/ALK4 and ACVR2a/b; BMPs through ACVR1/ALK1 and BMPR2; and TGFbeta through TGFbR1 and TGFbR2. The TGFbR-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: 270900 [Multi-domain]  Cd Length: 289  Bit Score: 61.30  E-value: 5.10e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfdLYEQRYAAVKIHQLN--KSWRDEKKEnyhkhacreYRIhKELDHPRIVKLYDYFSLDTDT---FCTVLEYC 493
Cdd:cd13998    8 FGEVWKA--SLKNEPVAVKIFSSRdkQSWFREKEI---------YRT-PMLKHENILQFIAADERDTALrteLWLVTAFH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 494 EGNDLDFYLKQHKLMSEKEARsIVMQIVNALRYLNE-------IKPPIIHYDLKPGNILLV-DGTACgeikITDFGLSkI 565
Cdd:cd13998   76 PNGSL*DYLSLHTIDWVSLCR-LALSVARGLAHLHSeipgctqGKPAIAHRDLKSKNILVKnDGTCC----IADFGLA-V 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 566 MDDDSYGVDGMDLTSQgAGTYWYLPPEcfvVGKEPPKISN-----KVDVWSVGVIFFQ 618
Cdd:cd13998  150 RLSPSTGEEDNANNGQ-VGTKRYMAPE---VLEGAINLRDfesfkRVDIYAMGLVLWE 203
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
460-640 5.66e-10

Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular carcinoma and Resting lymphocyte kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tec and Rlk (also named Txk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. Instead of PH, Rlk contains an N-terminal cysteine-rich region. In addition to PH, Tec also contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Tec kinases are expressed mainly by haematopoietic cells. Tec is more widely-expressed than other Tec-like subfamily kinases. It is found in endothelial cells, both B- and T-cells, and a variety of myeloid cells including mast cells, erythroid cells, platelets, macrophages and neutrophils. Rlk is expressed in T-cells and mast cell lines. Tec and Rlk are both key components of T-cell receptor (TCR) signaling. They are important in TCR-stimulated proliferation, IL-2 production and phopholipase C-gamma1 activation. The Tec/Rlk subfamily is part of a larger superfamily, that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270685 [Multi-domain]  Cd Length: 260  Bit Score: 60.65  E-value: 5.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHK-LMSEKEARSIVMQIVNALRYLNeiKPPIIHYD 538
Cdd:cd05114   49 EAKVMMKLTHPKLVQLYGVCTQQKPIY-IVTEFMENGCLLNYLRQRRgKLSRDMLLSMCQDVCEGMEYLE--RNNFIHRD 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLvdgTACGEIKITDFGLSKIMDDDSYgvdgmdLTSQGAG--TYWyLPPECFVVGkeppKISNKVDVWSVGVIF 616
Cdd:cd05114  126 LAARNCLV---NDTGVVKVSDFGMTRYVLDDQY------TSSSGAKfpVKW-SPPEVFNYS----KFSSKSDVWSFGVLM 191
                        170       180
                 ....*....|....*....|....*
gi 211971036 617 FQCLY-GRKPFgHNQSQQDILQENT 640
Cdd:cd05114  192 WEVFTeGKMPF-ESKSNYEVVEMVS 215
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
460-626 6.44e-10

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


Pssm-ID: 173631 [Multi-domain]  Cd Length: 290  Bit Score: 60.75  E-value: 6.44e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHK------------------------LMSEKEARS 515
Cdd:cd05045   53 EFNLLKQVNHPHVIKLYGACSQDGPLL-LIVEYAKYGSLRSFLRESRkvgpsylgsdgnrnssyldnpderALTMGDLIS 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 516 IVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACgeiKITDFGLSK-IMDDDSYGVdgmdlTSQGAGTYWYLPPECF 594
Cdd:cd05045  132 FAWQISRGMQYLAEMK--LVHRDLAARNVLVAEGRKM---KISDFGLSRdVYEEDSYVK-----RSKGRIPVKWMAIESL 201
                        170       180       190
                 ....*....|....*....|....*....|...
gi 211971036 595 VvgkePPKISNKVDVWSVGVIFFQCL-YGRKPF 626
Cdd:cd05045  202 F----DHIYTTQSDVWSFGVLLWEIVtLGGNPY 230
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
455-643 6.96e-10

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: 60.51  E-value: 6.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 455 KHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppI 534
Cdd:cd07846   45 KIAMREIKMLKQLRHENLVNLIEVFR-RKKRWYLVFEFVDHTVLDDLEKYPNGLDESRVRKYLFQILRGIDFCHSHN--I 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 535 IHYDLKPGNILLvdgTACGEIKITDFGLSKIMdddsyGVDGMDLTSQGAgTYWYLPPEcFVVGKepPKISNKVDVWSVGV 614
Cdd:cd07846  122 IHRDIKPENILV---SQSGVVKLCDFGFARTL-----AAPGEVYTDYVA-TRWYRAPE-LLVGD--TKYGKAVDVWAVGC 189
                        170       180
                 ....*....|....*....|....*....
gi 211971036 615 IFFQCLYGRKPFghnQSQQDILQENTILK 643
Cdd:cd07846  190 LVTEMLTGEPLF---PGDSDIDQLYHIIK 215
STKc_HIPK cd14211
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase; STKs ...
464-615 1.23e-09

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: 60.54  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 464 HKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFyLKQHKL--MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKP 541
Cdd:cd14211   54 QENADEFNFVRAYECFQ-HKNHTCLVFEMLEQNLYDF-LKQNKFspLPLKYIRPILQQVLTALLKLKSLG--LIHADLKP 129
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 211971036 542 GNILLVDGTACG-EIKITDFGLSKIMdddSYGVDGMDLTSQgagtyWYLPPEcFVVGKeppKISNKVDVWSVGVI 615
Cdd:cd14211  130 ENIMLVDPVRQPyRVKVIDFGSASHV---SKAVCSTYLQSR-----YYRAPE-IILGL---PFCEAIDMWSLGCV 192
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
419-633 1.46e-09

Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. CK2 is a tetrameric protein with two catalytic (alpha) and two regulatory (beta) subunits. It is constitutively active and ubiquitously expressed, and is found in the cytoplasm, nucleus, as well as in the plasma membrane. It phosphorylates a wide variety of substrates including gylcogen synthase, cell cycle proteins, nuclear proteins (e.g. DNA topoisomerase II), and ion channels (e.g. ENaC), among others. It may be considered a master kinase controlling the activity or lifespan of many other kinases and exerting its effect over cell fate, gene expression, protein synthesis and degradation, and viral infection. CK2 is implicated in every stage of the cell cycle and is required for cell cycle progression. It plays crucial roles in cell differentiation, proliferation, and survival, and is thus implicated in cancer. CK2 is not an oncogene by itself but elevated CK2 levels create an environment that enhances the survival of tumor cells. The CK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271034 [Multi-domain]  Cd Length: 306  Bit Score: 59.86  E-value: 1.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLnkswrdekKENYHKHACREYRIHKEL-DHPRIVKLYD-YFSLDTDTFCTVLEYCEGN 496
Cdd:cd14132   31 YSEVFEGINIGNNEKVVIKV--L--------KPVKKKKIKREIKILQNLrGGPNIVKLLDvVKDPQSKTPSLIFEYVNNT 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 497 DLD-FYLKqhklMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNIlLVDGTaCGEIKITDFGLSKI---MDDDSYG 572
Cdd:cd14132  101 DFKtLYPT----LTDYDIRYYMYELLKALDYCH--SKGIMHRDVKPHNI-MIDHE-KRKLRLIDWGLAEFyhpGQEYNVR 172
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211971036 573 VdgmdltsqgaGTYWYLPPECFVvgkEPPKISNKVDVWSVGVIFFQCLYGRKPF--GHNQSQQ 633
Cdd:cd14132  173 V----------ASRYYKGPELLV---DYQYYDYSLDMWSLGCMLASMIFRKEPFfhGHDNYDQ 222
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
486-674 1.62e-09

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: 59.26  E-value: 1.62e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 486 FCTVLEYCEGNDLdfylkqHKLMSEKEARSIVMQIVNALR-------YLNEIKppIIHYDLKPGNILLVDGTAcgeIKIT 558
Cdd:cd14150   70 FAIITQWCEGSSL------YRHLHVTETRFDTMQLIDVARqtaqgmdYLHAKN--IIHRDLKSNNIFLHEGLT---VKIG 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 559 DFGLSKIMDDDSygvdGMDLTSQGAGTYWYLPPECFVVgKEPPKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILqe 638
Cdd:cd14150  139 DFGLATVKTRWS----GSQQVEQPSGSILWMAPEVIRM-QDTNPYSFQSDVYAYGVVLYELMSGTLPYSNINNRDQII-- 211
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 211971036 639 ntILKATEVQFPVKPVVSSEAKAFIRR----CLAYRKEDR 674
Cdd:cd14150  212 --FMVGRGYLSPDLSKLSSNCPKAMKRllidCLKFKREER 249
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
419-716 1.64e-09

Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EGFR (HER1, ErbB1) is a receptor PTK (RTK) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands for EGFR include EGF, heparin binding EGF-like growth factor (HBEGF), epiregulin, amphiregulin, TGFalpha, and betacellulin. Upon ligand binding, EGFR can form homo- or heterodimers with other EGFR subfamily members. The EGFR signaling pathway is one of the most important pathways regulating cell proliferation, differentiation, survival, and growth. Overexpression and mutation in the kinase domain of EGFR have been implicated in the development and progression of a variety of cancers. A number of monoclonal antibodies and small molecule inhibitors have been developed that target EGFR, including the antibodies Cetuximab and Panitumumab, which are used in combination with other therapies for the treatment of colorectal cancer and non-small cell lung carcinoma (NSCLC). The small molecule inhibitors Gefitinib (Iressa) and Erlotinib (Tarceva), already used for NSCLC, are undergoing clinical trials for other types of cancer including gastrointestinal, breast, head and neck, and bladder. The EGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270683 [Multi-domain]  Cd Length: 313  Bit Score: 60.04  E-value: 1.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfdLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFCTVLeYCEGNDL 498
Cdd:cd05108   20 FGTVYKG--LWIPEGEKVKIPVAIKELREATSPKANKEILDEAYVMASVDNPHVCRLLGICLTSTVQLITQL-MPFGCLL 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DfYLKQHK-LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacgEIKITDFGLSKIM--DDDSYGVDG 575
Cdd:cd05108   97 D-YVREHKdNIGSQYLLNWCVQIAKGMNYLEDRR--LVHRDLAARNVLVKTPQ---HVKITDFGLAKLLgaEEKEYHAEG 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 -------MDLTSQGAGTYwylppecfvvgkeppkiSNKVDVWSVGVIFFQCL-YGRKPFGHNQSQQDilqeNTILKATEv 647
Cdd:cd05108  171 gkvpikwMALESILHRIY-----------------THQSDVWSYGVTVWELMtFGSKPYDGIPASEI----SSILEKGE- 228
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 648 QFPVKPVVSSEAKAFIRRCLAYRKEDR-------FDVHQLANDP--YLLPHmrrsnssGNLHMagltASPTPPSSSII 716
Cdd:cd05108  229 RLPQPPICTIDVYMIMVKCWMIDADSRpkfreliIEFSKMARDPqrYLVIQ-------GDERM----HLPSPTDSNFY 295
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
465-620 1.82e-09

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 60.27  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 465 KELDHPRIVKLYDYFSLDTDTfCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNI 544
Cdd:PHA03209 112 QNVNHPSVIRMKDTLVSGAIT-CMVLPHYSSDLYTYLTKRSRPLPIDQALIIEKQILEGLRYLHAQR--IIHRDVKTENI 188
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 545 LLVD-GTACgeikITDFGLSK--IMDDDSYGVdgmdltsqgAGTYWYLPPEcfVVGKEppKISNKVDVWSVGVIFFQCL 620
Cdd:PHA03209 189 FINDvDQVC----IGDLGAAQfpVVAPAFLGL---------AGTVETNAPE--VLARD--KYNSKADIWSAGIVLFEML 250
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
486-680 1.89e-09

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: 58.94  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 486 FCTVLEYCEGNDLdfYLKQHKLMSEKEARSIV---MQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGL 562
Cdd:cd14062   63 LAIVTQWCEGSSL--YKHLHVLETKFEMLQLIdiaRQTAQGMDYLHAKN--IIHRDLKSNNIFLHEDLT---VKIGDFGL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 563 SKIMDDDSygvdGMDLTSQGAGTYWYLPPECFVVGKEPPkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILqentil 642
Cdd:cd14062  136 ATVKTRWS----GSQQFEQPTGSILWMAPEVIRMQDENP-YSFQSDVYAFGIVLYELLTGQLPYSHINNRDQIL------ 204
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 211971036 643 katevqFPV-----KPVVS-------SEAKAFIRRCLAYRKEDRFDVHQL 680
Cdd:cd14062  205 ------FMVgrgylRPDLSkvrsdtpKALRRLMEDCIKFQRDERPLFPQI 248
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
459-626 1.89e-09

Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Abl (or c-Abl) is a ubiquitously-expressed cytoplasmic (or nonreceptor) PTK that contains SH3, SH2, and tyr kinase domains in its N-terminal region, as well as nuclear localization motifs, a putative DNA-binding domain, and F- and G-actin binding domains in its C-terminal tail. It also contains a short autoinhibitory cap region in its N-terminus. Abl function depends on its subcellular localization. In the cytoplasm, Abl plays a role in cell proliferation and survival. In response to DNA damage or oxidative stress, Abl is transported to the nucleus where it induces apoptosis. In chronic myelogenous leukemia (CML) patients, an aberrant translocation results in the replacement of the first exon of Abl with the BCR (breakpoint cluster region) gene. The resulting BCR-Abl fusion protein is constitutively active and associates into tetramers, resulting in a hyperactive kinase sending a continuous signal. This leads to uncontrolled proliferation, morphological transformation and anti-apoptotic effects. BCR-Abl is the target of selective inhibitors, such as imatinib (Gleevec), used in the treatment of CML. Abl2, also known as ARG (Abelson-related gene), is thought to play a cooperative role with Abl in the proper development of the nervous system. The Tel-ARG fusion protein, resulting from reciprocal translocation between chromosomes 1 and 12, is associated with acute myeloid leukemia (AML). The TEL gene is a frequent fusion partner of other tyr kinase oncogenes, including Tel/Abl, Tel/PDGFRbeta, and Tel/Jak2, found in patients with leukemia and myeloproliferative disorders. The Abl subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270645 [Multi-domain]  Cd Length: 263  Bit Score: 58.97  E-value: 1.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLDTdTFCTVLEY-CEGNDLDfYLKQHklmSEKEARSIVM-----QIVNALRYLNeiKP 532
Cdd:cd05052   51 KEAAVMKEIKHPNLVQLLGVCTREP-PFYIITEFmPYGNLLD-YLREC---NREELNAVVLlymatQIASAMEYLE--KK 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 533 PIIHYDLKPGNILLVDgtaCGEIKITDFGLSKIMDDDSYgvdgmdlTSQGAGTY---WYLPPecfvvGKEPPKISNKVDV 609
Cdd:cd05052  124 NFIHRDLAARNCLVGE---NHLVKVADFGLSRLMTGDTY-------TAHAGAKFpikWTAPE-----SLAYNKFSIKSDV 188
                        170
                 ....*....|....*...
gi 211971036 610 WSVGVIFFQ-CLYGRKPF 626
Cdd:cd05052  189 WAFGVLLWEiATYGMSPY 206
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
489-684 2.25e-09

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 60.27  E-value: 2.25e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 489 VLEYCEGNDLDFYLKQH----KLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSK 564
Cdd:PTZ00283 117 VLDYANAGDLRQEIKSRaktnRTFREHEAGLLFIQVLLAVHHVHSKH--MIHRDIKSANILLCSN---GLVKLGDFGFSK 191
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 565 IMdddSYGVDGmDLTSQGAGTYWYLPPEcfvVGKEPPkISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQentilKA 644
Cdd:PTZ00283 192 MY---AATVSD-DVGRTFCGTPYYVAPE---IWRRKP-YSKKADMFSLGVLLYELLTLKRPF-DGENMEEVMH-----KT 257
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 211971036 645 TEVQF-PVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLANDP 684
Cdd:PTZ00283 258 LAGRYdPLPPSISPEMQEIVTALLSSDPKRRPSSSKLLNMP 298
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
459-626 2.77e-09

Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Frk and Srk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Frk, also known as Rak, is specifically expressed in liver, lung, kidney, intestine, mammary glands, and the islets of Langerhans. Rodent homologs were previously referred to as GTK (gastrointestinal tyr kinase), BSK (beta-cell Src-like kinase), or IYK (intestinal tyr kinase). Studies in mice reveal that Frk is not essential for viability. It plays a role in the signaling that leads to cytokine-induced beta-cell death in Type I diabetes. It also regulates beta-cell number during embryogenesis and early in life. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Frk-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270653 [Multi-domain]  Cd Length: 267  Bit Score: 58.57  E-value: 2.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLD------TDTFC--TVLEYCEGNDLDFYLKQHKLMSEkearsivmQIVNALRYLNEI 530
Cdd:cd05068   52 REAQIMKKLRHPKLIQLYAVCTLEepiyiiTELMKhgSLLEYLQGKGRSLQLPQLIDMAA--------QVASGMAYLESQ 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 531 KppIIHYDLKPGNILLVDGTACgeiKITDFGLSK-IMDDDSY-GVDGMDL----TSQGAGTYwylppecfvvgkepPKIS 604
Cdd:cd05068  124 N--YIHRDLAARNVLVGENNIC---KVADFGLARvIKVEDEYeAREGAKFpikwTAPEAANY--------------NRFS 184
                        170       180
                 ....*....|....*....|...
gi 211971036 605 NKVDVWSVGVIFFQCL-YGRKPF 626
Cdd:cd05068  185 IKSDVWSFGILLTEIVtYGRIPY 207
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
443-662 3.79e-09

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: 58.47  E-value: 3.79e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRD-EKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIV 521
Cdd:cd07848   32 KKFKDsEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLY-LVFEYVEKNMLELLEEMPNGVPPEKVRSYIYQLI 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 522 NALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMdddSYGVDGMdlTSQGAGTYWYLPPEcFVVGKEPP 601
Cdd:cd07848  111 KAIHWCH--KNDIVHRDIKPENLLI---SHNDVLKLCDFGFARNL---SEGSNAN--YTEYVATRWYRSPE-LLLGAPYG 179
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 602 KisnKVDVWSVGVIFFQCLYGRKPFghnQSQQDILQENTILKAtevqfpVKPVVSSEAKAF 662
Cdd:cd07848  180 K---AVDMWSVGCILGELSDGQPLF---PGESEIDQLFTIQKV------LGPLPAEQMKLF 228
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
432-686 3.84e-09

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: 58.50  E-value: 3.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 432 RYAAVKIHQLNKSWRDEKKENyhkhacrEYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDLDfYLKQHKLMSEK 511
Cdd:cd06657   46 KLVAVKKMDLRKQQRRELLFN-------EVVIMRDYQHENVVEMYNSY-LVGDELWVVMEFLEGGALT-DIVTHTRMNEE 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 512 EARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDsygvdgMDLTSQGAGTYWYLPP 591
Cdd:cd06657  117 QIAAVCLAVLKALSVLH--AQGVIHRDIKSDSILL---THDGRVKLSDFGFCAQVSKE------VPRRKSLVGTPYWMAP 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 592 EcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPFGHNQ--SQQDILQENTILKATEVQfpvkpVVSSEAKAFIRRCLAY 669
Cdd:cd06657  186 E--LISRLP--YGPEVDIWSLGIMVIEMVDGEPPYFNEPplKAMKMIRDNLPPKLKNLH-----KVSPSLKGFLDRLLVR 256
                        250
                 ....*....|....*..
gi 211971036 670 RKEDRFDVHQLANDPYL 686
Cdd:cd06657  257 DPAQRATAAELLKHPFL 273
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
459-626 3.87e-09

Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Yes (or c-Yes) is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. c-Yes kinase is the cellular homolog of the oncogenic protein (v-Yes) encoded by the Yamaguchi 73 and Esh sarcoma viruses. It displays functional overlap with other Src subfamily members, particularly Src. It also shows some unique functions such as binding to occludins, transmembrane proteins that regulate extracellular interactions in tight junctions. Yes also associates with a number of proteins in different cell types that Src does not interact with, like JAK2 and gp130 in pre-adipocytes, and Pyk2 in treated pulmonary vein endothelial cells. Although the biological function of Yes remains unclear, it appears to have a role in regulating cell-cell interactions and vesicle trafficking in polarized cells. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Yes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270654 [Multi-domain]  Cd Length: 279  Bit Score: 58.54  E-value: 3.87e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSldTDTFCTVLEYC-EGNDLDFyLKQH--KLMSEKEARSIVMQIVNALRYLNEIKppII 535
Cdd:cd05069   56 QEAQIMKKLRHDKLVPLYAVVS--EEPIYIVTEFMgKGSLLDF-LKEGdgKYLKLPQLVDMAAQIADGMAYIERMN--YI 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 536 HYDLKPGNILLVDGTACgeiKITDFGLSKIMDDDSYgvdgmdLTSQGAG-TYWYLPPECFVVGkeppKISNKVDVWSVGV 614
Cdd:cd05069  131 HRDLRAANILVGDNLVC---KIADFGLARLIEDNEY------TARQGAKfPIKWTAPEAALYG----RFTIKSDVWSFGI 197
                        170
                 ....*....|...
gi 211971036 615 IFFQCLY-GRKPF 626
Cdd:cd05069  198 LLTELVTkGRVPY 210
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
419-686 4.22e-09

Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TNIK is an effector of Rap2, a small GTP-binding protein from the Ras family. TNIK specifically activates the c-Jun N-terminal kinase (JNK) pathway and plays a role in regulating the actin cytoskeleton. The TNIK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270807 [Multi-domain]  Cd Length: 296  Bit Score: 58.58  E-value: 4.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKEnyhkhacrEYRIHKELDHPR-IVKLYDYF------SLDtDTFCTVLE 491
Cdd:cd06637   19 YGQVYKGRHVKTGQLAAIKVMDVTGDEEEEIKQ--------EINMLKKYSHHRnIATYYGAFikknppGMD-DQLWLVME 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 492 YCEGNDLDFYLKQHK--LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDD 569
Cdd:cd06637   90 FCGAGSVTDLIKNTKgnTLKEEWIAYICREILRGLSHLHQHK--VIHRDIKGQNVLLTEN---AEVKLVDFGVSAQLDRT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 570 sygvdgMDLTSQGAGTYWYLPPECFVVGKEPPKISN-KVDVWSVGVIFFQCLYGRKPFG--HNQSQQDILQENTILKATE 646
Cdd:cd06637  165 ------VGRRNTFIGTPYWMAPEVIACDENPDATYDfKSDLWSLGITAIEMAEGAPPLCdmHPMRALFLIPRNPAPRLKS 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 211971036 647 VQFpvkpvvSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06637  239 KKW------SKKFQSFIESCLVKNHSQRPSTEQLMKHPFI 272
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
419-626 4.32e-09

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: 58.14  E-value: 4.32e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnkswrdEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGNDL 498
Cdd:cd06642   17 FGEVYKGIDNRTKEVVAIKIIDL------EEAEDEIEDIQQEITVLSQCDSPYITRYYGSY-LKGTKLWIIMEYLGGGSA 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKPpiIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSYGVDGMdl 578
Cdd:cd06642   90 LDLLKPGPL-EETYIATILREILKGLDYLHSERK--IHRDIKAANVLLSEQ---GDVKLADFGVAGQLTDTQIKRNTF-- 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 211971036 579 tsqgAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd06642  162 ----VGTPFWMAPEVI----KQSAYDFKADIWSLGITAIELAKGEPPN 201
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
460-626 4.74e-09

Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fyn and Yrk are members of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Fyn, together with Lck, plays a critical role in T-cell signal transduction by phosphorylating ITAM (immunoreceptor tyr activation motif) sequences on T-cell receptors, ultimately leading to the proliferation and differentiation of T-cells. In addition, Fyn is involved in the myelination of neurons, and is implicated in Alzheimer's and Parkinson's diseases. Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Fyn/Yrk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase.


Pssm-ID: 270655 [Multi-domain]  Cd Length: 274  Bit Score: 58.16  E-value: 4.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSldTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVM--QIVNALRYLNEIKppIIHY 537
Cdd:cd05070   54 EAQIMKKLKHDKLVQLYAVVS--EEPIYIVTEYMSKGSLLDFLKDGEGRALKLPNLVDMaaQVAAGMAYIERMN--YIHR 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLVDGTACgeiKITDFGLSKIMDDDSYgvdgmdLTSQGAG-TYWYLPPECFVVGkeppKISNKVDVWSVGVIF 616
Cdd:cd05070  130 DLRSANILVGNGLIC---KIADFGLARLIEDNEY------TARQGAKfPIKWTAPEAALYG----RFTIKSDVWSFGILL 196
                        170
                 ....*....|.
gi 211971036 617 FQCLY-GRKPF 626
Cdd:cd05070  197 TELVTkGRVPY 207
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
435-665 4.82e-09

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: 58.92  E-value: 4.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIhqLNKSWRDEKKENYHKHACREyrIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEAR 514
Cdd:cd05627   31 AMKI--LRKADMLEKEQVAHIRAERD--ILVEADGAWVVKMFYSFQ-DKRNLYLIMEFLPGGDMMTLLMKKDTLSEEATQ 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 515 SIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDD-------------------------- 568
Cdd:cd05627  106 FYIAETVLAIDAIHQLG--FIHRDIKPDNLLL---DAKGHVKLSDFGLCTGLKKahrtefyrnlthnppsdfsfqnmnsk 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 569 ---DSYGVDGMDLTSQGAGTYWYLPPECFVVGKeppkiSNKV-DVWSVGVIFFQCLYGRKPFGhNQSQQDILQENTILKA 644
Cdd:cd05627  181 rkaETWKKNRRQLAYSTVGTPDYIAPEVFMQTG-----YNKLcDWWSLGVIMYEMLIGYPPFC-SETPQETYRKVMNWKE 254
                        250       260
                 ....*....|....*....|.
gi 211971036 645 TEVqFPVKPVVSSEAKAFIRR 665
Cdd:cd05627  255 TLV-FPPEVPISEKAKDLILR 274
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
446-675 5.88e-09

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: 58.52  E-value: 5.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 446 RDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALR 525
Cdd:cd05625   37 KDVLLRNQVAHVKAERDILAEADNEWVVRLYYSFQ-DKDNLYFVMDYIPGGDMMSLLIRMGVFPEDLARFYIAELTCAVE 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 526 YLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLS---KIMDDDSY-------GVDGMDLTSQGA------------ 583
Cdd:cd05625  116 SVHKMG--FIHRDIKPDNILI---DRDGHIKLTDFGLCtgfRWTHDSKYyqsgdhlRQDSMDFSNEWGdpencrcgdrlk 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 584 -------------------GTYWYLPPECFVvgkePPKISNKVDVWSVGVIFFQCLYGRKPFghnQSQQDILQENTILK- 643
Cdd:cd05625  191 plerraarqhqrclahslvGTPNYIAPEVLL----RTGYTQLCDWWSVGVILFEMLVGQPPF---LAQTPLETQMKVINw 263
                        250       260       270
                 ....*....|....*....|....*....|..
gi 211971036 644 ATEVQFPVKPVVSSEAKAFIRRcLAYRKEDRF 675
Cdd:cd05625  264 QTSLHIPPQAKLSPEASDLIIK-LCRGPEDRL 294
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
425-640 5.98e-09

Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR2 is a receptor PTK (RTK) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDR2 results in a slow but sustained receptor activation. DDR2 binds mostly to fibrillar collagens as well as collagen X. DDR2 is widely expressed in many tissues with the highest levels found in skeletal muscle, skin, kidney and lung. It is important in cell proliferation and development. Mice, with a deletion of DDR2, suffer from dwarfism and delayed healing of epidermal wounds. DDR2 also contributes to collagen (type I) regulation by inhibiting fibrillogenesis and altering the morphology of collagen fibers. It is also expressed in immature dendritic cells (DCs), where it plays a role in DC activation and function. The DDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase (PI3K).


Pssm-ID: 270677 [Multi-domain]  Cd Length: 297  Bit Score: 58.08  E-value: 5.98e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 425 AFDLYEQRYAAVKIHQLnkswRDEKKENYHKHACREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDLDFYLKQ 504
Cdd:cd05095   38 ALEVSENQPVLVAVKML----RADANKNARNDFLKEIKIMSRLKDPNIIRLLA-VCITDDPLCMITEYMENGDLNQFLSR 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 505 HK------------LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSK-IMDDDSY 571
Cdd:cd05095  113 QQpegqlalpsnalTVSYSDLRFMAAQIASGMKYLSSLN--FVHRDLATRNCLVGKNYT---IKIADFGMSRnLYSGDYY 187
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 572 GVDGmdltsQGAGTYWYLPPECFVVGkeppKISNKVDVWSVGVIFFQCLY--GRKPFGHNQSQQDIlqENT 640
Cdd:cd05095  188 RIQG-----RAVLPIRWMSWESILLG----KFTTASDVWAFGVTLWETLTfcREQPYSQLSDEQVI--ENT 247
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
443-640 6.64e-09

Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. DDR-like proteins are members of the DDR subfamily, which are receptor PTKs (RTKs) containing an extracellular discoidin homology domain, a transmembrane segment, an extended juxtamembrane region, and an intracellular catalytic domain. The binding of the ligand, collagen, to DDRs results in a slow but sustained receptor activation. DDRs regulate cell adhesion, proliferation, and extracellular matrix remodeling. They have been linked to a variety of human cancers including breast, colon, ovarian, brain, and lung. There is no evidence showing that DDRs act as transforming oncogenes. They are more likely to play a role in the regulation of tumor growth and metastasis. The DDR-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133228 [Multi-domain]  Cd Length: 295  Bit Score: 57.68  E-value: 6.64e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSE-KEARSI----- 516
Cdd:cd05097   50 KMLRADVTKTARNDFLKEIKIMSRLKNPNIIRLLG-VCVSDDPLCMITEYMENGDLNQFLSQREIESTfTHANNIpsvsi 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 517 ------VMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSK-IMDDDSYGVDGmdltsQGAGTYWYL 589
Cdd:cd05097  129 anllymAVQIASGMKYLASLN--FVHRDLATRNCLVGNHYT---IKIADFGMSRnLYSGDYYRIQG-----RAVLPIRWM 198
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 211971036 590 PPECFVVGkeppKISNKVDVWSVGVIFFQ--CLYGRKPFGHNQSQQDIlqENT 640
Cdd:cd05097  199 AWESILLG----KFTTASDVWAFGVTLWEmfTLCKEQPYSLLSDEQVI--ENT 245
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
459-626 8.03e-09

Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Src (or c-Src) is a cytoplasmic (or non-receptor) PTK, containing an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region with a conserved tyr. It is activated by autophosphorylation at the tyr kinase domain, and is negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). c-Src is the vertebrate homolog of the oncogenic protein (v-Src) from Rous sarcoma virus. Together with other Src subfamily proteins, it is involved in signaling pathways that regulate cytokine and growth factor responses, cytoskeleton dynamics, cell proliferation, survival, and differentiation. Src also play a role in regulating cell adhesion, invasion, and motility in cancer cells and tumor vasculature, contributing to cancer progression and metastasis. Elevated levels of Src kinase activity have been reported in a variety of human cancers. Several inhibitors of Src have been developed as anti-cancer drugs. Src is also implicated in acute inflammatory responses and osteoclast function. The Src subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270656 [Multi-domain]  Cd Length: 277  Bit Score: 57.39  E-value: 8.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSldTDTFCTVLEYC-EGNDLDFYLKQH-KLMSEKEARSIVMQIVNALRYLNEIKppIIH 536
Cdd:cd05071   53 QEAQVMKKLRHEKLVQLYAVVS--EEPIYIVTEYMsKGSLLDFLKGEMgKYLRLPQLVDMAAQIASGMAYVERMN--YVH 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 537 YDLKPGNILLVDGTACgeiKITDFGLSKIMDDDSYgvdgmdLTSQGAG-TYWYLPPECFVVGkeppKISNKVDVWSVGVI 615
Cdd:cd05071  129 RDLRAANILVGENLVC---KVADFGLARLIEDNEY------TARQGAKfPIKWTAPEAALYG----RFTIKSDVWSFGIL 195
                        170
                 ....*....|..
gi 211971036 616 FFQ-CLYGRKPF 626
Cdd:cd05071  196 LTElTTKGRVPY 207
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
419-614 8.22e-09

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: 56.93  E-value: 8.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKEL-DHPRIVKLYDYFSlDTDTFCTVLEYCEGNd 497
Cdd:cd14050   14 FGEVFKVRSREDGKLYAVK-----RSRSRFRGEKDRKRKLEEVERHEKLgEHPNCVRFIKAWE-EKGILYIQTELCDTS- 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACgeiKITDFGLskIMDddsygVDGMD 577
Cdd:cd14050   87 LQQYCEETHSLPESEVWNILLDLLKGLKHLHDHG--LIHLDIKPANIFLSKDGVC---KLGDFGL--VVE-----LDKED 154
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 211971036 578 LTSQGAGTYWYLPPEcFVVGkeppKISNKVDVWSVGV 614
Cdd:cd14050  155 IHDAQEGDPRYMAPE-LLQG----SFTKAADIFSLGI 186
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
443-679 8.85e-09

Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Fes (or Fps) is a cytoplasmic (or nonreceptor) PTK containing an N-terminal region with FCH (Fes/Fer/CIP4 homology) and coiled-coil domains, followed by a SH2 domain, and a C-terminal catalytic domain. The genes for Fes (feline sarcoma) and Fps (Fujinami poultry sarcoma) were first isolated from tumor-causing retroviruses. The viral oncogenes encode chimeric Fes proteins consisting of Gag sequences at the N-termini, resulting in unregulated PTK activity. Fes kinase is expressed in myeloid, vascular endothelial, epithelial, and neuronal cells. It plays important roles in cell growth and differentiation, angiogenesis, inflammation and immunity, and cytoskeletal regulation. A recent study implicates Fes kinase as a tumor suppressor in colorectal cancer. The Fes subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270667 [Multi-domain]  Cd Length: 252  Bit Score: 56.86  E-value: 8.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 443 KSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQ--HKLMSeKEARSIVMQI 520
Cdd:cd05084   27 KSCRETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIY-IVMELVQGGDFLTFLRTegPRLKV-KELIRMVENA 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 521 VNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSKIMDDDSYGVDGmdlTSQGAGTYWyLPPECFVVGkep 600
Cdd:cd05084  105 AAGMEYLESKH--CIHRDLAARNCLVTEKNV---LKISDFGMSREEEDGVYAATG---GMKQIPVKW-TAPEALNYG--- 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 601 pKISNKVDVWSVGVIFFQCL-YGRKPFGH--NQSQQDILQENtilkateVQFPVKPVVSSEAKAFIRRCLAY--RKEDRF 675
Cdd:cd05084  173 -RYSSESDVWSFGILLWETFsLGAVPYANlsNQQTREAVEQG-------VRLPCPENCPDEVYRLMEQCWEYdpRKRPSF 244

                 ....*
gi 211971036 676 D-VHQ 679
Cdd:cd05084  245 StVHQ 249
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
459-674 9.16e-09

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak3 is expressed only in hematopoietic cells. It binds the shared receptor subunit common gamma chain and thus, is essential in the signaling of cytokines that use it such as IL-2, IL-4, IL-7, IL-9, IL-15, and IL-21. Jak3 is important in lymphoid development and myeloid cell differentiation. Inactivating mutations in Jak3 have been reported in humans with severe combined immunodeficiency (SCID). Jak3 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270665 [Multi-domain]  Cd Length: 283  Bit Score: 57.21  E-value: 9.16e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDY-FSLDTDTFCTVLEYCEGNDLDFYLKQHKlmSEKEARSIVM---QIVNALRYLNEIKppI 534
Cdd:cd05081   54 REIQILKALHSDFIVKYRGVsYGPGRRSLRLVMEYLPSGCLRDFLQRHR--ARLDASRLLLyssQICKGMEYLGSRR--C 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 535 IHYDLKPGNILLVDGTacgEIKITDFGLSKIM--DDDSYGVDgmdlTSQGAGTYWYLPPECfvvgkEPPKISNKVDVWSV 612
Cdd:cd05081  130 VHRDLAARNILVESEA---HVKIADFGLAKLLplDKDYYVVR----EPGQSPIFWYAPESL-----SDNIFSRQSDVWSF 197
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211971036 613 GVIFFQ----CLYGRKP-------FGHNQSQQDILQENTILKATEvQFPVKPVVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd05081  198 GVVLYElftyCDKSCSPsaeflrmMGCERDVPALCRLLELLEEGQ-RLPAPPACPAEVHELMKLCWAPSPQDR 269
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
419-592 9.65e-09

Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR2 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors, such as TGFbR2, are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. TGFbR2 acts as the receptor for TGFbeta, which is crucial in growth control and homeostasis in many different tissues. It plays roles in regulating apoptosis and in maintaining the balance between self renewal and cell loss. It also plays a key role in maintaining vascular integrity and in regulating responses to genotoxic stress. Mutations in TGFbR2 can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. The TGFbR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270957 [Multi-domain]  Cd Length: 295  Bit Score: 57.39  E-value: 9.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKA---FDLYEQ-RYAAVKIHQLN--KSWRDEKkENYHKHACReyrihkeldHPRIVKLY---DYFSLDTDTFCTV 489
Cdd:cd14055    8 FAEVWKAklkQNASGQyETVAVKIFPYEeyASWKNEK-DIFTDASLK---------HENILQFLtaeERGVGLDRQYWLI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 490 LEYCEGNDLDFYLKQHkLMSEKEARSIVMQIVNALRYLNE-------IKPPIIHYDLKPGNILL-VDGTACgeikITDFG 561
Cdd:cd14055   78 TAYHENGSLQDYLTRH-ILSWEDLCKMAGSLARGLAHLHSdrtpcgrPKIPIAHRDLKSSNILVkNDGTCV----LADFG 152
                        170       180       190
                 ....*....|....*....|....*....|..
gi 211971036 562 LSkIMDDDSYGVDgmDLTSQG-AGTYWYLPPE 592
Cdd:cd14055  153 LA-LRLDPSLSVD--ELANSGqVGTARYMAPE 181
STKc_HIPK3 cd14229
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 3; ...
468-622 9.71e-09

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: 57.73  E-value: 9.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 468 DHPRIVKLYDYFSLDTDTfCTVLEYCEGNDLDFyLKQHKL--MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNIL 545
Cdd:cd14229   59 DEFNFVRAYECFQHRNHT-CLVFEMLEQNLYDF-LKQNKFspLPLKVIRPILQQVATALKKLKSLG--LIHADLKPENIM 134
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 546 LVDGTACG-EIKITDFGLSKIMdddSYGVDGMDLTSQgagtyWYLPPEcFVVGKeppKISNKVDVWSVGVIFFQCLYG 622
Cdd:cd14229  135 LVDPVRQPyRVKVIDFGSASHV---SKTVCSTYLQSR-----YYRAPE-IILGL---PFCEAIDMWSLGCVIAELFLG 200
PTKc_Ror2 cd05091
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
419-637 1.06e-08

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror2 plays important roles in skeletal and heart formation. Ror2-deficient mice show widespread bone abnormalities, ventricular defects in the heart, and respiratory dysfunction. Mutations in human Ror2 result in two different bone development genetic disorders, recessive Robinow syndrome and brachydactyly type B. Ror2 is also implicated in neural development. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270673 [Multi-domain]  Cd Length: 284  Bit Score: 56.95  E-value: 1.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfDLYE----QRYAAVKIHQLNKSWRDEKKENYhKHacrEYRIHKELDHPRIVKLYDYFSLDtDTFCTVLEYCE 494
Cdd:cd05091   19 FGKVYKG-HLFGtapgEQTQAVAIKTLKDKAEGPLREEF-RH---EAMLRSRLQHPNIVCLLGVVTKE-QPMSMIFSYCS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 GNDLDFYLKQHKLMSE-------KEARS---------IVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacgEIKIT 558
Cdd:cd05091   93 HGDLHEFLVMRSPHSDvgstdddKTVKStlepadflhIVTQIAAGMEYLSSHH--VVHKDLATRNVLVFDKL---NVKIS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 559 DFGLSKimddDSYGVDGMDLTSQGAGTYWYLPPECFVVGKeppkISNKVDVWSVGVIFFQCL-YGRKPF-GHnqSQQDIL 636
Cdd:cd05091  168 DLGLFR----EVYAADYYKLMGNSLLPIRWMSPEAIMYGK----FSIDSDIWSYGVVLWEVFsYGLQPYcGY--SNQDVI 237

                 .
gi 211971036 637 Q 637
Cdd:cd05091  238 E 238
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
448-626 1.27e-08

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkB is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkB to its ligands, brain-derived neurotrophic factor (BDNF) or neurotrophin 4 (NT4), results in receptor oligomerization and activation of the catalytic domain. TrkB is broadly expressed in the nervous system and in some non-neural tissues. It plays important roles in cell proliferation, differentiation, and survival. BDNF/Trk signaling plays a key role in regulating activity-dependent synaptic plasticity. TrkB also contributes to protection against gp120-induced neuronal cell death. TrkB overexpression is associated with poor prognosis in neuroblastoma (NB) and other human cancers. It acts as a suppressor of anoikis (detachment-induced apoptosis) and contributes to tumor metastasis. The TrkB subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270675 [Multi-domain]  Cd Length: 288  Bit Score: 56.97  E-value: 1.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 448 EKKENYHKHACREYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDLDFYLKQHK----LMSE---------KEAR 514
Cdd:cd05093   45 DASDNARKDFHREAELLTNLQHEHIVKFYG-VCVEGDPLIMVFEYMKHGDLNKFLRAHGpdavLMAEgnrpaeltqSQML 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 515 SIVMQIVNALRYLneIKPPIIHYDLKPGNILLVDGTAcgeIKITDFGLSKimddDSYGVDGMDLTSQGAGTYWYLPPECF 594
Cdd:cd05093  124 HIAQQIAAGMVYL--ASQHFVHRDLATRNCLVGENLL---VKIGDFGMSR----DVYSTDYYRVGGHTMLPIRWMPPESI 194
                        170       180       190
                 ....*....|....*....|....*....|...
gi 211971036 595 VVgkepPKISNKVDVWSVGVIFFQCL-YGRKPF 626
Cdd:cd05093  195 MY----RKFTTESDVWSLGVVLWEIFtYGKQPW 223
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
419-626 1.61e-08

Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NIK, also called mitogen activated protein kinase kinase kinase 14 (MAP3K14), phosphorylates and activates Inhibitor of NF-KappaB Kinase (IKK) alpha, which is a regulator of NF-kB proteins, a family of transcription factors which are critical in many cellular functions including inflammatory responses, immune development, cell survival, and cell proliferation, among others. NIK is essential in the IKKalpha-mediated non-canonical NF-kB signaling pathway, in which IKKalpha processes the IkB-like C-terminus of NF-kB2/p100 to produce p52, allowing the p52/RelB dimer to migrate to the nucleus where it regulates gene transcription. NIK also plays an important role in Toll-like receptor 7/9 signaling cascades. The NIK subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270893 [Multi-domain]  Cd Length: 268  Bit Score: 56.37  E-value: 1.61e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnKSWRDEkkenyhkhacrEYRIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDL 498
Cdd:cd13991   19 FGEVHRMEDKQTGFQCAVKKVRL-EVFRAE-----------ELMACAGLTSPRVVPLYGAVR-EGPWVNIFMDLKEGGSL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtaCGEIKITDFGLSKIMDDDSYgvdGMDL 578
Cdd:cd13991   86 GQLIKEQGCLPEDRALHYLGQALEGLEYLHSRK--ILHGDVKADNVLLSSD--GSDAFLCDFGHAECLDPDGL---GKSL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 211971036 579 TSQG--AGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd13991  159 FTGDyiPGTETHMAPE--VVLGKP--CDAKVDVWSSCCMMLHMLNGCHPW 204
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
419-625 1.80e-08

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: 56.21  E-value: 1.80e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnkswrdEKKENYHKHACREYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYCEGND- 497
Cdd:cd06640   17 FGEVFKGIDNRTQQVVAIKIIDL------EEAEDEIEDIQQEITVLSQCDSPYVTKYYGSY-LKGTKLWIIMEYLGGGSa 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDfyLKQHKLMSEKEARSIVMQIVNALRYLNEIKPpiIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSYGVDGMd 577
Cdd:cd06640   90 LD--LLRAGPFDEFQIATMLKEILKGLDYLHSEKK--IHRDIKAANVLLSEQ---GDVKLADFGVAGQLTDTQIKRNTF- 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 211971036 578 ltsqgAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLYGRKP 625
Cdd:cd06640  162 -----VGTPFWMAPEVI----QQSAYDSKADIWSLGITAIELAKGEPP 200
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
419-653 2.32e-08

Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. EphA10, which contains an inactive tyr kinase domain, may function to attenuate signals of co-clustered active receptors. EphA10 is mainly expressed in the testis. Ephrin/EphR interaction results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. EphRs comprise the largest subfamily of receptor tyr kinases (RTKs). In general, class EphA receptors bind GPI-anchored ephrin-A ligands. There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). The EphA10 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 133195 [Multi-domain]  Cd Length: 266  Bit Score: 55.70  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKA-FDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACreyrIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGND 497
Cdd:cd05064   18 FGELCRGcLKLPSKRELPVAIHTLRAGCSDKQRRGFLAEAL----TLGQFDHSNIVRLEGVIT-RGNTMMIVTEYMSNGA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHK-LMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACgeiKITDFGlsKIMDDDSygvDGM 576
Cdd:cd05064   93 LDSFLRKHEgQLVAGQLMGMLPGLASGMKYLSEMG--YVHKGLAAHKVLVNSDLVC---KISGFR--RLQEDKS---EAI 162
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 577 DLTSQGAGTYWYLPPECFVVGKeppkISNKVDVWSVGVIFFQCL-YGRKPFgHNQSQQDilqentILKATEVQFPVKP 653
Cdd:cd05064  163 YTTMSGKSPVLWAAPEAIQYHH----FSSASDVWSFGIVMWEVMsYGERPY-WDMSGQD------VIKAVEDGFRLPA 229
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
459-626 2.35e-08

Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. TrkC is a receptor PTK (RTK) containing an extracellular region with arrays of leucine-rich motifs flanked by two cysteine-rich clusters followed by two immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. Binding of TrkC to its ligand, neurotrophin 3 (NT3), results in receptor oligomerization and activation of the catalytic domain. TrkC is broadly expressed in the nervous system and in some non-neural tissues including the developing heart. NT3/TrkC signaling plays an important role in the innervation of the cardiac conducting system and the development of smooth muscle cells. Mice deficient with NT3 and TrkC have multiple heart defects. NT3/TrkC signaling is also critical for the development and maintenance of enteric neurons that are important for the control of gut peristalsis. The TrkC subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270676 [Multi-domain]  Cd Length: 287  Bit Score: 56.17  E-value: 2.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDyFSLDTDTFCTVLEYCEGNDLDFYLKQH----KLMSEKEARS------------IVMQIVN 522
Cdd:cd05094   56 REAELLTNLQHDHIVKFYG-VCGDGDPLIMVFEYMKHGDLNKFLRAHgpdaMILVDGQPRQakgelglsqmlhIATQIAS 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 523 ALRYLneIKPPIIHYDLKPGNILLVDGTAcgeIKITDFGLSK-IMDDDSYGVDGMDLTSqgagtYWYLPPECFVVgkepP 601
Cdd:cd05094  135 GMVYL--ASQHFVHRDLATRNCLVGANLL---VKIGDFGMSRdVYSTDYYRVGGHTMLP-----IRWMPPESIMY----R 200
                        170       180
                 ....*....|....*....|....*.
gi 211971036 602 KISNKVDVWSVGVIFFQCL-YGRKPF 626
Cdd:cd05094  201 KFTTESDVWSFGVILWEIFtYGKQPW 226
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
419-665 2.37e-08

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: 56.21  E-value: 2.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNKswRDEKKENYHKHACREyRIHKEL----DHPRIVKL-YDYFSLDTDTFctVLEYC 493
Cdd:cd14223   13 FGEVYGCRKADTGKMYAMKC--LDK--KRIKMKQGETLALNE-RIMLSLvstgDCPFIVCMsYAFHTPDKLSF--ILDLM 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 494 EGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGtacGEIKITDFGLSkimdddsygv 573
Cdd:cd14223   86 NGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMH--SRFVVYRDLKPANILLDEF---GHVRISDLGLA---------- 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 574 dgMDLTSQ----GAGTYWYLPPECFVVGKeppKISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQDILQENTILKATEVQ 648
Cdd:cd14223  151 --CDFSKKkphaSVGTHGYMAPEVLQKGV---AYDSSADWFSLGCMLFKLLRGHSPFrQHKTKDKHEIDRMTLTMAVELP 225
                        250
                 ....*....|....*..
gi 211971036 649 FPVKPVVSSEAKAFIRR 665
Cdd:cd14223  226 DSFSPELRSLLEGLLQR 242
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
459-637 2.43e-08

Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily includes Ack1, thirty-eight-negative kinase 1 (Tnk1), and similar proteins. They are cytoplasmic (or nonreceptor) PTKs containing an N-terminal catalytic domain, an SH3 domain, a Cdc42-binding CRIB domain, and a proline-rich region. They are mainly expressed in brain and skeletal tissues and are involved in the regulation of cell adhesion and growth, receptor degradation, and axonal guidance. Ack1 is also associated with androgen-independent prostate cancer progression. Tnk1 regulates TNFalpha signaling and may play an important role in cell death. The Ack-like subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270636 [Multi-domain]  Cd Length: 258  Bit Score: 55.81  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYfsLDTDTFCTVLEYCEGNDLDFYLKQHKlmsekeARSIV-------MQIVNALRYLnEIK 531
Cdd:cd05040   47 KEVNAMHSLDHPNLIRLYGV--VLSSPLMMVTELAPLGSLLDRLRKDQ------GHFLIstlcdyaVQIANGMAYL-ESK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 532 PpIIHYDLKPGNILLVDGTacgEIKITDFGLSKIMD--DDSYgvdgmDLTSQGAGTYWYLPPECFVVGkeppKISNKVDV 609
Cdd:cd05040  118 R-FIHRDLAARNILLASKD---KVKIGDFGLMRALPqnEDHY-----VMQEHRKVPFAWCAPESLKTR----KFSHASDV 184
                        170       180       190
                 ....*....|....*....|....*....|
gi 211971036 610 WSVGVIFFQCL-YGRKPF-GHNQSQqdILQ 637
Cdd:cd05040  185 WMFGVTLWEMFtYGEEPWlGLNGSQ--ILE 212
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
460-637 2.51e-08

Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow kinase on the X chromosome; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Btk and Bmx (also named Etk) are members of the Tec-like subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs with similarity to Src kinases in that they contain Src homology protein interaction domains (SH3, SH2) N-terminal to the catalytic tyr kinase domain. Unlike Src kinases, most Tec subfamily members except Rlk also contain an N-terminal pleckstrin homology (PH) domain, which binds the products of PI3K and allows membrane recruitment and activation. In addition, Btk contains the Tec homology (TH) domain with proline-rich and zinc-binding regions. Btk is expressed in B-cells, and a variety of myeloid cells including mast cells, platelets, neutrophils, and dendrictic cells. It interacts with a variety of partners, from cytosolic proteins to nuclear transcription factors, suggesting a diversity of functions. Stimulation of a diverse array of cell surface receptors, including antigen engagement of the B-cell receptor, leads to PH-mediated membrane translocation of Btk and subsequent phosphorylation by Src kinase and activation. Btk plays an important role in the life cycle of B-cells including their development, differentiation, proliferation, survival, and apoptosis. Mutations in Btk cause the primary immunodeficiency disease, X-linked agammaglobulinaemia (XLA) in humans. Bmx is primarily expressed in bone marrow and the arterial endothelium, and plays an important role in ischemia-induced angiogenesis. It facilitates arterial growth, capillary formation, vessel maturation, and bone marrow-derived endothelial progenitor cell mobilization. The Btk/Bmx subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173657 [Multi-domain]  Cd Length: 256  Bit Score: 55.66  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQH-KLMSEKEARSIVMQIVNALRYLNEIKppIIHYD 538
Cdd:cd05113   49 EAKVMMNLSHEKLVQLYGVCTKQRPIF-IITEYMANGCLLNYLREMrKRFQTQQLLEMCKDVCEAMEYLESKQ--FLHRD 125
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLVDGtacGEIKITDFGLSKIMDDDSYgvdgmdLTSQGAG--TYWYlPPECFVVGkeppKISNKVDVWSVGVIF 616
Cdd:cd05113  126 LAARNCLVNDQ---GVVKVSDFGLSRYVLDDEY------TSSVGSKfpVRWS-PPEVLMYS----KFSSKSDVWAFGVLM 191
                        170       180
                 ....*....|....*....|..
gi 211971036 617 FQCL-YGRKPFGHNQSQQDILQ 637
Cdd:cd05113  192 WEVYsLGKMPYERFTNSETVEH 213
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
419-626 2.59e-08

Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase 8; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP3K8 is also called Tumor progression locus 2 (Tpl2) or Cancer Osaka thyroid (Cot), and was first identified as a proto-oncogene in T-cell lymphoma induced by MoMuL virus and in breast carcinoma induced by MMTV. Activated MAP3K8 induces various MAPK pathways including Extracellular Regulated Kinase (ERK) 1/2, c-Jun N-terminal kinase (JNK), and p38. It plays a pivotal role in innate immunity, linking Toll-like receptors to the production of TNF and the activation of ERK in macrophages. It is also required in interleukin-1beta production and is critical in host defense against Gram-positive bacteria. MAP3Ks (MKKKs or MAPKKKs) phosphorylate and activate MAPK kinases (MAPKKs or MKKs or MAP2Ks), which in turn phosphorylate and activate MAPKs during signaling cascades that are important in mediating cellular responses to extracellular signals. The MAP3K8 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270897 [Multi-domain]  Cd Length: 256  Bit Score: 55.40  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSwrdeKKENYHKHACreYRihkeldHPRIVKLYDYFSLDtDTFCTVLEYCEGNDL 498
Cdd:cd13995   17 FGKVYLAQDTKTKKRMACKLIPVEQF----KPSDVEIQAC--FR------HENIAELYGALLWE-ETVHLFMEAGEGGSV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACgeikITDFGLSKIMDDDSYgvdgmdL 578
Cdd:cd13995   84 LEKLESCGPMREFEIIWVTKHVLKGLDFLHSKN--IIHHDIKPSNIVFMSTKAV----LVDFGLSVQMTEDVY------V 151
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 211971036 579 TSQGAGTYWYLPPECFVVGKEppkiSNKVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd13995  152 PKDLRGTEIYMSPEVILCRGH----NTKADIYSLGATIIHMQTGSPPW 195
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
459-618 3.22e-08

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Jak2 is widely expressed in many tissues and is essential for the signaling of hormone-like cytokines such as growth hormone, erythropoietin, thrombopoietin, and prolactin, as well as some IFNs and cytokines that signal through the IL-3 and gp130 receptors. Disruption of Jak2 in mice results in an embryonic lethal phenotype with multiple defects including erythropoietic and cardiac abnormalities. It is the only Jak gene that results in a lethal phenotype when disrupted in mice. A mutation in the pseudokinase domain of Jak2, V617F, is present in many myeloproliferative diseases, including almost all patients with polycythemia vera, and 50% of patients with essential thrombocytosis and myelofibrosis. Jak2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal catalytic tyr kinase domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271107 [Multi-domain]  Cd Length: 284  Bit Score: 55.79  E-value: 3.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDY-FSLDTDTFCTVLEYCEGNDLDFYLKQHK-LMSEKEARSIVMQIVNALRYLNEIKppIIH 536
Cdd:cd14205   54 REIEILKSLQHDNIVKYKGVcYSAGRRNLRLIMEYLPYGSLRDYLQKHKeRIDHIKLLQYTSQICKGMEYLGTKR--YIH 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 537 YDLKPGNILLVDGTacgEIKITDFGLSKIM--DDDSYGVDgmdlTSQGAGTYWYLPPECfvvgkEPPKISNKVDVWSVGV 614
Cdd:cd14205  132 RDLATRNILVENEN---RVKIGDFGLTKVLpqDKEYYKVK----EPGESPIFWYAPESL-----TESKFSVASDVWSFGV 199

                 ....
gi 211971036 615 IFFQ 618
Cdd:cd14205  200 VLYE 203
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
460-636 3.28e-08

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: 55.42  E-value: 3.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSldTDTFCTVLEYCEGNDLDFYLK-QHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYD 538
Cdd:cd14149   58 EVAVLRKTRHVNILLFMGYMT--KDNLAIVTQWCEGSSLYKHLHvQETKFQMFQLIDIARQTAQGMDYLHAKN--IIHRD 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLVDGTAcgeIKITDFGLSKIMDDDSygvdGMDLTSQGAGTYWYLPPECFVVGKEPPkISNKVDVWSVGVIFFQ 618
Cdd:cd14149  134 MKSNNIFLHEGLT---VKIGDFGLATVKSRWS----GSQQVEQPTGSILWMAPEVIRMQDNNP-FSFQSDVYSYGIVLYE 205
                        170
                 ....*....|....*...
gi 211971036 619 CLYGRKPFGHNQSQQDIL 636
Cdd:cd14149  206 LMTGELPYSHINNRDQII 223
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
419-616 4.02e-08

Catalytic domain of the Serine/Threonine Kinase, 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. 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 CdkB subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270830 [Multi-domain]  Cd Length: 294  Bit Score: 55.23  E-value: 4.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKELDH-PRIVKLYDYFSLDTD---TFCTVLEYCE 494
Cdd:cd07837   14 YGKVYKARDKNTGKLVALK-----KTRLEMEEEGVPSTALREVSLLQMLSQsIYIVRLLDVEHVEENgkpLLYLVFEYLD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 495 gNDLDFYLKQHKL-----MSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACgeIKITDFGLSKimddd 569
Cdd:cd07837   89 -TDLKKFIDSYGRgphnpLPAKTIQSFMYQLCKGVAHCH--SHGVMHRDLKPQNLLVDKQKGL--LKIADLGLGR----- 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 211971036 570 SYGVDGMDLTSQGAgTYWYLPPECFVVGKEppkISNKVDVWSVGVIF 616
Cdd:cd07837  159 AFTIPIKSYTHEIV-TLWYRAPEVLLGSTH---YSTPVDMWSVGCIF 201
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
498-684 4.31e-08

Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER2 (ErbB2, HER2/neu) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. HER2 does not bind to any known EGFR subfamily ligands, but contributes to the kinase activity of all possible heterodimers. It acts as the preferred partner of other ligand-bound EGFR proteins and functions as a signal amplifier, with the HER2-HER3 heterodimer being the most potent pair in mitogenic signaling. HER2 plays an important role in cell development, proliferation, survival and motility. Overexpression of HER2 results in its activation and downstream signaling, even in the absence of ligand. HER2 overexpression, mainly due to gene amplification, has been shown in a variety of human cancers. Its role in breast cancer is especially well-documented. HER2 is up-regulated in about 25% of breast tumors and is associated with increases in tumor aggressiveness, recurrence and mortality. HER2 is a target for monoclonal antibodies and small molecule inhibitors, which are being developed as treatments for cancer. The first humanized antibody approved for clinical use is Trastuzumab (Herceptin), which is being used in combination with other therapies to improve the survival rates of patients with HER2-overexpressing breast cancer. The HER2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270684 [Multi-domain]  Cd Length: 279  Bit Score: 55.03  E-value: 4.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacgEIKITDFGLSKIMDDD--SYGVDG 575
Cdd:cd05109   96 LDYVRENKDRIGSQDLLNWCVQIAKGMSYLEEVR--LVHRDLAARNVLVKSPN---HVKITDFGLARLLDIDetEYHADG 170
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 mdltsqGAGTYWYLPPECFVvgkePPKISNKVDVWSVGVIFFQCL-YGRKPFGHNQSQQ--DILQENTilkatevQFPVK 652
Cdd:cd05109  171 ------GKVPIKWMALESIL----HRRFTHQSDVWSYGVTVWELMtFGAKPYDGIPAREipDLLEKGE-------RLPQP 233
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 211971036 653 PVVSSEAKAFIRRCLAYRKEDR-------FDVHQLANDP 684
Cdd:cd05109  234 PICTIDVYMIMVKCWMIDSECRprfrelvDEFSRMARDP 272
PTKc_Ror1 cd05090
Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor ...
459-646 4.96e-08

Catalytic domain of the Protein Tyrosine Kinase, Receptor tyrosine kinase-like Orphan Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Ror kinases are expressed in many tissues during development. Avian Ror1 was found to be involved in late limb development. Studies in mice reveal that Ror1 is important in the regulation of neurite growth in central neurons, as well as in respiratory development. Loss of Ror1 also enhances the heart and skeletal abnormalities found in Ror2-deficient mice. Ror proteins are orphan receptor PTKs (RTKs) containing an extracellular region with immunoglobulin-like, cysteine-rich, and kringle domains, a transmembrane segment, and an intracellular catalytic domain. Ror RTKs are unrelated to the nuclear receptor subfamily called retinoid-related orphan receptors (RORs). RTKs are usually activated through ligand binding, which causes dimerization and autophosphorylation of the intracellular tyr kinase catalytic domain. The Ror1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270672 [Multi-domain]  Cd Length: 283  Bit Score: 55.02  E-value: 4.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLDTDTfCTVLEYCEGNDLDFYLKQHKLMSEKEARS-----------------IVMQIV 521
Cdd:cd05090   56 QEASLMTELHHPNIVCLLGVVTQEQPV-CMLFEFMNQGDLHEFLIMRSPHSDVGCSSdedgtvkssldhgdflhIAIQIA 134
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 522 NALRYLNEikPPIIHYDLKPGNILLvdgtacGE---IKITDFGLSKimddDSYGVDGMDLTSQGAGTYWYLPPECFVVGK 598
Cdd:cd05090  135 AGMEYLSS--HFFVHKDLAARNILV------GEqlhVKISDLGLSR----EIYSSDYYRVQNKSLLPIRWMPPEAIMYGK 202
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 211971036 599 eppkISNKVDVWSVGVIFFQCL-YGRKPFG--HNQSQQDILQENTILKATE 646
Cdd:cd05090  203 ----FSSDSDIWSFGVVLWEIFsFGLQPYYgfSNQEVIEMVRKRQLLPCSE 249
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
497-686 5.30e-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: 54.27  E-value: 5.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 497 DLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTACgEIKITDFglskimdDDSYGVDGM 576
Cdd:cd14022   70 DMHSFVRTCKKLREEEAARLFYQIASAVAHCHD--GGLVLRDLKLRKFVFKDEERT-RVKLESL-------EDAYILRGH 139
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 577 DLT-SQGAGTYWYLPPEcfVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFghnqsqQDILQENTILKATEVQFPVKPVV 655
Cdd:cd14022  140 DDSlSDKHGCPAYVSPE--ILNTSGSYSGKAADVWSLGVMLYTMLVGRYPF------HDIEPSSLFSKIRRGQFNIPETL 211
                        170       180       190
                 ....*....|....*....|....*....|.
gi 211971036 656 SSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14022  212 SPKAKCLIRSILRREPSERLTSQEILDHPWF 242
PKc_DYRK2_3 cd14224
Catalytic domain of the protein kinases, Dual-specificity tYrosine-phosphorylated and ...
419-633 6.22e-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: 55.52  E-value: 6.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqlnksWRDEKKenYHKHACREYRIhkeLDHPR---------IVKLYDYFSLDTDTfCTV 489
Cdd:cd14224   78 FGQVVKAYDHKTHQHVALKM------VRNEKR--FHRQAAEEIRI---LEHLKkqdkdntmnVIHMLESFTFRNHI-CMT 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 490 LEYCEGNdLDFYLKQHKL------MSEKEARSIvMQIVNALrYLNEikppIIHYDLKPGNILLVDGTACGeIKITDFGLS 563
Cdd:cd14224  146 FELLSMN-LYELIKKNKFqgfslqLVRKFAHSI-LQCLDAL-HRNK----IIHCDLKPENILLKQQGRSG-IKVIDFGSS 217
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 211971036 564 KIMDDDSYgvdgmdltsqgagTY----WYLPPECFVVGkeppKISNKVDVWSVGVIFFQCLYGRKPF-GHNQSQQ 633
Cdd:cd14224  218 CYEHQRIY-------------TYiqsrFYRAPEVILGA----RYGMPIDMWSFGCILAELLTGYPLFpGEDEGDQ 275
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
419-626 6.53e-08

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: 54.63  E-value: 6.53e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKEnyhkhacrEYRIHKELDHPR-IVKLYDYFSLDT-----DTFCTVLEY 492
Cdd:cd06636   29 YGQVYKGRHVKTGQLAAIKVMDVTEDEEEEIKL--------EINMLKKYSHHRnIATYYGAFIKKSppghdDQLWLVMEF 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 493 CEGNDLDFYLKQHKLMSEKE--ARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDDDs 570
Cdd:cd06636  101 CGAGSVTDLVKNTKGNALKEdwIAYICREILRGLAHLHAHK--VIHRDIKGQNVLL---TENAEVKLVDFGVSAQLDRT- 174
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 571 ygvdgMDLTSQGAGTYWYLPPECFVVGKEPPKISN-KVDVWSVGVIFFQCLYGRKPF 626
Cdd:cd06636  175 -----VGRRNTFIGTPYWMAPEVIACDENPDATYDyRSDIWSLGITAIEMAEGAPPL 226
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
460-674 6.59e-08

Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Hck is a member of the Src subfamily of proteins, which are cytoplasmic (or non-receptor) PTKs. Hck is present in myeloid and lymphoid cells that play a role in the development of cancer. It may be important in the oncogenic signaling of the protein Tel-Abl, which induces a chronic myelogenous leukemia (CML)-like disease. Hck also acts as a negative regulator of G-CSF-induced proliferation of granulocytic precursors, suggesting a possible role in the development of acute myeloid leukemia (AML). In addition, Hck is essential in regulating the degranulation of polymorphonuclear leukocytes. Genetic polymorphisms affect the expression level of Hck, which affects PMN mediator release and influences the development of chronic obstructive pulmonary disease (COPD). Src kinases contain an N-terminal SH4 domain with a myristoylation site, followed by SH3 and SH2 domains, a tyr kinase domain, and a regulatory C-terminal region containing a conserved tyr. They are activated by autophosphorylation at the tyr kinase domain, but are negatively regulated by phosphorylation at the C-terminal tyr by Csk (C-terminal Src Kinase). The Hck subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270658 [Multi-domain]  Cd Length: 265  Bit Score: 54.65  E-value: 6.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSldTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSI--VMQIVNALRYLNeiKPPIIHY 537
Cdd:cd05073   56 EANVMKTLQHDKLVKLHAVVT--KEPIYIITEFMAKGSLLDFLKSDEGSKQPLPKLIdfSAQIAEGMAFIE--QRNYIHR 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLVDGTACgeiKITDFGLSKIMDDDSYgvdgmdLTSQGAG-TYWYLPPECFVVGkeppKISNKVDVWSVGVIF 616
Cdd:cd05073  132 DLRAANILVSASLVC---KIADFGLARVIEDNEY------TAREGAKfPIKWTAPEAINFG----SFTIKSDVWSFGILL 198
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 617 FQCL-YGRKPFGHNQSQQdilqentILKATE--VQFPVKPVVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd05073  199 MEIVtYGRIPYPGMSNPE-------VIRALErgYRMPRPENCPEELYNIMMRCWKNRPEER 252
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
419-686 6.75e-08

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: 54.61  E-value: 6.75e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqLNK-SWRDEKKEnyhkhacREYRIHKEL-DHPRIVKLYDYF----SLDTDTFCTVLEY 492
Cdd:cd06639   35 YGKVYKVTNKKDGSLAAVKI--LDPiSDVDEEIE-------AEYNILRSLpNHPNVVKFYGMFykadQYVGGQLWLVLEL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 493 CEGND----LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKimdd 568
Cdd:cd06639  106 CNGGSvtelVKGLLKCGQRLDEAMISYILYGALLGLQHLHNNR--IIHRDVKGNNILL---TTEGGVKLVDFGVSA---- 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 569 dsygvdgmDLTS------QGAGTYWYLPPECFVVGKE-PPKISNKVDVWSVGVIFFQCLYGRKPFGhnqsqqDILQENTI 641
Cdd:cd06639  177 --------QLTSarlrrnTSVGTPFWMAPEVIACEQQyDYSYDARCDVWSLGITAIELADGDPPLF------DMHPVKAL 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 211971036 642 LKatevqFPVKPVVS--------SEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd06639  243 FK-----IPRNPPPTllnpekwcRGFSHFISQCLIKDFEKRPSVTHLLEHPFI 290
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
435-665 7.78e-08

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: 55.05  E-value: 7.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIhqLNKSWRDEKKENYHKHACREyrIHKELDHPRIVKLYDYFSlDTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEAR 514
Cdd:cd05628   30 AMKI--LRKADMLEKEQVGHIRAERD--ILVEADSLWVVKMFYSFQ-DKLNLYLIMEFLPGGDMMTLLMKKDTLTEEETQ 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 515 SIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdgTACGEIKITDFGLSKIMDD-------------------------- 568
Cdd:cd05628  105 FYIAETVLAIDSIHQLG--FIHRDIKPDNLLL---DSKGHVKLSDFGLCTGLKKahrtefyrnlnhslpsdftfqnmnsk 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 569 ---DSYGVDGMDLTSQGAGTYWYLPPECFVVGKeppkiSNKV-DVWSVGVIFFQCLYGRKPFGhNQSQQDILQENTILKA 644
Cdd:cd05628  180 rkaETWKRNRRQLAFSTVGTPDYIAPEVFMQTG-----YNKLcDWWSLGVIMYEMLIGYPPFC-SETPQETYKKVMNWKE 253
                        250       260
                 ....*....|....*....|.
gi 211971036 645 TeVQFPVKPVVSSEAKAFIRR 665
Cdd:cd05628  254 T-LIFPPEVPISEKAKDLILR 273
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
419-651 1.00e-07

Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor 2-Alpha Kinase 2 or Heme-Regulated Inhibitor kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. HRI (or EIF2AK1) contains an N-terminal regulatory heme-binding domain and a C-terminal catalytic kinase domain. It is suppressed under normal conditions by binding of the heme iron, and is activated during heme deficiency. It functions as a critical regulator that ensures balanced synthesis of globins and heme, in order to form stable hemoglobin during erythroid differentiation and maturation. HRI also protects cells and enhances survival under iron-deficient conditions. EIF2AKs phosphorylate the alpha subunit of eIF-2, resulting in the downregulation of protein synthesis. The HRI 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: 270951 [Multi-domain]  Cd Length: 284  Bit Score: 54.05  E-value: 1.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLNKSWRDekkeNYHKHaCREYRIHKELDHPRIV-----------------------KL 475
Cdd:cd14049   19 YGKVYKVRNKLDGQYYAIKKILIKKVTKR----DCMKV-LREVKVLAGLQHPNIVgyhtawmehvqlmlyiqmqlcelSL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 476 YDYFSlDTDTFCTVLEYCEGNdldfylkqHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvDGTACgEI 555
Cdd:cd14049   94 WDWIV-ERNKRPCEEEFKSAP--------YTPVDVDVTTKILQQLLEGVTYIHSMG--IVHRDLKPRNIFL-HGSDI-HV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 556 KITDFGLS----KIMDDDSYGVDGMD--LTSQGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFFQCLygrKPFGHN 629
Cdd:cd14049  161 RIGDFGLAcpdiLQDGNDSTTMSRLNglTHTSGVGTCLYAAPEQL----EGSHYDFKSDMYSIGVILLELF---QPFGTE 233
                        250       260
                 ....*....|....*....|....*
gi 211971036 630 QSQQDI---LQENTILKATEVQFPV 651
Cdd:cd14049  234 MERAEVltqLRNGQIPKSLCKRWPV 258
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
435-615 1.25e-07

Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The InsR subfamily is composed of InsR, Insulin-like Growth Factor-1 Receptor (IGF-1R), and similar proteins. InsR and IGF-1R are receptor PTKs (RTKs) composed of two alphabeta heterodimers. Binding of the ligand (insulin, IGF-1, or IGF-2) to the extracellular alpha subunit activates the intracellular tyr kinase domain of the transmembrane beta subunit. Receptor activation leads to autophosphorylation, stimulating downstream kinase activities, which initiate signaling cascades and biological function. InsR and IGF-1R, which share 84% sequence identity in their kinase domains, display physiologically distinct yet overlapping functions in cell growth, differentiation, and metabolism. InsR activation leads primarily to metabolic effects while IGF-1R activation stimulates mitogenic pathways. In cells expressing both receptors, InsR/IGF-1R hybrids are found together with classical receptors. Both receptors can interact with common adaptor molecules such as IRS-1 and IRS-2. The InsR-like subfamily 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: 173625 [Multi-domain]  Cd Length: 277  Bit Score: 53.89  E-value: 1.25e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIHQLNKSWRDekKENYHKHAcreyRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDLDFYLKQHklMSEKEAR 514
Cdd:cd05032   40 AIKTVNENASMRE--RIEFLNEA----SVMKEFNCHHVVRLLGVVSTGQPTL-VVMELMAKGDLKSYLRSR--RPEAENN 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 515 SIVM------------QIVNALRYLNEIKppIIHYDLKPGNILLV-DGTacgeIKITDFGLSK-IMDDDSYGVDGmdlts 580
Cdd:cd05032  111 PGLGpptlqkfiqmaaEIADGMAYLAAKK--FVHRDLAARNCMVAeDLT----VKIGDFGMTRdIYETDYYRKGG----- 179
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 211971036 581 QGAGTYWYLPPECFVVGKeppkISNKVDVWSVGVI 615
Cdd:cd05032  180 KGLLPVRWMAPESLKDGV----FTTKSDVWSFGVV 210
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
405-641 1.41e-07

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: 53.30  E-value: 1.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 405 NERYLLLHLLGRGGFSEVYKAFDLYEQ--RYAAVKIHQLNkswrDEKKEnyhkhACREYRIHKELDHPRIVKLYDYFSlD 482
Cdd:cd14112    2 TGRFSFGSEIFRGRFSVIVKAVDSTTEtdAHCAVKIFEVS----DEASE-----AVREFESLRTLQHENVQRLIAAFK-P 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 483 TDTFCTVLEYCEGNDLDFYLKQHKlMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTACgEIKITDFGl 562
Cdd:cd14112   72 SNFAYLVMEKLQEDVFTRFSSNDY-YSEEQVATTVRQILDALHYLHF--KGIAHLDVQPDNIMFQSVRSW-QVKLVDFG- 146
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 563 skimddDSYGVDGMDLTSQGAGTYWyLPPEcfVVGKEPPkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTI 641
Cdd:cd14112  147 ------RAQKVSKLGKVPVDGDTDW-ASPE--FHNPETP-ITVQSDIWGLGVLTFCLLSGFHPFTSEYDDEEETKENVI 215
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
449-675 1.49e-07

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: 53.82  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 449 KKENYHKHACREYRIHKELDHPRIVKL-YDYFSldTDTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSI--VMQIVNALR 525
Cdd:cd05632   41 KKRKGESMALNEKQILEKVNSQFVVNLaYAYET--KDALCLVLTIMNGGDLKFHIYNMGNPGFEEERALfyAAEILCGLE 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 526 YLNeiKPPIIHYDLKPGNILLVDGtacGEIKITDFGLS-KIMDDDSygVDGMdltsqgAGTYWYLPPEcfVVGKEPPKIS 604
Cdd:cd05632  119 DLH--RENTVYRDLKPENILLDDY---GHIRISDLGLAvKIPEGES--IRGR------VGTVGYMAPE--VLNNQRYTLS 183
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 605 NkvDVWSVGVIFFQCLYGRKPFghNQSQQDILQENTILKATEVQFPVKPVVSSEAKAFIRRCLAYRKEDRF 675
Cdd:cd05632  184 P--DYWGLGCLIYEMIEGQSPF--RGRKEKVKREEVDRRVLETEEVYSAKFSEEAKSICKMLLTKDPKQRL 250
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
419-561 1.49e-07

Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large family of typical PKs that includes serine/threonine kinases (STKs), protein tyrosine kinases (PTKs), and dual-specificity PKs that phosphorylate both serine/threonine and tyrosine residues of target proteins, as well as pseudokinases that lack crucial residues for catalytic activity and/or ATP binding. It also includes phosphoinositide 3-kinases (PI3Ks), aminoglycoside 3'-phosphotransferases (APHs), choline kinase (ChoK), Actin-Fragmin Kinase (AFK), and the atypical RIO and Abc1p-like protein kinases. These proteins catalyze the transfer of the gamma-phosphoryl group from ATP to their target substrates; these include serine/threonine/tyrosine residues in proteins for typical or atypical PKs, the 3-hydroxyl of the inositol ring of D-myo-phosphatidylinositol (PtdIns) or its derivatives for PI3Ks, the 4-hydroxyl of PtdIns for PI4Ks, and other small molecule substrates for APH/ChoK and similar proteins such as aminoglycosides, macrolides, choline, ethanolamine, and homoserine.


Pssm-ID: 270870 [Multi-domain]  Cd Length: 136  Bit Score: 50.90  E-value: 1.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqlNKSWRDEKKENYHKhacrEYRIHKELDHPR--IVKLYDYFSLDTDTFCTVlEYCEGN 496
Cdd:cd13968    6 SAKVFWAEGECTTIGVAVKI---GDDVNNEEGEDLES----EMDILRRLKGLElnIPKVLVTEDVDGPNILLM-ELVKGG 77
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 211971036 497 DLDFYLkQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFG 561
Cdd:cd13968   78 TLIAYT-QEEELDEKDVESIMYQLAECMRLLHSFH--LIHRDLNNDNILLSED---GNVKLIDFG 136
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
419-614 1.50e-07

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: 53.49  E-value: 1.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQLnkswrdEKKENYhKHACREYRIHKELDHPRIVKLY-DYFSLDTDTFCtvLEYCEGND 497
Cdd:cd06646   22 YGDVYKARNLHTGELAAVKIIKL------EPGDDF-SLIQQEIFMVKECKHCNIVAYFgSYLSREKLWIC--MEYCGGGS 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 498 LDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKPpiIHYDLKPGNILLVDGtacGEIKITDFGLSKIMdddsygVDGMD 577
Cdd:cd06646   93 LQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGK--MHRDIKGANILLTDN---GDVKLADFGVAAKI------TATIA 161
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 211971036 578 LTSQGAGTYWYLPPECFVVGKEpPKISNKVDVWSVGV 614
Cdd:cd06646  162 KRKSFIGTPYWMAPEVAAVEKN-GGYNQLCDIWAVGI 197
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
460-666 1.53e-07

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 54.23  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSLDTDTfCTVLEYCEgNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDL 539
Cdd:PHA03212 133 EAHILRAINHPSIIQLKGTFTYNKFT-CLILPRYK-TDLYCYLAAKRNIAICDILAIERSVLRAIQYLHENR--IIHRDI 208
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 540 KPGNILLvdgTACGEIKITDFGLS----KIMDDDSYGvdgmdltsqGAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVI 615
Cdd:PHA03212 209 KAENIFI---NHPGDVCLGDFGAAcfpvDINANKYYG---------WAGTIATNAPE--LLARDP--YGPAVDIWSAGIV 272
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 616 FFQCLYGRKPF-------GHNQSQQDIlqeNTILKATEV---QFPVKPvVSSEAKAFIRRC 666
Cdd:PHA03212 273 LFEMATCHDSLfekdgldGDCDSDRQI---KLIIRRSGThpnEFPIDA-QANLDEIYIGLA 329
STKc_LRRK1 cd14067
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 1; STKs catalyze ...
459-632 1.56e-07

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: 53.43  E-value: 1.56e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLydyFSLDTDTFCTVLEYCEGNDLDFYLKQ-HK---------LMSEKearsIVMQIVNALRYLN 528
Cdd:cd14067   59 QEASMLHSLQHPCIVYL---IGISIHPLCFALELAPLGSLNTVLEEnHKgssfmplghMLTFK----IAYQIAAGLAYLH 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 529 eiKPPIIHYDLKPGNILL--VDGTACGEIKITDFGLSKimddDSY--GVDGMDltsqgaGTYWYLPPECfvvgkePPKI- 603
Cdd:cd14067  132 --KKNIIFCDLKSDNILVwsLDVQEHINIKLSDYGISR----QSFheGALGVE------GTPGYQAPEI------RPRIv 193
                        170       180       190
                 ....*....|....*....|....*....|.
gi 211971036 604 -SNKVDVWSVGVIFFQCLYGRKP-FGHNQSQ 632
Cdd:cd14067  194 yDEKVDMFSYGMVLYELLSGQRPsLGHHQLQ 224
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
460-681 1.97e-07

Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. HER4 (ErbB4) is a member of the EGFR (HER, ErbB) subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular EGF-related ligand-binding region, a transmembrane helix, and a cytoplasmic region with a tyr kinase domain and a regulatory C-terminal tail. Unlike other PTKs, phosphorylation of the activation loop of EGFR proteins is not critical to their activation. Instead, they are activated by ligand-induced dimerization, leading to the phosphorylation of tyr residues in the C-terminal tail, which serve as binding sites for downstream signaling molecules. Ligands that bind HER4 fall into two groups, the neuregulins (or heregulins) and some EGFR (HER1) ligands including betacellulin, HBEGF, and epiregulin. All four neuregulins (NRG1-4) interact with HER4. Upon ligand binding, HER4 forms homo- or heterodimers with other HER proteins. HER4 is essential in embryonic development. It is implicated in mammary gland, cardiac, and neural development. As a postsynaptic receptor of NRG1, HER4 plays an important role in synaptic plasticity and maturation. The impairment of NRG1/HER4 signaling may contribute to schizophrenia. The HER4 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173655 [Multi-domain]  Cd Length: 303  Bit Score: 53.53  E-value: 1.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFSLDTDTFCTVLeYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDL 539
Cdd:cd05110   59 EALIMASMDHPHLVRLLGVCLSPTIQLVTQL-MPHGCLLDYVHEHKDNIGSQLLLNWCVQIAKGMMYLEERR--LVHRDL 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 540 KPGNILLvdgTACGEIKITDFGLSKIM--DDDSYGVDGmdltsqGAGTYWYLPPECFvvgkEPPKISNKVDVWSVGVIFF 617
Cdd:cd05110  136 AARNVLV---KSPNHVKITDFGLARLLegDEKEYNADG------GKMPIKWMALECI----HYRKFTHQSDVWSYGVTIW 202
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 618 QCL-YGRKPFGHNQSQQ--DILQENTilkatevQFPVKPVVSSEAKAFIRRCLAYRKEDRFDVHQLA 681
Cdd:cd05110  203 ELMtFGGKPYDGIPTREipDLLEKGE-------RLPQPPICTIDVYMVMVKCWMIDADSRPKFKELA 262
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
419-621 2.30e-07

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: 53.38  E-value: 2.30e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDL-YEQRYAAVKIHQLNkswrdekkENYHKHACREYRIHKEL-DHPR-----IVKLYDYFSlDTDTFCTVLE 491
Cdd:cd14135   13 FSNVVRARDLaRGNQEVAIKIIRNN--------ELMHKAGLKELEILKKLnDADPddkkhCIRLLRHFE-HKNHLCLVFE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 492 YCEGN---DLDFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACgeIKITDFG-LSKIMD 567
Cdd:cd14135   84 SLSMNlreVLKKYGKNVGL-NIKAVRSYAQQLFLALKHLKKCN--ILHADIKPDNILVNEKKNT--LKLCDFGsASDIGE 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 211971036 568 DD--SYgvdgmdLTSQgagtyWYLPPEcFVVGKeppKISNKVDVWSVGViffqCLY 621
Cdd:cd14135  159 NEitPY------LVSR-----FYRAPE-IILGL---PYDYPIDMWSVGC----TLY 195
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
465-686 2.58e-07

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: 52.71  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 465 KELDHPRIVKLYDyfSLDTDT----FCT---------VL-EYCEGNDLDFYLKQHKLmSEKEARSIVMQIVNALRYL-NE 529
Cdd:cd14011   57 TRLRHPRILTVQH--PLEESReslaFATepvfaslanVLgERDNMPSPPPELQDYKL-YDVEIKYGLLQISEALSFLhND 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 530 IKppIIHYDLKPGNILLvdgTACGEIKITDFGLSkimdddsygvdgmdLTSQGAGTYWYLPPEcFVVGKEPPKISN---- 605
Cdd:cd14011  134 VK--LVHGNICPESVVI---NSNGEWKLAGFDFC--------------ISSEQATDQFPYFRE-YDPNLPPLAQPNlnyl 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 606 ------------KVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENtILKATEVQFPVKPVVSSEAKAFIRRCLAYRKED 673
Cdd:cd14011  194 apeyilsktcdpASDMFSLGVLIYAIYNKGKPLFDCVNNLLSYKKN-SNQLRQLSLSLLEKVPEELRDHVKTLLNVTPEV 272
                        250
                 ....*....|...
gi 211971036 674 RFDVHQLANDPYL 686
Cdd:cd14011  273 RPDAEQLSKIPFF 285
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
419-622 3.37e-07

Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LRRK2 is one of two vertebrate LRRKs which show complementary expression in the brain. Mutations in LRRK2, found in the kinase, ROC-COR, and WD40 domains, are linked to both familial and sporadic forms of Parkinson's disease. The most prevalent mutation, G2019S located in the activation loop of the kinase domain, increases kinase activity. The R1441C/G mutations in the GTPase domain have also been reported to influence kinase activity. 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 LRRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270970 [Multi-domain]  Cd Length: 252  Bit Score: 52.26  E-value: 3.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfdLYEQRYAAVKIHQLNKSWRDEKKEnyhkhacreYRIHKELDHPRIVKLydyFSLDTDTFCTVLEYCEGNDL 498
Cdd:cd14068    7 FGSVYRA--VYRGEDVAVKIFNKHTSFRLLRQE---------LVVLSHLHHPSLVAL---LAAGTAPRMLVMELAPKGSL 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKL-MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEI--KITDFGLSKIMddDSYGVDg 575
Cdd:cd14068   73 DALLQQDNAsLTRTLQHRIALHVADGLRYLHSAM--IIYRDLKPHNVLLFTLYPNCAIiaKIADYGIAQYC--CRMGIK- 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 211971036 576 mdlTSQgaGTYWYLPPEcfvVGKEPPKISNKVDVWSVGVIFFQCLYG 622
Cdd:cd14068  148 ---TSE--GTPGFRAPE---VARGNVIYNQQADVYSFGLLLYDILTC 186
STKc_PINK1 cd14018
Catalytic domain of the Serine/Threonine protein kinase, Pten INduced Kinase 1; STKs catalyze ...
462-665 7.01e-07

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: 51.73  E-value: 7.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 462 RIHKE-LDHPR----IVKLYDyfsldtdtfCTVLEYCEGNDLDFYLkqhklmsekeARSIVMQIVNALRYLneIKPPIIH 536
Cdd:cd14018  103 RLNPSgLGHNRtlflVMKNYP---------CTLRQYLWVNTPSYRL----------ARVMILQLLEGVDHL--VRHGIAH 161
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 537 YDLKPGNILL-VDGTACGEIKITDFGLSkiMDDDSYGVDgMDLTS---QGAGTYWYLPPECFVVGKEPPKISN--KVDVW 610
Cdd:cd14018  162 RDLKSDNILLeLDFDGCPWLVIADFGCC--LADDSIGLQ-LPFSSwyvDRGGNACLMAPEVSTAVPGPGVVINysKADAW 238
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 611 SVGVIFFQCLYGRKPFghnQSQQDILQENTILKatEVQFP-----VKPVVSSEAKAFIRR 665
Cdd:cd14018  239 AVGAIAYEIFGLSNPF---YGLGDTMLESRSYQ--ESQLPalpsaVPPDVRQVVKDLLQR 293
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
404-561 7.71e-07

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. They play important roles in mediating pre-mRNA processing and mRNA maturation, as well as other cellular functions such as chromatin reorganization, cell cycle and p53 regulation, and metabolic signaling. Vertebrates contain three distinct SRPKs, called SRPK1-3. The SRPK homolog in budding yeast, Sky1p, recognizes and phosphorylates its substrate Npl3p, which lacks a classic RS domain but contains a single RS dipeptide at the C-terminus of its RGG domain. Npl3p is a shuttling heterogeneous nuclear ribonucleoprotein (hnRNP) that exports a distinct class of mRNA from the nucleus to the cytoplasm. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271038 [Multi-domain]  Cd Length: 320  Bit Score: 51.81  E-value: 7.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 404 LNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWR----DEKK------ENYHKHACREyrihkeldhpRIV 473
Cdd:cd14136    8 YNGRYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVVKSAQHYTeaalDEIKllkcvrEADPKDPGRE----------HVV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 474 KLYDYFSL---DTDTFCTVLEYCeGNDLDFYLKQ--HKLMSEKEARSIVMQIVNALRYLNEiKPPIIHYDLKPGNILLVD 548
Cdd:cd14136   78 QLLDDFKHtgpNGTHVCMVFEVL-GPNLLKLIKRynYRGIPLPLVKKIARQVLQGLDYLHT-KCGIIHTDIKPENVLLCI 155
                        170
                 ....*....|...
gi 211971036 549 GTAcgEIKITDFG 561
Cdd:cd14136  156 SKI--EVKIADLG 166
PK_MADML cd14035
Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to ...
467-557 7.76e-07

Pseudokinase domain of MLF1-ADaptor Molecule-Like; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. MADML has been shown to be expressed throughout development in Xenopus laevis with highest expression found in the developing lens and retina. It may play an important role in embryonic eye development. The MADML 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: 270937 [Multi-domain]  Cd Length: 263  Bit Score: 51.08  E-value: 7.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 467 LDHPRIVKLYDYFSLDTDTFCTVL---EYCEGNDLDFYLKQ----HKLMSEKEARSIVMQIVNALRYLNEIKPPIIHYDL 539
Cdd:cd14035   52 VDHPNIVKFHKYWLDVKDNHARVVfitEYVSSGSLKQFLKKtkknHKTMNARAWKRWCTQILSALSYLHSCEPPIIHGNL 131
                         90
                 ....*....|....*...
gi 211971036 540 KPGNILLVDGtacGEIKI 557
Cdd:cd14035  132 TSDTIFIQHN---GLIKI 146
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
453-544 9.09e-07

Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Wee1 is a nuclear 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. There are two distinct Wee1 proteins in vertebrates showing different expression patterns, called Wee1a and Wee1b. They are functionally dstinct and are implicated in different steps of egg maturation and embryo development. The 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: 270953 [Multi-domain]  Cd Length: 275  Bit Score: 51.25  E-value: 9.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 453 YHKHACREYRIHKEL-DHPRIVKLYDYFSLDtDTFCTVLEYCEGNDLDFYLKQHK----LMSEKEARSIVMQIVNALRYL 527
Cdd:cd14051   42 DEQNALNEVYAHAVLgKHPHVVRYYSAWAED-DHMIIQNEYCNGGSLADAISENEkageRFSEAELKDLLLQVAQGLKYI 120
                         90
                 ....*....|....*..
gi 211971036 528 NEIKppIIHYDLKPGNI 544
Cdd:cd14051  121 HSQN--LVHMDIKPGNI 135
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
419-686 1.10e-06

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 51.57  E-value: 1.10e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENyhkhacREYRIHKELDHPRIVKLYDYFSldTDTFCTVLEYCEGNDL 498
Cdd:PTZ00036  79 FGVVYEAICIDTSEKVAIK-----KVLQDPQYKN------RELLIMKNLNHINIIFLKDYYY--TECFKKNEKNIFLNVV 145
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQ--HKLMS--EKEARSIVM--------QIVNALRYLNEikPPIIHYDLKPGNILLVDGTAcgEIKITDFGLSKIM 566
Cdd:PTZ00036 146 MEFIPQtvHKYMKhyARNNHALPLflvklysyQLCRALAYIHS--KFICHRDLKPQNLLIDPNTH--TLKLCDFGSAKNL 221
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 567 dddsygvdgmdLTSQGAGTY----WYLPPEcFVVGKEppKISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTIL 642
Cdd:PTZ00036 222 -----------LAGQRSVSYicsrFYRAPE-LMLGAT--NYTTHIDLWSLGCIIAEMILGYPIFSGQSSVDQLVRIIQVL 287
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 643 KA-------------TEVQFP-VKPV---------VSSEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:PTZ00036 288 GTptedqlkemnpnyADIKFPdVKPKdlkkvfpkgTPDDAINFISQFLKYEPLKRLNPIEALADPFF 354
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
399-633 1.94e-06

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: 50.47  E-value: 1.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 399 KDHptLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIhqlnksWRDEKKenYHKHACREYRIhkeLDHPR------- 471
Cdd:cd14225   38 HDH--IAYRYEILEVIGKGSFGQVVKALDHKTNEHVAIKI------IRNKKR--FHHQALVEVKI---LDALRrkdrdns 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 472 --IVKLYDYFSLdTDTFCTVLEYCeGNDLDFYLKQHKL--MSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLv 547
Cdd:cd14225  105 hnVIHMKEYFYF-RNHLCITFELL-GMNLYELIKKNNFqgFSLSLIRRFAISLLQCLRLLY--RERIIHCDLKPENILL- 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 548 DGTACGEIKITDFGLSKIMDDDSYgvdgmdltsqgagTY----WYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQcLYGR 623
Cdd:cd14225  180 RQRGQSSIKVIDFGSSCYEHQRVY-------------TYiqsrFYRSPE--VILGLP--YSMAIDMWSLGCILAE-LYTG 241
                        250
                 ....*....|..
gi 211971036 624 KPF--GHNQSQQ 633
Cdd:cd14225  242 YPLfpGENEVEQ 253
PK_GC-A_B cd14042
Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The ...
460-682 2.14e-06

Pseudokinase domain of the membrane Guanylate Cyclase receptors, GC-A and GC-B; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. GC-A binds and is activated by the atrial and B-type natriuretic peptides, ANP and BNP, which are important in blood pressure regulation and cardiac pathophysiology. GC-B binds the C-type natriuretic peptide, CNP, which is a potent vasorelaxant and functions in vascular remodeling and bone growth regulation. Membrane (or particulate) GCs consist of an extracellular ligand-binding domain, a single transmembrane region, and an intracellular tail that contains a PK-like domain, an amphiphatic region and a catalytic GC domain that catalyzes the conversion of GTP into cGMP and pyrophosphate. Membrane GCs act as receptors that transduce an extracellular signal to the intracellular production of cGMP, which has been implicated in many processes including cell proliferation, phototransduction, and muscle contractility, through its downstream effectors such as PKG. The PK-like domain of GCs functions as a negative regulator of the catalytic GC domain and may also act as a docking site for interacting proteins such as GC-activating proteins. The GC-A/B subfamily is part of a larger superfamily that includes the catalytic domains of protein serine/threonine kinases, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270944 [Multi-domain]  Cd Length: 279  Bit Score: 49.90  E-value: 2.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 460 EYRIHKELDHPRIVKLYDYFsLDTDTFCTVLEYC-----------EGNDLDFYLKQhklmsekearSIVMQIVNALRYLN 528
Cdd:cd14042   52 ELKHMRDLQHDNLTRFIGAC-VDPPNICILTEYCpkgslqdilenEDIKLDWMFRY----------SLIHDIVKGMHYLH 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 529 --EIKppiIHYDLKPGNiLLVDGTACgeIKITDFGLSKIMDDDSYgvdgmdltSQGAGTYW----YLPPECFVVGKEPPK 602
Cdd:cd14042  121 dsEIK---SHGNLKSSN-CVVDSRFV--LKITDFGLHSFRSGQEP--------PDDSHAYYakllWTAPELLRDPNPPPP 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 603 ISNKVDVWSVGVIFFQCLYGRKPFG---HNQSQQDILQEntiLKATEVQFPVKPVVSS-----EAKAFIRRCLAYRKEDR 674
Cdd:cd14042  187 GTQKGDVYSFGIILQEIATRQGPFYeegPDLSPKEIIKK---KVRNGEKPPFRPSLDElecpdEVLSLMQRCWAEDPEER 263

                 ....*...
gi 211971036 675 FDVHQLAN 682
Cdd:cd14042  264 PDFSTLRN 271
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
473-642 2.19e-06

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: 50.39  E-value: 2.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 473 VKLYDYFSLDTDtFCTVLEYCEGNDLDFyLKQHKLMSE--KEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDG- 549
Cdd:cd14214   79 VLMSDWFNFHGH-MCIAFELLGKNTFEF-LKENNFQPYplPHIRHMAYQLCHALKFLHENQ--LTHTDLKPENILFVNSe 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 550 --------TACGE-------IKITDFGlSKIMDDDSYgvdgmdltSQGAGTYWYLPPECFV-VGKEPPkisnkVDVWSVG 613
Cdd:cd14214  155 fdtlynesKSCEEksvkntsIRVADFG-SATFDHEHH--------TTIVATRHYRPPEVILeLGWAQP-----CDVWSLG 220
                        170       180
                 ....*....|....*....|....*....
gi 211971036 614 VIFFQCLYGRKPFGHNQSQQDILQENTIL 642
Cdd:cd14214  221 CILFEYYRGFTLFQTHENREHLVMMEKIL 249
STKc_HIPK1 cd14228
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 1; ...
440-622 2.34e-06

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: 50.47  E-value: 2.34e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 440 QLNKSWRDEKKE-----------NYHKHACREYRIHKEL-----DHPRIVKLYDYFSLDTDTfCTVLEYCEGNDLDFyLK 503
Cdd:cd14228   30 QVAKCWKRSTKEivaikilknhpSYARQGQIEVSILSRLssenaDEYNFVRSYECFQHKNHT-CLVFEMLEQNLYDF-LK 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 504 QHKL--MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACG-EIKITDFGLSKIMdddSYGVDGMDLTS 580
Cdd:cd14228  108 QNKFspLPLKYIRPILQQVATALMKLKSLG--LIHADLKPENIMLVDPVRQPyRVKVIDFGSASHV---SKAVCSTYLQS 182
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 211971036 581 QgagtyWYLPPEcFVVGKeppKISNKVDVWSVGVIFFQCLYG 622
Cdd:cd14228  183 R-----YYRAPE-IILGL---PFCEAIDMWSLGCVIAELFLG 215
STKc_HIPK2 cd14227
Catalytic domain of the Serine/Threonine Kinase, Homeodomain-Interacting Protein Kinase 2; ...
468-622 2.56e-06

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: 50.09  E-value: 2.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 468 DHPRIVKLYDYFSLDTDTfCTVLEYCEGNDLDFyLKQHKL--MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNIL 545
Cdd:cd14227   74 DDYNFVRAYECFQHKNHT-CLVFEMLEQNLYDF-LKQNKFspLPLKYIRPILQQVATALMKLKSLG--LIHADLKPENIM 149
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 546 LVDGTACG-EIKITDFGLSKIMdddSYGVDGMDLTSQgagtyWYLPPEcFVVGKeppKISNKVDVWSVGVIFFQCLYG 622
Cdd:cd14227  150 LVDPSRQPyRVKVIDFGSASHV---SKAVCSTYLQSR-----YYRAPE-IILGL---PFCEAIDMWSLGCVIAELFLG 215
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
489-674 2.70e-06

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: 49.67  E-value: 2.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 489 VLEYCEGNDLDFYLKQHKLMSE-KEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTAcgeIKITDFGLSKIMD 567
Cdd:cd14151   81 VTQWCEGSSLYHHLHIIETKFEmIKLIDIARQTAQGMDYLH--AKSIIHRDLKSNNIFLHEDLT---VKIGDFGLATVKS 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 568 DDSygvdGMDLTSQGAGTYWYLPPECFVVGKEPPkISNKVDVWSVGVIFFQCLYGRKPFGHNQSQQDILQENTILKATEV 647
Cdd:cd14151  156 RWS----GSHQFEQLSGSILWMAPEVIRMQDKNP-YSFQSDVYAFGIVLYELMTGQLPYSNINNRDQIIFMVGRGYLSPD 230
                        170       180
                 ....*....|....*....|....*..
gi 211971036 648 QFPVKPVVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd14151  231 LSKVRSNCPKAMKRLMAECLKKKRDER 257
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
455-546 2.81e-06

Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1a, Xenopus laevis Wee1b (XeWee1b) and similar vertebrate proteins. Members of this subfamily show a wide expression pattern. XeWee1b functions after the first zygotic cell divisions. It is expressed in all tissues and is also present after the gastrulation stage of embryos. 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 Wee1a 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: 271040 [Multi-domain]  Cd Length: 276  Bit Score: 49.64  E-value: 2.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 455 KHACREYRIHKEL-DHPRIVKLYDYFSLDtDTFCTVLEYCEGNDL-DFYLKQHKLM---SEKEARSIVMQIVNALRYLNE 529
Cdd:cd14138   49 QNALREVYAHAVLgQHSHVVRYYSAWAED-DHMLIQNEYCNGGSLaDAISENYRIMsyfTEPELKDLLLQVARGLKYIHS 127
                         90
                 ....*....|....*..
gi 211971036 530 IKppIIHYDLKPGNILL 546
Cdd:cd14138  128 MS--LVHMDIKPSNIFI 142
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
419-625 3.51e-06

Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. Members of this subfamily include LIMK, Testicular or testis-specific protein kinase (TESK), and similar proteins. LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-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: 270967 [Multi-domain]  Cd Length: 252  Bit Score: 49.03  E-value: 3.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIhqlnkswrdEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYCEGNDL 498
Cdd:cd14065    6 FGEVYKVTHRETGKVMVMKE---------LKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLN-FITEYVNGGTL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKL-MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSY--GVDG 575
Cdd:cd14065   76 EELLKSMDEqLPWSQRVSLAKDIASGMAYLHSKN--IIHRDLNSKNCLVREANRGRNAVVADFGLAREMPDEKTkkPDRK 153
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 211971036 576 MDLTSQGAgTYWyLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLyGRKP 625
Cdd:cd14065  154 KRLTVVGS-PYW-MAPE--MLRGES--YDEKVDVFSFGIVLCEII-GRVP 196
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
497-686 3.53e-06

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: 48.89  E-value: 3.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 497 DLDFYLKQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILLVDGTACgEIKITDFGLSKIMDDDSygvdgm 576
Cdd:cd14023   70 DMHSYVRSCKRLREEEAARLFKQIVSAVAHCH--QSAIVLGDLKLRKFVFSDEERT-QLRLESLEDTHIMKGED------ 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 577 DLTSQGAGTYWYLPPEcfVVGKEPPKISNKVDVWSVGVIFFQCLYGRKPFgHNQSQQDILQentilKATEVQFPVKPVVS 656
Cdd:cd14023  141 DALSDKHGCPAYVSPE--ILNTTGTYSGKSADVWSLGVMLYTLLVGRYPF-HDSDPSALFS-----KIRRGQFCIPDHVS 212
                        170       180       190
                 ....*....|....*....|....*....|
gi 211971036 657 SEAKAFIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14023  213 PKARCLIRSLLRREPSERLTAPEILLHPWF 242
STKc_SNT7_plant cd14013
Catalytic domain of the Serine/Threonine kinase, Plant SNT7; STKs catalyze the transfer of the ...
514-686 5.48e-06

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: 48.97  E-value: 5.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 514 RSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacGEIKITDFGLSKimdDDSYGV-----DGMdLTSQgagtywY 588
Cdd:cd14013  123 KSIMRQILVALRKLHSTG--IVHRDVKPQNIIVSEGD--GQFKIIDLGAAA---DLRIGInyipkEFL-LDPR------Y 188
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 589 LPPECFVVGKE----PPKI--------------SNKVDVWSVGVIFFQCLygrkpFGHNQSQQDILQENTILKATEVQFP 650
Cdd:cd14013  189 APPEQYIMSTQtpsaPPAPvaaalspvlwqmnlPDRFDMYSAGVILLQMA-----FPNLRSDSNLIAFNRQLKQCDYDLN 263
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 211971036 651 -----VKPVVSSEAKA--------------FIRRCLAYRKEDRFDVHQLANDPYL 686
Cdd:cd14013  264 awrmlVEPRASADLREgfeildlddgagwdLVTKLIRYKPRGRLSASAALAHPYF 318
STKc_SRPK1 cd14216
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs ...
404-546 6.03e-06

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK1 binds with high affinity the alternative splicing factor, SRSF1 (serine/arginine-rich splicing factor 1), and regiospecifically phosphorylates 10-12 serines in its RS domain. It plays a role in the regulation of pre-mRNA splicing, chromatin structure, and germ cell development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271118 [Multi-domain]  Cd Length: 349  Bit Score: 48.87  E-value: 6.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 404 LNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQlnkswrdeKKENYHKHACREYRIHKEL-----DHP---RIVKL 475
Cdd:cd14216    8 FNGRYHVIRKLGWGHFSTVWLSWDIQGKRFVAMKVVK--------SAEHYTETALDEIKLLKSVrnsdpNDPnreMVVQL 79
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 211971036 476 YDYFSL---DTDTFCTVLEYCEGNDLDFYLK-QHKLMSEKEARSIVMQIVNALRYLNEiKPPIIHYDLKPGNILL 546
Cdd:cd14216   80 LDDFKIsgvNGTHICMVFEVLGHHLLKWIIKsNYQGLPLPCVKKIIRQVLQGLDYLHT-KCRIIHTDIKPENILL 153
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
441-643 6.07e-06

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: 48.87  E-value: 6.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 441 LNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDT--DTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVM 518
Cdd:cd07876   51 VKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKslEEFQDVYLVMELMDANLCQVIHMELDHERMSYLLY 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 519 QIVNALRYLNEIKppIIHYDLKPGNILLvdGTACgEIKITDFGLSKIMDDDSygvdgmdLTSQGAGTYWYLPPECfVVGK 598
Cdd:cd07876  131 QMLCGIKHLHSAG--IIHRDLKPSNIVV--KSDC-TLKILDFGLARTACTNF-------MMTPYVVTRYYRAPEV-ILGM 197
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 211971036 599 eppKISNKVDVWSVGVIFFQCLYGRKPFghnQSQQDILQENTILK 643
Cdd:cd07876  198 ---GYKENVDIWSVGCIMGELVKGSVIF---QGTDHIDQWNKVIE 236
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
459-620 9.13e-06

Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyk2 is widely expressed in many tissues. It is involved in signaling via the cytokine receptors IFN-alphabeta, IL-6, IL-10, IL-12, IL-13, and IL-23. It mediates cell surface urokinase receptor (uPAR) signaling and plays a role in modulating vascular smooth muscle cell (VSMC) functional behavior in response to injury. Tyk2 is also important in dendritic cell function and T helper (Th)1 cell differentiation. A homozygous mutation of Tyk2 was found in a patient with hyper-IgE syndrome (HIES), a primary immunodeficiency characterized by recurrent skin abscesses, pneumonia, and elevated serum IgE. This suggests that Tyk2 may play important roles in multiple cytokine signaling involved in innate and adaptive immunity. Tyk2 is a member of the Janus kinase (Jak) subfamily of proteins, which are cytoplasmic (or nonreceptor) PTKs containing an N-terminal FERM domain, followed by a Src homology 2 (SH2) domain, a pseudokinase domain, and a C-terminal tyr kinase catalytic domain. Jaks are crucial for cytokine receptor signaling. They are activated by autophosphorylation upon cytokine-induced receptor aggregation, and subsequently trigger downstream signaling events such as the phosphorylation of signal transducers and activators of transcription (STATs). The Tyk2 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270664 [Multi-domain]  Cd Length: 283  Bit Score: 47.97  E-value: 9.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLDTD-TFCTVLEYCEGNDLDFYLKQHKLmSEKEARSIVMQIVNALRYLNEIKppIIHY 537
Cdd:cd05080   55 QEIDILKTLYHENIVKYKGCCSEQGGkSLQLIMEYVPLGSLRDYLPKHSI-GLAQLLLFAQQICEGMAYLHSQH--YIHR 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLVDGTAcgeIKITDFGLSKIMDDdsyGVDGMDLTSQGAGTYWYLPPECFvvgKEpPKISNKVDVWSVGVIFF 617
Cdd:cd05080  132 DLAARNVLLDNDRL---VKIGDFGLAKAVPE---GHEYYRVREDGDSPVFWYAPECL---KE-YKFYYASDVWSFGVTLY 201

                 ...
gi 211971036 618 QCL 620
Cdd:cd05080  202 ELL 204
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
518-626 9.28e-06

Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Chk is also referred to as megakaryocyte-associated tyrosine kinase (Matk). Chk inhibits Src kinases using a noncatalytic mechanism by simply binding to them. As a negative regulator of Src kinases, Chk may play important roles in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Chk is expressed in brain and hematopoietic cells. Like Csk, it is a cytoplasmic (or nonreceptor) tyr kinase containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases that are anchored to the plasma membrane, Chk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Studies in mice reveal that Chk is not functionally redundant with Csk and that it plays an important role as a regulator of immune responses. Chk also plays a role in neural differentiation in a manner independent of Src by enhancing Mapk activation via Ras-mediated signaling. The Chk subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270666 [Multi-domain]  Cd Length: 254  Bit Score: 47.95  E-value: 9.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 518 MQIVNALRYLNEIKppIIHYDLKPGNILLVDGtacGEIKITDFGLSKImddDSYGVDGMDLTSQgagtywYLPPECFVVG 597
Cdd:cd05083  107 LDVAEGMEYLESKK--LVHRDLAARNILVSED---GVAKISDFGLAKV---GSMGVDNSRLPVK------WTAPEALKNK 172
                         90       100       110
                 ....*....|....*....|....*....|
gi 211971036 598 KeppkISNKVDVWSVGVIFFQCL-YGRKPF 626
Cdd:cd05083  173 K----FSSKSDVWSYGVLLWEVFsYGRAPY 198
PK_GC_unk cd14045
Pseudokinase domain of the unknown subfamily of membrane Guanylate Cyclase receptors; The ...
428-618 1.06e-05

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


Pssm-ID: 270947 [Multi-domain]  Cd Length: 269  Bit Score: 47.93  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 428 LYEQRYAAVKIHQ-----LNKSWRDEKKENyhkhacreyrihKELDHPRIVKLYDYfSLDTDTFCTVLEYCEGNDL-DFY 501
Cdd:cd14045   27 IYDGRTVAIKKIAkksftLSKRIRKEVKQV------------RELDHPNLCKFIGG-CIEVPNVAIITEYCPKGSLnDVL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 502 LKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACgeiKITDFGLSKIMDDDSygvdgmdltSQ 581
Cdd:cd14045   94 LNEDIPLNWGFRFSFATDIARGMAYLHQHK--IYHGRLKSSNCVIDDRWVC---KIADYGLTTYRKEDG---------SE 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 211971036 582 GAGTYW------YLPPECFVVGKEPPkiSNKVDVWSVGVIFFQ 618
Cdd:cd14045  160 NASGYQqrlmqvYLPPENHSNTDTEP--TQATDVYSYAIILLE 200
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
470-674 1.23e-05

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: 47.54  E-value: 1.23e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 470 PRIVKLYDYFsLDTDTFCTVLEYCEGNDLDFYL-------KQHKLMSEKEARSIV---------------MQIVNALRYL 527
Cdd:cd05576   51 PNMVCLRKYI-ISEESVFLVLQHAEGGKLWSYLskflndkEIHQLFADLDERLAAasrfyipeeciqrwaAEMVVALDAL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 528 NEikPPIIHYDLKPGNILLVDGtacGEIKITDFGLSKIMDD--DSYGVDGMdltsqgagtywYLPPECFVVGKEppkiSN 605
Cdd:cd05576  130 HR--EGIVCRDLNPNNILLNDR---GHIQLTYFSRWSEVEDscDSDAIENM-----------YCAPEVGGISEE----TE 189
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 211971036 606 KVDVWSVGVIFFQCLYGRK-----PFGhnqsqqdilqentILKATEVQFPvkPVVSSEAKAFIRRCLAYRKEDR 674
Cdd:cd05576  190 ACDWWSLGALLFELLTGKAlvechPAG-------------INTHTTLNIP--EWVSEEARSLLQQLLQFNPTER 248
Bud32 COG3642
tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and ...
459-574 1.42e-05

tRNA A-37 threonylcarbamoyl transferase component Bud32 [Translation, ribosomal structure and biogenesis]; tRNA A-37 threonylcarbamoyl transferase component Bud32 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 442859 [Multi-domain]  Cd Length: 159  Bit Score: 45.72  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKEL-----DHPRIvklYDYfslDTDTFCTVLEYCEGNDLDFYLKQHKLMSEkearsIVMQIVNALRYLNEIKpp 533
Cdd:COG3642    5 REARLLRELreagvPVPKV---LDV---DPDDADLVMEYIEGETLADLLEEGELPPE-----LLRELGRLLARLHRAG-- 71
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 211971036 534 IIHYDLKPGNILLVDgtacGEIKITDFGLSKIMDDDS-YGVD 574
Cdd:COG3642   72 IVHGDLTTSNILVDD----GGVYLIDFGLARYSDPLEdKAVD 109
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
419-625 1.44e-05

Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine or tyrosine residues on protein substrates. This group is composed of uncharacterized proteins with similarity to LIMK and Testicular or testis-specific protein kinase (TESK). LIMKs are characterized as serine/threonine kinases (STKs) while TESKs are dual-specificity protein kinases. Both LIMK and TESK phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They are implicated in many cellular functions including cell spreading, motility, morphogenesis, meiosis, mitosis, and spermatogenesis. The LIMK-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: 271058 [Multi-domain]  Cd Length: 256  Bit Score: 47.13  E-value: 1.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKIHQlNKSWRDEkkenyhkhACREYRIHKELDHPRIVKlYDYFSLDTDTFCTVLEYCEGNDL 498
Cdd:cd14156    6 FSKVYKVTHGATGKVMVVKIYK-NDVDQHK--------IVREISLLQKLSHPNIVR-YLGICVKDEKLHPILEYVSGGCL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 499 DFYLKQHKL-MSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTACGEIKITDFGLSKIMDDDSYGVDGMD 577
Cdd:cd14156   76 EELLAREELpLSWREKVELACDISRGMVYLHSKN--IYHRDLNSKNCLIRVTPRGREAVVTDFGLAREVGEMPANDPERK 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 211971036 578 LTSqgAGTYWYLPPEcfVVGKEPpkISNKVDVWSVGVIFFQCLyGRKP 625
Cdd:cd14156  154 LSL--VGSAFWMAPE--MLRGEP--YDRKVDVFSFGIVLCEIL-ARIP 194
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
497-672 1.68e-05

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: 47.04  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 497 DLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGtACGEIKITDFGLSKIMDDDSygvdgm 576
Cdd:cd13976   70 DLHSYVRSRKRLREPEAARLFRQIASAVAHCHR--NGIVLRDLKLRKFVFADE-ERTKLRLESLEDAVILEGED------ 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 577 DLTSQGAGTYWYLPPECFVVGKEppkISNK-VDVWSVGVIFFQCLYGRKPFghnqsqQDILQENTILKATEVQFPVKPVV 655
Cdd:cd13976  141 DSLSDKHGCPAYVSPEILNSGAT---YSGKaADVWSLGVILYTMLVGRYPF------HDSEPASLFAKIRRGQFAIPETL 211
                        170
                 ....*....|....*..
gi 211971036 656 SSEAKAFIRRCLayRKE 672
Cdd:cd13976  212 SPRARCLIRSLL--RRE 226
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
388-626 1.89e-05

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: 47.35  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 388 KRINNEDNSQFKDHP-TLNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKE 466
Cdd:cd07875    5 KRDNNFYSVEIGDSTfTVLKRYQNLKPIGSGAQGIVCAAYDAILERNVAIK-----KLSRPFQNQTHAKRAYRELVLMKC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 467 LDHPRIVKLYDYFSLDT--DTFCTVLEYCEGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNI 544
Cdd:cd07875   80 VNHKNIIGLLNVFTPQKslEEFQDVYIVMELMDANLCQVIQMELDHERMSYLLYQMLCGIKHLHSAG--IIHRDLKPSNI 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 545 LLvdGTACgEIKITDFGLSKImdddsygvdgmdltsqgAGTYWYLPPECFVVGKEPPKI------SNKVDVWSVGVIFFQ 618
Cdd:cd07875  158 VV--KSDC-TLKILDFGLART-----------------AGTSFMMTPYVVTRYYRAPEVilgmgyKENVDIWSVGCIMGE 217

                 ....*...
gi 211971036 619 CLYGRKPF 626
Cdd:cd07875  218 MIKGGVLF 225
STKc_ACVR1_ALK1 cd14142
Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin ...
435-618 2.00e-05

Catalytic domain of the Serine/Threonine Kinases, Activin Type I Receptor and Activin receptor-Like Kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR1, also called Activin receptor-Like Kinase 2 (ALK2), and ALK1 act as receptors for bone morphogenetic proteins (BMPs) and they activate SMAD1/5/8. ACVR1 is widely expressed while ALK1 is limited mainly to endothelial cells. The specificity of BMP binding to type I receptors is affected by type II receptors. ACVR1 binds BMP6/7/9/10 and can also bind anti-Mullerian hormone (AMH) in the presence of AMHR2. ALK1 binds BMP9/10 as well as TGFbeta in endothelial cells. A missense mutation in the GS domain of ACVR1 causes fibrodysplasia ossificans progressiva, a complex and disabling disease characterized by congenital skeletal malformations and extraskeletal bone formation. ACVR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors, and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like ACVR1 and ALK1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The ACVR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271044 [Multi-domain]  Cd Length: 298  Bit Score: 47.05  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 435 AVKIHqlnkSWRDEKKENyhkhacREYRIHKE--LDHPRIVKLY--DYFSLDTDT-FCTVLEYCEGNDLDFYLKQHKLMS 509
Cdd:cd14142   32 AVKIF----SSRDEKSWF------RETEIYNTvlLRHENILGFIasDMTSRNSCTqLWLITHYHENGSLYDYLQRTTLDH 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 510 EKEARsIVMQIVNALRYLN-EI-----KPPIIHYDLKPGNILL-VDGTACgeikITDFGLSKImddDSYGVDGMDL-TSQ 581
Cdd:cd14142  102 QEMLR-LALSAASGLVHLHtEIfgtqgKPAIAHRDLKSKNILVkSNGQCC----IADLGLAVT---HSQETNQLDVgNNP 173
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 211971036 582 GAGTYWYLPPE---------CFVVGKeppkisnKVDVWSVGVIFFQ 618
Cdd:cd14142  174 RVGTKRYMAPEvldetintdCFESYK-------RVDIYAFGLVLWE 212
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
489-618 2.53e-05

Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I Receptor and Activin Type IB/IC Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. TGFbR1, also called Activin receptor-Like Kinase 5 (ALK5), functions as a receptor for TGFbeta and phoshorylates SMAD2/3. TGFbeta proteins are cytokines that regulate cell growth, differentiation, and survival, and are critical in the development and progression of many human cancers. Mutations in TGFbR1 (and TGFbR2) can cause aortic aneurysm disorders such as Loeys-Dietz and Marfan syndromes. ACVR1b (also called ALK4) and ACVR1c (also called ALK7) act as receptors for activin A and B, respectively. TGFbR1, ACVR1b, and ACVR1c belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, bone morphogenetic proteins, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like TGFbR1, ACVR1b, and ACVR1c, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The TGFbR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271045 [Multi-domain]  Cd Length: 288  Bit Score: 46.67  E-value: 2.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 489 VLEYCEGNDLDFYLKQHKLMSEKEARsIVMQIVNALRYL-NEI-----KPPIIHYDLKPGNILL-VDGTACgeikITDFG 561
Cdd:cd14143   71 VSDYHEHGSLFDYLNRYTVTVEGMIK-LALSIASGLAHLhMEIvgtqgKPAIAHRDLKSKNILVkKNGTCC----IADLG 145
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 562 LSKIMDDDSygvDGMDLTS-QGAGTYWYLPPECF--VVGKEPPKISNKVDVWSVGVIFFQ 618
Cdd:cd14143  146 LAVRHDSAT---DTIDIAPnHRVGTKRYMAPEVLddTINMKHFESFKRADIYALGLVFWE 202
PK_NRBP1 cd14034
Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows ...
466-565 3.67e-05

Pseudokinase domain of Nuclear Receptor Binding Protein 1; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity and/or ATP binding. NRBP1, also called MLF1-adaptor molecule (MADM), was originally named based on the presence of nuclear binding and localization motifs prior to functional analyses. It is expressed ubiquitously and is found to localize in the cytoplasm, not the nucleus. NRBP1 is an adaptor protein that interacts with myeloid leukemia factor 1 (MLF1), an oncogene that enhances myeloid development of hematopoietic cells. It also interacts with the small GTPase Rac3. NRBP1 may also be involved in Golgi to ER trafficking and actin dynamics. The NRBP1-like 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: 270936 [Multi-domain]  Cd Length: 277  Bit Score: 46.28  E-value: 3.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 466 ELDHPRIVKLYDYFSLDTDTFCTVL---EYCEGNDLDFYLKQ----HKLMSEKEARSIVMQIVNALRYLNEIKPPIIHyd 538
Cdd:cd14034   66 QLEHLNIVKFHKYWADVKENRARVIfitEYMSSGSLKQFLKKtkknHKTMNEKAWKRWCTQILSALSYLHSCDPPIIH-- 143
                         90       100
                 ....*....|....*....|....*..
gi 211971036 539 lkpGNIllvdgtACGEIKITDFGLSKI 565
Cdd:cd14034  144 ---GNL------TCDTIFIQHNGLIKI 161
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
489-618 3.84e-05

Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The PDGFR subfamily consists of PDGFR alpha, PDGFR beta, KIT, CSF-1R, the mammalian FLT3, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with five immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. PDGFR kinase domains are autoinhibited by their juxtamembrane regions containing tyr residues. The binding to their ligands leads to receptor dimerization, trans phosphorylation and activation, and intracellular signaling. PDGFR subfamily receptors are important in the development of a variety of cells. PDGFRs are expressed in a many cells including fibroblasts, neurons, endometrial cells, mammary epithelial cells, and vascular smooth muscle cells. PDGFR signaling is critical in normal embryonic development, angiogenesis, and wound healing. Kit is important in the development of melanocytes, germ cells, mast cells, hematopoietic stem cells, the interstitial cells of Cajal, and the pacemaker cells of the GI tract. CSF-1R signaling is critical in the regulation of macrophages and osteoclasts. Mammalian FLT3 plays an important role in the survival, proliferation, and differentiation of stem cells. The PDGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 133186 [Multi-domain]  Cd Length: 302  Bit Score: 46.32  E-value: 3.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 489 VLEYCEGNDLDFYL--KQHKLMSEKEARSIVMQIVNALRYLNEikPPIIHYDLKPGNILLVDGTAcgeIKITDFGLSK-I 565
Cdd:cd05055  117 ITEYCCYGDLLNFLrrKRESFLTLEDLLSFSYQVAKGMAFLAS--KNCIHRDLAARNVLLTHGKI---VKICDFGLARdI 191
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 211971036 566 MDDDSYGVDGmdltSQGAGTYWYLPPECFvvgkePPKISNKVDVWSVGVIFFQ 618
Cdd:cd05055  192 MNDSNYVVKG----NARLPVKWMAPESIF-----NCVYTFESDVWSYGILLWE 235
STKc_KIS cd14020
Catalytic domain of the Serine/Threonine Kinase, Kinase Interacting with Stathmin (also called ...
469-633 3.98e-05

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: 46.08  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 469 HPRIVKLY----DYFSLDTDTFCTVLEYcegndLDFYLKQHKLMSEKEARSIVM------QIVNALRYLNeiKPPIIHYD 538
Cdd:cd14020   63 HRNIVTLYgvftNHYSANVPSRCLLLEL-----LDVSVSELLLRSSNQGCSMWMiqhcarDVLEALAFLH--HEGYVHAD 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 539 LKPGNILLVDGTACgeIKITDFGLS--------KIMDDDSYGVDGMDLTSQGAGTYWYLPPECfvvgkeppkiSNKVDVW 610
Cdd:cd14020  136 LKPRNILWSAEDEC--FKLIDFGLSfkegnqdvKYIQTDGYRAPEAELQNCLAQAGLQSETEC----------TSAVDLW 203
                        170       180
                 ....*....|....*....|...
gi 211971036 611 SVGVIFFQCLYGRKPFGHNQSQQ 633
Cdd:cd14020  204 SLGIVLLEMFSGMKLKHTVRSQE 226
STKc_SRPK3 cd14218
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs ...
404-546 4.05e-05

Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. SRPK3 is highly expressed in the heart and skeletal muscles, and is controlled by a muscle-specific enhancer that is regulated by MEF2. It may play an important role in muscle development. SRPKs phosphorylate and regulate splicing factors from the SR protein family by specifically phosphorylating multiple serine residues residing in SR/RS dipeptide motifs (also known as RS domains). Phosphorylation of the RS domains enhances interaction with transportin SR and facilitates entry of the SR proteins into the nucleus. SRPKs contain a nonconserved insert domain, within the well-conserved catalytic kinase domain, that regulates their subcellular localization. The SRPK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271120 [Multi-domain]  Cd Length: 365  Bit Score: 46.55  E-value: 4.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 404 LNERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKIHQLNKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDT 483
Cdd:cd14218    8 FNGRYHVVRKLGWGHFSTVWLCWDIQRKRFVALKVVKSAVHYTETAVDEIKLLKCVRDSDPSDPKRETIVQLIDDFKISG 87
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 211971036 484 DT---FCTVLEYCEGNDLDFYLK-QHKLMSEKEARSIVMQIVNALRYLNeIKPPIIHYDLKPGNILL 546
Cdd:cd14218   88 VNgvhVCMVLEVLGHQLLKWIIKsNYQGLPLPCVKSILRQVLQGLDYLH-TKCKIIHTDIKPENILM 153
PTKc_VEGFR1 cd14207
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
515-650 5.02e-05

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR1 (or Flt1) binds VEGFA, VEGFB, and placenta growth factor (PLGF). It regulates monocyte and macrophage migration, vascular permeability, haematopoiesis, and the recruitment of haematopietic progenitor cells from the bone marrow. VEGFR1 is a member of the VEGFR subfamily of proteins, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. The VEGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271109 [Multi-domain]  Cd Length: 340  Bit Score: 46.15  E-value: 5.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 515 SIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSKimddDSYgvDGMDLTSQGAGTY---WYLPP 591
Cdd:cd14207  184 SYSFQVARGMEFLSSRK--CIHRDLAARNILLSENNV---VKICDFGLAR----DIY--KNPDYVRKGDARLplkWMAPE 252
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 211971036 592 ECFvvgkepPKI-SNKVDVWSVGVIFFQCL-YGRKPFGHNQSQQDI---LQENTILKATEVQFP 650
Cdd:cd14207  253 SIF------DKIySTKSDVWSYGVLLWEIFsLGASPYPGVQIDEDFcskLKEGIRMRAPEFATS 310
PK_KSR2 cd14153
Pseudokinase domain of Kinase Suppressor of Ras 2; The pseudokinase domain shows similarity to ...
459-674 6.13e-05

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


Pssm-ID: 271055 [Multi-domain]  Cd Length: 270  Bit Score: 45.38  E-value: 6.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVkLYDYFSLDTDTFCTVLEYCEGNDLDFYLKQHKLMSE-KEARSIVMQIVNALRYLNeiKPPIIHY 537
Cdd:cd14153   45 REVMAYRQTRHENVV-LFMGACMSPPHLAIITSLCKGRTLYSVVRDAKVVLDvNKTRQIAQEIVKGMGYLH--AKGILHK 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 538 DLKPGNILLVDGtacgEIKITDFGLSKIMDDDSYGVDGMDLTSQgAGTYWYLPPEcfVVGKEPPK-------ISNKVDVW 610
Cdd:cd14153  122 DLKSKNVFYDNG----KVVITDFGLFTISGVLQAGRREDKLRIQ-SGWLCHLAPE--IIRQLSPEteedklpFSKHSDVF 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 211971036 611 SVGVIFFQcLYGRK-PFGHNQSQQDILQENTILKATEVQFPVKPVVSSeakaFIRRCLAYRKEDR 674
Cdd:cd14153  195 AFGTIWYE-LHAREwPFKTQPAEAIIWQVGSGMKPNLSQIGMGKEISD----ILLFCWAYEQEER 254
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
419-592 6.65e-05

Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and Anti-Muellerian Hormone Type II Receptors; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR2 and AMHR2 belong to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, activins, growth and differentiation factors (GDFs), and AMH, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane region, and a cytoplasmic catalytic kinase domain. Type II receptors are high-affinity receptors which bind ligands, autophosphorylate, as well as trans-phosphorylate and activate low-affinity type I receptors. BMPR2 and AMHR2 act primarily as a receptor for BMPs and AMH, respectively. BMPs induce bone and cartilage formation, as well as regulate tooth, kidney, skin, hair, haematopoietic, and neuronal development. Mutations in BMPR2A is associated with familial pulmonary arterial hypertension. AMH is mainly responsible for the regression of Mullerian ducts during male sex differentiation. It is expressed exclusively by somatic cells of the gonads. Mutations in either AMH or AMHR2 cause persistent Mullerian duct syndrome (PMDS), a rare form of male pseudohermaphroditism characterized by the presence of Mullerian derivatives (ovary and tubes) in otherwise normally masculine males. The BMPR2/AMHR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270956 [Multi-domain]  Cd Length: 300  Bit Score: 45.43  E-value: 6.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAfdLYEQRYAAVKIhqLNKSWRDekkeNYHKhacrEYRIHK--ELDHPRIVKLY---DYFSLDTDT-FCTVLEY 492
Cdd:cd14054    8 YGTVWKG--SLDERPVAVKV--FPARHRQ----NFQN----EKDIYElpLMEHSNILRFIgadERPTADGRMeYLLVLEY 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 493 CEGNDLDFYLKQHKL---MSEKEARSIVmqivNALRYLNE-------IKPPIIHYDLKPGNILL-VDGTACgeikITDFG 561
Cdd:cd14054   76 APKGSLCSYLRENTLdwmSSCRMALSLT----RGLAYLHTdlrrgdqYKPAIAHRDLNSRNVLVkADGSCV----ICDFG 147
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 211971036 562 LSKIMDDDSYGVDGMDLTSQGA----GTYWYLPPE 592
Cdd:cd14054  148 LAMVLRGSSLVRGRPGAAENASisevGTLRYMAPE 182
PTKc_Wee1b cd14139
Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the ...
419-546 6.93e-05

Catalytic domain of the Protein Tyrosine Kinase, Wee1b; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. This subfamily is composed of human Wee1b (also called Wee2), Xenopus laevis Wee1a (XeWee1a) and similar vertebrate proteins. XeWee1a accumulates after exiting the metaphase II stage in oocytes and in early mitotic cells. It functions during the first zygotic cell division and not during subsequent divisions. Mammalian Wee2/Wee1b is an oocyte-specific inhibitor of meiosis that functions downstream of cAMP. 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 Wee1b 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: 271041 [Multi-domain]  Cd Length: 274  Bit Score: 45.30  E-value: 6.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 419 FSEVYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKEL-DHPRIVKLYDYFSLDtDTFCTVLEYCEGND 497
Cdd:cd14139   13 FGSVYKCIKRLDGCVYAIK-----RSMRPFAGSSNEQLALHEVYAHAVLgHHPHVVRYYSAWAED-DHMIIQNEYCNGGS 86
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 211971036 498 LDFYL----KQHKLMSEKEARSIVMQIVNALRYLNeiKPPIIHYDLKPGNILL 546
Cdd:cd14139   87 LQDAIsentKSGNHFEEPELKDILLQVSMGLKYIH--NSGLVHLDIKPSNIFI 137
EnvC COG4942
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ...
157-378 7.97e-05

Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443969 [Multi-domain]  Cd Length: 377  Bit Score: 45.53  E-value: 7.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 157 KQLSFKIIQTDLTMLKLAALESNKIQDLEKKEGRIDDLLRANCDLRRQIDEQQKLLEKYKERLNKcisMSKKLlieKSTQ 236
Cdd:COG4942   30 EQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAE---LRAEL---EAQK 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 237 EKLSSREKSMQDRLRLGHFTTVRHGASFTEQWTDGFAFQNLVKQQEwvnQQREDIERQRKLLAKRKPPTANNSQAPSTNS 316
Cdd:COG4942  104 EELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLQYLKYLAPARR---EQAEELRADLAELAALRAELEAERAELEALL 180
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 211971036 317 EPKQRKNKAVNGAENDpfvrpnlpQLLTLAEYHEQEEIFKLRLGHLKKEEAEIQAELERLER 378
Cdd:COG4942  181 AELEEERAALEALKAE--------RQKLLARLEKELAELAAELAELQQEAEELEALIARLEA 234
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
422-615 1.17e-04

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: 45.08  E-value: 1.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 422 VYKAFDLYEQRYAAVKihqlnKSWRDEKKENYHKHACREYRIHKELDHPRIVKLYDYFSLDT--DTFCTVLEYCEGNDLD 499
Cdd:cd07874   33 VCAAYDAVLDRNVAIK-----KLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKslEEFQDVYLVMELMDAN 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 500 FYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLvdGTACgEIKITDFGLSKImdddsygvdgmdlt 579
Cdd:cd07874  108 LCQVIQMELDHERMSYLLYQMLCGIKHLHSAG--IIHRDLKPSNIVV--KSDC-TLKILDFGLART-------------- 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 211971036 580 sqgAGTYWYLPPECFVVGKEPPKI------SNKVDVWSVGVI 615
Cdd:cd07874  169 ---AGTSFMMTPYVVTRYYRAPEVilgmgyKENVDIWSVGCI 207
PTZ00284 PTZ00284
protein kinase; Provisional
406-546 1.80e-04

protein kinase; Provisional


Pssm-ID: 140307 [Multi-domain]  Cd Length: 467  Bit Score: 44.57  E-value: 1.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 406 ERYLLLHLLGRGGFSEVYKAFDLYEQRYAAVKI-HQLNKSWRDEKKENYHKHACREYRIHkelDHPRIVKLYDYFSLDTD 484
Cdd:PTZ00284 129 QRFKILSLLGEGTFGKVVEAWDRKRKEYCAVKIvRNVPKYTRDAKIEIQFMEKVRQADPA---DRFPLMKIQRYFQNETG 205
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 211971036 485 TFCTVLEYCEGNDLDFYLKqHKLMSEKEARSIVMQIVNALRYLN-EIKppIIHYDLKPGNILL 546
Cdd:PTZ00284 206 HMCIVMPKYGPCLLDWIMK-HGPFSHRHLAQIIFQTGVALDYFHtELH--LMHTDLKPENILM 265
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
490-626 2.56e-04

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Alternative splicing of FGFR1 transcripts produces a variety of isoforms, which are differentially expressed in cells. FGFR1 binds the ligands, FGF1 and FGF2, with high affinity and has also been reported to bind FGF4, FGF6, and FGF9. FGFR1 signaling is critical in the control of cell migration during embryo development. It promotes cell proliferation in fibroblasts. Nuclear FGFR1 plays a role in the regulation of transcription. Mutations, insertions or deletions of FGFR1 have been identified in patients with Kallman's syndrome (KS), an inherited disorder characterized by hypogonadotropic hypogonadism and loss of olfaction. Aberrant FGFR1 expression has been found in some human cancers including 8P11 myeloproliferative syndrome (EMS), breast cancer, and pancreatic adenocarcinoma. FGFR1 is part of the FGFR subfamily, which are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, results in receptor dimerization and activation, and intracellular signaling. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. The FGFR1 subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270678 [Multi-domain]  Cd Length: 302  Bit Score: 43.85  E-value: 2.56e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 490 LEYCEGNDLDfylkQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSKimddD 569
Cdd:cd05098  118 MEYCYNPSHN----PEEQLSSKDLVSCAYQVARGMEYLASKK--CIHRDLAARNVLVTEDNV---MKIADFGLAR----D 184
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 570 SYGVDGMDLTSQGAGTYWYLPPECFVvgkepPKI-SNKVDVWSVGVIFFQCL-YGRKPF 626
Cdd:cd05098  185 IHHIDYYKKTTNGRLPVKWMAPEALF-----DRIyTHQSDVWSFGVLLWEIFtLGGSPY 238
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
450-618 3.78e-04

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 43.73  E-value: 3.78e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 450 KENYHKHACREYRIHKELDHPRIVKLYDYFSLDTDTfCTVL-EYceGNDLDFYL-KQHKLMSEKEARSIVMQIVNALRYL 527
Cdd:PHA03211 200 KAGWYASSVHEARLLRRLSHPAVLALLDVRVVGGLT-CLVLpKY--RSDLYTYLgARLRPLGLAQVTAVARQLLSAIDYI 276
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 528 NeiKPPIIHYDLKPGNIlLVDGTAcgEIKITDFGLSKIMDDD-----SYGVdgmdltsqgAGTYWYLPPEcfVVGKEPpk 602
Cdd:PHA03211 277 H--GEGIIHRDIKTENV-LVNGPE--DICLGDFGAACFARGSwstpfHYGI---------AGTVDTNAPE--VLAGDP-- 338
                        170
                 ....*....|....*.
gi 211971036 603 ISNKVDVWSVGVIFFQ 618
Cdd:PHA03211 339 YTPSVDIWSAGLVIFE 354
STKc_BMPR1 cd14144
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; ...
489-618 4.52e-04

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type I Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1 functions as a receptor for morphogenetic proteins (BMPs), which are involved in the regulation of cell proliferation, survival, differentiation, and apoptosis. BMPs are able to induce bone, cartilage, ligament, and tendon formation, and may play roles in bone diseases and tumors. Vertebrates contain two type I BMP receptors, BMPR1a and BMPR1b. BMPR1 belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that also includes TGFbeta, activins, growth and differentiation factors, and anti-Mullerian hormone, among others. These receptors contain an extracellular domain that binds ligands, a single transmembrane (TM) region, and a cytoplasmic catalytic kinase domain. Type I receptors, like BMPR1, are low-affinity receptors that bind ligands only after they are recruited by the ligand/type II high-affinity receptor complex. Following activation, they start intracellular signaling to the nucleus by phosphorylating SMAD proteins. Type I receptors contain an additional domain located between the TM and kinase domains called the GS domain, which contains the activating phosphorylation site and confers preference for specific SMAD proteins. The BMPR1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271046 [Multi-domain]  Cd Length: 287  Bit Score: 42.85  E-value: 4.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 489 VLEYCEGNDLDFYLKQHKLMSEKEARsIVMQIVNALRYLN-EI-----KPPIIHYDLKPGNILL-VDGTACgeikITDFG 561
Cdd:cd14144   71 ITDYHENGSLYDFLRGNTLDTQSMLK-LAYSAACGLAHLHtEIfgtqgKPAIAHRDIKSKNILVkKNGTCC----IADLG 145
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 211971036 562 LSKIMDDDSYGVDGMDLTSQgaGTYWYLPPECF--VVGKEPPKISNKVDVWSVGVIFFQ 618
Cdd:cd14144  146 LAVKFISETNEVDLPPNTRV--GTKRYMAPEVLdeSLNRNHFDAYKMADMYSFGLVLWE 202
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
459-616 5.08e-04

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK1 activation is induced by bone morphogenic protein, vascular endothelial growth factor, and thrombin. It plays roles in microtubule disassembly and cell cycle progression, and is critical in the regulation of neurite outgrowth. LIMK1 knockout mice show abnormalities in dendritic spine morphology and synaptic function. LIMK1 is one of the genes deleted in patients with Williams Syndrome, which is characterized by distinct craniofacial features, cardiovascular problems, as well as behavioral and neurological abnormalities. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. The LIMK1 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271123 [Multi-domain]  Cd Length: 267  Bit Score: 42.64  E-value: 5.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 459 REYRIHKELDHPRIVKLYDYFSLDTD-TFCTvlEYCEGNDLDFYLKQHKLMSEKEAR-SIVMQIVNALRYLNEIKppIIH 536
Cdd:cd14221   39 KEVKVMRCLEHPNVLKFIGVLYKDKRlNFIT--EYIKGGTLRGIIKSMDSHYPWSQRvSFAKDIASGMAYLHSMN--IIH 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 537 YDLKPGNILLVDGtacGEIKITDFGLSKIMDDDSYGVDGMDLTSQG--------AGTYWYLPPEcFVVGKEppkISNKVD 608
Cdd:cd14221  115 RDLNSHNCLVREN---KSVVVADFGLARLMVDEKTQPEGLRSLKKPdrkkrytvVGNPYWMAPE-MINGRS---YDEKVD 187

                 ....*...
gi 211971036 609 VWSVGVIF 616
Cdd:cd14221  188 VFSFGIVL 195
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
473-642 5.22e-04

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: 42.70  E-value: 5.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 473 VKLYDYFSLDTDtFCTVLEYCEGNDLDFyLKQHKLM--SEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDG- 549
Cdd:cd14215   78 VQMFDWFDYHGH-MCISFELLGLSTFDF-LKENNYLpyPIHQVRHMAFQVCQAVKFLHDNK--LTHTDLKPENILFVNSd 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 550 ---------------TACGEIKITDFGlSKIMDDDSYgvdgmdltSQGAGTYWYLPPECFV-VGKEPPkisnkVDVWSVG 613
Cdd:cd14215  154 yeltynlekkrdersVKSTAIRVVDFG-SATFDHEHH--------STIVSTRHYRAPEVILeLGWSQP-----CDVWSIG 219
                        170       180
                 ....*....|....*....|....*....
gi 211971036 614 VIFFQCLYGRKPFGHNQSQQDILQENTIL 642
Cdd:cd14215  220 CIIFEYYVGFTLFQTHDNREHLAMMERIL 248
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
447-615 5.40e-04

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMKs phosphorylate and inactivate cofilin, an actin depolymerizing factor, to induce the reorganization of the actin cytoskeleton. They act downstream of Rho GTPases and are expressed ubiquitously. As regulators of actin dynamics, they contribute to diverse cellular functions such as cell motility, morphogenesis, differentiation, apoptosis, meiosis, mitosis, and neurite extension. LIMKs contain the LIM (two repeats), PDZ, and catalytic kinase domains. Vertebrate have two members, LIMK1 and LIMK2. The LIMK subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271056 [Multi-domain]  Cd Length: 272  Bit Score: 42.49  E-value: 5.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 447 DEKKENYHKhacrEYRIHKELDHPRIVK----LYDYFSLDTdtfctVLEYCEGNDLDFYLK-QHKLMSEKEARSIVMQIV 521
Cdd:cd14154   31 EEAQRNFLK----EVKVMRSLDHPNVLKfigvLYKDKKLNL-----ITEYIPGGTLKDVLKdMARPLPWAQRVRFAKDIA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 522 NALRYLNEIKppIIHYDLKPGNILLVDGTacgEIKITDFGLSKIMDDDSYGVDGMDLTSQG--------------AGTYW 587
Cdd:cd14154  102 SGMAYLHSMN--IIHRDLNSHNCLVREDK---TVVVADFGLARLIVEERLPSGNMSPSETLrhlkspdrkkrytvVGNPY 176
                        170       180
                 ....*....|....*....|....*...
gi 211971036 588 YLPPECFvVGKeppKISNKVDVWSVGVI 615
Cdd:cd14154  177 WMAPEML-NGR---SYDEKVDIFSFGIV 200
PTKc_VEGFR cd05054
Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; ...
494-626 5.48e-04

Catalytic domain of the Protein Tyrosine Kinases, Vascular Endothelial Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The VEGFR subfamily consists of VEGFR1 (Flt1), VEGFR2 (Flk1), VEGFR3 (Flt4), and similar proteins. VEGFR subfamily members are receptor PTKss (RTKs) containing an extracellular ligand-binding region with seven immunoglobulin (Ig)-like domains, a transmembrane segment, and an intracellular catalytic domain. In VEGFR3, the fifth Ig-like domain is replaced by a disulfide bridge. The binding of VEGFRs to their ligands, the VEGFs, leads to receptor dimerization, activation, and intracellular signaling. There are five VEGF ligands in mammals, which bind, in an overlapping pattern to the three VEGFRs, which can form homo or heterodimers. VEGFRs regulate the cardiovascular system. They are critical for vascular development during embryogenesis and blood vessel formation in adults. They induce cellular functions common to other growth factor receptors such as cell migration, survival, and proliferation. The VEGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270647 [Multi-domain]  Cd Length: 298  Bit Score: 42.48  E-value: 5.48e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 494 EGNDLDFYLKQHKLMseKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTAcgeIKITDFGLSKIMDDDSygv 573
Cdd:cd05054  123 EEEDDDELYKEPLTL--EDLICYSFQVARGMEFLASRK--CIHRDLAARNILLSENNV---VKICDFGLARDIYKDP--- 192
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 211971036 574 dgmDLTSQGAGTY---WYLPPECFvvgkepPKI-SNKVDVWSVGVIFFQCL-YGRKPF 626
Cdd:cd05054  193 ---DYVRKGDARLplkWMAPESIF------DKVyTTQSDVWSFGVLLWEIFsLGASPY 241
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
489-618 6.20e-04

Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The FGFR subfamily consists of FGFR1, FGFR2, FGFR3, FGFR4, and similar proteins. They are receptor PTKs (RTKs) containing an extracellular ligand-binding region with three immunoglobulin-like domains, a transmembrane segment, and an intracellular catalytic domain. The binding of FGFRs to their ligands, the FGFs, and to heparin/heparan sulfate (HS) results in the formation of a ternary complex, which leads to receptor dimerization and activation, and intracellular signaling. There are at least 23 FGFs and four types of FGFRs. The binding of FGFs to FGFRs is promiscuous, in that a receptor may be activated by several ligands and a ligand may bind to more that one type of receptor. FGF/FGFR signaling is important in the regulation of embryonic development, homeostasis, and regenerative processes. Depending on the cell type and stage, FGFR signaling produces diverse cellular responses including proliferation, growth arrest, differentiation, and apoptosis. Aberrant signaling leads to many human diseases such as skeletal, olfactory, and metabolic disorders, as well as cancer. The FGFR subfamily is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase .


Pssm-ID: 270646 [Multi-domain]  Cd Length: 294  Bit Score: 42.40  E-value: 6.20e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 211971036 489 VLEYCEGNDLDFYLKQH----------------KLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTac 552
Cdd:cd05053   95 VVEYASKGNLREFLRARrppgeeaspddprvpeEQLTQKDLVSFAYQVARGMEYLASKK--CIHRDLAARNVLVTEDN-- 170
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 211971036 553 gEIKITDFGLSKimddDSYGVDGMDLTSQGAGTYWYLPPECfvvgkeppkISNKV-----DVWSVGVIFFQ 618
Cdd:cd05053  171 -VMKIADFGLAR----DIHHIDYYRKTTNGRLPVKWMAPEA---------LFDRVythqsDVWSFGVLLWE 227
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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