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Conserved domains on  [gi|929654453|dbj|BAA34501|]
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KIAA0781 protein [Homo sapiens]

Protein Classification

serine/threonine-protein kinase SIK2( domain architecture ID 10197334)

serine/threonine-protein kinase SIK2 (salt-inducible kinase 2) catalyzes the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates; it phosphorylates 'Ser-794' of IRS1 in insulin-stimulated adipocytes

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
19-271 0e+00

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: 592.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14071    1 FYDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCG 178
Cdd:cd14071   81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLKTWCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSK 258
Cdd:cd14071  161 SPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDPSK 240
                        250
                 ....*....|...
gi 929654453 259 RLTIAQIKEHKWM 271
Cdd:cd14071  241 RLTIEQIKKHKWM 253
UBA_SIK2 cd14409
UBA domain found in salt-inducible kinase 2 (SIK2); SIK2, also called Qin-induced kinase or ...
297-341 9.71e-22

UBA domain found in salt-inducible kinase 2 (SIK2); SIK2, also called Qin-induced kinase or serine/threonine-protein kinase SNF1-like kinase 2 (SNF1LK2), is a serine/threonine kinase highly expressed in adipocytes. It belongs to the AMP-activated protein kinases (AMPK) family involved in the regulation of metabolism during energy stress. It plays an important role in the insulin-signaling pathway during adipocyte differentiation, as well as in autophagy progression. Moreover, SIK2 plays a critical role in neuronal survival and modulates cAMP responsive element binding protein (CREB)-mediated gene expression in response to hormones and nutrients. SIK2 acts as a critical determinant in autophagy progression. In addition, SIK2 localizes at the centrosome and functions as a centrosome kinase required for bipolar mitotic spindle formation. It is involved in the initiation of mitosis, and regulates the localization of the centrosome linker protein, C-Nap1, through S2392 phosphorylation. SIK2 contains an N-terminal protein kinase catalytic domain followed by an ubiquitin-associated (UBA) domain.


:

Pssm-ID: 270592  Cd Length: 45  Bit Score: 88.92  E-value: 9.71e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 297 NEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAIYFLLVERLKSHR 341
Cdd:cd14409    1 NEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAIYYLLVERLKSHR 45
 
Name Accession Description Interval E-value
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
19-271 0e+00

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: 592.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14071    1 FYDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCG 178
Cdd:cd14071   81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLKTWCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSK 258
Cdd:cd14071  161 SPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDPSK 240
                        250
                 ....*....|...
gi 929654453 259 RLTIAQIKEHKWM 271
Cdd:cd14071  241 RLTIEQIKKHKWM 253
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
20-271 2.32e-105

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 326.79  E-value: 2.32e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453    20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDaVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIK-KDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGS 179
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFVGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   180 PPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGP-TLPILRQRVLEGRFRIPYFM---SEDCEHLIRRMLVLD 255
Cdd:smart00220 160 PEYMAPEVLLGKGY-GKAVDIWSLGVILYELLTGKPPFPGDdQLLELFKKIGKPKPPFPPPEwdiSPEAKDLIRKLLVKD 238
                          250
                   ....*....|....*.
gi 929654453   256 PSKRLTIAQIKEHKWM 271
Cdd:smart00220 239 PEKRLTAEEALQHPFF 254
Pkinase pfam00069
Protein kinase domain;
20-271 2.01e-66

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 221.35  E-value: 2.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  100 KNGEIFDYLANHGRLNESEARRKFWQILSAVdychgrkivhrdlkaenllldnnmnikiadfgfgnffKSGELLATWCGS 179
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL-------------------------------------ESGSSLTTFVGT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  180 PPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYF---MSEDCEHLIRRMLVLDP 256
Cdd:pfam00069 124 PWYMAPEVLGGNPY-GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLLKKDP 202
                         250
                  ....*....|....*
gi 929654453  257 SKRLTIAQIKEHKWM 271
Cdd:pfam00069 203 SKRLTATQALQHPWF 217
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
14-259 9.76e-56

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 200.62  E-value: 9.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  14 PVRVGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKII-DKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSML 92
Cdd:COG0515    3 ALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLrPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  93 YLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL 172
Cdd:COG0515   83 YLVMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 LAT--WCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIP----YFMSEDCEH 246
Cdd:COG0515  163 TQTgtVVGTPGYMAPEQARGEPV-DPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPselrPDLPPALDA 241
                        250
                 ....*....|...
gi 929654453 247 LIRRMLVLDPSKR 259
Cdd:COG0515  242 IVLRALAKDPEER 254
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
20-270 8.90e-49

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 176.16  E-value: 8.90e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQ-LDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNffKSGELLATWCG 178
Cdd:PTZ00263 100 VVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAK--KVPDRTFTLCG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSK 258
Cdd:PTZ00263 178 TPEYLAPEVIQSKGH-GKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTDHTK 256
                        250
                 ....*....|....*..
gi 929654453 259 RL-----TIAQIKEHKW 270
Cdd:PTZ00263 257 RLgtlkgGVADVKNHPY 273
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
20-221 8.72e-30

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 125.29  E-value: 8.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIdKSQL--DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTE 97
Cdd:NF033483   9 YEIGERIGRGGMAEVYLAKDTRLDRDVAVKVL-RPDLarDPEFVARFRREAQSAASLSHPNIVSVYDVGEDGGIPYIVME 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKS------GE 171
Cdd:NF033483  88 YVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALSSttmtqtNS 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 929654453 172 LLatwcGSPPYAAPEvfegqQYEG----PQLDIWSMGVVLYVLVCGALPFDGPT 221
Cdd:NF033483 168 VL----GTVHYLSPE-----QARGgtvdARSDIYSLGIVLYEMLTGRPPFDGDS 212
UBA_SIK2 cd14409
UBA domain found in salt-inducible kinase 2 (SIK2); SIK2, also called Qin-induced kinase or ...
297-341 9.71e-22

UBA domain found in salt-inducible kinase 2 (SIK2); SIK2, also called Qin-induced kinase or serine/threonine-protein kinase SNF1-like kinase 2 (SNF1LK2), is a serine/threonine kinase highly expressed in adipocytes. It belongs to the AMP-activated protein kinases (AMPK) family involved in the regulation of metabolism during energy stress. It plays an important role in the insulin-signaling pathway during adipocyte differentiation, as well as in autophagy progression. Moreover, SIK2 plays a critical role in neuronal survival and modulates cAMP responsive element binding protein (CREB)-mediated gene expression in response to hormones and nutrients. SIK2 acts as a critical determinant in autophagy progression. In addition, SIK2 localizes at the centrosome and functions as a centrosome kinase required for bipolar mitotic spindle formation. It is involved in the initiation of mitosis, and regulates the localization of the centrosome linker protein, C-Nap1, through S2392 phosphorylation. SIK2 contains an N-terminal protein kinase catalytic domain followed by an ubiquitin-associated (UBA) domain.


Pssm-ID: 270592  Cd Length: 45  Bit Score: 88.92  E-value: 9.71e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 297 NEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAIYFLLVERLKSHR 341
Cdd:cd14409    1 NEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAIYYLLVERLKSHR 45
 
Name Accession Description Interval E-value
STKc_SIK cd14071
Catalytic domain of the Serine/Threonine Kinases, Salt-Inducible kinases; STKs catalyze the ...
19-271 0e+00

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: 592.44  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14071    1 FYDIERTIGKGNFAVVKLARHRITKTEVAIKIIDKSQLDEENLKKIYREVQIMKMLNHPHIIKLYQVMETKDMLYLVTEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCG 178
Cdd:cd14071   81 ASNGEIFDYLAQHGRMSEKEARKKFWQILSAVEYCHKRHIVHRDLKAENLLLDANMNIKIADFGFSNFFKPGELLKTWCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSK 258
Cdd:cd14071  161 SPPYAAPEVFEGKEYEGPQLDIWSLGVVLYVLVCGALPFDGSTLQTLRDRVLSGRFRIPFFMSTDCEHLIRRMLVLDPSK 240
                        250
                 ....*....|...
gi 929654453 259 RLTIAQIKEHKWM 271
Cdd:cd14071  241 RLTIEQIKKHKWM 253
STKc_AMPK-like cd14003
Catalytic domain of AMP-activated protein kinase-like Serine/Threonine Kinases; STKs catalyze ...
20-270 1.09e-155

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: 457.36  E-value: 1.09e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14003    2 YELGKTLGEGSFGKVKLARHKLTGEKVAIKIIDKSKLKEEIEEKIKREIEIMKLLNHPNIIKLYEVIETENKIYLVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGS 179
Cdd:cd14003   82 SGGELFDYIVNNGRLSEDEARRFFQQLISAVDYCHSNGIVHRDLKLENILLDKNGNLKIIDFGLSNEFRGGSLLKTFCGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKR 259
Cdd:cd14003  162 PAYAAPEVLLGRKYDGPKADVWSLGVILYAMLTGYLPFDDDNDSKLFRKILKGKYPIPSHLSPDARDLIRRMLVVDPSKR 241
                        250
                 ....*....|.
gi 929654453 260 LTIAQIKEHKW 270
Cdd:cd14003  242 ITIEEILNHPW 252
STKc_MARK cd14072
Catalytic domain of the Serine/Threonine Kinases, MAP/microtubule affinity-regulating kinases; ...
20-271 6.78e-138

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: 411.53  E-value: 6.78e-138
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14072    2 YRLLKTIGKGNFAKVKLARHVLTGREVAIKIIDKTQLNPSSLQKLFREVRIMKILNHPNIVKLFEVIETEKTLYLVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGS 179
Cdd:cd14072   82 SGGEVFDYLVAHGRMKEKEARAKFRQIVSAVQYCHQKRIVHRDLKAENLLLDADMNIKIADFGFSNEFTPGNKLDTFCGS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKR 259
Cdd:cd14072  162 PPYAAPELFQGKKYDGPEVDVWSLGVILYTLVSGSLPFDGQNLKELRERVLRGKYRIPFYMSTDCENLLKKFLVLNPSKR 241
                        250
                 ....*....|..
gi 929654453 260 LTIAQIKEHKWM 271
Cdd:cd14072  242 GTLEQIMKDRWM 253
STKc_AMPK_alpha cd14079
Catalytic domain of the Alpha subunit of the Serine/Threonine Kinase, AMP-activated protein ...
17-271 4.96e-122

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: 370.45  E-value: 4.96e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  17 VGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNL-EKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLV 95
Cdd:cd14079    1 IGNYILGKTLGVGSFGKVKLAEHELTGHKVAVKILNRQKIKSLDMeEKIRREIQILKLFRHPHIIRLYEVIETPTDIFMV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLAT 175
Cdd:cd14079   81 MEYVSGGELFDYIVQKGRLSEDEARRFFQQIISGVEYCHRHMVVHRDLKPENLLLDSNMNVKIADFGLSNIMRDGEFLKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLD 255
Cdd:cd14079  161 SCGSPNYAAPEVISGKLYAGPEVDVWSCGVILYALLCGSLPFDDEHIPNLFKKIKSGIYTIPSHLSPGARDLIKRMLVVD 240
                        250
                 ....*....|....*.
gi 929654453 256 PSKRLTIAQIKEHKWM 271
Cdd:cd14079  241 PLKRITIPEIRQHPWF 256
STKc_BRSK1_2 cd14081
Catalytic domain of Brain-specific serine/threonine-protein kinases 1 and 2; STKs catalyze the ...
18-271 2.87e-117

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: 358.10  E-value: 2.87e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  18 GFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLE-KIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVT 96
Cdd:cd14081    1 GPYRLGKTLGKGQTGLVKLAKHCVTGQKVAIKIVNKEKLSKESVLmKVEREIAIMKLIEHPNVLKLYDVYENKKYLYLVL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATW 176
Cdd:cd14081   81 EYVSGGELFDYLVKKGRLTEKEARKFFRQIISALDYCHSHSICHRDLKPENLLLDEKNNIKIADFGMASLQPEGSLLETS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDP 256
Cdd:cd14081  161 CGSPHYACPEVIKGEKYDGRKADIWSCGVILYALLVGALPFDDDNLRQLLEKVKRGVFHIPHFISPDAQDLLRRMLEVNP 240
                        250
                 ....*....|....*
gi 929654453 257 SKRLTIAQIKEHKWM 271
Cdd:cd14081  241 EKRITIEEIKKHPWF 255
STKc_CAMK cd05117
The catalytic domain of CAMK family Serine/Threonine Kinases; STKs catalyze the transfer of ...
19-270 5.42e-112

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: 344.46  E-value: 5.42e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd05117    1 KYELGKVLGRGSFGVVRLAVHKKTGEEYAVKIIDKKKLKSEDEEMLRREIEILKRLDHPNIVKLYEVFEDDKNLYLVMEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDN---NMNIKIADFGFGNFFKSGELLAT 175
Cdd:cd05117   81 CTGGELFDRIVKKGSFSEREAAKIMKQILSAVAYLHSQGIVHRDLKPENILLASkdpDSPIKIIDFGLAKIFEEGEKLKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFM----SEDCEHLIRRM 251
Cdd:cd05117  161 VCGTPYYVAPEVLKGKGY-GKKCDIWSLGVILYILLCGYPPFYGETEQELFEKILKGKYSFDSPEwknvSEEAKDLIKRL 239
                        250
                 ....*....|....*....
gi 929654453 252 LVLDPSKRLTIAQIKEHKW 270
Cdd:cd05117  240 LVVDPKKRLTAAEALNHPW 258
STKc_NIM1 cd14075
Catalytic domain of the Serine/Threonine Kinase, NIM1; STKs catalyze the transfer of the ...
17-271 1.07e-106

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: 330.45  E-value: 1.07e-106
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  17 VGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVT 96
Cdd:cd14075    1 IGFYRIRGELGSGNFSQVKLGIHQLTKEKVAIKILDKTKLDQKTQRLLSREISSMEKLHHPNIIRLYEVVETLSKLHLVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATW 176
Cdd:cd14075   81 EYASGGELYTKISTEGKLSESEAKPLFAQIVSAVKHMHENNIIHRDLKAENVFYASNNCVKVGDFGFSTHAKRGETLNTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDP 256
Cdd:cd14075  161 CGSPPYAAPELFKDEHYIGIYVDIWALGVLLYFMVTGVMPFRAETVAKLKKCILEGTYTIPSYVSEPCQELIRGILQPVP 240
                        250
                 ....*....|....*
gi 929654453 257 SKRLTIAQIKEHKWM 271
Cdd:cd14075  241 SDRYSIDEIKNSEWL 255
S_TKc smart00220
Serine/Threonine protein kinases, catalytic domain; Phosphotransferases. Serine or ...
20-271 2.32e-105

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


Pssm-ID: 214567 [Multi-domain]  Cd Length: 254  Bit Score: 326.79  E-value: 2.32e-105
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453    20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDaVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:smart00220   1 YEILEKLGEGSFGKVYLARDKKTGKLVAIKVIKKKKIK-KDRERILREIKILKKLKHPNIVRLYDVFEDEDKLYLVMEYC 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGS 179
Cdd:smart00220  80 EGGDLFDLLKKRGRLSEDEARFYLRQILSALEYLHSKGIVHRDLKPENILLDEDGHVKLADFGLARQLDPGEKLTTFVGT 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   180 PPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGP-TLPILRQRVLEGRFRIPYFM---SEDCEHLIRRMLVLD 255
Cdd:smart00220 160 PEYMAPEVLLGKGY-GKAVDIWSLGVILYELLTGKPPFPGDdQLLELFKKIGKPKPPFPPPEwdiSPEAKDLIRKLLVKD 238
                          250
                   ....*....|....*.
gi 929654453   256 PSKRLTIAQIKEHKWM 271
Cdd:smart00220 239 PEKRLTAEEALQHPFF 254
STKc_NUAK cd14073
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK; STKs catalyze ...
20-270 1.20e-101

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: 317.02  E-value: 1.20e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14073    3 YELLETLGKGTYGKVKLAIERATGREVAIKSIKKDKIeDEQDMVRIRREIEIMSSLNHPHIIRIYEVFENKDKIVIVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCG 178
Cdd:cd14073   83 ASGGELYDYISERRRLPEREARRIFRQIVSAVHYCHKNGVVHRDLKLENILLDQNGNAKIADFGLSNLYSKDKLLQTFCG 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEhLIRRMLVLDPSK 258
Cdd:cd14073  163 SPLYASPEIVNGTPYQGPEVDCWSLGVLLYTLVYGTMPFDGSDFKRLVKQISSGDYREPTQPSDASG-LIRWMLTVNPKR 241
                        250
                 ....*....|..
gi 929654453 259 RLTIAQIKEHKW 270
Cdd:cd14073  242 RATIEDIANHWW 253
STKc_SNRK cd14074
Catalytic domain of the Serine/Threonine Kinase, SNF1-related kinase; STKs catalyze the ...
17-271 9.21e-100

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: 312.42  E-value: 9.21e-100
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  17 VGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVT 96
Cdd:cd14074    2 AGLYDLEETLGRGHFAVVKLARHVFTGEKVAVKVIDKTKLDDVSKAHLFQEVRCMKLVQHPNVVRLYEVIDTQTKLYLIL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNGEIFDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL-DNNMNIKIADFGFGNFFKSGELLA 174
Cdd:cd14074   82 ELGDGGDMYDYIMKHENgLNEDLARKYFRQIVSAISYCHKLHVVHRDLKPENVVFfEKQGLVKLTDFGFSNKFQPGEKLE 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPF----DGPTLpilrQRVLEGRFRIPYFMSEDCEHLIRR 250
Cdd:cd14074  162 TSCGSLAYSAPEILLGDEYDAPAVDIWSLGVILYMLVCGQPPFqeanDSETL----TMIMDCKYTVPAHVSPECKDLIRR 237
                        250       260
                 ....*....|....*....|.
gi 929654453 251 MLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14074  238 MLIRDPKKRASLEEIENHPWL 258
STKc_SnRK3 cd14663
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
20-270 2.16e-98

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: 308.56  E-value: 2.16e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNL-EKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14663    2 YELGRTLGEGTFAKVKFARNTKTGESVAIKIIDKEQVAREGMvEQIKREIAIMKLLRHPNIVELHEVMATKTKIFFVMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG---NFFKSGELLAT 175
Cdd:cd14663   82 VTGGELFSKIAKNGRLKEDKARKYFQQLIDAVDYCHSRGVFHRDLKPENLLLDEDGNLKISDFGLSalsEQFRQDGLLHT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLD 255
Cdd:cd14663  162 TCGTPNYVAPEVLARRGYDGAKADIWSCGVILFVLLAGYLPFDDENLMALYRKIMKGEFEYPRWFSPGAKSLIKRILDPN 241
                        250
                 ....*....|....*
gi 929654453 256 PSKRLTIAQIKEHKW 270
Cdd:cd14663  242 PSTRITVEQIMASPW 256
STKc_MELK cd14078
Catalytic domain of the Serine/Threonine Kinase, Maternal Embryonic Leucine zipper Kinase; ...
18-271 4.28e-95

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: 300.07  E-value: 4.28e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  18 GFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAvNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTE 97
Cdd:cd14078    3 KYYELHETIGSGGFAKVKLATHILTGEKVAIKIMDKKALGD-DLPRVKTEIEALKNLSHQHICRLYHVIETDNKIFMVLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSG--ELLAT 175
Cdd:cd14078   82 YCPGGELFDYIVAKDRLSEDEARVFFRQIVSAVAYVHSQGYAHRDLKPENLLLDEDQNLKLIDFGLCAKPKGGmdHHLET 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLD 255
Cdd:cd14078  162 CCGSPAYAAPELIQGKPYIGSEADVWSMGVLLYALLCGFLPFDDDNVMALYRKIQSGKYEEPEWLSPSSKLLLDQMLQVD 241
                        250
                 ....*....|....*.
gi 929654453 256 PSKRLTIAQIKEHKWM 271
Cdd:cd14078  242 PKKRITVKELLNHPWV 257
STKc_Aurora cd14007
Catalytic domain of the Serine/Threonine kinase, Aurora kinase; STKs catalyze the transfer of ...
20-272 1.83e-88

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: 282.06  E-value: 1.83e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEK-IYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14007    2 FEIGKPLGKGKFGNVYLAREKKSGFIVALKVISKSQLQKSGLEHqLRREIEIQSHLRHPNILRLYGYFEDKKRIYLILEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLaTWCG 178
Cdd:cd14007   82 APNGELYKELKKQKRFDEKEAAKYIYQLALALDYLHSKNIIHRDIKPENILLGSNGELKLADFGWSVHAPSNRRK-TFCG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSK 258
Cdd:cd14007  161 TLDYLPPEMVEGKEY-DYKVDIWSLGVLCYELLVGKPPFESKSHQETYKRIQNVDIKFPSSVSPEAKDLISKLLQKDPSK 239
                        250
                 ....*....|....
gi 929654453 259 RLTIAQIKEHKWML 272
Cdd:cd14007  240 RLSLEQVLNHPWIK 253
STKc_TSSK-like cd14080
Catalytic domain of testis-specific serine/threonine kinases and similar proteins; STKs ...
20-271 5.62e-88

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: 281.38  E-value: 5.62e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLG--RHRITKTEVAIKIIDKSQLDAVNLEKIY-REVQIMKMLDHPHIIKLYQVMETKSMLYLVT 96
Cdd:cd14080    2 YRLGKTIGEGSYSKVKLAeyTKSGLKEKVACKIIDKKKAPKDFLEKFLpRELEILRKLRHPNIIQVYSIFERGSKVFIFM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE---LL 173
Cdd:cd14080   82 EYAEHGDLLEYIQKRGALSESQARIWFRQLALAVQYLHSLDIAHRDLKCENILLDSNNNVKLSDFGFARLCPDDDgdvLS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIP---YFMSEDCEHLIRR 250
Cdd:cd14080  162 KTFCGSAAYAAPEILQGIPYDPKKYDIWSLGVILYIMLCGSMPFDDSNIKKMLKDQQNRKVRFPssvKKLSPECKDLIDQ 241
                        250       260
                 ....*....|....*....|.
gi 929654453 251 MLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14080  242 LLEPDPTKRATIEEILNHPWL 262
STKc_Kin1_2 cd14077
Catalytic domain of Kin1, Kin2, and simlar Serine/Threonine Kinases; STKs catalyze the ...
18-271 8.56e-88

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: 280.87  E-value: 8.56e-88
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  18 GFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKII-------------DKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQ 84
Cdd:cd14077    1 GNWEFVKTIGAGSMGKVKLAKHIRTGEKCAIKIIprasnaglkkereKRLEKEISRDIRTIREAALSSLLNHPHICRLRD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  85 VMETKSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG 164
Cdd:cd14077   81 FLRTPNHYYMLFEYVDGGQLLDYIISHGKLKEKQARKFARQIASALDYLHRNSIVHRDLKIENILISKSGNIKIIDFGLS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 165 NFFKSGELLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDC 244
Cdd:cd14077  161 NLYDPRRLLRTFCGSLYFAAPELLQAQPYTGPEVDVWSFGVVLYVLVCGKVPFDDENMPALHAKIKKGKVEYPSYLSSEC 240
                        250       260
                 ....*....|....*....|....*..
gi 929654453 245 EHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14077  241 KSLISRMLVVDPKKRATLEQVLNHPWM 267
STKc_NUAK2 cd14161
Catalytic domain of the Serine/Threonine Kinase, novel (nua) kinase family NUAK 2; STKs ...
20-271 1.21e-84

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: 272.21  E-value: 1.21e-84
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRiTKTEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14161    5 YEFLETLGKGTYGRVKKARDS-SGRLVAIKSIRKDRIkDEQDLLHIRREIEIMSSLNHPHIISVYEVFENSSKIVIVMEY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCG 178
Cdd:cd14161   84 ASRGDLYDYISERQRLSELEARHFFRQIVSAVHYCHANGIVHRDLKLENILLDANGNIKIADFGLSNLYNQDKFLQTYCG 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCeHLIRRMLVLDPSK 258
Cdd:cd14161  164 SPLYASPEIVNGRPYIGPEVDSWSLGVLLYILVHGTMPFDGHDYKILVKQISSGAYREPTKPSDAC-GLIRWLLMVNPER 242
                        250
                 ....*....|...
gi 929654453 259 RLTIAQIKEHKWM 271
Cdd:cd14161  243 RATLEDVASHWWV 255
STKc_LKB1_CaMKK cd14008
Catalytic domain of the Serine/Threonine kinases, Liver Kinase B1, Calmodulin Dependent ...
26-271 1.28e-81

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: 264.42  E-value: 1.28e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQL------------DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSM-- 91
Cdd:cd14008    1 LGRGSFGKVKLALDTETGQLYAIKIFNKSRLrkrregkndrgkIKNALDDVRREIAIMKKLDHPNIVRLYEVIDDPESdk 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  92 LYLVTEYAKNGEIFDYLANHGR--LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFF-K 168
Cdd:cd14008   81 LYLVLEYCEGGPVMELDSGDRVppLPEETARKYFRDLVLGLEYLHENGIVHRDIKPENLLLTADGTVKISDFGVSEMFeD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 SGELLATWCGSPPYAAPEVFEG--QQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYF--MSEDC 244
Cdd:cd14008  161 GNDTLQKTAGTPAFLAPELCDGdsKTYSGKAADIWALGVTLYCLVFGRLPFNGDNILELYEAIQNQNDEFPIPpeLSPEL 240
                        250       260
                 ....*....|....*....|....*..
gi 929654453 245 EHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14008  241 KDLLRRMLEKDPEKRITLKEIKEHPWV 267
STKc_TSSK4-like cd14162
Catalytic domain of testis-specific serine/threonine kinase 4 and similar proteins; STKs ...
20-270 8.27e-80

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: 259.15  E-value: 8.27e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIY-REVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14162    2 YIVGKTLGHGSYAVVKKAYSTKHKCKVAIKIVSKKKAPEDYLQKFLpREIEVIKGLKHPNLICFYEAIETTSRVYIIMEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG--------NFFKsg 170
Cdd:cd14162   82 AENGDLLDYIRKNGALPEPQARRWFRQLVAGVEYCHSKGVVHRDLKCENLLLDKNNNLKITDFGFArgvmktkdGKPK-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 eLLATWCGSPPYAAPEVFEGQQYEgPQL-DIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEG-RFRIPYFMSEDCEHLI 248
Cdd:cd14162  160 -LSETYCGSYAYASPEILRGIPYD-PFLsDIWSMGVVLYTMVYGRLPFDDSNLKVLLKQVQRRvVFPKNPTVSEECKDLI 237
                        250       260
                 ....*....|....*....|..
gi 929654453 249 RRMLVLDPsKRLTIAQIKEHKW 270
Cdd:cd14162  238 LRMLSPVK-KRITIEEIKRDPW 258
STKc_TSSK1_2-like cd14165
Catalytic domain of testis-specific serine/threonine kinase 1, TSSK2, and similar proteins; ...
20-271 6.78e-77

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: 251.62  E-value: 6.78e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIY-REVQIMKMLDHPHIIKLYQVMETKS-MLYLVTE 97
Cdd:cd14165    3 YILGINLGEGSYAKVKSAYSERLKCNVAIKIIDKKKAPDDFVEKFLpRELEILARLNHKSIIKTYEIFETSDgKVYIVME 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG---NFFKSGE--L 172
Cdd:cd14165   83 LGVQGDLLEFIKLRGALPEDVARKMFHQLSSAIKYCHELDIVHRDLKCENLLLDKDFNIKLTDFGFSkrcLRDENGRivL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 LATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIP--YFMSEDCEHLIRR 250
Cdd:cd14165  163 SKTFCGSAAYAAPEVLQGIPYDPRIYDIWSLGVILYIMVCGSMPYDDSNVKKMLKIQKEHRVRFPrsKNLTSECKDLIYR 242
                        250       260
                 ....*....|....*....|.
gi 929654453 251 MLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14165  243 LLQPDVSQRLCIDEVLSHPWL 263
STKc_ATG1_ULK_like cd14009
Catalytic domain of the Serine/Threonine kinases, Autophagy-related protein 1 and Unc-51-like ...
26-270 9.72e-75

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: 245.21  E-value: 9.72e-75
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14009    1 IGRGSFATVWKGRHKQTGEVVAIKEISRKKLNKKLQENLESEIAILKSIKHPNIVRLYDVQKTEDFIYLVLEYCAGGDLS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFFKSGELLATWCGSPPY 182
Cdd:cd14009   81 QYIRKRGRLPEAVARHFMQQLASGLKFLRSKNIIHRDLKPQNLLLstsGDDPVLKIADFGFARSLQPASMAETLCGSPLY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEG----RFRIPYFMSEDCEHLIRRMLVLDPSK 258
Cdd:cd14009  161 MAPEILQFQKYDA-KADLWSVGAILFEMLVGKPPFRGSNHVQLLRNIERSdaviPFPIAAQLSPDCKDLLRRLLRRDPAE 239
                        250
                 ....*....|..
gi 929654453 259 RLTIAQIKEHKW 270
Cdd:cd14009  240 RISFEEFFAHPF 251
STKc_Kin4 cd14076
Catalytic domain of the yeast Serine/Threonine Kinase, Kin4; STKs catalyze the transfer of the ...
18-271 6.28e-74

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: 243.93  E-value: 6.28e-74
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  18 GFYDIEGTLGKGNFAVVKLG------RHRITKtEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKS 90
Cdd:cd14076    1 GPYILGRTLGEGEFGKVKLGwplpkaNHRSGV-QVAIKLIRRDTQqENCQTSKIMREINILKGLTHPNIVRLLDVLKTKK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  91 MLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFF--K 168
Cdd:cd14076   80 YIGIVLEFVSGGELFDYILARRRLKDSVACRLFAQLISGVAYLHKKGVVHRDLKLENLLLDKNRNLVITDFGFANTFdhF 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 SGELLATWCGSPPYAAPE-VFEGQQYEGPQLDIWSMGVVLYVLVCGALPFD-------GPTLPILRQRVLEGRFRIPYFM 240
Cdd:cd14076  160 NGDLMSTSCGSPCYAAPElVVSDSMYAGRKADIWSCGVILYAMLAGYLPFDddphnpnGDNVPRLYRYICNTPLIFPEYV 239
                        250       260       270
                 ....*....|....*....|....*....|.
gi 929654453 241 SEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14076  240 TPKARDLLRRILVPNPRKRIRLSAIMRHAWL 270
PKc cd00180
Catalytic domain of Protein Kinases; PKs catalyze the transfer of the gamma-phosphoryl group ...
26-268 1.33e-72

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: 238.32  E-value: 1.33e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAvNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd00180    1 LGKGSFGKVYKARDKETGKKVAVKVIPKEKLKK-LLEELLREIEILKKLNHPNIVKLYDVFETENFLYLVMEYCEGGSLK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELL---ATWCGSPP 181
Cdd:cd00180   80 DLLKENkGPLSEEEALSILRQLLSALEYLHSNGIIHRDLKPENILLDSDGTVKLADFGLAKDLDSDDSLlktTGGTTPPY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVFEGQQYeGPQLDIWSMGVVLYVLvcgalpfdgptlpilrqrvlegrfripyfmsEDCEHLIRRMLVLDPSKRLT 261
Cdd:cd00180  160 YAPPELLGGRYY-GPKVDIWSLGVILYEL-------------------------------EELKDLIRRMLQYDPKKRPS 207

                 ....*..
gi 929654453 262 IAQIKEH 268
Cdd:cd00180  208 AKELLEH 214
STKc_PLK cd14099
Catalytic domain of the Serine/Threonine Kinases, Polo-like kinases; STKs catalyze the ...
26-271 1.87e-71

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: 236.68  E-value: 1.87e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd14099    9 LGKGGFAKCYEVTDMSTGKVYAGKVVPKSSLtKPKQREKLKSEIKIHRSLKHPNIVKFHDCFEDEENVYILLELCSNGSL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKS-GELLATWCGSPPYA 183
Cdd:cd14099   89 MELLKRRKALTEPEVRYFMRQILSGVKYLHSNRIIHRDLKLGNLFLDENMNVKIGDFGLAARLEYdGERKKTLCGTPNYI 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 184 APEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYF--MSEDCEHLIRRMLVLDPSKRLT 261
Cdd:cd14099  169 APEVLEKKKGHSFEVDIWSLGVILYTLLVGKPPFETSDVKETYKRIKKNEYSFPSHlsISDEAKDLIRSMLQPDPTKRPS 248
                        250
                 ....*....|
gi 929654453 262 IAQIKEHKWM 271
Cdd:cd14099  249 LDEILSHPFF 258
STKc_Nek cd08215
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase; ...
20-265 7.87e-71

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: 235.05  E-value: 7.87e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd08215    2 YEKIRVIGKGSFGSAYLVRRKSDGKLYVLKEIDLSNMSEKEREEALNEVKLLSKLKHPNIVKYYESFEENGKLCIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYL----ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA- 174
Cdd:cd08215   82 DGGDLAQKIkkqkKKGQPFPEEQILDWFVQICLALKYLHSRKILHRDLKTQNIFLTKDGVVKLGDFGISKVLESTTDLAk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TWCGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFR-IPYFMSEDCEHLIRRMLV 253
Cdd:cd08215  162 TVVGTPYYLSPELCENKPYNYKS-DIWALGCVLYELCTLKHPFEANNLPALVYKIVKGQYPpIPSQYSSELRDLVNSMLQ 240
                        250
                 ....*....|..
gi 929654453 254 LDPSKRLTIAQI 265
Cdd:cd08215  241 KDPEKRPSANEI 252
STKc_DCKL cd14095
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase (also called ...
20-270 1.55e-69

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: 231.45  E-value: 1.55e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLdaVNLEK-IYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14095    2 YDIGRVIGDGNFAVVKECRDKATDKEYALKIIDKAKC--KGKEHmIENEVAILRRVKHPNIVQLIEEYDTDTELYLVMEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL----DNNMNIKIADFGFGNFFKsgELLA 174
Cdd:cd14095   80 VKGGDLFDAITSSTKFTERDASRMVTDLAQALKYLHSLSIVHRDIKPENLLVveheDGSKSLKLADFGLATEVK--EPLF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGP--TLPILRQRVLEGRFRI--PYF--MSEDCEHLI 248
Cdd:cd14095  158 TVCGTPTYVAPEILAETGY-GLKVDIWAAGVITYILLCGFPPFRSPdrDQEELFDLILAGEFEFlsPYWdnISDSAKDLI 236
                        250       260
                 ....*....|....*....|..
gi 929654453 249 RRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd14095  237 SRMLVVDPEKRYSAGQVLDHPW 258
STKc_AGC cd05123
Catalytic domain of AGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
26-271 4.38e-69

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: 230.10  E-value: 4.38e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEK-IYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05123    1 LGKGSFGKVLLVRKKDTGKLYAMKVLRKKEIIKRKEVEhTLNERNILERVNHPFIVKLHYAFQTEEKLYLVLDYVPGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARrkFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA-TWCGSPP 181
Cdd:cd05123   81 FSHLSKEGRFPEERAR--FYaaEIVLALEYLHSLGIIYRDLKPENILLDSDGHIKLTDFGLAKELSSDGDRTyTFCGTPE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLT 261
Cdd:cd05123  159 YLAPEVLLGKGY-GKAVDWWSLGVLLYEMLTGKPPFYAENRKEIYEKILKSPLKFPEYVSPEAKSLISGLLQKDPTKRLG 237
                        250
                 ....*....|...
gi 929654453 262 ---IAQIKEHKWM 271
Cdd:cd05123  238 sggAEEIKAHPFF 250
STKc_Chk2 cd14084
Catalytic domain of the Serine/Threonine kinase, Cell cycle Checkpoint Kinase 2; STKs catalyze ...
20-271 7.47e-67

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: 224.96  E-value: 7.47e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL------DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLY 93
Cdd:cd14084    8 YIMSRTLGSGACGEVKLAYDKSTCKKVAIKIINKRKFtigsrrEINKPRNIETEIEILKKLSHPCIIKIEDFFDAEDDYY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMN---IKIADFGFGNFFKSG 170
Cdd:cd14084   88 IVLELMEGGELFDRVVSNKRLKEAICKLYFYQMLLAVKYLHSNGIIHRDLKPENVLLSSQEEeclIKITDFGLSKILGET 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 ELLATWCGSPPYAAPEV--FEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPI-LRQRVLEGRFR-IPYF---MSED 243
Cdd:cd14084  168 SLMKTLCGTPTYLAPEVlrSFGTEGYTRAVDCWSLGVILFICLSGYPPFSEEYTQMsLKEQILSGKYTfIPKAwknVSEE 247
                        250       260
                 ....*....|....*....|....*...
gi 929654453 244 CEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14084  248 AKDLVKKMLVVDPSRRPSIEEALEHPWL 275
STKc_PhKG cd14093
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma subunit; STKs ...
20-271 8.30e-67

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: 224.54  E-value: 8.30e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKS------QLDAVNLEKIYREVQIMKMLD-HPHIIKLYQVMETKSML 92
Cdd:cd14093    5 YEPKEILGRGVSSTVRRCIEKETGQEFAVKIIDITgeksseNEAEELREATRREIEILRQVSgHPNIIELHDVFESPTFI 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  93 YLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL 172
Cdd:cd14093   85 FLVFELCRKGELFDYLTEVVTLSEKKTRRIMRQLFEAVEFLHSLNIVHRDLKPENILLDDNLNVKISDFGFATRLDEGEK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 LATWCGSPPYAAPEVFEGQQYE-----GPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGR--FRIPYF--MSED 243
Cdd:cd14093  165 LRELCGTPGYLAPEVLKCSMYDnapgyGKEVDMWACGVIMYTLLAGCPPFWHRKQMVMLRNIMEGKyeFGSPEWddISDT 244
                        250       260
                 ....*....|....*....|....*...
gi 929654453 244 CEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14093  245 AKDLISKLLVVDPKKRLTAEEALEHPFF 272
Pkinase pfam00069
Protein kinase domain;
20-271 2.01e-66

Protein kinase domain;


Pssm-ID: 459660 [Multi-domain]  Cd Length: 217  Bit Score: 221.35  E-value: 2.01e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:pfam00069   1 YEVLRKLGSGSFGTVYKAKHRDTGKIVAIKKIKKEKIKKKKDKNILREIKILKKLNHPNIVRLYDAFEDKDNLYLVLEYV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  100 KNGEIFDYLANHGRLNESEARRKFWQILSAVdychgrkivhrdlkaenllldnnmnikiadfgfgnffKSGELLATWCGS 179
Cdd:pfam00069  81 EGGSLFDLLSEKGAFSEREAKFIMKQILEGL-------------------------------------ESGSSLTTFVGT 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  180 PPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYF---MSEDCEHLIRRMLVLDP 256
Cdd:pfam00069 124 PWYMAPEVLGGNPY-GPKVDVWSLGCILYELLTGKPPFPGINGNEIYELIIDQPYAFPELpsnLSEEAKDLLKKLLKKDP 202
                         250
                  ....*....|....*
gi 929654453  257 SKRLTIAQIKEHKWM 271
Cdd:pfam00069 203 SKRLTATQALQHPWF 217
STKc_Chk1 cd14069
Catalytic domain of the Serine/Threonine kinase, Checkpoint kinase 1; STKs catalyze the ...
20-270 5.46e-66

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: 221.82  E-value: 5.46e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14069    3 WDLVQTLGEGAFGEVFLAVNRNTEEAVAVKFVDMKRAPGDCPENIKKEVCIQKMLSHKNVVRFYGHRREGEFQYLFLEYA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK-SGE--LLATW 176
Cdd:cd14069   83 SGGELFDKIEPDVGMPEDVAQFYFQQLMAGLKYLHSCGITHRDIKPENLLLDENDNLKISDFGLATVFRyKGKerLLNKM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLP-ILRQRVLEGR---FRIPYFMSEDCEHLIRRML 252
Cdd:cd14069  163 CGTLPYVAPELLAKKKYRAEPVDVWSCGIVLFAMLAGELPWDQPSDScQEYSDWKENKktyLTPWKKIDTAALSLLRKIL 242
                        250
                 ....*....|....*...
gi 929654453 253 VLDPSKRLTIAQIKEHKW 270
Cdd:cd14069  243 TENPNKRITIEDIKKHPW 260
STKc_PDK1 cd05581
Catalytic domain of the Serine/Threonine Kinase, Phosphoinositide-dependent kinase 1; STKs ...
20-270 3.31e-65

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: 220.55  E-value: 3.31e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL------DAVNLEKIyrevqIMKMLDHPHIIKLYQVMETKSMLY 93
Cdd:cd05581    3 FKFGKPLGEGSYSTVVLAKEKETGKEYAIKVLDKRHIikekkvKYVTIEKE-----VLSRLAHPGIVKLYYTFQDESKLY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL- 172
Cdd:cd05581   78 FVLEYAPNGDLLEYIRKYGSLDEKCTRFYTAEIVLALEYLHSKGIIHRDLKPENILLDEDMHIKITDFGTAKVLGPDSSp 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 -----------------LATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFR 235
Cdd:cd05581  158 estkgdadsqiaynqarAASFVGTAEYVSPELLNEKPA-GKSSDLWALGCIIYQMLTGKPPFRGSNEYLTFQKIVKLEYE 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 929654453 236 IPYFMSEDCEHLIRRMLVLDPSKRLTIA------QIKEHKW 270
Cdd:cd05581  237 FPENFPPDAKDLIQKLLVLDPSKRLGVNenggydELKAHPF 277
STKc_SnRK2 cd14662
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
20-270 6.38e-65

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: 218.87  E-value: 6.38e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQ-LDavnlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14662    2 YELVKDIGSGNFGVARLMRNKETKELVAVKYIERGLkID----ENVQREIINHRSLRHPNIIRFKEVVLTPTHLAIVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNM--NIKIADFGFGnffKSGELLA-- 174
Cdd:cd14662   78 AAGGELFERICNAGRFSEDEARYFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYS---KSSVLHSqp 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 -TWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPI-LR---QRVLEGRFRIPYF--MSEDCEHL 247
Cdd:cd14662  155 kSTVGTPAYIAPEVLSRKEYDGKVADVWSCGVTLYVMLVGAYPFEDPDDPKnFRktiQRIMSVQYKIPDYvrVSQDCRHL 234
                        250       260
                 ....*....|....*....|...
gi 929654453 248 IRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd14662  235 LSRIFVANPAKRITIPEIKNHPW 257
STKc_SnRK2-3 cd14665
Catalytic domain of the Serine/Threonine Kinases, Sucrose nonfermenting 1-related protein ...
20-270 7.01e-64

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: 216.00  E-value: 7.01e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQ-LDavnlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14665    2 YELVKDIGSGNFGVARLMRDKQTKELVAVKYIERGEkID----ENVQREIINHRSLRHPNIVRFKEVILTPTHLAIVMEY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNM--NIKIADFGFGnffKSGELLA-- 174
Cdd:cd14665   78 AAGGELFERICNAGRFSEDEARFFFQQLISGVSYCHSMQICHRDLKLENTLLDGSPapRLKICDFGYS---KSSVLHSqp 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 -TWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLP----ILRQRVLEGRFRIPYF--MSEDCEHL 247
Cdd:cd14665  155 kSTVGTPAYIAPEVLLKKEYDGKIADVWSCGVTLYVMLVGAYPFEDPEEPrnfrKTIQRILSVQYSIPDYvhISPECRHL 234
                        250       260
                 ....*....|....*....|...
gi 929654453 248 IRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd14665  235 ISRIFVADPATRITIPEIRNHEW 257
STKc_HUNK cd14070
Catalytic domain of the Serine/Threonine Kinase, Hormonally up-regulated Neu-associated kinase ...
17-271 2.44e-63

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: 214.68  E-value: 2.44e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  17 VGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDK--SQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYL 94
Cdd:cd14070    1 VGSYLIGRKLGEGSFAKVREGLHAVTGEKVAIKVIDKkkAKKDSYVTKNLRREGRIQQMIRHPNITQLLDILETENSYYL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKS---GE 171
Cdd:cd14070   81 VMELCPGGNLMHRIYDKKRLEEREARRYIRQLVSAVEHLHRAGVVHRDLKIENLLLDENDNIKLIDFGLSNCAGIlgySD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 LLATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPF--DGPTLPILRQRVLEGRFR-IPYFMSEDCEHLI 248
Cdd:cd14070  161 PFSTQCGSPAYAAPELLARKKY-GPKVDVWSIGVNMYAMLTGTLPFtvEPFSLRALHQKMVDKEMNpLPTDLSPGAISFL 239
                        250       260
                 ....*....|....*....|...
gi 929654453 249 RRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14070  240 RSLLEPDPLKRPNIKQALANRWL 262
STKc_PknB_like cd14014
Catalytic domain of bacterial Serine/Threonine kinases, PknB and similar proteins; STKs ...
20-264 1.19e-61

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: 209.75  E-value: 1.19e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14014    2 YRLVRLLGRGGMGEVYRARDTLLGRPVAIKVLRPELAeDEEFRERFLREARALARLSHPNIVRVYDVGEDDGRPYIVMEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLAT--W 176
Cdd:cd14014   82 VEGGSLADLLRERGPLPPREALRILAQIADALAAAHRAGIVHRDIKPANILLTEDGRVKLTDFGIARALGDSGLTQTgsV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPY----FMSEDCEHLIRRML 252
Cdd:cd14014  162 LGTPAYMAPEQARGGPV-DPRSDIYSLGVVLYELLTGRPPFDGDSPAAVLAKHLQEAPPPPSplnpDVPPALDAIILRAL 240
                        250
                 ....*....|..
gi 929654453 253 VLDPSKRLTIAQ 264
Cdd:cd14014  241 AKDPEERPQSAA 252
STKc_MLCK-like cd14006
Catalytic kinase domain of Myosin Light Chain Kinase-like Serine/Threonine Kinases; STKs ...
26-270 2.26e-61

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: 208.66  E-value: 2.26e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKsqlDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14006    1 LGRGRFGVVKRCIEKATGREFAAKFIPK---RDKKKEAVLREISILNQLQHPRIIQLHEAYESPTELVLILELCSGGELL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNM--NIKIADFGFGNFFKSGELLATWCGSPPYA 183
Cdd:cd14006   78 DRLAERGSLSEEEVRTYMRQLLEGLQYLHNHHILHLDLKPENILLADRPspQIKIIDFGLARKLNPGEELKEIFGTPEFV 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 184 APEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRI--PYF--MSEDCEHLIRRMLVLDPSKR 259
Cdd:cd14006  158 APEIVNGEPV-SLATDMWSIGVLTYVLLSGLSPFLGEDDQETLANISACRVDFseEYFssVSQEAKDFIRKLLVKEPRKR 236
                        250
                 ....*....|.
gi 929654453 260 LTIAQIKEHKW 270
Cdd:cd14006  237 PTAQEALQHPW 247
STKc_Rad53_Cds1 cd14098
Catalytic domain of the yeast Serine/Threonine Kinases, Rad53 and Cds1; STKs catalyze the ...
20-270 1.38e-60

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: 207.33  E-value: 1.38e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQ--LDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTE 97
Cdd:cd14098    2 YQIIDRLGSGTFAEVKKAVEVETGKMRAIKQIVKRKvaGNDKNLQLFQREINILKSLEHPGIVRLIDWYEDDQHIYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL--DNNMNIKIADFGFGNFFKSGELLAT 175
Cdd:cd14098   82 YVEGGDLMDFIMAWGAIPEQHARELTKQILEAMAYTHSMGITHRDLKPENILItqDDPVIVKISDFGLAKVIHTGTFLVT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYEGP-----QLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIP----YFMSEDCEH 246
Cdd:cd14098  162 FCGTMAYLAPEILMSKEQNLQggysnLVDMWSVGCLVYVMLTGALPFDGSSQLPVEKRIRKGRYTQPplvdFNISEEAID 241
                        250       260
                 ....*....|....*....|....
gi 929654453 247 LIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd14098  242 FILRLLDVDPEKRMTAAQALDHPW 265
STKc_CAMKK cd14118
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase; ...
26-270 2.46e-60

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: 206.83  E-value: 2.46e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-------------------DAVN--LEKIYREVQIMKMLDHPHIIKLYQ 84
Cdd:cd14118    2 IGKGSYGIVKLAYNEEDNTLYAMKILSKKKLlkqagffrrppprrkpgalGKPLdpLDRVYREIAILKKLDHPNVVKLVE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  85 VME--TKSMLYLVTEYAKNGEIFDYLANHgRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG 162
Cdd:cd14118   82 VLDdpNEDNLYMVFELVDKGAVMEVPTDN-PLSEETARSYFRDIVLGIEYLHYQKIIHRDIKPSNLLLGDDGHVKIADFG 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 163 FGNFFKSGE-LLATWCGSPPYAAPEVF--EGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIP-- 237
Cdd:cd14118  161 VSNEFEGDDaLLSSTAGTPAFMAPEALseSRKKFSGKALDIWAMGVTLYCFVFGRCPFEDDHILGLHEKIKTDPVVFPdd 240
                        250       260       270
                 ....*....|....*....|....*....|...
gi 929654453 238 YFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd14118  241 PVVSEQLKDLILRMLDKNPSERITLPEIKEHPW 273
STKc_MSK_C cd14092
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
20-271 2.95e-60

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: 207.92  E-value: 2.95e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDI---EGTLGKGNFAVVKLGRHRITKTEVAIKIIDKsQLDAVnlekiyREVQIMKMLD-HPHIIKLYQVMETKSMLYLV 95
Cdd:cd14092    5 YELdlrEEALGDGSFSVCRKCVHKKTGQEFAVKIVSR-RLDTS------REVQLLRLCQgHPNIVKLHEVFQDELHTYLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFFKSGEL 172
Cdd:cd14092   78 MELLRGGELLERIRKKKRFTESEASRIMRQLVSAVSFMHSKGVVHRDLKPENLLFtdeDDDAEIKIVDFGFARLKPENQP 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 LATWCGSPPYAAPEVFEGQQYEG---PQLDIWSMGVVLYVLVCGALPFDGPT----LPILRQRVLEGRFRipyF------ 239
Cdd:cd14092  158 LKTPCFTLPYAAPEVLKQALSTQgydESCDLWSLGVILYTMLSGQVPFQSPSrnesAAEIMKRIKSGDFS---Fdgeewk 234
                        250       260       270
                 ....*....|....*....|....*....|...
gi 929654453 240 -MSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14092  235 nVSSEAKSLIQGLLTVDPSKRLTMSELRNHPWL 267
STKc_TSSK3-like cd14163
Catalytic domain of testis-specific serine/threonine kinase 3 and similar proteins; STKs ...
20-271 4.07e-60

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: 205.61  E-value: 4.07e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIY-REVQIMKMLDHPHIIKLYQVME-TKSMLYLVTE 97
Cdd:cd14163    2 YQLGKTIGEGTYSKVKEAFSKKHQRKVAIKIIDKSGGPEEFIQRFLpRELQIVERLDHKNIIHVYEMLEsADGKIYLVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLdNNMNIKIADFGFGNFFKSG--ELLAT 175
Cdd:cd14163   82 LAEDGDVFDCVLHGGPLPEHRAKALFRQLVEAIRYCHGCGVAHRDLKCENALL-QGFTLKLTDFGFAKQLPKGgrELSQT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGrFRIPYFM--SEDCEHLIRRMLV 253
Cdd:cd14163  161 FCGSTAYAAPEVLQGVPHDSRKGDIWSMGVVLYVMLCAQLPFDDTDIPKMLCQQQKG-VSLPGHLgvSRTCQDLLKRLLE 239
                        250
                 ....*....|....*...
gi 929654453 254 LDPSKRLTIAQIKEHKWM 271
Cdd:cd14163  240 PDMVLRPSIEEVSWHPWL 257
STKc_PKA_like cd05580
Catalytic subunit of the Serine/Threonine Kinases, cAMP-dependent protein kinases; STKs ...
20-270 7.41e-60

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: 205.89  E-value: 7.41e-60
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQ---LDAVnlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVT 96
Cdd:cd05580    3 FEFLKTLGTGSFGRVRLVKHKDSGKYYALKILKKAKiikLKQV--EHVLNEKRILSEVRHPFIVNLLGSFQDDRNLYMVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNGEIFDYLANHGRLNESEArrKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKsgELLA 174
Cdd:cd05580   81 EYVPGGELFSLLRRSGRFPNDVA--KFYaaEVVLALEYLHSLDIVYRDLKPENLLLDSDGHIKITDFGFAKRVK--DRTY 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPF--DGPTLpiLRQRVLEGRFRIPYFMSEDCEHLIRRML 252
Cdd:cd05580  157 TLCGTPEYLAPEIILSKGH-GKAVDWWALGILIYEMLAGYPPFfdENPMK--IYEKILEGKIRFPSFFDPDAKDLIKRLL 233
                        250       260
                 ....*....|....*....|...
gi 929654453 253 VLDPSKRL-----TIAQIKEHKW 270
Cdd:cd05580  234 VVDLTKRLgnlknGVEDIKNHPW 256
STKc_CaMKI cd14083
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
20-270 2.90e-59

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: 203.37  E-value: 2.90e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14083    5 YEFKEVLGTGAFSEVVLAEDKATGKLVAIKCIDKKALKGKE-DSLENEIAVLRKIKHPNIVQLLDIYESKSHLYLVMELV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLL---LDNNMNIKIADFGFGNfFKSGELLATW 176
Cdd:cd14083   84 TGGELFDRIVEKGSYTEKDASHLIRQVLEAVDYLHSLGIVHRDLKPENLLyysPDEDSKIMISDFGLSK-MEDSGVMSTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEG--RFRIPYF--MSEDCEHLIRRML 252
Cdd:cd14083  163 CGTPGYVAPEVLAQKPY-GKAVDCWSIGVISYILLCGYPPFYDENDSKLFAQILKAeyEFDSPYWddISDSAKDFIRHLM 241
                        250
                 ....*....|....*...
gi 929654453 253 VLDPSKRLTIAQIKEHKW 270
Cdd:cd14083  242 EKDPNKRYTCEQALEHPW 259
STKc_RSK_C cd14091
C-terminal catalytic domain of the Serine/Threonine Kinases, Ribosomal S6 kinases; STKs ...
20-291 7.41e-59

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: 203.25  E-value: 7.41e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAvnlekiYREVQI-MKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14091    2 YEIKEEIGKGSYSVCKRCIHKATGKEYAVKIIDKSKRDP------SEEIEIlLRYGQHPNIITLRDVYDDGNSVYLVTEL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLL----LDNNMNIKIADFGFGNFFKSGE-LL 173
Cdd:cd14091   76 LRGGELLDRILRQKFFSEREASAVMKTLTKTVEYLHSQGVVHRDLKPSNILyadeSGDPESLRICDFGFAKQLRAENgLL 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPF-----DGPTLpILrQRVLEGRFRI--PYF--MSEDC 244
Cdd:cd14091  156 MTPCYTANFVAPEVLKKQGYDA-ACDIWSLGVLLYTMLAGYTPFasgpnDTPEV-IL-ARIGSGKIDLsgGNWdhVSDSA 232
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 929654453 245 EHLIRRMLVLDPSKRLTIAQIKEHKWMlievpVQRPVLyPQEQENEP 291
Cdd:cd14091  233 KDLVRKMLHVDPSQRPTAAQVLQHPWI-----RNRDSL-PQRQLTDP 273
STKc_LKB1 cd14119
Catalytic domain of the Serine/Threonine kinase, Liver Kinase B1; STKs catalyze the transfer ...
26-271 8.55e-59

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: 201.72  E-value: 8.55e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVN--LEKIYREVQIMKMLDHPHIIKLYQVM--ETKSMLYLVTEYAKN 101
Cdd:cd14119    1 LGEGSYGKVKEVLDTETLCRRAVKILKKRKLRRIPngEANVKREIQILRRLNHRNVIKLVDVLynEEKQKLYMVMEYCVG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 G--EIFDYLANHgRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNF---FKSGELLATW 176
Cdd:cd14119   81 GlqEMLDSAPDK-RLPIWQAHGYFVQLIDGLEYLHSQGIIHKDIKPGNLLLTTDGTLKISDFGVAEAldlFAEDDTCTTS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQ-YEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLD 255
Cdd:cd14119  160 QGSPAFQPPEIANGQDsFSGFKVDIWSAGVTLYNMTTGKYPFEGDNIYKLFENIGKGEYTIPDDVDPDLQDLLRGMLEKD 239
                        250
                 ....*....|....*.
gi 929654453 256 PSKRLTIAQIKEHKWM 271
Cdd:cd14119  240 PEKRFTIEQIRQHPWF 255
STKc_DCKL3 cd14185
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 3 (also called ...
19-270 1.95e-58

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: 200.94  E-value: 1.95e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14185    1 HYEIGRTIGDGNFAVVKECRHWNENQEYAMKIIDKSKLKGKE-DMIESEILIIKSLSHPNIVKLFEVYETEKEIYLILEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL----DNNMNIKIADFGFGNFFKSGelLA 174
Cdd:cd14185   80 VRGGDLFDAIIESVKFTEHDAALMIIDLCEALVYIHSKHIVHRDLKPENLLVqhnpDKSTTLKLADFGLAKYVTGP--IF 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGP--TLPILRQRVLEGRFRI--PYF--MSEDCEHLI 248
Cdd:cd14185  158 TVCGTPTYVAPEILSEKGY-GLEVDMWAAGVILYILLCGFPPFRSPerDQEELFQIIQLGHYEFlpPYWdnISEAAKDLI 236
                        250       260
                 ....*....|....*....|..
gi 929654453 249 RRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd14185  237 SRLLVVDPEKRYTAKQVLQHPW 258
STKc_PASK cd14004
Catalytic domain of the Serine/Threonine kinase, Per-ARNT-Sim (PAS) domain Kinase; STKs ...
20-271 2.56e-58

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: 200.69  E-value: 2.56e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-------DAVnLEKIYREVQIMKMLD---HPHIIKLYQVMETK 89
Cdd:cd14004    2 YTILKEMGEGAYGQVNLAIYKSKGKEVVIKFIFKERIlvdtwvrDRK-LGTVPLEIHILDTLNkrsHPNIVKLLDFFEDD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  90 SMLYLVTEYAKNG-EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK 168
Cdd:cd14004   81 EFYYLVMEKHGSGmDLFDFIERKPNMDEKEAKYIFRQVADAVKHLHDQGIVHRDIKDENVILDGNGTIKLIDFGSAAYIK 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 SGElLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFdgptlpILRQRVLEGRFRIPYFMSEDCEHLI 248
Cdd:cd14004  161 SGP-FDTFVGTIDYAAPEVLRGNPYGGKEQDIWALGVLLYTLVFKENPF------YNIEEILEADLRIPYAVSEDLIDLI 233
                        250       260
                 ....*....|....*....|...
gi 929654453 249 RRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14004  234 SRMLNRDVGDRPTIEELLTDPWL 256
STKc_cGK cd05572
Catalytic domain of the Serine/Threonine Kinase, cGMP-dependent protein kinase (cGK or PKG); ...
26-270 1.26e-57

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: 198.60  E-value: 1.26e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEK-IYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05572    1 LGVGGFGRVELVQLKSKGRTFALKCVKKRHIVQTRQQEhIFSEKEILEECNSPFIVKLYRTFKDKKYLYMLMEYCLGGEL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPYAA 184
Cdd:cd05572   81 WTILRDRGLFDEYTARFYTACVVLAFEYLHSRGIIYRDLKPENLLLDSNGYVKLVDFGFAKKLGSGRKTWTFCGTPEYVA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 185 PEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGP-TLPILR-QRVLEGRFRI--PYFMSEDCEHLIRRMLVLDPSKRL 260
Cdd:cd05572  161 PEIILNKGY-DFSVDYWSLGILLYELLTGRPPFGGDdEDPMKIyNIILKGIDKIefPKYIDKNAKNLIKQLLRRNPEERL 239
                        250
                 ....*....|....*
gi 929654453 261 -----TIAQIKEHKW 270
Cdd:cd05572  240 gylkgGIRDIKKHKW 254
STKc_MAST_like cd05579
Catalytic domain of Microtubule-associated serine/threonine (MAST) kinase-like proteins; STKs ...
28-270 3.15e-57

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: 198.21  E-value: 3.15e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  28 KGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNL-EKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFD 106
Cdd:cd05579    3 RGAYGRVYLAKKKSTGDLYAIKVIKKRDMIRKNQvDSVLAERNILSQAQNPFVVKLYYSFQGKKNLYLVMEYLPGGDLYS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 107 YLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNF------FKSGELLATW---- 176
Cdd:cd05579   83 LLENVGALDEDVARIYIAEIVLALEYLHSHGIIHRDLKPDNILIDANGHLKLTDFGLSKVglvrrqIKLSIQKKSNgape 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 ------CGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYF--MSEDCEHLI 248
Cdd:cd05579  163 kedrriVGTPDYLAPEILLGQGH-GKTVDWWSLGVILYEFLVGIPPFHAETPEEIFQNILNGKIEWPEDpeVSDEAKDLI 241
                        250       260
                 ....*....|....*....|....*
gi 929654453 249 RRMLVLDPSKRL---TIAQIKEHKW 270
Cdd:cd05579  242 SKLLTPDPEKRLgakGIEEIKNHPF 266
STKc_MAP3K-like cd13999
Catalytic domain of Mitogen-Activated Protein Kinase (MAPK) Kinase Kinase-like Serine ...
26-265 3.47e-57

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: 196.99  E-value: 3.47e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRitKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd13999    1 IGSGSFGEVYKGKWR--GTDVAIKKLKVEDDNDELLKEFRREVSILSKLRHPNIVQFIGACLSPPPLCIVTEYMPGGSLY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYL-ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATW-CGSPPYA 183
Cdd:cd13999   79 DLLhKKKIPLSWSLRLKIALDIARGMNYLHSPPIIHRDLKSLNILLDENFTVKIADFGLSRIKNSTTEKMTGvVGTPRWM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 184 APEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDG-PTLPILRQRVLEGRFR-IPYFMSEDCEHLIRRMLVLDPSKRLT 261
Cdd:cd13999  159 APEVLRGEPY-TEKADVYSFGIVLWELLTGEVPFKElSPIQIAAAVVQKGLRPpIPPDCPPELSKLIKRCWNEDPEKRPS 237

                 ....
gi 929654453 262 IAQI 265
Cdd:cd13999  238 FSEI 241
STKc_DAPK cd14105
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase; STKs ...
19-271 1.08e-56

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: 196.55  E-value: 1.08e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDA----VNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYL 94
Cdd:cd14105    6 FYDIGEELGSGQFAVVKKCREKSTGLEYAAKFIKKRRSKAsrrgVSREDIEREVSILRQVLHPNIITLHDVFENKTDVVL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAEN-LLLDNNM---NIKIADFGFGNFFKSG 170
Cdd:cd14105   86 ILELVAGGELFDFLAEKESLSEEEATEFLKQILDGVNYLHTKNIAHFDLKPENiMLLDKNVpipRIKLIDFGLAHKIEDG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 ELLATWCGSPPYAAPEVFegqQYE--GPQLDIWSMGVVLYVLVCGALPFDGPTlpilRQRVLEG------RFRIPYF--M 240
Cdd:cd14105  166 NEFKNIFGTPEFVAPEIV---NYEplGLEADMWSIGVITYILLSGASPFLGDT----KQETLANitavnyDFDDEYFsnT 238
                        250       260       270
                 ....*....|....*....|....*....|.
gi 929654453 241 SEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14105  239 SELAKDFIRQLLVKDPRKRMTIQESLRHPWI 269
SPS1 COG0515
Serine/threonine protein kinase [Signal transduction mechanisms];
14-259 9.76e-56

Serine/threonine protein kinase [Signal transduction mechanisms];


Pssm-ID: 440281 [Multi-domain]  Cd Length: 482  Bit Score: 200.62  E-value: 9.76e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  14 PVRVGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKII-DKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSML 92
Cdd:COG0515    3 ALLLGRYRILRLLGRGGMGVVYLARDLRLGRPVALKVLrPELAADPEARERFRREARALARLNHPNIVRVYDVGEEDGRP 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  93 YLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL 172
Cdd:COG0515   83 YLVMEYVEGESLADLLRRRGPLPPAEALRILAQLAEALAAAHAAGIVHRDIKPANILLTPDGRVKLIDFGIARALGGATL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 LAT--WCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIP----YFMSEDCEH 246
Cdd:COG0515  163 TQTgtVVGTPGYMAPEQARGEPV-DPRSDVYSLGVTLYELLTGRPPFDGDSPAELLRAHLREPPPPPselrPDLPPALDA 241
                        250
                 ....*....|...
gi 929654453 247 LIRRMLVLDPSKR 259
Cdd:COG0515  242 IVLRALAKDPEER 254
STKc_MAPKKK cd06606
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase Kinase ...
25-270 1.27e-55

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: 193.12  E-value: 1.27e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd06606    7 LLGKGSFGSVYLALNLDTGELMAVKEVELSGDSEEELEALEREIRILSSLKHPNIVRYLGTERTENTLNIFLEYVPGGSL 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA---TWCGSPP 181
Cdd:cd06606   87 ASLLKKFGKLPEPVVRKYTRQILEGLEYLHSNGIVHRDIKGANILVDSDGVVKLADFGCAKRLAEIATGEgtkSLRGTPY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPF--------------DGPTLPilrqrvlegrfRIPYFMSEDCEHL 247
Cdd:cd06606  167 WMAPEVIRGEGY-GRAADIWSLGCTVIEMATGKPPWselgnpvaalfkigSSGEPP-----------PIPEHLSEEAKDF 234
                        250       260
                 ....*....|....*....|...
gi 929654453 248 IRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd06606  235 LRKCLQRDPKKRPTADELLQHPF 257
STKc_CaMKIV cd14085
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
19-271 4.54e-55

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: 192.73  E-value: 4.54e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSqldaVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14085    4 FFEIESELGRGATSVVYRCRQKGTQKPYAVKKLKKT----VDKKIVRTEIGVLLRLSHPNIIKLKEIFETPTEISLVLEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDN---NMNIKIADFGFGNFFKSGELLAT 175
Cdd:cd14085   80 VTGGELFDRIVEKGYYSERDAADAVKQILEAVAYLHENGIVHRDLKPENLLYATpapDAPLKIADFGLSKIVDQQVTMKT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPF-DGPTLPILRQRVL--EGRFRIPYF--MSEDCEHLIRR 250
Cdd:cd14085  160 VCGTPGYCAPEILRGCAY-GPEVDMWSVGVITYILLCGFEPFyDERGDQYMFKRILncDYDFVSPWWddVSLNAKDLVKK 238
                        250       260
                 ....*....|....*....|.
gi 929654453 251 MLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14085  239 LIVLDPKKRLTTQQALQHPWV 259
STKc_DAPK1 cd14194
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 1; STKs ...
19-271 1.50e-54

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: 190.62  E-value: 1.50e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDK----SQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYL 94
Cdd:cd14194    6 YYDTGEELGSGQFAVVKKCREKSTGLQYAAKFIKKrrtkSSRRGVSREDIEREVSILKEIQHPNVITLHEVYENKTDVIL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAEN-LLLDNNM---NIKIADFGFGNFFKSG 170
Cdd:cd14194   86 ILELVAGGELFDFLAEKESLTEEEATEFLKQILNGVYYLHSLQIAHFDLKPENiMLLDRNVpkpRIKIIDFGLAHKIDFG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 ELLATWCGSPPYAAPEVFegqQYE--GPQLDIWSMGVVLYVLVCGALPFDGPTlpilRQRVLEGRFRIPYFMSED----- 243
Cdd:cd14194  166 NEFKNIFGTPEFVAPEIV---NYEplGLEADMWSIGVITYILLSGASPFLGDT----KQETLANVSAVNYEFEDEyfsnt 238
                        250       260       270
                 ....*....|....*....|....*....|.
gi 929654453 244 ---CEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14194  239 salAKDFIRRLLVKDPKKRMTIQDSLQHPWI 269
PKc_STE cd05122
Catalytic domain of STE family Protein Kinases; PKs catalyze the transfer of the ...
20-270 3.45e-54

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: 188.95  E-value: 3.45e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDavNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd05122    2 FEILEKIGKGGFGVVYKARHKKTGQIVAIKKINLESKE--KKESILNEIAILKKCKHPNIVKYYGSYLKKDELWIVMEFC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGR-LNESE----ARrkfwQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA 174
Cdd:cd05122   80 SGGSLKDLLKNTNKtLTEQQiayvCK----EVLKGLEYLHSHGIIHRDIKAANILLTSDGEVKLIDFGLSAQLSDGKTRN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFdgPTLPILRQRVLEGR-----FRIPYFMSEDCEHLIR 249
Cdd:cd05122  156 TFVGTPYWMAPEVIQGKPY-GFKADIWSLGITAIEMAEGKPPY--SELPPMKALFLIATngppgLRNPKKWSKEFKDFLK 232
                        250       260
                 ....*....|....*....|.
gi 929654453 250 RMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd05122  233 KCLQKDPEKRPTAEQLLKHPF 253
STKc_STK33 cd14097
Catalytic domain of Serine/Threonine Kinase 33; STKs catalyze the transfer of the ...
26-271 9.16e-54

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: 188.14  E-value: 9.16e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14097    9 LGQGSFGVVIEATHKETQTKWAIKKINREKAGSSAVKLLEREVDILKHVNHAHIIHLEEVFETPKRMYLVMELCEDGELK 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL-----DNNM--NIKIADFGFG--NFFKSGELLATW 176
Cdd:cd14097   89 ELLLRKGFFSENETRHIIQSLASAVAYLHKNDIVHRDLKLENILVkssiiDNNDklNIKVTDFGLSvqKYGLGEDMLQET 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYF----MSEDCEHLIRRML 252
Cdd:cd14097  169 CGTPIYMAPEVISAHGYS-QQCDIWSIGVIMYMLLCGEPPFVAKSEEKLFEEIRKGDLTFTQSvwqsVSDAAKNVLQQLL 247
                        250
                 ....*....|....*....
gi 929654453 253 VLDPSKRLTIAQIKEHKWM 271
Cdd:cd14097  248 KVDPAHRMTASELLDNPWI 266
STKc_DRAK cd14106
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
19-271 1.82e-53

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: 187.17  E-value: 1.82e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGT-LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKM-LDHPHIIKLYQVMETKSMLYLVT 96
Cdd:cd14106    8 VYTVESTpLGRGKFAVVRKCIHKETGKEYAAKFLRKRRRGQDCRNEILHEIAVLELcKDCPRVVNLHEVYETRSELILIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFFKSGELL 173
Cdd:cd14106   88 ELAAGGELQTLLDEEECLTEADVRRLMRQILEGVQYLHERNIVHLDLKPQNILLtseFPLGDIKLCDFGISRVIGEGEEI 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYAAPEVFegqQYE--GPQLDIWSMGVVLYVLVCGALPFDGPT-----LPILRQRVlegRFRIPYF--MSEDC 244
Cdd:cd14106  168 REILGTPDYVAPEIL---SYEpiSLATDMWSIGVLTYVLLTGHSPFGGDDkqetfLNISQCNL---DFPEELFkdVSPLA 241
                        250       260
                 ....*....|....*....|....*..
gi 929654453 245 EHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14106  242 IDFIKRLLVKDPEKRLTAKECLEHPWL 268
STKc_STK36 cd14002
Catalytic domain of Serine/Threonine Kinase 36; STKs catalyze the transfer of the ...
20-268 3.52e-53

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: 185.92  E-value: 3.52e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14002    3 YHVLELIGEGSFGKVYKGRRKYTGQVVALKFIPKRGKSEKELRNLRQEIEILRKLNHPNIIEMLDSFETKKEFVVVTEYA 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KnGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWC-G 178
Cdd:cd14002   83 Q-GELFQILEDDGTLPEEEVRSIAKQLVSALHYLHSNRIIHRDMKPQNILIGKGGVVKLCDFGFARAMSCNTLVLTSIkG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSK 258
Cdd:cd14002  162 TPLYMAPELVQEQPYD-HTADLWSLGCILYELFVGQPPFYTNSIYQLVQMIVKDPVKWPSNMSPEFKSFLQGLLNKDPSK 240
                        250
                 ....*....|
gi 929654453 259 RLTIAQIKEH 268
Cdd:cd14002  241 RLSWPDLLEH 250
STKc_CaMKI_alpha cd14167
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
20-271 4.55e-53

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: 186.00  E-value: 4.55e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14167    5 YDFREVLGTGAFSEVVLAEEKRTQKLVAIKCIAKKALEGKE-TSIENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLL---LDNNMNIKIADFGFGNFFKSGELLATW 176
Cdd:cd14167   84 SGGELFDRIVEKGFYTERDASKLIFQILDAVKYLHDMGIVHRDLKPENLLyysLDEDSKIMISDFGLSKIEGSGSVMSTA 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVL--EGRFRIPYF--MSEDCEHLIRRML 252
Cdd:cd14167  164 CGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILkaEYEFDSPYWddISDSAKDFIQHLM 242
                        250
                 ....*....|....*....
gi 929654453 253 VLDPSKRLTIAQIKEHKWM 271
Cdd:cd14167  243 EKDPEKRFTCEQALQHPWI 261
STKc_TSSK6-like cd14164
Catalytic domain of testis-specific serine/threonine kinase 6 and similar proteins; STKs ...
25-271 4.58e-53

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: 185.83  E-value: 4.58e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEK-IYREVQIMKMLDHPHIIKLYQVME-TKSMLYLVTEYAKNg 102
Cdd:cd14164    7 TIGEGSFSKVKLATSQKYCCKVAIKIVDRRRASPDFVQKfLPRELSILRRVNHPNIVQMFECIEvANGRLYIVMEAAAT- 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD-NNMNIKIADFGFGNFFKS-GELLATWCGSP 180
Cdd:cd14164   86 DLLQKIQEVHHIPKDLARDMFAQMVGAVNYLHDMNIVHRDLKCENILLSaDDRKIKIADFGFARFVEDyPELSTTFCGSR 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 181 PYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRL 260
Cdd:cd14164  166 AYTPPEVILGTPYDPKKYDVWSLGVVLYVMVTGTMPFDETNVRRLRLQQRGVLYPSGVALEEPCRALIRTLLQFNPSTRP 245
                        250
                 ....*....|.
gi 929654453 261 TIAQIKEHKWM 271
Cdd:cd14164  246 SIQQVAGNSWL 256
STKc_DAPK2 cd14196
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 2; STKs ...
19-271 8.05e-53

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: 185.55  E-value: 8.05e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDA----VNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYL 94
Cdd:cd14196    6 FYDIGEELGSGQFAIVKKCREKSTGLEYAAKFIKKRQSRAsrrgVSREEIEREVSILRQVLHPNIITLHDVYENRTDVVL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAEN-LLLDNNM---NIKIADFGFGNFFKSG 170
Cdd:cd14196   86 ILELVSGGELFDFLAQKESLSEEEATSFIKQILDGVNYLHTKKIAHFDLKPENiMLLDKNIpipHIKLIDFGLAHEIEDG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 ELLATWCGSPPYAAPEVFegqQYE--GPQLDIWSMGVVLYVLVCGALPFDGPTlpilRQRVLEGRFRIPY--------FM 240
Cdd:cd14196  166 VEFKNIFGTPEFVAPEIV---NYEplGLEADMWSIGVITYILLSGASPFLGDT----KQETLANITAVSYdfdeeffsHT 238
                        250       260       270
                 ....*....|....*....|....*....|.
gi 929654453 241 SEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14196  239 SELAKDFIRKLLVKETRKRLTIQEALRHPWI 269
STKc_ULK1_2-like cd14120
Catalytic domain of the Serine/Threonine kinases, Unc-51-like kinases 1 and 2, and similar ...
26-260 9.49e-53

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: 184.88  E-value: 9.49e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHR-ITKTEVAIKIIDKSqldavNLEK----IYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAK 100
Cdd:cd14120    1 IGHGAFAVVFKGRHRkKPDLPVAIKCITKK-----NLSKsqnlLGKEIKILKELSHENVVALLDCQETSSSVYLVMEYCN 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNN---------MNIKIADFGFGNFFKSGE 171
Cdd:cd14120   76 GGDLADYLQAKGTLSEDTIRVFLQQIAAAMKALHSKGIVHRDLKPQNILLSHNsgrkpspndIRLKIADFGFARFLQDGM 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 LLATWCGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDGPTLPILRQ---RVLEGRFRIPYFMSEDCEHLI 248
Cdd:cd14120  156 MAATLCGSPMYMAPEVIMSLQYDA-KADLWSIGTIVYQCLTGKAPFQAQTPQELKAfyeKNANLRPNIPSGTSPALKDLL 234
                        250
                 ....*....|..
gi 929654453 249 RRMLVLDPSKRL 260
Cdd:cd14120  235 LGLLKRNPKDRI 246
STKc_PIM cd14005
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
20-271 1.34e-52

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: 184.36  E-value: 1.34e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQ----LDAVNLEKIYREVQIMKM---LDHPHIIKLYQVMETKSML 92
Cdd:cd14005    2 YEVGDLLGKGGFGTVYSGVRIRDGLPVAVKFVPKSRvtewAMINGPVPVPLEIALLLKaskPGVPGVIRLLDWYERPDGF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  93 YLVTEYAKNGE-IFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD-NNMNIKIADFGFGNFFKSG 170
Cdd:cd14005   82 LLIMERPEPCQdLFDFITERGALSENLARIIFRQVVEAVRHCHQRGVLHRDIKDENLLINlRTGEVKLIDFGCGALLKDS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 eLLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGptlpilRQRVLEGRFRIPYFMSEDCEHLIRR 250
Cdd:cd14005  162 -VYTDFDGTRVYSPPEWIRHGRYHGRPATVWSLGILLYDMLCGDIPFEN------DEQILRGNVLFRPRLSKECCDLISR 234
                        250       260
                 ....*....|....*....|.
gi 929654453 251 MLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14005  235 CLQFDPSKRPSLEQILSHPWF 255
STKc_Aurora-A cd14116
Catalytic domain of the Serine/Threonine kinase, Aurora-A kinase; STKs catalyze the transfer ...
20-271 2.59e-52

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: 183.62  E-value: 2.59e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLE-KIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14116    7 FEIGRPLGKGKFGNVYLAREKQSKFILALKVLFKAQLEKAGVEhQLRREVEIQSHLRHPNILRLYGYFHDATRVYLILEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGElLATWCG 178
Cdd:cd14116   87 APLGTVYRELQKLSKFDEQRTATYITELANALSYCHSKRVIHRDIKPENLLLGSAGELKIADFGWSVHAPSSR-RTTLCG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSK 258
Cdd:cd14116  166 TLDYLPPEMIEGRMHD-EKVDLWSLGVLCYEFLVGKPPFEANTYQETYKRISRVEFTFPDFVTEGARDLISRLLKHNPSQ 244
                        250
                 ....*....|...
gi 929654453 259 RLTIAQIKEHKWM 271
Cdd:cd14116  245 RPMLREVLEHPWI 257
STKc_PhKG2 cd14181
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 2 subunit; STKs ...
20-268 3.53e-52

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: 184.02  E-value: 3.53e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIID-------KSQLDAVNlEKIYREVQIMKML-DHPHIIKLYQVMETKSM 91
Cdd:cd14181   12 YDPKEVIGRGVSSVVRRCVHRHTGQEFAVKIIEvtaerlsPEQLEEVR-SSTLKEIHILRQVsGHPSIITLIDSYESSTF 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  92 LYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE 171
Cdd:cd14181   91 IFLVFDLMRRGELFDYLTEKVTLSEKETRSIMRSLLEAVSYLHANNIVHRDLKPENILLDDQLHIKLSDFGFSCHLEPGE 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 LLATWCGSPPYAAPEVFEGQQYE-----GPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRI--PYF--MSE 242
Cdd:cd14181  171 KLRELCGTPGYLAPEILKCSMDEthpgyGKEVDLWACGVILFTLLAGSPPFWHRRQMLMLRMIMEGRYQFssPEWddRSS 250
                        250       260
                 ....*....|....*....|....*.
gi 929654453 243 DCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14181  251 TVKDLISRLLVVDPEIRLTAEQALQH 276
STKc_CaMKII cd14086
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
20-271 4.26e-52

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: 184.55  E-value: 4.26e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14086    3 YDLKEELGKGAFSVVRRCVQKSTGQEFAAKIINTKKLSARDHQKLEREARICRLLKHPNIVRLHDSISEEGFHYLVFDLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFFKSGEllATW 176
Cdd:cd14086   83 TGGELFEDIVAREFYSEADASHCIQQILESVNHCHQNGIVHRDLKPENLLLaskSKGAAVKLADFGLAIEVQGDQ--QAW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 ---CGSPPYAAPEVFEGQQYEGPqLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPY----FMSEDCEHLIR 249
Cdd:cd14086  161 fgfAGTPGYLSPEVLRKDPYGKP-VDIWACGVILYILLVGYPPFWDEDQHRLYAQIKAGAYDYPSpewdTVTPEAKDLIN 239
                        250       260
                 ....*....|....*....|..
gi 929654453 250 RMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14086  240 QMLTVNPAKRITAAEALKHPWI 261
STKc_Nek2 cd08217
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
20-268 5.84e-52

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: 183.13  E-value: 5.84e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQ--VMETKSMLYLVTE 97
Cdd:cd08217    2 YEVLETIGKGSFGTVRKVRRKSDGKILVWKEIDYGKMSEKEKQQLVSEVNILRELKHPNIVRYYDriVDRANTTLYIVME 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGE----IFDYLANHGRLNESEARRKFWQILSAVDYCHGR-----KIVHRDLKAENLLLDNNMNIKIADFGFGNFFK 168
Cdd:cd08217   82 YCEGGDlaqlIKKCKKENQYIPEEFIWKIFTQLLLALYECHNRsvgggKILHRDLKPANIFLDSDNNVKLGDFGLARVLS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 SGELLA-TWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRF-RIPYFMSEDCEH 246
Cdd:cd08217  162 HDSSFAkTYVGTPYYMSPELLNEQSYD-EKSDIWSLGCLIYELCALHPPFQAANQLELAKKIKEGKFpRIPSRYSSELNE 240
                        250       260
                 ....*....|....*....|..
gi 929654453 247 LIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd08217  241 VIKSMLNVDPDKRPSVEELLQL 262
STKc_CaMKI_gamma cd14166
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
20-289 1.71e-51

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: 182.50  E-value: 1.71e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDA-VNLEKiyrEVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14166    5 FIFMEVLGSGAFSEVYLVKQRSTGKLYALKCIKKSPLSRdSSLEN---EIAVLKRIKHENIVTLEDIYESTTHYYLVMQL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFFKSGeLLAT 175
Cdd:cd14166   82 VSGGELFDRILERGVYTEKDASRVINQVLSAVKYLHENGIVHRDLKPENLLYltpDENSKIMITDFGLSKMEQNG-IMST 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEG--RFRIPYF--MSEDCEHLIRRM 251
Cdd:cd14166  161 ACGTPGYVAPEVLAQKPYS-KAVDCWSIGVITYILLCGYPPFYEETESRLFEKIKEGyyEFESPFWddISESAKDFIRHL 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 929654453 252 LVLDPSKRLTIAQIKEHKWMLIEVPVQRPVlYP----QEQEN 289
Cdd:cd14166  240 LEKNPSKRYTCEKALSHPWIIGNTALHRDI-YPsvseQIQKN 280
STKc_DAPK3 cd14195
Catalytic domain of the Serine/Threonine Kinase, Death-Associated Protein Kinase 3; STKs ...
19-271 1.95e-51

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: 181.74  E-value: 1.95e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDA----VNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYL 94
Cdd:cd14195    6 HYEMGEELGSGQFAIVRKCREKGTGKEYAAKFIKKRRLSSsrrgVSREEIEREVNILREIQHPNIITLHDIFENKTDVVL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAEN-LLLDNNM---NIKIADFGFGNFFKSG 170
Cdd:cd14195   86 ILELVSGGELFDFLAEKESLTEEEATQFLKQILDGVHYLHSKRIAHFDLKPENiMLLDKNVpnpRIKLIDFGIAHKIEAG 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 ELLATWCGSPPYAAPEVFegqQYE--GPQLDIWSMGVVLYVLVCGALPFDGPTlpilRQRVLEG------RFRIPYF--M 240
Cdd:cd14195  166 NEFKNIFGTPEFVAPEIV---NYEplGLEADMWSIGVITYILLSGASPFLGET----KQETLTNisavnyDFDEEYFsnT 238
                        250       260       270
                 ....*....|....*....|....*....|.
gi 929654453 241 SEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14195  239 SELAKDFIRRLLVKDPKKRMTIAQSLEHSWI 269
STKc_HAL4_like cd13994
Catalytic domain of Fungal Halotolerance protein 4-like Serine/Threonine kinases; STKs ...
26-271 3.67e-51

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: 180.58  E-value: 3.67e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEV--AIKIIDKSqlDAVNLEKIYREVQ-----IMKMLDHPHIIKLYQVMETKSMLY-LVTE 97
Cdd:cd13994    1 IGKGATSVVRIVTKKNPRSGVlyAVKEYRRR--DDESKRKDYVKRLtseyiISSKLHHPNIVKVLDLCQDLHGKWcLVME 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK-SGELLATW 176
Cdd:cd13994   79 YCPGGDLFTLIEKADSLSLEEKDCFFKQILRGVAYLHSHGIAHRDLKPENILLDEDGVLKLTDFGTAEVFGmPAEKESPM 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 ----CGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTL--PILRQRVLEGRFRI----PYFMS--EDC 244
Cdd:cd13994  159 saglCGSEPYMAPEVFTSGSYDGRAVDVWSCGIVLFALFTGRFPWRSAKKsdSAYKAYEKSGDFTNgpyePIENLlpSEC 238
                        250       260
                 ....*....|....*....|....*..
gi 929654453 245 EHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd13994  239 RRLIYRMLHPDPEKRITIDEALNDPWV 265
STKc_PSKH1 cd14087
Catalytic domain of the Protein Serine/Threonine kinase H1; STKs catalyze the transfer of the ...
20-271 3.67e-51

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: 180.42  E-value: 3.67e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKsqlDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14087    3 YDIKALIGRGSFSRVVRVEHRVTRQPYAIKMIET---KCRGREVCESELNVLRRVRHTNIIQLIEVFETKERVYMVMELA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFFKSG--ELLA 174
Cdd:cd14087   80 TGGELFDRIIAKGSFTERDATRVLQMVLDGVKYLHGLGITHRDLKPENLLYyhpGPDSKIMITDFGLASTRKKGpnCLMK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TWCGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRI-PYF---MSEDCEHLIRR 250
Cdd:cd14087  160 TTCGTPEYIAPEILLRKPYTQ-SVDMWAVGVIAYILLSGTMPFDDDNRTRLYRQILRAKYSYsGEPwpsVSNLAKDFIDR 238
                        250       260
                 ....*....|....*....|.
gi 929654453 251 MLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14087  239 LLTVNPGERLSATQALKHPWI 259
STKc_PKA cd14209
Catalytic subunit of the Serine/Threonine Kinase, cAMP-dependent protein kinase; STKs catalyze ...
20-270 8.73e-51

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: 180.68  E-value: 8.73e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLdaVNL---EKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVT 96
Cdd:cd14209    3 FDRIKTLGTGSFGRVMLVRHKETGNYYAMKILDKQKV--VKLkqvEHTLNEKRILQAINFPFLVKLEYSFKDNSNLYMVM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSgellATW 176
Cdd:cd14209   81 EYVPGGEMFSHLRRIGRFSEPHARFYAAQIVLAFEYLHSLDLIYRDLKPENLLIDQQGYIKVTDFGFAKRVKG----RTW 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 --CGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVL 254
Cdd:cd14209  157 tlCGTPEYLAPEIILSKGY-NKAVDWWALGVLIYEMAAGYPPFFADQPIQIYEKIVSGKVRFPSHFSSDLKDLLRNLLQV 235
                        250       260
                 ....*....|....*....|.
gi 929654453 255 DPSKRL-----TIAQIKEHKW 270
Cdd:cd14209  236 DLTKRFgnlknGVNDIKNHKW 256
STKc_MLCK cd14103
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase; STKs catalyze the ...
26-271 2.60e-50

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: 177.80  E-value: 2.60e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQldAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14103    1 LGRGKFGTVYRCVEKATGKELAAKFIKCRK--AKDREDVRNEIEIMNQLRHPRLLQLYDAFETPREMVLVMEYVAGGELF 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLL-LDNNMN-IKIADFGFGNFFKSGELLATWCGSPPY 182
Cdd:cd14103   79 ERVVDDDfELTERDCILFMRQICEGVQYMHKQGILHLDLKPENILcVSRTGNqIKIIDFGLARKYDPDKKLKVLFGTPEF 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFegqQYE--GPQLDIWSMGVVLYVLVCGALPF----DGPTLpilrQRVLEGR--FRIPYF--MSEDCEHLIRRML 252
Cdd:cd14103  159 VAPEVV---NYEpiSYATDMWSVGVICYVLLSGLSPFmgdnDAETL----ANVTRAKwdFDDEAFddISDEAKDFISKLL 231
                        250
                 ....*....|....*....
gi 929654453 253 VLDPSKRLTIAQIKEHKWM 271
Cdd:cd14103  232 VKDPRKRMSAAQCLQHPWL 250
STKc_PhKG1 cd14182
Catalytic domain of the Serine/Threonine Kinase, Phosphorylase kinase Gamma 1 subunit; STKs ...
20-268 3.85e-50

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: 178.18  E-value: 3.85e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKI-------YREVQIM-KMLDHPHIIKLYQVMETKSM 91
Cdd:cd14182    5 YEPKEILGRGVSSVVRRCIHKPTRQEYAVKIIDITGGGSFSPEEVqelreatLKEIDILrKVSGHPNIIQLKDTYETNTF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  92 LYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE 171
Cdd:cd14182   85 FFLVFDLMKKGELFDYLTEKVTLSEKETRKIMRALLEVICALHKLNIVHRDLKPENILLDDDMNIKLTDFGFSCQLDPGE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 LLATWCGSPPYAAPEVFE-----GQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEG--RFRIPYF--MSE 242
Cdd:cd14182  165 KLREVCGTPGYLAPEIIEcsmddNHPGYGKEVDMWSTGVIMYTLLAGSPPFWHRKQMLMLRMIMSGnyQFGSPEWddRSD 244
                        250       260
                 ....*....|....*....|....*.
gi 929654453 243 DCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14182  245 TVKDLISRFLVVQPQKRYTAEEALAH 270
STKc_PRKX_like cd05612
Catalytic domain of PRKX-like Protein Serine/Threonine Kinases; STKs catalyze the transfer of ...
20-270 1.08e-49

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: 177.63  E-value: 1.08e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQ-LDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd05612    3 FERIKTIGTGTFGRVHLVRDRISEHYYALKVMAIPEvIRLKQEQHVHNEKRVLKEVSHPFIIRLFWTEHDQRFLYMLMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNffksgELL-ATW- 176
Cdd:cd05612   83 VPGGELFSYLRNSGRFSNSTGLFYASEIVCALEYLHSKEIVYRDLKPENILLDKEGHIKLTDFGFAK-----KLRdRTWt 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 -CGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLD 255
Cdd:cd05612  158 lCGTPEYLAPEVIQSKGH-NKAVDWWALGILIYEMLVGYPPFFDDNPFGIYEKILAGKLEFPRHLDLYAKDLIKKLLVVD 236
                        250       260
                 ....*....|....*....|
gi 929654453 256 PSKRL-----TIAQIKEHKW 270
Cdd:cd05612  237 RTRRLgnmknGADDVKNHRW 256
STKc_Aurora-B_like cd14117
Catalytic domain of the Serine/Threonine kinase, Aurora-B kinase and similar proteins; STKs ...
20-271 1.62e-49

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: 176.21  E-value: 1.62e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLE-KIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14117    8 FDIGRPLGKGKFGNVYLAREKQSKFIVALKVLFKSQIEKEGVEhQLRREIEIQSHLRHPNILRLYNYFHDRKRIYLILEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGElLATWCG 178
Cdd:cd14117   88 APRGELYKELQKHGRFDEQRTATFMEELADALHYCHEKKVIHRDIKPENLLMGYKGELKIADFGWSVHAPSLR-RRTMCG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSK 258
Cdd:cd14117  167 TLDYLPPEMIEGRTHD-EKVDLWCIGVLCYELLVGMPPFESASHTETYRRIVKVDLKFPPFLSDGSRDLISKLLRYHPSE 245
                        250
                 ....*....|...
gi 929654453 259 RLTIAQIKEHKWM 271
Cdd:cd14117  246 RLPLKGVMEHPWV 258
STKc_CaMKI_beta cd14169
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
20-271 2.02e-49

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: 176.23  E-value: 2.02e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14169    5 YELKEKLGEGAFSEVVLAQERGSQRLVALKCIPKKALRGKE-AMVENEIAVLRRINHENIVSLEDIYESPTHLYLAMELV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDN---NMNIKIADFGFGNFFKSGeLLATW 176
Cdd:cd14169   84 TGGELFDRIIERGSYTEKDASQLIGQVLQAVKYLHQLGIVHRDLKPENLLYATpfeDSKIMISDFGLSKIEAQG-MLSTA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVL--EGRFRIPYF--MSEDCEHLIRRML 252
Cdd:cd14169  163 CGTPGYVAPELLEQKPY-GKAVDVWAIGVISYILLCGYPPFYDENDSELFNQILkaEYEFDSPYWddISESAKDFIRHLL 241
                        250
                 ....*....|....*....
gi 929654453 253 VLDPSKRLTIAQIKEHKWM 271
Cdd:cd14169  242 ERDPEKRFTCEQALQHPWI 260
STKc_RCK1-like cd14096
Catalytic domain of RCK1-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
20-271 3.85e-49

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: 176.09  E-value: 3.85e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRH-RITKTEVAIKIIDKSQLDAVNLE-----KIYREVQIMKMLDHPHIIKLYQVMETKSMLY 93
Cdd:cd14096    3 YRLINKIGEGAFSNVYKAVPlRNTGKPVAIKVVRKADLSSDNLKgssraNILKEVQIMKRLSHPNIVKLLDFQESDEYYY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLL---------------LDNNMN--- 155
Cdd:cd14096   83 IVLELADGGEIFHQIVRLTYFSEDLSRHVITQVASAVKYLHEIGVVHRDIKPENLLfepipfipsivklrkADDDETkvd 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 156 ---------------IKIADFGFGNFFKSGELLaTWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGP 220
Cdd:cd14096  163 egefipgvggggigiVKLADFGLSKQVWDSNTK-TPCGTVGYTAPEVVKDERYS-KKVDMWALGCVLYTLLCGFPPFYDE 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 929654453 221 TLPILRQRVLEG--RFRIPYF--MSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14096  241 SIETLTEKISRGdyTFLSPWWdeISKSAKDLISHLLTVDPAKRYDIDEFLAHPWI 295
STKc_PLK4 cd14186
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 4; STKs catalyze the ...
20-271 5.97e-49

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: 174.28  E-value: 5.97e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNL-EKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14186    3 FKVLNLLGKGSFACVYRARSLHTGLEVAIKMIDKKAMQKAGMvQRVRNEVEIHCQLKHPSILELYNYFEDSNYVYLVLEM 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK-SGELLATW 176
Cdd:cd14186   83 CHNGEMSRYLKNRKKpFTEDEARHFMHQIVTGMLYLHSHGILHRDLTLSNLLLTRNMNIKIADFGLATQLKmPHEKHFTM 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVfEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDP 256
Cdd:cd14186  163 CGTPNYISPEI-ATRSAHGLESDVWSLGCMFYTLLVGRPPFDTDTVKNTLNKVVLADYEMPAFLSREAQDLIHQLLRKNP 241
                        250
                 ....*....|....*
gi 929654453 257 SKRLTIAQIKEHKWM 271
Cdd:cd14186  242 ADRLSLSSVLDHPFM 256
PTZ00263 PTZ00263
protein kinase A catalytic subunit; Provisional
20-270 8.90e-49

protein kinase A catalytic subunit; Provisional


Pssm-ID: 140289 [Multi-domain]  Cd Length: 329  Bit Score: 176.16  E-value: 8.90e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQ-LDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:PTZ00263  20 FEMGETLGTGSFGRVRIAKHKGTGEYYAIKCLKKREiLKMKQVQHVAQEKSILMELSHPFIVNMMCSFQDENRVYFLLEF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNffKSGELLATWCG 178
Cdd:PTZ00263 100 VVGGELFTHLRKAGRFPNDVAKFYHAELVLAFEYLHSKDIIYRDLKPENLLLDNKGHVKVTDFGFAK--KVPDRTFTLCG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSK 258
Cdd:PTZ00263 178 TPEYLAPEVIQSKGH-GKAVDWWTMGVLLYEFIAGYPPFFDDTPFRIYEKILAGRLKFPNWFDGRARDLVKGLLQTDHTK 256
                        250
                 ....*....|....*..
gi 929654453 259 RL-----TIAQIKEHKW 270
Cdd:PTZ00263 257 RLgtlkgGVADVKNHPY 273
STKc_DCKL2 cd14184
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 2 (also called ...
20-270 1.21e-48

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: 173.29  E-value: 1.21e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14184    3 YKIGKVIGDGNFAVVKECVERSTGKEFALKIIDKAKCCGKE-HLIENEVSILRRVKHPNIIMLIEEMDTPAELYLVMELV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL----DNNMNIKIADFGFGNFFKSGelLAT 175
Cdd:cd14184   82 KGGDLFDAITSSTKYTERDASAMVYNLASALKYLHGLCIVHRDIKPENLLVceypDGTKSLKLGDFGLATVVEGP--LYT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPF--DGPTLPILRQRVLEGR--FRIPYF--MSEDCEHLIR 249
Cdd:cd14184  160 VCGTPTYVAPEIIAETGY-GLKVDIWAAGVITYILLCGFPPFrsENNLQEDLFDQILLGKleFPSPYWdnITDSAKELIS 238
                        250       260
                 ....*....|....*....|.
gi 929654453 250 RMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd14184  239 HMLQVNVEARYTAEQILSHPW 259
STKc_ULK3 cd14121
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 3; STKs catalyze the ...
26-270 2.50e-48

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: 172.09  E-value: 2.50e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVV-KLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd14121    3 LGSGTYATVyKAYRKSGAREVVAVKCVSKSSLNKASTENLLTEIELLKKLKHPHIVELKDFQWDEEHIYLIMEYCSGGDL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMN--IKIADFGFGNFFKSGELLATWCGSPPY 182
Cdd:cd14121   83 SRFIRSRRTLPESTVRRFLQQLASALQFLREHNISHMDLKPQNLLLSSRYNpvLKLADFGFAQHLKPNDEAHSLRGSPLY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLP-----ILRQRVLEGRFRIPyfMSEDCEHLIRRMLVLDPS 257
Cdd:cd14121  163 MAPEMILKKKY-DARVDLWSVGVILYECLFGRAPFASRSFEeleekIRSSKPIEIPTRPE--LSADCRDLLLRLLQRDPD 239
                        250
                 ....*....|...
gi 929654453 258 KRLTIAQIKEHKW 270
Cdd:cd14121  240 RRISFEEFFAHPF 252
STKc_PKB cd05571
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B; STKs catalyze the transfer ...
26-270 3.82e-48

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: 174.08  E-value: 3.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVN-LEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05571    3 LGKGTFGKVILCREKATGELYAIKILKKEVIIAKDeVAHTLTENRVLQNTRHPFLTSLKYSFQTNDRLCFVMEYVNGGEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLneSEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG-------FGNFFKsgellaT 175
Cdd:cd05571   83 FFHLSRERVF--SEDRTRFYgaEIVLALGYLHSQGIVYRDLKLENLLLDKDGHIKITDFGlckeeisYGATTK------T 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLD 255
Cdd:cd05571  155 FCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNRDHEVLFELILMEEVRFPSTLSPEAKSLLAGLLKKD 233
                        250       260
                 ....*....|....*....|
gi 929654453 256 PSKRL-----TIAQIKEHKW 270
Cdd:cd05571  234 PKKRLgggprDAKEIMEHPF 253
STKc_Nek8 cd08220
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
20-265 7.11e-48

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: 171.07  E-value: 7.11e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd08220    2 YEKIRVVGRGAYGTVYLCRRKDDNKLVIIKQIPVEQMTKEERQAALNEVKVLSMLHHPNIIEYYESFLEDKALMIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGR--LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNI-KIADFGFGNFFKSGELLATW 176
Cdd:cd08220   82 PGGTLFEYIQQRKGslLSEEEILHFFVQILLALHHVHSKQILHRDLKTQNILLNKKRTVvKIGDFGISKILSSKSKAYTV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFR-IPYFMSEDCEHLIRRMLVLD 255
Cdd:cd08220  162 VGTPCYISPELCEGKPYN-QKSDIWALGCVLYELASLKRAFEAANLPALVLKIMRGTFApISDRYSEELRHLILSMLHLD 240
                        250
                 ....*....|
gi 929654453 256 PSKRLTIAQI 265
Cdd:cd08220  241 PNKRPTLSEI 250
STKc_DCKL1 cd14183
Catalytic domain of the Serine/Threonine Kinase, Doublecortin-like kinase 1 (also called ...
20-271 7.37e-48

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: 171.72  E-value: 7.37e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14183    8 YKVGRTIGDGNFAVVKECVERSTGREYALKIINKSKCRGKE-HMIQNEVSILRRVKHPNIVLLIEEMDMPTELYLVMELV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL----DNNMNIKIADFGFGNFFKSGelLAT 175
Cdd:cd14183   87 KGGDLFDAITSTNKYTERDASGMLYNLASAIKYLHSLNIVHRDIKPENLLVyehqDGSKSLKLGDFGLATVVDGP--LYT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPT--LPILRQRVLEGR--FRIPYF--MSEDCEHLIR 249
Cdd:cd14183  165 VCGTPTYVAPEIIAETGY-GLKVDIWAAGVITYILLCGFPPFRGSGddQEVLFDQILMGQvdFPSPYWdnVSDSAKELIT 243
                        250       260
                 ....*....|....*....|..
gi 929654453 250 RMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14183  244 MMLQVDVDQRYSALQVLEHPWV 265
STKc_Yank1 cd05578
Catalytic domain of the Serine/Threonine Kinase, Yank1; STKs catalyze the transfer of the ...
27-271 3.00e-47

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: 169.36  E-value: 3.00e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  27 GKGNFAVVKLGRHRITKTEVAIKIIDKSQ---LDAVNleKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd05578    9 GKGSFGKVCIVQKKDTKKMFAMKYMNKQKcieKDSVR--NVLNELEILQELEHPFLVNLWYSFQDEEDMYMVVDLLLGGD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANHGRLneSEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPP 181
Cdd:cd05578   87 LRYHLQQKVKF--SEETVKFYicEIVLALDYLHSKNIIHRDIKPDNILLDEQGHVHITDFNIATKLTDGTLATSTSGTKP 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPI---LRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSK 258
Cdd:cd05578  165 YMAPEVFMRAGY-SFAVDWWSLGVTAYEMLRGKRPYEIHSRTSieeIRAKFETASVLYPAGWSEEAIDLINKLLERDPQK 243
                        250
                 ....*....|....
gi 929654453 259 RL-TIAQIKEHKWM 271
Cdd:cd05578  244 RLgDLSDLKNHPYF 257
STKc_ULK1 cd14202
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 1; STKs catalyze the ...
26-254 5.41e-47

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: 169.04  E-value: 5.41e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKT-EVAIKIIDKSQLdAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd14202   10 IGHGAFAVVFKGRHKEKHDlEVAVKCINKKNL-AKSQTLLGKEIKILKELKHENIVALYDFQEIANSVYLVMEYCNGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD---------NNMNIKIADFGFGNFFKSGELLAT 175
Cdd:cd14202   89 ADYLHTMRTLSEDTIRLFLQQIAGAMKMLHSKGIIHRDLKPQNILLSysggrksnpNNIRIKIADFGFARYLQNNMMAAT 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 929654453 176 WCGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVL 254
Cdd:cd14202  169 LCGSPMYMAPEVIMSQHYDA-KADLWSIGTIIYQCLTGKAPFQASSPQDLRLFYEKNKSLSPNIPRETSSHLRQLLLGL 246
STKc_CDK_like cd07829
Catalytic domain of Cyclin-Dependent protein Kinase-like Serine/Threonine Kinases; STKs ...
20-270 6.61e-47

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: 169.20  E-value: 6.61e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKiidKSQLDAvNLEKI----YREVQIMKMLDHPHIIKLYQVMETKSMLYLV 95
Cdd:cd07829    1 YEKLEKLGEGTYGVVYKAKDKKTGEIVALK---KIRLDN-EEEGIpstaLREISLLKELKHPNIVKLLDVIHTENKLYLV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNgEIFDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGfgnffksgelLA 174
Cdd:cd07829   77 FEYCDQ-DLKKYLDKRPGpLPPNLIKSIMYQLLRGLAYCHSHRILHRDLKPQNLLINRDGVLKLADFG----------LA 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TWCGSPP-----------YAAPEVFEGQQYEGPQLDIWSMGVVLYVL---------------------VCG--------- 213
Cdd:cd07829  146 RAFGIPLrtythevvtlwYRAPEILLGSKHYSTAVDIWSVGCIFAELitgkplfpgdseidqlfkifqILGtpteeswpg 225
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 929654453 214 --ALPFDGPTLPILRQRVLEGRFRIpyfMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07829  226 vtKLPDYKPTFPKWPKNDLEKVLPR---LDPEGIDLLSKMLQYNPAKRISAKEALKHPY 281
STKc_CASK cd14094
Catalytic domain of the Serine/Threonine Kinase, Calcium/calmodulin-dependent serine protein ...
20-271 8.51e-47

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: 169.64  E-value: 8.51e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDA---VNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVT 96
Cdd:cd14094    5 YELCEVIGKGPFSVVRRCIHRETGQQFAVKIVDVAKFTSspgLSTEDLKREASICHMLKHPHIVELLETYSSDGMLYMVF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNG----EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFFKS 169
Cdd:cd14094   85 EFMDGAdlcfEIVKRADAGFVYSEAVASHYMRQILEALRYCHDNNIIHRDVKPHCVLLaskENSAPVKLGGFGVAIQLGE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 170 GELLATW-CGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPiLRQRVLEGRFRIPYFM----SEDC 244
Cdd:cd14094  165 SGLVAGGrVGTPHFMAPEVVKREPY-GKPVDVWGCGVILFILLSGCLPFYGTKER-LFEGIIKGKYKMNPRQwshiSESA 242
                        250       260
                 ....*....|....*....|....*..
gi 929654453 245 EHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14094  243 KDLVRRMLMLDPAERITVYEALNHPWI 269
TyrKc smart00219
Tyrosine kinase, catalytic domain; Phosphotransferases. Tyrosine-specific kinase subfamily.
25-267 4.56e-46

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


Pssm-ID: 197581 [Multi-domain]  Cd Length: 257  Bit Score: 165.78  E-value: 4.56e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453    25 TLGKGNFAVVKLGRHRI----TKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAK 100
Cdd:smart00219   6 KLGEGAFGEVYKGKLKGkggkKKVEVAVKTL-KEDASEQQIEEFLREARIMRKLDHPNVVKLLGVCTEEEPLYIVMEYME 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   101 NGEIFDYL-ANHGRLNESEaRRKF-WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCG 178
Cdd:smart00219  85 GGDLLSYLrKNRPKLSLSD-LLSFaLQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYRKRGG 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   179 SPPYA--APEVFEGQQYeGPQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEG-RFRIPYFMSEDCEHLIRRMLVL 254
Cdd:smart00219 164 KLPIRwmAPESLKEGKF-TSKSDVWSFGVLLWeIFTLGEQPYPGMSNEEVLEYLKNGyRLPQPPNCPPELYDLMLQCWAE 242
                          250
                   ....*....|...
gi 929654453   255 DPSKRLTIAQIKE 267
Cdd:smart00219 243 DPEDRPTFSELVE 255
STYKc smart00221
Protein kinase; unclassified specificity; Phosphotransferases. The specificity of this class ...
25-267 5.41e-46

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: 165.80  E-value: 5.41e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453    25 TLGKGNFAVVKLGRHRI----TKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAK 100
Cdd:smart00221   6 KLGEGAFGEVYKGTLKGkgdgKEVEVAVKTL-KEDASEQQIEEFLREARIMRKLDHPNIVKLLGVCTEEEPLMIVMEYMP 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   101 NGEIFDYLANHGRLNESEARR-KF-WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCG 178
Cdd:smart00221  85 GGDLLDYLRKNRPKELSLSDLlSFaLQIARGMEYLESKNFIHRDLAARNCLVGENLVVKISDFGLSRDLYDDDYYKVKGG 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   179 SPPYA--APEVFEGQQYeGPQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEG-RFRIPYFMSEDCEHLIRRMLVL 254
Cdd:smart00221 165 KLPIRwmAPESLKEGKF-TSKSDVWSFGVLLWeIFTLGEEPYPGMSNAEVLEYLKKGyRLPKPPNCPPELYKLMLQCWAE 243
                          250
                   ....*....|...
gi 929654453   255 DPSKRLTIAQIKE 267
Cdd:smart00221 244 DPEDRPTFSELVE 256
STKc_RSK1_C cd14175
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 1 (also called ...
20-289 6.83e-46

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: 166.74  E-value: 6.83e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVnlekiyREVQIM-KMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14175    3 YVVKETIGVGSYSVCKRCVHKATNMEYAVKVIDKSKRDPS------EEIEILlRYGQHPNIITLKDVYDDGKHVYLVTEL 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLL-LDNNMN---IKIADFGFGNFFKSGE-LL 173
Cdd:cd14175   77 MRGGELLDKILRQKFFSEREASSVLHTICKTVEYLHSQGVVHRDLKPSNILyVDESGNpesLRICDFGFAKQLRAENgLL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYAAPEVFEGQQY-EGpqLDIWSMGVVLYVLVCGALPF-DGP--TLPILRQRVLEGRFRIP----YFMSEDCE 245
Cdd:cd14175  157 MTPCYTANFVAPEVLKRQGYdEG--CDIWSLGILLYTMLAGYTPFaNGPsdTPEEILTRIGSGKFTLSggnwNTVSDAAK 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 929654453 246 HLIRRMLVLDPSKRLTIAQIKEHKWMlievpVQRPVLyPQEQEN 289
Cdd:cd14175  235 DLVSKMLHVDPHQRLTAKQVLQHPWI-----TQKDKL-PQSQLN 272
STKc_FA2-like cd08529
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii FA2 and similar ...
20-265 9.83e-46

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: 164.89  E-value: 9.83e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd08529    2 FEILNKLGKGSFGVVYKVVRKVDGRVYALKQIDISRMSRKMREEAIDEARVLSKLNSPYVIKYYDSFVDKGKLNIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYL-ANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA-TW 176
Cdd:cd08529   82 ENGDLHSLIkSQRGRpLPEDQIWKFFIQTLLGLSHLHSKKILHRDIKSMNIFLDKGDNVKIGDLGVAKILSDTTNFAqTI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFR-IPYFMSEDCEHLIRRMLVLD 255
Cdd:cd08529  162 VGTPYYLSPELCEDKPYN-EKSDVWALGCVLYELCTGKHPFEAQNQGALILKIVRGKYPpISASYSQDLSQLIDSCLTKD 240
                        250
                 ....*....|
gi 929654453 256 PSKRLTIAQI 265
Cdd:cd08529  241 YRQRPDTTEL 250
STKc_CNK2-like cd08530
Catalytic domain of the Serine/Threonine Kinases, Chlamydomonas reinhardtii CNK2 and similar ...
26-265 1.02e-45

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: 164.87  E-value: 1.02e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIID------KSQLDAVNlekiyrEVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd08530    8 LGKGSYGSVYKVKRLSDNQVYALKEVNlgslsqKEREDSVN------EIRLLASVNHPNIIRYKEAFLDGNRLCIVMEYA 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGR----LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGeLLAT 175
Cdd:cd08530   82 PFGDLSKLISKRKKkrrlFPEDDIWRIFIQMLRGLKALHDQKILHRDLKSANILLSAGDLVKIGDLGISKVLKKN-LAKT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRF-RIPYFMSEDCEHLIRRMLVL 254
Cdd:cd08530  161 QIGTPLYAAPEVWKGRPYDYKS-DIWSLGCLLYEMATFRPPFEARTMQELRYKVCRGKFpPIPPVYSQDLQQIIRSLLQV 239
                        250
                 ....*....|.
gi 929654453 255 DPSKRLTIAQI 265
Cdd:cd08530  240 NPKKRPSCDKL 250
STKc_MAPKAPK cd14089
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase-activated ...
39-270 2.38e-45

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: 164.00  E-value: 2.38e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  39 HRITKTEVAIKIIDKSQldavnleKIYREVQI-MKMLDHPHIIKLYQVMET----KSMLYLVTEYAKNGEIFDYLANHGR 113
Cdd:cd14089   22 HKKTGEKFALKVLRDNP-------KARREVELhWRASGCPHIVRIIDVYENtyqgRKCLLVVMECMEGGELFSRIQERAD 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 114 LN--ESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL-DNNMN--IKIADFGFGNFFKSGELLATWCGSPPYAAPEVF 188
Cdd:cd14089   95 SAftEREAAEIMRQIGSAVAHLHSMNIAHRDLKPENLLYsSKGPNaiLKLTDFGFAKETTTKKSLQTPCYTPYYVAPEVL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 189 EGQQYEgPQLDIWSMGVVLYVLVCGALPF---DG-PTLPILRQRVLEGRFRIPY----FMSEDCEHLIRRMLVLDPSKRL 260
Cdd:cd14089  175 GPEKYD-KSCDMWSLGVIMYILLCGYPPFysnHGlAISPGMKKRIRNGQYEFPNpewsNVSEEAKDLIRGLLKTDPSERL 253
                        250
                 ....*....|
gi 929654453 261 TIAQIKEHKW 270
Cdd:cd14089  254 TIEEVMNHPW 263
STKc_CaMKK2 cd14199
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 2; ...
20-271 4.94e-45

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: 163.98  E-value: 4.94e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL------------------------DAVNLEKIYREVQIMKMLD 75
Cdd:cd14199    4 YKLKDEIGKGSYGVVKLAYNEDDNTYYAMKVLSKKKLmrqagfprrppprgaraapegctqPRGPIERVYQEIAILKKLD 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  76 HPHIIKLYQVMETKS--MLYLVTEYAKNGEIFDyLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNN 153
Cdd:cd14199   84 HPNVVKLVEVLDDPSedHLYMVFELVKQGPVME-VPTLKPLSEDQARFYFQDLIKGIEYLHYQKIIHRDVKPSNLLVGED 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 154 MNIKIADFGFGNFFK-SGELLATWCGSPPYAAPEVFEGQQ--YEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVL 230
Cdd:cd14199  163 GHIKIADFGVSNEFEgSDALLTNTVGTPAFMAPETLSETRkiFSGKALDVWAMGVTLYCFVFGQCPFMDERILSLHSKIK 242
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 929654453 231 EGRFRIP--YFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14199  243 TQPLEFPdqPDISDDLKDLLFRMLDKNPESRISVPEIKLHPWV 285
STKc_PKC cd05570
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase C; STKs catalyze the transfer ...
26-269 2.74e-44

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: 162.77  E-value: 2.74e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKS---QLDAVNLEKIYREVqIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd05570    3 LGKGSFGKVMLAERKKTDELYAIKVLKKEviiEDDDVECTMTEKRV-LALANRHPFLTGLHACFQTEDRLYFVMEYVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNESEARrkFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF---GnfFKSGELLATWC 177
Cdd:cd05570   82 DLMFHIQRARRFTEERAR--FYaaEICLALQFLHERGIIYRDLKLDNVLLDAEGHIKIADFGMckeG--IWGGNTTSTFC 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 GSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPS 257
Cdd:cd05570  158 GTPDYIAPEILREQDY-GFSVDWWALGVLLYEMLAGQSPFEGDDEDELFEAILNDEVLYPRWLSREAVSILKGLLTKDPA 236
                        250
                 ....*....|....*..
gi 929654453 258 KRLTI-----AQIKEHK 269
Cdd:cd05570  237 RRLGCgpkgeADIKAHP 253
STKc_PKB_beta cd05595
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B beta (also called Akt2); ...
26-327 7.14e-44

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: 162.10  E-value: 7.14e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVN-LEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05595    3 LGKGTFGKVILVREKATGRYYAMKILRKEVIIAKDeVAHTVTESRVLQNTRHPFLTALKYAFQTHDRLCFVMEYANGGEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGSPPYA 183
Cdd:cd05595   83 FFHLSRERVFTEDRARFYGAEIVSALEYLHSRDVVYRDIKLENLMLDKDGHIKITDFGLcKEGITDGATMKTFCGTPEYL 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 184 APEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRL--- 260
Cdd:cd05595  163 APEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHERLFELILMEEIRFPRTLSPEAKSLLAGLLKKDPKQRLggg 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 929654453 261 --TIAQIKEHKWML---IEVPVQR---PVLYPQ---EQENEPSIGEFNEQVLRLMHSLGIDQQKTIESLQNKSYNHFA 327
Cdd:cd05595  242 psDAKEVMEHRFFLsinWQDVVQKkllPPFKPQvtsEVDTRYFDDEFTAQSITITPPDRYDSLDLLESDQRTHFPQFS 319
STKc_CaMKK1 cd14200
Catalytic domain of the Serine/Threonine kinase, Calmodulin Dependent Protein Kinase Kinase 1; ...
20-271 7.50e-44

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: 160.50  E-value: 7.50e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL------------------------DAVNLEKIYREVQIMKMLD 75
Cdd:cd14200    2 YKLQSEIGKGSYGVVKLAYNESDDKYYAMKVLSKKKLlkqygfprrppprgskaaqgeqakPLAPLERVYQEIAILKKLD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  76 HPHIIKLYQVME--TKSMLYLVTEYAKNGEIFDYLANHGrLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNN 153
Cdd:cd14200   82 HVNIVKLIEVLDdpAEDNLYMVFDLLRKGPVMEVPSDKP-FSEDQARLYFRDIVLGIEYLHYQKIVHRDIKPSNLLLGDD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 154 MNIKIADFGFGNFFKSGE-LLATWCGSPPYAAPEVF--EGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVL 230
Cdd:cd14200  161 GHVKIADFGVSNQFEGNDaLLSSTAGTPAFMAPETLsdSGQSFSGKALDVWAMGVTLYCFVYGKCPFIDEFILALHNKIK 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 929654453 231 EGRFRIPY--FMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14200  241 NKPVEFPEepEISEELKDLILKMLDKNPETRITVPEIKVHPWV 283
STKc_RSK3_C cd14178
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 3 (also called ...
20-272 8.45e-44

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: 160.95  E-value: 8.45e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVnlekiyREVQIM-KMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14178    5 YEIKEDIGIGSYSVCKRCVHKATSTEYAVKIIDKSKRDPS------EEIEILlRYGQHPNIITLKDVYDDGKFVYLVMEL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLL-LDNNMN---IKIADFGFGNFFKSGE-LL 173
Cdd:cd14178   79 MRGGELLDRILRQKCFSEREASAVLCTITKTVEYLHSQGVVHRDLKPSNILyMDESGNpesIRICDFGFAKQLRAENgLL 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPF-DGP--TLPILRQRVLEGRFRIPY----FMSEDCEH 246
Cdd:cd14178  159 MTPCYTANFVAPEVLKRQGYDA-ACDIWSLGILLYTMLAGFTPFaNGPddTPEEILARIGSGKYALSGgnwdSISDAAKD 237
                        250       260
                 ....*....|....*....|....*.
gi 929654453 247 LIRRMLVLDPSKRLTIAQIKEHKWML 272
Cdd:cd14178  238 IVSKMLHVDPHQRLTAPQVLRHPWIV 263
STKc_PIM2 cd14101
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
20-271 1.85e-43

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: 158.47  E-value: 1.85e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGrHRIT-KTEVAIKIIDK------SQLDAVNLEKIyrEVQIMKML----DHPHIIKLYQVMET 88
Cdd:cd14101    2 YTMGNLLGKGGFGTVYAG-HRISdGLQVAIKQISRnrvqqwSKLPGVNPVPN--EVALLQSVgggpGHRGVIRLLDWFEI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  89 KSMLYLVTEYAKNGE-IFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNM-NIKIADFGFGNF 166
Cdd:cd14101   79 PEGFLLVLERPQHCQdLFDYITERGALDESLARRFFKQVVEAVQHCHSKGVVHRDIKDENILVDLRTgDIKLIDFGSGAT 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 167 FKSgELLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPtlpilrQRVLEGRFRIPYFMSEDCEH 246
Cdd:cd14101  159 LKD-SMYTDFDGTRVYSPPEWILYHQYHALPATVWSLGILLYDMVCGDIPFERD------TDILKAKPSFNKRVSNDCRS 231
                        250       260
                 ....*....|....*....|....*
gi 929654453 247 LIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14101  232 LIRSCLAYNPSDRPSLEQILLHPWM 256
STKc_RSK4_C cd14177
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 4 (also called ...
20-288 1.94e-43

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: 159.80  E-value: 1.94e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVnlekiyREVQI-MKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14177    6 YELKEDIGVGSYSVCKRCIHRATNMEFAVKIIDKSKRDPS------EEIEIlMRYGQHPNIITLKDVYDDGRYVYLVTEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLL-LDNNMN---IKIADFGFGNFFKSGE-LL 173
Cdd:cd14177   80 MKGGELLDRILRQKFFSEREASAVLYTITKTVDYLHCQGVVHRDLKPSNILyMDDSANadsIRICDFGFAKQLRGENgLL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPF-DGP--TLPILRQRVLEGRFRIP----YFMSEDCEH 246
Cdd:cd14177  160 LTPCYTANFVAPEVLMRQGYDA-ACDIWSLGVLLYTMLAGYTPFaNGPndTPEEILLRIGSGKFSLSggnwDTVSDAAKD 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 929654453 247 LIRRMLVLDPSKRLTIAQIKEHKWmlIEVPVQRPVLYPQEQE 288
Cdd:cd14177  239 LLSHMLHVDPHQRYTAEQVLKHSW--IACRDQLPHYQLNRQD 278
STKc_RSK2_C cd14176
C-terminal catalytic domain of the Serine/Threonine Kinase, Ribosomal S6 kinase 2 (also called ...
20-272 3.64e-43

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: 160.57  E-value: 3.64e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVnlekiyREVQIM-KMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14176   21 YEVKEDIGVGSYSVCKRCIHKATNMEFAVKIIDKSKRDPT------EEIEILlRYGQHPNIITLKDVYDDGKYVYVVTEL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLL-LDNNMN---IKIADFGFGNFFKSGE-LL 173
Cdd:cd14176   95 MKGGELLDKILRQKFFSEREASAVLFTITKTVEYLHAQGVVHRDLKPSNILyVDESGNpesIRICDFGFAKQLRAENgLL 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPF-DGP--TLPILRQRVLEGRFRIP--YF--MSEDCEH 246
Cdd:cd14176  175 MTPCYTANFVAPEVLERQGYDA-ACDIWSLGVLLYTMLTGYTPFaNGPddTPEEILARIGSGKFSLSggYWnsVSDTAKD 253
                        250       260
                 ....*....|....*....|....*.
gi 929654453 247 LIRRMLVLDPSKRLTIAQIKEHKWML 272
Cdd:cd14176  254 LVSKMLHVDPHQRLTAALVLRHPWIV 279
STKc_PAK cd06614
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase; STKs catalyze the ...
26-271 6.81e-43

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: 156.99  E-value: 6.81e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDksqLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06614    8 IGEGASGEVYKATDRATGKEVAIKKMR---LRKQNKELIINEILIMKECKHPNIVDYYDSYLVGDELWVVMEYMDGGSLT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGSPPYA 183
Cdd:cd06614   85 DIITQNPvRMNESQIAYVCREVLQGLEYLHSQNVIHRDIKSDNILLSKDGSVKLADFGFaAQLTKEKSKRNSVVGTPYWM 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 184 APEVFEGQQYeGPQLDIWSMGVVLYVLVCGALP-FDGPTLPILRQRVLEG--RFRIPYFMSEDCEHLIRRMLVLDPSKRL 260
Cdd:cd06614  165 APEVIKRKDY-GPKVDIWSLGIMCIEMAEGEPPyLEEPPLRALFLITTKGipPLKNPEKWSPEFKDFLNKCLVKDPEKRP 243
                        250
                 ....*....|.
gi 929654453 261 TIAQIKEHKWM 271
Cdd:cd06614  244 SAEELLQHPFL 254
STKc_ULK2 cd14201
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 2; STKs catalyze the ...
20-254 7.05e-43

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: 157.48  E-value: 7.05e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHR-ITKTEVAIKIIDKSQLDAVNLeKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14201    8 YSRKDLVGHGAFAVVFKGRHRkKTDWEVAIKSINKKNLSKSQI-LLGKEIKILKELQHENIVALYDVQEMPNSVFLVMEY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD---------NNMNIKIADFGFGNFFKS 169
Cdd:cd14201   87 CNGGDLADYLQAKGTLSEDTIRVFLQQIAAAMRILHSKGIIHRDLKPQNILLSyasrkkssvSGIRIKIADFGFARYLQS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 170 GELLATWCGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIR 249
Cdd:cd14201  167 NMMAATLCGSPMYMAPEVIMSQHYDA-KADLWSIGTVIYQCLVGKPPFQANSPQDLRMFYEKNKNLQPSIPRETSPYLAD 245

                 ....*
gi 929654453 250 RMLVL 254
Cdd:cd14201  246 LLLGL 250
STKc_CDK7 cd07841
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 7; STKs ...
20-270 8.06e-43

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: 158.12  E-value: 8.06e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIID----KSQLDAVNLEKIyREVQIMKMLDHPHIIKLYQVMETKSMLYLV 95
Cdd:cd07841    2 YEKGKKLGEGTYAVVYKARDKETGRIVAIKKIKlgerKEAKDGINFTAL-REIKLLQELKHPNIIGLLDVFGHKSNINLV 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYA--------KNGEIfdylanhgRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGfgnff 167
Cdd:cd07841   81 FEFMetdlekviKDKSI--------VLTPADIKSYMLMTLRGLEYLHSNWILHRDLKPNNLLIASDGVLKLADFG----- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 168 ksgelLATWCGSPP-----------YAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGA--LPFDGPtlpiLRQ-----RV 229
Cdd:cd07841  148 -----LARSFGSPNrkmthqvvtrwYRAPELLFGARHYGVGVDMWSVGCIFAELLLRVpfLPGDSD----IDQlgkifEA 218
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 929654453 230 L--------EGRFRIPYFM-----------------SEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07841  219 LgtpteenwPGVTSLPDYVefkpfpptplkqifpaaSDDALDLLQRLLTLNPNKRITARQALEHPY 284
STKc_Mnk cd14090
Catalytic domain of the Serine/Threonine kinases, Mitogen-activated protein kinase ...
20-270 1.37e-42

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: 157.19  E-value: 1.37e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGT-LGKGNFAVVKLGRHRITKTEVAIKIIDKSQldAVNLEKIYREVQIMKMLD-HPHIIKLYQVMETKSMLYLVTE 97
Cdd:cd14090    3 YKLTGElLGEGAYASVQTCINLYTGKEYAVKIIEKHP--GHSRSRVFREVETLHQCQgHPNILQLIEYFEDDERFYLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLL---LDNNMNIKIADFGFGNFFKSGEL-- 172
Cdd:cd14090   81 KMRGGPLLSHIEKRVHFTEQEASLVVRDIASALDFLHDKGIAHRDLKPENILcesMDKVSPVKICDFDLGSGIKLSSTsm 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 -------LATWCGSPPYAAPEVFEGQQYEG----PQLDIWSMGVVLYVLVCGALPFDG--------------PTLP-ILR 226
Cdd:cd14090  161 tpvttpeLLTPVGSAEYMAPEVVDAFVGEAlsydKRCDLWSLGVILYIMLCGYPPFYGrcgedcgwdrgeacQDCQeLLF 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 929654453 227 QRVLEGRFRIP----YFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd14090  241 HSIQEGEYEFPekewSHISAEAKDLISHLLVRDASQRYTAEQVLQHPW 288
PTKc cd00192
Catalytic domain of Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
26-268 3.33e-42

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: 155.00  E-value: 3.33e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRI---TKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd00192    3 LGEGAFGEVYKGKLKGgdgKTVDVAVKTL-KEDASESERKDFLKEARVMKKLGHPNVVRLLGVCTEEEPLYLVMEYMEGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNESEARRKF---------WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF------GNFF 167
Cdd:cd00192   82 DLLDFLRKSRPVFPSPEPSTLslkdllsfaIQIAKGMEYLASKKFVHRDLAARNCLVGEDLVVKISDFGLsrdiydDDYY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 168 KSGELLAT---WCgsppyaAPEVFEGQQYeGPQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEGrFRIPyfMSED 243
Cdd:cd00192  162 RKKTGGKLpirWM------APESLKDGIF-TSKSDVWSFGVLLWeIFTLGATPYPGLSNEEVLEYLRKG-YRLP--KPEN 231
                        250       260
                 ....*....|....*....|....*....
gi 929654453 244 CEHLIRRMLV----LDPSKRLTIAQIKEH 268
Cdd:cd00192  232 CPDELYELMLscwqLDPEDRPTFSELVER 260
PKc_MAPKK_plant_like cd06623
Catalytic domain of Plant dual-specificity Mitogen-Activated Protein Kinase Kinases and ...
26-271 4.48e-42

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: 154.67  E-value: 4.48e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06623    9 LGQGSSGVVYKVRHKPTGKIYALKKI-HVDGDEEFRKQLLRELKTLRSCESPYVVKCYGAFYKEGEISIVLEYMDGGSLA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHG-RKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGSPPYA 183
Cdd:cd06623   88 DLLKKVGKIPEPVLAYIARQILKGLDYLHTkRHIIHRDIKPSNLLINSKGEVKIADFGIsKVLENTLDQCNTFVGTVTYM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 184 APEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPF---DGPTLPILRQRVLEGRfriPYF-----MSEDCEHLIRRMLVLD 255
Cdd:cd06623  168 SPERIQGESYSYAA-DIWSLGLTLLECALGKFPFlppGQPSFFELMQAICDGP---PPSlpaeeFSPEFRDFISACLQKD 243
                        250
                 ....*....|....*.
gi 929654453 256 PSKRLTIAQIKEHKWM 271
Cdd:cd06623  244 PKKRPSAAELLQHPFI 259
STKc_CaMKI_delta cd14168
Catalytic domain of the Serine/Threonine kinase, Calcium/calmodulin-dependent protein kinase ...
20-271 5.23e-42

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: 155.98  E-value: 5.23e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14168   12 FEFKEVLGTGAFSEVVLAEERATGKLFAVKCIPKKALKGKE-SSIENEIAVLRKIKHENIVALEDIYESPNHLYLVMQLV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFFKSGELLATW 176
Cdd:cd14168   91 SGGELFDRIVEKGFYTEKDASTLIRQVLDAVYYLHRMGIVHRDLKPENLLYfsqDEESKIMISDFGLSKMEGKGDVMSTA 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEG--RFRIPYF--MSEDCEHLIRRML 252
Cdd:cd14168  171 CGTPGYVAPEVLAQKPYS-KAVDCWSIGVIAYILLCGYPPFYDENDSKLFEQILKAdyEFDSPYWddISDSAKDFIRNLM 249
                        250
                 ....*....|....*....
gi 929654453 253 VLDPSKRLTIAQIKEHKWM 271
Cdd:cd14168  250 EKDPNKRYTCEQALRHPWI 268
STKc_PKB_gamma cd05593
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B gamma (also called Akt3); ...
20-260 1.47e-41

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: 156.01  E-value: 1.47e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVN-LEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd05593   17 FDYLKLLGKGTFGKVILVREKASGKYYAMKILKKEVIIAKDeVAHTLTESRVLKNTRHPFLTSLKYSFQTKDRLCFVMEY 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWC 177
Cdd:cd05593   97 VNGGELFFHLSRERVFSEDRTRFYGAEIVSALDYLHSGKIVYRDLKLENLMLDKDGHIKITDFGLcKEGITDAATMKTFC 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 GSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPS 257
Cdd:cd05593  177 GTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEDIKFPRTLSADAKSLLSGLLIKDPN 255

                 ...
gi 929654453 258 KRL 260
Cdd:cd05593  256 KRL 258
STKc_CMGC cd05118
Catalytic domain of CMGC family Serine/Threonine Kinases; STKs catalyze the transfer of the ...
20-270 3.27e-41

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: 151.62  E-value: 3.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIdksQLDAVNLEKIYREVQIMKML----DHPHIIKLYQVMETKSM--LY 93
Cdd:cd05118    1 YEVLRKIGEGAFGTVWLARDKVTGEKVAIKKI---KNDFRHPKAALREIKLLKHLndveGHPNIVKLLDVFEHRGGnhLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAknGE-IFDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDN-NMNIKIADFGFGNFFKSG 170
Cdd:cd05118   78 LVFELM--GMnLYELIKDYPRgLPLDLIKSYLYQLLQALDFLHSNGIIHRDLKPENILINLeLGQLKLADFGLARSFTSP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 ElLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLpiLRQrvLEGRFRIpyFMSEDCEHLIRR 250
Cdd:cd05118  156 P-YTPYVATRWYRAPEVLLGAKPYGSSIDIWSLGCILAELLTGRPLFPGDSE--VDQ--LAKIVRL--LGTPEALDLLSK 228
                        250       260
                 ....*....|....*....|
gi 929654453 251 MLVLDPSKRLTIAQIKEHKW 270
Cdd:cd05118  229 MLKYDPAKRITASQALAHPY 248
STKc_Nek6_7 cd08224
Catalytic domain of the Serine/Threonine Kinases, Never In Mitosis gene A (NIMA)-related ...
20-265 4.27e-41

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: 152.04  E-value: 4.27e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIID-KSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd08224    2 YEIEKKIGKGQFSVVYRARCLLDGRLVALKKVQiFEMMDAKARQDCLKEIDLLQQLNHPNIIKYLASFIENNELNIVLEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEI---FDYLANHGRL-NESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA 174
Cdd:cd08224   82 ADAGDLsrlIKHFKKQKRLiPERTIWKYFVQLCSALEHMHSKRIMHRDIKPANVFITANGVVKLGDLGLGRFFSSKTTAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 -TWCGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPF--DGPTLPILRQRVLEGRFR-IP-YFMSEDCEHLIR 249
Cdd:cd08224  162 hSLVGTPYYMSPERIREQGYDFKS-DIWSLGCLLYEMAALQSPFygEKMNLYSLCKKIEKCEYPpLPaDLYSQELRDLVA 240
                        250
                 ....*....|....*.
gi 929654453 250 RMLVLDPSKRLTIAQI 265
Cdd:cd08224  241 ACIQPDPEKRPDISYV 256
STKc_PKD cd14082
Catalytic domain of the Serine/Threonine kinase, Protein Kinase D; STKs catalyze the transfer ...
25-270 4.40e-41

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: 151.80  E-value: 4.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKnGEI 104
Cdd:cd14082   10 VLGSGQFGIVYGGKHRKTGRDVAIKVIDKLRFPTKQESQLRNEVAILQQLSHPGVVNLECMFETPERVFVVMEKLH-GDM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANH--GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMN---IKIADFGFGNFFKSGELLATWCGS 179
Cdd:cd14082   89 LEMILSSekGRLPERITKFLVTQILVALRYLHSKNIVHCDLKPENVLLASAEPfpqVKLCDFGFARIIGEKSFRRSVVGT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTlpILRQRVLEGRFRIP----YFMSEDCEHLIRRMLVLD 255
Cdd:cd14082  169 PAYLAPEVLRNKGYN-RSLDMWSVGVIIYVSLSGTFPFNEDE--DINDQIQNAAFMYPpnpwKEISPDAIDLINNLLQVK 245
                        250
                 ....*....|....*
gi 929654453 256 PSKRLTIAQIKEHKW 270
Cdd:cd14082  246 MRKRYSVDKSLSHPW 260
STKc_ROCK_NDR_like cd05573
Catalytic domain of Rho-associated coiled-coil containing protein kinase (ROCK)- and Nuclear ...
20-270 5.67e-41

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: 154.36  E-value: 5.67e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYR-EVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd05573    3 FEVIKVIGRGAFGEVWLVRDKDTGQVYAMKILRKSDMLKREQIAHVRaERDILADADSPWIVRLHYAFQDEDHLYLVMEY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG---------------- 162
Cdd:cd05573   83 MPGGDLMNLLIKYDVFPEETARFYIAELVLALDSLHKLGFIHRDIKPDNILLDADGHIKLADFGlctkmnksgdresyln 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 163 --FGNFFKSGELLATW------------CGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQR 228
Cdd:cd05573  163 dsVNTLFQDNVLARRRphkqrrvraysaVGTPDYIAPEVLRGTGY-GPECDWWSLGVILYEMLYGFPPFYSDSLVETYSK 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 929654453 229 VLEGR--FRIPY--FMSEDCEHLIRRmLVLDPSKRLTIA-QIKEHKW 270
Cdd:cd05573  242 IMNWKesLVFPDdpDVSPEAIDLIRR-LLCDPEDRLGSAeEIKAHPF 287
STKc_Rim15_like cd05611
Catalytic domain of fungal Rim15-like Protein Serine/Threonine Kinases; STKs catalyze the ...
28-270 8.61e-41

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: 151.09  E-value: 8.61e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  28 KGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVN-LEKIYREVQIMKML-DHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd05611    6 KGAFGSVYLAKKRSTGDYFAIKVLKKSDMIAKNqVTNVKAERAIMMIQgESPYVAKLYYSFQSKDYLYLVMEYLNGGDCA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPYAAP 185
Cdd:cd05611   86 SLIKTLGGLPEDWAKQYIAEVVLGVEDLHQRGIIHRDIKPENLLIDQTGHLKLTDFGLSRNGLEKRHNKKFVGTPDYLAP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 186 EVFEGQQyEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCE----HLIRRMLVLDPSKRL- 260
Cdd:cd05611  166 ETILGVG-DDKMSDWWSLGCVIFEFLFGYPPFHAETPDAVFDNILSRRINWPEEVKEFCSpeavDLINRLLCMDPAKRLg 244
                        250
                 ....*....|..
gi 929654453 261 --TIAQIKEHKW 270
Cdd:cd05611  245 anGYQEIKSHPF 256
STKc_MSK1_C cd14179
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
23-271 1.26e-40

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: 152.12  E-value: 1.26e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  23 EGTLGKGNFAVVKLGRHRITKTEVAIKIIDKsQLDAvnleKIYREVQIMKMLD-HPHIIKLYQVMETKSMLYLVTEYAKN 101
Cdd:cd14179   12 DKPLGEGSFSICRKCLHKKTNQEYAVKIVSK-RMEA----NTQREIAALKLCEgHPNIVKLHEVYHDQLHTFLVMELLKG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFF-KSGELLATWC 177
Cdd:cd14179   87 GELLERIKKKQHFSETEASHIMRKLVSAVSHMHDVGVVHRDLKPENLLFtdeSDNSEIKIIDFGFARLKpPDNQPLKTPC 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 GSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFD--GPTLPI-----LRQRVLEGRFRIP----YFMSEDCEH 246
Cdd:cd14179  167 FTLHYAAPELLNYNGYD-ESCDLWSLGVILYTMLSGQVPFQchDKSLTCtsaeeIMKKIKQGDFSFEgeawKNVSQEAKD 245
                        250       260
                 ....*....|....*....|....*
gi 929654453 247 LIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14179  246 LIQGLLTVDPNKRIKMSGLRYNEWL 270
STKc_SBK1 cd13987
Catalytic domain of the Serine/Threonine kinase, SH3 Binding Kinase 1; STKs catalyze the ...
26-268 1.79e-40

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: 150.17  E-value: 1.79e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQldaVNLEKIYREVQIMKML-DHPHIIKLYQVM-ETKSMLYLVTEYAKNGE 103
Cdd:cd13987    1 LGEGTYGKVLLAVHKGSGTKMALKFVPKPS---TKLKDFLREYNISLELsVHPHIIKTYDVAfETEDYYVFAQEYAPYGD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAEN-LLLDNNMN-IKIADFGFGnfFKSGELLATWCGSPP 181
Cdd:cd13987   78 LFSIIPPQVGLPEERVKRCAAQLASALDFMHSKNLVHRDIKPENvLLFDKDCRrVKLCDFGLT--RRVGSTVKRVSGTIP 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVFEGQQYEG----PQLDIWSMGVVLYVLVCGALPF------DGPTLPILR--QRVLEG------RFripyfmSED 243
Cdd:cd13987  156 YTAPEVCEAKKNEGfvvdPSIDVWAFGVLLFCCLTGNFPWekadsdDQFYEEFVRwqKRKNTAvpsqwrRF------TPK 229
                        250       260
                 ....*....|....*....|....*
gi 929654453 244 CEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd13987  230 ALRMFKKLLAPEPERRCSIKEVFKY 254
STKc_MSK2_C cd14180
C-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
23-272 2.02e-40

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: 151.56  E-value: 2.02e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  23 EGTLGKGNFAVVKLGRHRITKTEVAIKIIDKsQLDAvnleKIYREVQIMKMLD-HPHIIKLYQVMETKSMLYLVTEYAKN 101
Cdd:cd14180   11 EPALGEGSFSVCRKCRHRQSGQEYAVKIISR-RMEA----NTQREVAALRLCQsHPNIVALHEVLHDQYHTYLVMELLRG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDN---NMNIKIADFGFGNFFKSG-ELLATWC 177
Cdd:cd14180   86 GELLDRIKKKARFSESEASQLMRSLVSAVSFMHEAGVVHRDLKPENILYADesdGAVLKVIDFGFARLRPQGsRPLQTPC 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 GSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPT-------LPILRQRVLEGRFRIP----YFMSEDCEH 246
Cdd:cd14180  166 FTLQYAAPELFSNQGYD-ESCDLWSLGVILYTMLSGQVPFQSKRgkmfhnhAADIMHKIKEGDFSLEgeawKGVSEEAKD 244
                        250       260
                 ....*....|....*....|....*.
gi 929654453 247 LIRRMLVLDPSKRLTIAQIKEHKWML 272
Cdd:cd14180  245 LVRGLLTVDPAKRLKLSELRESDWLQ 270
STKc_Cdc7_like cd06627
Catalytic domain of Cell division control protein 7-like Serine/Threonine Kinases; STKs ...
26-271 2.07e-40

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: 149.68  E-value: 2.07e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06627    8 IGRGAFGSVYKGLNLNTGEFVAIKQISLEKIPKSDLKSVMGEIDLLKKLNHPNIVKYIGSVKTKDSLYIILEYVENGSLA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG-NFFKSGELLATWCGSPPYAA 184
Cdd:cd06627   88 SIIKKFGKFPESLVAVYIYQVLEGLAYLHEQGVIHRDIKGANILTTKDGLVKLADFGVAtKLNEVEKDENSVVGTPYWMA 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 185 PEVFEGQQYeGPQLDIWSMGVVLYVLVCGALP-FDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTIA 263
Cdd:cd06627  168 PEVIEMSGV-TTASDIWSVGCTVIELLTGNPPyYDLQPMAALFRIVQDDHPPLPENISPELRDFLLQCFQKDPTLRPSAK 246

                 ....*...
gi 929654453 264 QIKEHKWM 271
Cdd:cd06627  247 ELLKHPWL 254
STKc_Trio_C cd14113
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
19-271 6.11e-40

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: 148.58  E-value: 6.11e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAvnlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14113    8 FYSEVAELGRGRFSVVKKCDQRGTKRAVATKFVNKKLMKR---DQVTHELGVLQSLQHPQLVGLLDTFETPTSYILVLEM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMN---IKIADFGFGNFFKSGELLAT 175
Cdd:cd14113   85 ADQGRLLDYVVRWGNLTEEKIRFYLREILEALQYLHNCRIAHLDLKPENILVDQSLSkptIKLADFGDAVQLNTTYYIHQ 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPF-----DGPTLPILRqrvLEGRFRIPYF--MSEDCEHLI 248
Cdd:cd14113  165 LLGSPEFAAPEIILGNPVSLTS-DLWSIGVLTYVLLSGVSPFldesvEETCLNICR---LDFSFPDDYFkgVSQKAKDFV 240
                        250       260
                 ....*....|....*....|...
gi 929654453 249 RRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14113  241 CFLLQMDPAKRPSAALCLQEQWL 263
STKc_PLK1 cd14187
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 1; STKs catalyze the ...
26-265 8.28e-40

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: 148.16  E-value: 8.28e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd14187   15 LGKGGFAKCYEITDADTKEVFAGKIVPKSLLlKPHQKEKMSMEIAIHRSLAHQHVVGFHGFFEDNDFVYVVLELCRRRSL 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK-SGELLATWCGSPPYA 183
Cdd:cd14187   95 LELHKRRKALTEPEARYYLRQIILGCQYLHRNRVIHRDLKLGNLFLNDDMEVKIGDFGLATKVEyDGERKKTLCGTPNYI 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 184 APEVF--EGQQYEgpqLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLT 261
Cdd:cd14187  175 APEVLskKGHSFE---VDIWSIGCIMYTLLVGKPPFETSCLKETYLRIKKNEYSIPKHINPVAASLIQKMLQTDPTARPT 251

                 ....
gi 929654453 262 IAQI 265
Cdd:cd14187  252 INEL 255
STKc_nPKC_eta cd05590
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C eta; STKs catalyze the ...
26-268 1.45e-39

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: 149.67  E-value: 1.45e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQ-LDAVNLEKIYREVQIMKML-DHPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd05590    3 LGKGSFGKVMLARLKESGRLYAVKVLKKDViLQDDDVECTMTEKRILSLArNHPFLTQLYCCFQTPDRLFFVMEFVNGGD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGSPPY 182
Cdd:cd05590   83 LMFHIQKSRRFDEARARFYAAEITSALMFLHDKGIIYRDLKLDNVLLDHEGHCKLADFGMcKEGIFNGKTTSTFCGTPDY 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRL-T 261
Cdd:cd05590  163 IAPEILQEMLY-GPSVDWWAMGVLLYEMLCGHAPFEAENEDDLFEAILNDEVVYPTWLSQDAVDILKAFMTKNPTMRLgS 241

                 ....*..
gi 929654453 262 IAQIKEH 268
Cdd:cd05590  242 LTLGGEE 248
STKc_PLK3 cd14189
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 3; STKs catalyze the ...
26-270 1.60e-39

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: 147.00  E-value: 1.60e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNL-EKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd14189    9 LGKGGFARCYEMTDLATNKTYAVKVIPHSRVAKPHQrEKIVNEIELHRDLHHKHVVKFSHHFEDAENIYIFLELCSRKSL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA-TWCGSPPYA 183
Cdd:cd14189   89 AHIWKARHTLLEPEVRYYLKQIISGLKYLHLKGILHRDLKLGNFFINENMELKVGDFGLAARLEPPEQRKkTICGTPNYL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 184 APEVFEgQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTIA 263
Cdd:cd14189  169 APEVLL-RQGHGPESDVWSLGCVMYTLLCGNPPFETLDLKETYRCIKQVKYTLPASLSLPARHLLAGILKRNPGDRLTLD 247

                 ....*..
gi 929654453 264 QIKEHKW 270
Cdd:cd14189  248 QILEHEF 254
STKc_MAPKAPK5 cd14171
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
26-271 1.81e-39

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: 147.99  E-value: 1.81e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIdksqldaVNLEKIYREVQIMKML-DHPHIIKLYQV----------METKSMLYL 94
Cdd:cd14171   14 LGTGISGPVRVCVKKSTGERFALKIL-------LDRPKARTEVRLHMMCsGHPNIVQIYDVyansvqfpgeSSPRARLLI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMN---IKIADFGFGNfFKSGE 171
Cdd:cd14171   87 VMELMEGGELFDRISQHRHFTEKQAAQYTKQIALAVQHCHSLNIAHRDLKPENLLLKDNSEdapIKLCDFGFAK-VDQGD 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 LLaTWCGSPPYAAPEVFEGQQYEGPQL----------------DIWSMGVVLYVLVCGALPF--DGPTLPI---LRQRVL 230
Cdd:cd14171  166 LM-TPQFTPYYVAPQVLEAQRRHRKERsgiptsptpytydkscDMWSLGVIIYIMLCGYPPFysEHPSRTItkdMKRKIM 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 231 EGRFRIP----YFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14171  245 TGSYEFPeeewSQISEMAKDIVRKLLCVDPEERMTIEEVLHHPWL 289
PK_Tyr_Ser-Thr pfam07714
Protein tyrosine and serine/threonine kinase; Protein phosphorylation, which plays a key role ...
25-268 1.96e-39

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: 146.87  E-value: 1.96e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   25 TLGKGNFAVVKLGRHRI----TKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAK 100
Cdd:pfam07714   6 KLGEGAFGEVYKGTLKGegenTKIKVAVKTL-KEGADEEEREDFLEEASIMKKLDHPNIVKLLGVCTQGEPLYIVTEYMP 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  101 NGEIFDYLANHGR-LNESEaRRKF-WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG-------FGNFFKSGE 171
Cdd:pfam07714  85 GGDLLDFLRKHKRkLTLKD-LLSMaLQIAKGMEYLESKNFVHRDLAARNCLVSENLVVKISDFGlsrdiydDDYYRKRGG 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  172 LLatwcGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLPILRQRVLEG-RFRIPYFMSEDCEHLIR 249
Cdd:pfam07714 164 GK----LPIKWMAPESLKDGKFT-SKSDVWSFGVLLWEIFTlGEQPYPGMSNEEVLEFLEDGyRLPQPENCPDELYDLMK 238
                         250
                  ....*....|....*....
gi 929654453  250 RMLVLDPSKRLTIAQIKEH 268
Cdd:pfam07714 239 QCWAYDPEDRPTFSELVED 257
STKc_PKB_alpha cd05594
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase B alpha (also called Akt1); ...
7-327 2.56e-39

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: 149.79  E-value: 2.56e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   7 PRHlqrgpvRVGFYDIE--GTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVN-LEKIYREVQIMKMLDHPHIIKLY 83
Cdd:cd05594   18 PKH------KVTMNDFEylKLLGKGTFGKVILVKEKATGRYYAMKILKKEVIVAKDeVAHTLTENRVLQNSRHPFLTALK 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  84 QVMETKSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHG-RKIVHRDLKAENLLLDNNMNIKIADFG 162
Cdd:cd05594   92 YSFQTHDRLCFVMEYANGGELFFHLSRERVFSEDRARFYGAEIVSALDYLHSeKNVVYRDLKLENLMLDKDGHIKITDFG 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 163 F-GNFFKSGELLATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMS 241
Cdd:cd05594  172 LcKEGIKDGATMKTFCGTPEYLAPEVLEDNDY-GRAVDWWGLGVVMYEMMCGRLPFYNQDHEKLFELILMEEIRFPRTLS 250
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 242 EDCEHLIRRMLVLDPSKRL-----TIAQIKEHK------WMLIEVPVQRPVLYPQ---EQENEPSIGEFNEQVLRLMHSL 307
Cdd:cd05594  251 PEAKSLLSGLLKKDPKQRLgggpdDAKEIMQHKffagivWQDVYEKKLVPPFKPQvtsETDTRYFDEEFTAQMITITPPD 330
                        330       340
                 ....*....|....*....|
gi 929654453 308 GIDQQKTIESLQNKSYNHFA 327
Cdd:cd05594  331 QDDSMETVDNERRPHFPQFS 350
STKc_Nek11 cd08222
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
20-265 2.80e-39

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: 146.80  E-value: 2.80e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKI---IDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVT 96
Cdd:cd08222    2 YRVVRKLGSGNFGTVYLVSDLKATADEELKVlkeISVGELQPDETVDANREAKLLSKLDHPAIVKFHDSFVEKESFCIVT 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNGE----IFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMnIKIADFGFGNFFK-SGE 171
Cdd:cd08222   82 EYCEGGDlddkISEYKKSGTTIDENQILDWFIQLLLAVQYMHERRILHRDLKAKNIFLKNNV-IKVGDFGISRILMgTSD 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 LLATWCGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRF-RIPYFMSEDCEHLIRR 250
Cdd:cd08222  161 LATTFTGTPYYMSPEVLKHEGYNSKS-DIWSLGCILYEMCCLKHAFDGQNLLSVMYKIVEGETpSLPDKYSKELNAIYSR 239
                        250
                 ....*....|....*
gi 929654453 251 MLVLDPSKRLTIAQI 265
Cdd:cd08222  240 MLNKDPALRPSAAEI 254
STKc_CDK9_like cd07840
Catalytic domain of Cyclin-Dependent protein Kinase 9-like Serine/Threonine Kinases; STKs ...
20-270 4.63e-39

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: 146.94  E-value: 4.63e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQldavnlEK------IYREVQIMKMLDHPHIIKLYQVM------E 87
Cdd:cd07840    1 YEKIAQIGEGTYGQVYKARNKKTGELVALKKIRMEN------EKegfpitAIREIKLLQKLDHPNVVRLKEIVtskgsaK 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  88 TKSMLYLVTEYakngeiFDY-----LANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADF 161
Cdd:cd07840   75 YKGSIYMVFEY------MDHdltglLDNPEvKFTESQIKCYMKQLLEGLQYLHSNGILHRDIKGSNILINNDGVLKLADF 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 162 GFGNFFKSGELLA------T-WcgsppYAAPEVFEGQ-QYeGPQLDIWSMGVVLYVLVCGALPFDG-------------- 219
Cdd:cd07840  149 GLARPYTKENNADytnrviTlW-----YRPPELLLGAtRY-GPEVDMWSVGCILAELFTGKPIFQGkteleqlekifelc 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 929654453 220 --PT---------LP----ILRQRVLEGRFRIPY--FMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07840  223 gsPTeenwpgvsdLPwfenLKPKKPYKRRLREVFknVIDPSALDLLDKLLTLDPKKRISADQALQHEY 290
STKc_MSK_N cd05583
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
26-271 6.87e-39

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: 145.61  E-value: 6.87e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGN----FAVVKLGRHRiTKTEVAIKIIDKSQL--DAVNLEKIYREVQIMKML-DHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd05583    2 LGTGAygkvFLVRKVGGHD-AGKLYAMKVLKKATIvqKAKTAEHTMTERQVLEAVrQSPFLVTLHYAFQTDAKLHLILDY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLAT--W 176
Cdd:cd05583   81 VNGGELFTHLYQREHFTESEVRIYIGEIVLALEHLHKLGIIYRDIKLENILLDSEGHVVLTDFGLSKEFLPGENDRAysF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGqqyeGPQ-----LDIWSMGVVLYVLVCGALPF--DGP--TLPILRQRVLEGRFRIPYFMSEDCEHL 247
Cdd:cd05583  161 CGTIEYMAPEVVRG----GSDghdkaVDWWSLGVLTYELLTGASPFtvDGErnSQSEISKRILKSHPPIPKTFSAEAKDF 236
                        250       260
                 ....*....|....*....|....*....
gi 929654453 248 IRRMLVLDPSKRL-----TIAQIKEHKWM 271
Cdd:cd05583  237 ILKLLEKDPKKRLgagprGAHEIKEHPFF 265
STKc_CDKL cd07833
Catalytic domain of Cyclin-Dependent protein Kinase Like Serine/Threonine Kinases; STKs ...
20-268 1.28e-38

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: 145.54  E-value: 1.28e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd07833    3 YEVLGVVGEGAYGVVLKCRNKATGEIVAIKKFKESEDDEDVKKTALREVKVLRQLRHENIVNLKEAFRRKGRLYLVFEYV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNgEIFDYL-ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSG------EL 172
Cdd:cd07833   83 ER-TLLELLeASPGGLPPDAVRSYIWQLLQAIAYCHSHNIIHRDIKPENILVSESGVLKLCDFGFARALTARpaspltDY 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 LAT-WcgsppYAAPEVFEGQQYEGPQLDIWSMGVV-------------------LYVL--VCGALP------------FD 218
Cdd:cd07833  162 VATrW-----YRAPELLVGDTNYGKPVDVWAIGCImaelldgeplfpgdsdidqLYLIqkCLGPLPpshqelfssnprFA 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 929654453 219 GPTLPILRQRV-LEGRFriPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd07833  237 GVAFPEPSQPEsLERRY--PGKVSSPALDFLKACLRMDPKERLTCDELLQH 285
STKc_EIF2AK cd13996
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
26-265 2.77e-38

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: 144.36  E-value: 2.77e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd13996   14 LGSGGFGSVYKVRNKVDGVTYAIKKI-RLTEKSSASEKVLREVKALAKLNHPNIVRYYTAWVEEPPLYIQMELCEGGTLR 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYL---ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNN-MNIKIADFGFGNFFKSGELLATW----- 176
Cdd:cd13996   93 DWIdrrNSSSKNDRKLALELFKQILKGVSYIHSKGIVHRDLKPSNIFLDNDdLQVKIGDFGLATSIGNQKRELNNlnnnn 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 ----------CGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCgalPFDG-----PTLPILRQRVLEgrfriPYFMS 241
Cdd:cd13996  173 ngntsnnsvgIGTPLYASPEQLDGENY-NEKADIYSLGIILFEMLH---PFKTamersTILTDLRNGILP-----ESFKA 243
                        250       260
                 ....*....|....*....|....*.
gi 929654453 242 E-DCEH-LIRRMLVLDPSKRLTIAQI 265
Cdd:cd13996  244 KhPKEAdLIQSLLSKNPEERPSAEQL 269
STKc_Pat1_like cd13993
Catalytic domain of Fungal Pat1-like Serine/Threonine kinases; STKs catalyze the transfer of ...
20-261 3.06e-38

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: 144.03  E-value: 3.06e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKI-----YREVQIMKML-DHPHIIKLYQVMETKSMLY 93
Cdd:cd13993    2 YQLISPIGEGAYGVVYLAVDLRTGRKYAIKCLYKSGPNSKDGNDFqklpqLREIDLHRRVsRHPNIITLHDVFETEVAIY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKNGEIFDYLAN--HGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNN-MNIKIADFGfgnffksg 170
Cdd:cd13993   82 IVLEYCPNGDLFEAITEnrIYVGKTELIKNVFLQLIDAVKHCHSLGIYHRDIKPENILLSQDeGTVKLCDFG-------- 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 elLATW--------CGSPPYAAPEVF-----EGQQYEGPQLDIWSMGVVLYVLVCGALPFD--GPTLPILRQRVLEGR-- 233
Cdd:cd13993  154 --LATTekismdfgVGSEFYMAPECFdevgrSLKGYPCAAGDIWSLGIILLNLTFGRNPWKiaSESDPIFYDYYLNSPnl 231
                        250       260
                 ....*....|....*....|....*...
gi 929654453 234 FRIPYFMSEDCEHLIRRMLVLDPSKRLT 261
Cdd:cd13993  232 FDVILPMSDDFYNLLRQIFTVNPNNRIL 259
STKc_ULK4 cd14010
Catalytic domain of the Serine/Threonine kinase, Unc-51-like kinase 4; STKs catalyze the ...
26-268 5.91e-38

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: 143.20  E-value: 5.91e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDavnleKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14010    8 IGRGKHSVVYKGRRKGTIEFVAIKCVDKSKRP-----EVLNEVRLTHELKHPNVLKFYEWYETSNHLWLVVEYCTGGDLE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG------------FGNFFKSGELL 173
Cdd:cd14010   83 TLLRQDGNLPESSVRKFGRDLVRGLHYIHSKGIIYCDLKPSNILLDGNGTLKLSDFGlarregeilkelFGQFSDEGNVN 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWC-----GSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLP-----ILRQRVLEGRFRIPYFMSED 243
Cdd:cd14010  163 KVSKkqakrGTPYYMAPELFQGGVHS-FASDLWALGCVLYEMFTGKPPFVAESFTelvekILNEDPPPPPPKVSSKPSPD 241
                        250       260
                 ....*....|....*....|....*
gi 929654453 244 CEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14010  242 FKSLLKGLLEKDPAKRLSWDELVKH 266
STKc_nPKC_theta_like cd05592
Catalytic domain of the Serine/Threonine Kinases, Novel Protein Kinase C theta, delta, and ...
26-260 6.42e-38

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: 144.45  E-value: 6.42e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQL---DAVNLEKIYREVQIMKMlDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd05592    3 LGKGSFGKVMLAELKGTNQYFAIKALKKDVVledDDVECTMIERRVLALAS-QHPFLTHLFCTFQTESHLFFVMEYLNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA-TWCGSPP 181
Cdd:cd05592   82 DLMFHIQQSGRFDEDRARFYGAEIICGLQFLHSRGIIYRDLKLDNVLLDREGHIKIADFGMCKENIYGENKAsTFCGTPD 161
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 929654453 182 YAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRL 260
Cdd:cd05592  162 YIAPEILKGQKYNQ-SVDWWSFGVLLYEMLIGQSPFHGEDEDELFWSICNDTPHYPRWLTKEAASCLSLLLERNPEKRL 239
STKc_phototropin_like cd05574
Catalytic domain of Phototropin-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
26-270 9.11e-38

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: 143.92  E-value: 9.11e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNleKIYR---EVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd05574    9 LGKGDVGRVYLVRLKGTGKLFAMKVLDKEEMIKRN--KVKRvltEREILATLDHPFLPTLYASFQTSTHLCFVMDYCPGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYL--ANHGRLNESEARrkFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADF----------------- 161
Cdd:cd05574   87 ELFRLLqkQPGKRLPEEVAR--FYaaEVLLALEYLHLLGFVYRDLKPENILLHESGHIMLTDFdlskqssvtpppvrksl 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 162 ---GFGNFFKSGELLATWC----------GSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTlpilRQ- 227
Cdd:cd05574  165 rkgSRRSSVKSIEKETFVAepsarsnsfvGTEEYIAPEVIKGDGH-GSAVDWWTLGILLYEMLYGTTPFKGSN----RDe 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 929654453 228 ---RVLEGRFRIP--YFMSEDCEHLIRRMLVLDPSKRL----TIAQIKEHKW 270
Cdd:cd05574  240 tfsNILKKELTFPesPPVSSEAKDLIRKLLVKDPSKRLgskrGASEIKRHPF 291
STKc_Twitchin_like cd14114
The catalytic domain of the Giant Serine/Threonine Kinases, Twitchin and Projectin; STKs ...
19-271 9.79e-38

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: 142.34  E-value: 9.79e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQldAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14114    3 HYDILEELGTGAFGVVHRCTERATGNNFAAKFIMTPH--ESDKETVRKEIQIMNQLHHPKLINLHDAFEDDNEMVLILEF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLAN-HGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD--NNMNIKIADFGFGNFFKSGELLAT 175
Cdd:cd14114   81 LSGGELFERIAAeHYKMSEAEVINYMRQVCEGLCHMHENNIVHLDIKPENIMCTtkRSNEVKLIDFGLATHLDPKESVKV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPT-LPILRQ-RVLEGRFRIPYF--MSEDCEHLIRRM 251
Cdd:cd14114  161 TTGTAEFAAPEIVEREPV-GFYTDMWAVGVLSYVLLSGLSPFAGENdDETLRNvKSCDWNFDDSAFsgISEEAKDFIRKL 239
                        250       260
                 ....*....|....*....|
gi 929654453 252 LVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14114  240 LLADPNKRMTIHQALEHPWL 259
STKc_MAST cd05609
Catalytic domain of the Protein Serine/Threonine Kinase, Microtubule-associated serine ...
29-268 9.88e-38

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: 142.93  E-value: 9.88e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  29 GNFAVVKLGRHRITKTEVAIKIIDKSQLDAVN-LEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDY 107
Cdd:cd05609   11 GAYGAVYLVRHRETRQRFAMKKINKQNLILRNqIQQVFVERDILTFAENPFVVSMYCSFETKRHLCMVMEYVEGGDCATL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 108 LANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGnffKSGEL-LAT----------- 175
Cdd:cd05609   91 LKNIGPLPVDMARMYFAETVLALEYLHSYGIVHRDLKPDNLLITSMGHIKLTDFGLS---KIGLMsLTTnlyeghiekdt 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 -------WCGSPPYAAPEVFEGQQYEGPqLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPY---FMSEDCE 245
Cdd:cd05609  168 refldkqVCGTPEYIAPEVILRQGYGKP-VDWWAMGIILYEFLVGCVPFFGDTPEELFGQVISDEIEWPEgddALPDDAQ 246
                        250       260
                 ....*....|....*....|....*.
gi 929654453 246 HLIRRMLVLDPSKRLTIA---QIKEH 268
Cdd:cd05609  247 DLITRLLQQNPLERLGTGgaeEVKQH 272
STKc_Mnk2 cd14173
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
23-271 2.10e-37

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: 142.09  E-value: 2.10e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  23 EGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQldAVNLEKIYREVQIM-KMLDHPHIIKLYQVMETKSMLYLVTEYAKN 101
Cdd:cd14173    7 EEVLGEGAYARVQTCINLITNKEYAVKIIEKRP--GHSRSRVFREVEMLyQCQGHRNVLELIEFFEEEDKFYLVFEKMRG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNI---KIADFGFGNFFK--------SG 170
Cdd:cd14173   85 GSILSHIHRRRHFNELEASVVVQDIASALDFLHNKGIAHRDLKPENILCEHPNQVspvKICDFDLGSGIKlnsdcspiST 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 ELLATWCGSPPYAAPEVFEGQQYEGP----QLDIWSMGVVLYVLVCGALPF-----------DGPTLP----ILRQRVLE 231
Cdd:cd14173  165 PELLTPCGSAEYMAPEVVEAFNEEASiydkRCDLWSLGVILYIMLSGYPPFvgrcgsdcgwdRGEACPacqnMLFESIQE 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 929654453 232 GRFRIP----YFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14173  245 GKYEFPekdwAHISCAAKDLISKLLVRDAKQRLSAAQVLQHPWV 288
STKc_PLK2 cd14188
Catalytic domain of the Serine/Threonine Kinase, Polo-like kinase 2; STKs catalyze the ...
26-268 3.49e-37

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: 140.53  E-value: 3.49e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNL-EKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd14188    9 LGKGGFAKCYEMTDLTTNKVYAAKIIPHSRVSKPHQrEKIDKEIELHRILHHKHVVQFYHYFEDKENIYILLEYCSRRSM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK-SGELLATWCGSPPYA 183
Cdd:cd14188   89 AHILKARKVLTEPEVRYYLRQIVSGLKYLHEQEILHRDLKLGNFFINENMELKVGDFGLAARLEpLEHRRRTICGTPNYL 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 184 APEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTIA 263
Cdd:cd14188  169 SPEVLNKQGH-GCESDIWALGCVMYTMLLGRPPFETTNLKETYRCIREARYSLPSSLLAPAKHLIASMLSKNPEDRPSLD 247

                 ....*
gi 929654453 264 QIKEH 268
Cdd:cd14188  248 EIIRH 252
STKc_SGK cd05575
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase; ...
25-269 3.62e-37

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: 142.46  E-value: 3.62e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEK-IYREVQI-MKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd05575    2 VIGKGSFGKVLLARHKAEGKLYAVKVLQKKAILKRNEVKhIMAERNVlLKNVKHPFLVGLHYSFQTKDKLYFVLDYVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLneSEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGS 179
Cdd:cd05575   82 ELFFHLQRERHF--PEPRARFYaaEIASALGYLHSLNIIYRDLKPENILLDSQGHVVLTDFGLcKEGIEPSDTTSTFCGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKR 259
Cdd:cd05575  160 PEYLAPEVLRKQPY-DRTVDWWCLGAVLYEMLYGLPPFYSRDTAEMYDNILHKPLRLRTNVSPSARDLLEGLLQKDRTKR 238
                        250
                 ....*....|....
gi 929654453 260 L----TIAQIKEHK 269
Cdd:cd05575  239 LgsgnDFLEIKNHS 252
STKc_PIM3 cd14102
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
20-271 4.59e-37

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: 140.09  E-value: 4.59e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLD---AVNLEKIYREVQIMKMLDHPH--IIKLYQVMETKSMLYL 94
Cdd:cd14102    2 YQVGSVLGSGGFGTVYAGSRIADGLPVAVKHVVKERVTewgTLNGVMVPLEIVLLKKVGSGFrgVIKLLDWYERPDGFLI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAK-NGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD-NNMNIKIADFGFGNFFKSgEL 172
Cdd:cd14102   82 VMERPEpVKDLFDFITEKGALDEDTARGFFRQVLEAVRHCYSCGVVHRDIKDENLLVDlRTGELKLIDFGSGALLKD-TV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 LATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPtlpilrQRVLEGRFRIPYFMSEDCEHLIRRML 252
Cdd:cd14102  161 YTDFDGTRVYSPPEWIRYHRYHGRSATVWSLGVLLYDMVCGDIPFEQD------EEILRGRLYFRRRVSPECQQLIKWCL 234
                        250
                 ....*....|....*....
gi 929654453 253 VLDPSKRLTIAQIKEHKWM 271
Cdd:cd14102  235 SLRPSDRPTLEQIFDHPWM 253
STKc_MEKK3_like cd06625
Catalytic domain of Mitogen-Activated Protein (MAP)/Extracellular signal-Regulated Kinase (ERK) ...
26-270 5.17e-37

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: 140.18  E-value: 5.17e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDA-----VN-LEkiyREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd06625    8 LGQGAFGQVYLCYDADTGRELAVKQVEIDPINTeaskeVKaLE---CEIQLLKNLQHERIVQYYGCLQDEKSLSIFMEYM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGfgnffkSGELLATWC-- 177
Cdd:cd06625   85 PGGSVKDEIKAYGALTENVTRKYTRQILEGLAYLHSNMIVHRDIKGANILRDSNGNVKLGDFG------ASKRLQTICss 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 -------GSPPYAAPEVFEGQQYeGPQLDIWSMG-VVLYVLVCGALPFD-GPTLPILRQRVLEGRFRIPYFMSEDCEHLI 248
Cdd:cd06625  159 tgmksvtGTPYWMSPEVINGEGY-GRKADIWSVGcTVVEMLTTKPPWAEfEPMAAIFKIATQPTNPQLPPHVSEDARDFL 237
                        250       260
                 ....*....|....*....|..
gi 929654453 249 RRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd06625  238 SLIFVRNKKQRPSAEELLSHSF 259
STKc_PIM1 cd14100
Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) ...
20-271 6.85e-37

Catalytic domain of the Serine/Threonine kinase, Proviral Integration Moloney virus (PIM) kinase 1; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. The PIM gene locus was discovered as a result of the cloning of retroviral intergration sites in murine Moloney leukemia virus, leading to the identification of PIM kinases. They are constitutively active STKs with a broad range of cellular targets and are overexpressed in many haematopoietic malignancies and solid cancers. Vertebrates contain three distinct PIM kinase genes (PIM1-3); each gene may result in mutliple protein isoforms. There are two PIM1 isoforms resulting from alternative translation initiation sites. PIM1 is the founding member of the PIM subfamily. It is involved in regulating cell growth, differentiation, and apoptosis. It promotes cancer development when overexpressed by inhibiting apoptosis, promoting cell proliferation, and promoting genomic instability. The PIM1 subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271002 [Multi-domain]  Cd Length: 254  Bit Score: 139.72  E-value: 6.85e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL----DAVNLEKIYREVQIMKMLDHPH--IIKLYQVMETKSMLY 93
Cdd:cd14100    2 YQVGPLLGSGGFGSVYSGIRVADGAPVAIKHVEKDRVsewgELPNGTRVPMEIVLLKKVGSGFrgVIRLLDWFERPDSFV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKN-GEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD-NNMNIKIADFGFGNFFKSgE 171
Cdd:cd14100   82 LVLERPEPvQDLFDFITERGALPEELARSFFRQVLEAVRHCHNCGVLHRDIKDENILIDlNTGELKLIDFGSGALLKD-T 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 LLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTlPILRQRVLeGRFRIpyfmSEDCEHLIRRM 251
Cdd:cd14100  161 VYTDFDGTRVYSPPEWIRFHRYHGRSAAVWSLGILLYDMVCGDIPFEHDE-EIIRGQVF-FRQRV----SSECQHLIKWC 234
                        250       260
                 ....*....|....*....|
gi 929654453 252 LVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14100  235 LALRPSDRPSFEDIQNHPWM 254
STKc_CaMK_like cd14088
Catalytic domain of an Uncharacterized group of Serine/Threonine kinases with similarity to ...
67-271 9.51e-37

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: 139.39  E-value: 9.51e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  67 EVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAE 146
Cdd:cd14088   49 EINILKMVKHPNILQLVDVFETRKEYFIFLELATGREVFDWILDQGYYSERDTSNVIRQVLEAVAYLHSLKIVHRNLKLE 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 147 NLLLDNNM---NIKIADFGFGNFFKSgeLLATWCGSPPYAAPEVFEGQQYEGPqLDIWSMGVVLYVLVCGALPF------ 217
Cdd:cd14088  129 NLVYYNRLknsKIVISDFHLAKLENG--LIKEPCGTPEYLAPEVVGRQRYGRP-VDCWAIGVIMYILLSGNPPFydeaee 205
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929654453 218 ---DGPTLPILRqRVLEG--RFRIPYF--MSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14088  206 ddyENHDKNLFR-KILAGdyEFDSPYWddISQAAKDLVTRLMEVEQDQRITAEEAISHEWI 265
STKc_MST3_like cd06609
Catalytic domain of Mammalian Ste20-like protein kinase 3-like Serine/Threonine Kinases; STKs ...
26-270 2.74e-36

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: 138.53  E-value: 2.74e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDksqLDAVN--LEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd06609    9 IGKGSFGEVYKGIDKRTNQVVAIKVID---LEEAEdeIEDIQQEIQFLSQCDSPYITKYYGSFLKGSKLWIIMEYCGGGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDyLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFgnffkSGELLATWC------ 177
Cdd:cd06609   86 VLD-LLKPGPLDETYIAFILREVLLGLEYLHSEGKIHRDIKAANILLSEEGDVKLADFGV-----SGQLTSTMSkrntfv 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 GSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDG--PtlpilrQRVLegrFRIP---------YFMSEDCEH 246
Cdd:cd06609  160 GTPFWMAPEVIKQSGYDE-KADIWSLGITAIELAKGEPPLSDlhP------MRVL---FLIPknnppslegNKFSKPFKD 229
                        250       260
                 ....*....|....*....|....
gi 929654453 247 LIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd06609  230 FVELCLNKDPKERPSAKELLKHKF 253
STKc_Mnk1 cd14174
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase ...
26-271 3.07e-36

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: 139.01  E-value: 3.07e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQldAVNLEKIYREVQIM-KMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd14174   10 LGEGAYAKVQGCVSLQNGKEYAVKIIEKNA--GHSRSRVFREVETLyQCQGNKNILELIEFFEDDTRFYLVFEKLRGGSI 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFFK--------SGELL 173
Cdd:cd14174   88 LAHIQKRKHFNEREASRVVRDIASALDFLHTKGIAHRDLKPENILCespDKVSPVKICDFDLGSGVKlnsactpiTTPEL 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYAAPEVFE----GQQYEGPQLDIWSMGVVLYVLVCGALPF-----------DGPTLPI----LRQRVLEGRF 234
Cdd:cd14174  168 TTPCGSAEYMAPEVVEvftdEATFYDKRCDLWSLGVILYIMLSGYPPFvghcgtdcgwdRGEVCRVcqnkLFESIQEGKY 247
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 929654453 235 RIP----YFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14174  248 EFPdkdwSHISSEAKDLISKLLVRDAKERLSAAQVLQHPWV 288
STKc_MEKK4 cd06626
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
27-270 3.75e-36

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: 137.82  E-value: 3.75e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  27 GKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFD 106
Cdd:cd06626    9 GEGTFGKVYTAVNLDTGELMAMKEIRFQDNDPKTIKEIADEMKVLEGLDHPNLVRYYGVEVHREEVYIFMEYCQEGTLEE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 107 YLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL------LATWCGSP 180
Cdd:cd06626   89 LLRHGRILDEAVIRVYTLQLLEGLAYLHENGIVHRDIKPANIFLDSNGLIKLGDFGSAVKLKNNTTtmapgeVNSLVGTP 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 181 PYAAPEVFEGQQYEGPQ--LDIWSMGVVLYVLVCGALP---FDGPtLPILRQRVLEGRFRIP--YFMSEDCEHLIRRMLV 253
Cdd:cd06626  169 AYMAPEVITGNKGEGHGraADIWSLGCVVLEMATGKRPwseLDNE-WAIMYHVGMGHKPPIPdsLQLSPEGKDFLSRCLE 247
                        250
                 ....*....|....*..
gi 929654453 254 LDPSKRLTIAQIKEHKW 270
Cdd:cd06626  248 SDPKKRPTASELLDHPF 264
PTZ00426 PTZ00426
cAMP-dependent protein kinase catalytic subunit; Provisional
25-270 5.34e-36

cAMP-dependent protein kinase catalytic subunit; Provisional


Pssm-ID: 173616 [Multi-domain]  Cd Length: 340  Bit Score: 139.73  E-value: 5.34e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLGRHRITK-TEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:PTZ00426  37 TLGTGSFGRVILATYKNEDfPPVAIKRFEKSKIiKQKQVDHVFSERKILNYINHPFCVNLYGSFKDESYLYLVLEFVIGG 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELlaTWCGSPPY 182
Cdd:PTZ00426 117 EFFTFLRRNKRFPNDVGCFYAAQIVLIFEYLQSLNIVYRDLKPENLLLDKDGFIKMTDFGFAKVVDTRTY--TLCGTPEY 194
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRL-- 260
Cdd:PTZ00426 195 IAPEILLNVGH-GKAADWWTLGIFIYEILVGCPPFYANEPLLIYQKILEGIIYFPKFLDNNCKHLMKKLLSHDLTKRYgn 273
                        250
                 ....*....|...
gi 929654453 261 ---TIAQIKEHKW 270
Cdd:PTZ00426 274 lkkGAQNVKEHPW 286
STKc_MEKK1_plant cd06632
Catalytic domain of the Serine/Threonine Kinase, Plant Mitogen-Activated Protein (MAP) ...
26-268 1.06e-35

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: 136.38  E-value: 1.06e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIK---IIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd06632    8 LGSGSFGSVYEGFNGDTGDFFAVKevsLVDDDKKSRESVKQLEQEIALLSKLRHPNIVQYYGTEREEDNLYIFLEYVPGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPY 182
Cdd:cd06632   88 SIHKLLQRYGAFEEPVIRLYTRQILSGLAYLHSRNTVHRDIKGANILVDTNGVVKLADFGMAKHVEAFSFAKSFKGSPYW 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYE-GPQLDIWSMGVVLYVLVCGALPFD-----GPTLPILRQRVLEgrfRIPYFMSEDCEHLIRRMLVLDP 256
Cdd:cd06632  168 MAPEVIMQKNSGyGLAVDIWSLGCTVLEMATGKPPWSqyegvAAIFKIGNSGELP---PIPDHLSPDAKDFIRLCLQRDP 244
                        250
                 ....*....|..
gi 929654453 257 SKRLTIAQIKEH 268
Cdd:cd06632  245 EDRPTASQLLEH 256
STKc_aPKC_zeta cd05617
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C zeta; STKs catalyze ...
17-334 2.17e-35

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: 138.23  E-value: 2.17e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  17 VGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLD-HPHIIKLYQVMETKSMLYL 94
Cdd:cd05617   14 LQDFDLIRVIGRGSYAKVLLVRLKKNDQIYAMKVVKKELVhDDEDIDWVQTEKHVFEQASsNPFLVGLHSCFQTTSRLFL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELL 173
Cdd:cd05617   94 VIEYVNGGDLMFHMQRQRKLPEEHARFYAAEICIALNFLHERGIIYRDLKLDNVLLDADGHIKLTDYGMcKEGLGPGDTT 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPF----DGP---TLPILRQRVLEGRFRIPYFMSEDCEH 246
Cdd:cd05617  174 STFCGTPNYIAPEILRGEEY-GFSVDWWALGVLMFEMMAGRSPFdiitDNPdmnTEDYLFQVILEKPIRIPRFLSVKASH 252
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 247 LIRRMLVLDPSKRL------TIAQIKEHK------WMLIEVPVQRPVLYPQEQENEpSIGEFNEQVLRLMHSLGIDQQKT 314
Cdd:cd05617  253 VLKGFLNKDPKERLgcqpqtGFSDIKSHTffrsidWDLLEKKQVTPPFKPQITDDY-GLENFDTQFTSEPVQLTPDDEDV 331
                        330       340
                 ....*....|....*....|
gi 929654453 315 IESLQNKSYNHFAAIYFLLV 334
Cdd:cd05617  332 IKRIDQSEFEGFEYINPLLL 351
STKc_GSK3 cd14137
The catalytic domain of the Serine/Threonine Kinase, Glycogen Synthase Kinase 3; STKs catalyze ...
20-268 4.02e-35

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: 135.71  E-value: 4.02e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIK--IIDKSQldavnlekIYREVQIMKMLDHPHIIKL----YQVMETKSMLY 93
Cdd:cd14137    6 YTIEKVIGSGSFGVVYQAKLLETGEVVAIKkvLQDKRY--------KNRELQIMRRLKHPNIVKLkyffYSSGEKKDEVY 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 L--VTEY-----AKngEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD-NNMNIKIADFGFGN 165
Cdd:cd14137   78 LnlVMEYmpetlYR--VIRHYSKNKQTIPIIYVKLYSYQLFRGLAYLHSLGICHRDIKPQNLLVDpETGVLKLCDFGSAK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 166 FFKSGELLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG----------------PTL------- 222
Cdd:cd14137  156 RLVPGEPNVSYICSRYYRAPELIFGATDYTTAIDIWSAGCVLAELLLGQPLFPGessvdqlveiikvlgtPTReqikamn 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 929654453 223 ------------PILRQRVLegrfriPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14137  236 pnytefkfpqikPHPWEKVF------PKRTPPDAIDLLSKILVYNPSKRLTALEALAH 287
STKc_MAK_like cd07830
Catalytic domain of Male germ cell-Associated Kinase-like Serine/Threonine Kinases; STKs ...
20-271 4.14e-35

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: 135.35  E-value: 4.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDK---SQLDAVNLekiyREVQ-IMKMLDHPHIIKLYQVMETKSMLYLV 95
Cdd:cd07830    1 YKVIKQLGDGTFGSVYLARNKETGELVAIKKMKKkfySWEECMNL----REVKsLRKLNEHPNIVKLKEVFRENDELYFV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAkNGEIFDYL--ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSgell 173
Cdd:cd07830   77 FEYM-EGNLYQLMkdRKGKPFSESVIRSIIYQILQGLAHIHKHGFFHRDLKPENLLVSGPEVVKIADFGLAREIRS---- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 atwcgSPP---------YAAPEVFEGQQYEGPQLDIWSMGVV---LYV---LVCGALPFD---------G-PTlpilRQR 228
Cdd:cd07830  152 -----RPPytdyvstrwYRAPEILLRSTSYSSPVDIWALGCImaeLYTlrpLFPGSSEIDqlykicsvlGtPT----KQD 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929654453 229 VLEG-------RFRIPYFM-----------SEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd07830  223 WPEGyklasklGFRFPQFAptslhqlipnaSPEAIDLIKDMLRWDPKKRPTASQALQHPYF 283
STKc_MST1_2 cd06612
Catalytic domain of the Serine/Threonine Kinases, Mammalian STe20-like protein kinase 1 and 2; ...
19-268 4.34e-35

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: 134.32  E-value: 4.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKiyrEVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd06612    4 VFDILEKLGEGSYGSVYKAIHKETGQVVAIKVV-PVEEDLQEIIK---EISILKQCDSPYIVKYYGSYFKNTDLWIVMEY 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG-----FGNFFKSGEL 172
Cdd:cd06612   80 CGAGSVSDIMKITNKtLTEEEIAAILYQTLKGLEYLHSNKKIHRDIKAGNILLNEEGQAKLADFGvsgqlTDTMAKRNTV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 LatwcGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDGptLPILRQRVLEGR-----FRIPYFMSEDCEHL 247
Cdd:cd06612  160 I----GTPFWMAPEVIQEIGYNN-KADIWSLGITAIEMAEGKPPYSD--IHPMRAIFMIPNkppptLSDPEKWSPEFNDF 232
                        250       260
                 ....*....|....*....|.
gi 929654453 248 IRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd06612  233 VKKCLVKDPEERPSAIQLLQH 253
STKc_MLCK2 cd14190
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 2; STKs catalyze ...
26-271 8.14e-35

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: 133.89  E-value: 8.14e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSqlDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14190   12 LGGGKFGKVHTCTEKRTGLKLAAKVINKQ--NSKDKEMVLLEIQVMNQLNHRNLIQLYEAIETPNEIVLFMEYVEGGELF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMN--IKIADFGFGNFFKSGELLATWCGSPPY 182
Cdd:cd14190   90 ERIVDEDyHLTEVDAMVFVRQICEGIQFMHQMRVLHLDLKPENILCVNRTGhqVKIIDFGLARRYNPREKLKVNFGTPEF 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPF----DGPTLpilrQRVLEGRFripYF-------MSEDCEHLIRRM 251
Cdd:cd14190  170 LSPEVVNYDQVSFPT-DMWSMGVITYMLLSGLSPFlgddDTETL----NNVLMGNW---YFdeetfehVSDEAKDFVSNL 241
                        250       260
                 ....*....|....*....|
gi 929654453 252 LVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14190  242 IIKERSARMSATQCLKHPWL 261
STKc_MAPKAPK3 cd14172
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
39-271 8.53e-35

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: 133.96  E-value: 8.53e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  39 HRITKTEVAIKIIDKSqldavnlEKIYREVQI-MKMLDHPHIIKLYQVMET----KSMLYLVTEYAKNGEIFDYLANHG- 112
Cdd:cd14172   25 HRRTGQKCALKLLYDS-------PKARREVEHhWRASGGPHIVHILDVYENmhhgKRCLLIIMECMEGGELFSRIQERGd 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 113 -RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFFKSGELLATWCGSPPYAAPEVF 188
Cdd:cd14172   98 qAFTEREASEIMRDIGTAIQYLHSMNIAHRDVKPENLLYtskEKDAVLKLTDFGFAKETTVQNALQTPCYTPYYVAPEVL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 189 EGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPT----LPILRQRVLEGRFRIP----YFMSEDCEHLIRRMLVLDPSKRL 260
Cdd:cd14172  178 GPEKYD-KSCDMWSLGVIMYILLCGFPPFYSNTgqaiSPGMKRRIRMGQYGFPnpewAEVSEEAKQLIRHLLKTDPTERM 256
                        250
                 ....*....|.
gi 929654453 261 TIAQIKEHKWM 271
Cdd:cd14172  257 TITQFMNHPWI 267
STKc_CDKL1_4 cd07847
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 1 and 4; ...
20-271 1.10e-34

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: 134.04  E-value: 1.10e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVnLEKI-YREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd07847    3 YEKLSKIGEGSYGVVFKCRNRETGQIVAIKKFVESEDDPV-IKKIaLREIRMLKQLKHPNLVNLIEVFRRKRKLHLVFEY 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL-----L 173
Cdd:cd07847   82 CDHTVLNELEKNPRGVPEHLIKKIIWQTLQAVNFCHKHNCIHRDVKPENILITKQGQIKLCDFGFARILTGPGDdytdyV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 AT-WcgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGA----------------------LP-----------FDG 219
Cdd:cd07847  162 ATrW-----YRAPELLVGDTQYGPPVDVWAIGCVFAELLTGQplwpgksdvdqlylirktlgdlIPrhqqifstnqfFKG 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 929654453 220 PTLPILRQRV-LEGRFR-IPY----FMsEDCehlirrmLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd07847  237 LSIPEPETREpLESKFPnISSpalsFL-KGC-------LQMDPTERLSCEELLEHPYF 286
STKc_YPK1_like cd05585
Catalytic domain of Yeast Protein Kinase 1-like Serine/Threonine Kinases; STKs catalyze the ...
26-270 1.28e-34

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: 135.01  E-value: 1.28e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05585    2 IGKGSFGKVMQVRKKDTSRIYALKTIRKAHIvSRSEVTHTLAERTVLAQVDCPFIVPLKFSFQSPEKLYLVLAFINGGEL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNF-FKSGELLATWCGSPPYA 183
Cdd:cd05585   82 FHHLQREGRFDLSRARFYTAELLCALECLHKFNVIYRDLKPENILLDYTGHIALCDFGLCKLnMKDDDKTNTFCGTPEYL 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 184 APEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTI- 262
Cdd:cd05585  162 APELLLGHGYT-KAVDWWTLGVLLYEMLTGLPPFYDENTNEMYRKILQEPLRFPDGFDRDAKDLLIGLLNRDPTKRLGYn 240
                        250
                 ....*....|
gi 929654453 263 --AQIKEHKW 270
Cdd:cd05585  241 gaQEIKNHPF 250
STKc_nPKC_theta cd05619
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C theta; STKs catalyze ...
26-329 1.63e-34

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: 135.05  E-value: 1.63e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQL---DAVNLEKIYREVQIMKMlDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd05619   13 LGKGSFGKVFLAELKGTNQFFAIKALKKDVVlmdDDVECTMVEKRVLSLAW-EHPFLTHLFCTFQTKENLFFVMEYLNGG 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL-LATWCGSPP 181
Cdd:cd05619   92 DLMFHIQSCHKFDLPRATFYAAEIICGLQFLHSKGIVYRDLKLDNILLDKDGHIKIADFGMCKENMLGDAkTSTFCGTPD 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLT 261
Cdd:cd05619  172 YIAPEILLGQKY-NTSVDWWSFGVLLYEMLIGQSPFHGQDEEELFQSIRMDNPFYPRWLEKEAKDILVKLFVREPERRLG 250
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 929654453 262 I-AQIKEH------KWMLIEVPVQRPVLYPQEQENEpSIGEFNEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAI 329
Cdd:cd05619  251 VrGDIRQHpffreiNWEALEEREIEPPFKPKVKSPF-DCSNFDKEFLNEKPRLSFADRALINSMDQNMFRNFSFV 324
STKc_MSK2_N cd05614
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
24-303 1.91e-34

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: 135.05  E-value: 1.91e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  24 GTLGKgNFAVVKLGRHRITKTeVAIKIIDKSQL--DAVNLEKIYREVQIMKML-DHPHIIKLYQVMETKSMLYLVTEYAK 100
Cdd:cd05614   11 GAYGK-VFLVRKVSGHDANKL-YAMKVLRKAALvqKAKTVEHTRTERNVLEHVrQSPFLVTLHYAFQTDAKLHLILDYVS 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATW--CG 178
Cdd:cd05614   89 GGELFTHLYQRDHFSEDEVRFYSGEIILALEHLHKLGIVYRDIKLENILLDSEGHVVLTDFGLSKEFLTEEKERTYsfCG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPF----DGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVL 254
Cdd:cd05614  169 TIEYMAPEIIRGKSGHGKAVDWWSLGILMFELLTGASPFtlegEKNTQSEVSRRILKCDPPFPSFIGPVARDLLQKLLCK 248
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 255 DPSKRLTIA-----QIKEH------KWMLIEVPVQRPVLYPQEQeNEPSIGEFNEQVLRL 303
Cdd:cd05614  249 DPKKRLGAGpqgaqEIKEHpffkglDWEALALRKVNPPFRPSIR-SELDVGNFAEEFTNL 307
STKc_DRAK1 cd14197
Catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
26-271 2.23e-34

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: 132.75  E-value: 2.23e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKML-DHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd14197   17 LGRGKFAVVRKCVEKDSGKEFAAKFMRKRRKGQDCRMEIIHEIAVLELAqANPWVINLHEVYETASEMILVLEYAAGGEI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLA--NHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNM---NIKIADFGFGNFFKSGELLATWCGS 179
Cdd:cd14197   97 FNQCVadREEAFKEKDVKRLMKQILEGVSFLHNNNVVHLDLKPQNILLTSESplgDIKIVDFGLSRILKNSEELREIMGT 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFegqQYE--GPQLDIWSMGVVLYVLVCGALPFDGPTlpiLRQRVLE-GRFRIPYfMSEDCEHL-------IR 249
Cdd:cd14197  177 PEYVAPEIL---SYEpiSTATDMWSIGVLAYVMLTGISPFLGDD---KQETFLNiSQMNVSY-SEEEFEHLsesaidfIK 249
                        250       260
                 ....*....|....*....|..
gi 929654453 250 RMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14197  250 TLLIKKPENRATAEDCLKHPWL 271
STKc_nPKC_delta cd05620
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C delta; STKs catalyze ...
26-329 2.61e-34

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: 133.92  E-value: 2.61e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQL---DAVNLEKIYREVQIMKMlDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd05620    3 LGKGSFGKVLLAELKGKGEYFAVKALKKDVVlidDDVECTMVEKRVLALAW-ENPFLTHLYCTFQTKEHLFFVMEFLNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA-TWCGSPP 181
Cdd:cd05620   82 DLMFHIQDKGRFDLYRATFYAAEIVCGLQFLHSKGIIYRDLKLDNVMLDRDGHIKIADFGMCKENVFGDNRAsTFCGTPD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLT 261
Cdd:cd05620  162 YIAPEILQGLKYTF-SVDWWSFGVLLYEMLIGQSPFHGDDEDELFESIRVDTPHYPRWITKESKDILEKLFERDPTRRLG 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 262 I-AQIKEH------KWMLIE-----VPVQRPVLYPQEQENepsigeFNEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAI 329
Cdd:cd05620  241 VvGNIRGHpffktiNWTALEkreldPPFKPKVKSPSDYSN------FDREFLSEKPRLSYSDKNLIDSMDQSAFAGFSFI 314
STKc_p70S6K cd05584
Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs ...
26-270 3.14e-34

Catalytic domain of the Serine/Threonine Kinase, 70 kDa ribosomal protein S6 kinase; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. p70S6K (or S6K) contains only one catalytic kinase domain, unlike p90 ribosomal S6 kinases (RSKs). It acts as a downstream effector of the STK mTOR (mammalian Target of Rapamycin) and plays a role in the regulation of the translation machinery during protein synthesis. p70S6K also plays a pivotal role in regulating cell size and glucose homeostasis. Its targets include S6, the translation initiation factor eIF3, and the insulin receptor substrate IRS-1, among others. Mammals contain two isoforms of p70S6K, named S6K1 and S6K2 (or S6K-beta). The p70S6K subfamily is part of a larger superfamily that includes the catalytic domains of other protein STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270736 [Multi-domain]  Cd Length: 323  Bit Score: 134.07  E-value: 3.14e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTE---VAIKIIDK-----SQLDAVNLEKiyrEVQIMKMLDHPHIIKLYQVMETKSMLYLVTE 97
Cdd:cd05584    4 LGKGGYGKVFQVRKTTGSDKgkiFAMKVLKKasivrNQKDTAHTKA---ERNILEAVKHPFIVDLHYAFQTGGKLYLILE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATW 176
Cdd:cd05584   81 YLSGGELFMHLEREGIFMEDTACFYLAEITLALGHLHSLGIIYRDLKPENILLDAQGHVKLTDFGLcKESIHDGTVTHTF 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEgQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDP 256
Cdd:cd05584  161 CGTIEYMAPEILT-RSGHGKAVDWWSLGALMYDMLTGAPPFTAENRKKTIDKILKGKLNLPPYLTNEARDLLKKLLKRNV 239
                        250
                 ....*....|....*....
gi 929654453 257 SKRL-----TIAQIKEHKW 270
Cdd:cd05584  240 SSRLgsgpgDAEEIKAHPF 258
STKc_OSR1_SPAK cd06610
Catalytic domain of the Serine/Threonine Kinases, Oxidative stress response kinase and ...
20-269 4.24e-34

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: 131.71  E-value: 4.24e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAvNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd06610    3 YELIEVIGSGATAVVYAAYCLPKKEKVAIKRIDLEKCQT-SMDELRKEIQAMSQCNHPNVVSYYTSFVVGDELWLVMPLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFD---YLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLA- 174
Cdd:cd06610   82 SGGSLLDimkSSYPRGGLDEAIIATVLKEVLKGLEYLHSNGQIHRDVKAGNILLGEDGSVKIADFGVsASLATGGDRTRk 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 ---TWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPF---------------DGPTLPilrqrvlEGRFRI 236
Cdd:cd06610  162 vrkTFVGTPCWMAPEVMEQVRGYDFKADIWSFGITAIELATGAAPYskyppmkvlmltlqnDPPSLE-------TGADYK 234
                        250       260       270
                 ....*....|....*....|....*....|...
gi 929654453 237 PYfmSEDCEHLIRRMLVLDPSKRLTIAQIKEHK 269
Cdd:cd06610  235 KY--SKSFRKMISLCLQKDPSKRPTAEELLKHK 265
STKc_CDK1_CdkB_like cd07835
Catalytic domain of Cyclin-Dependent protein Kinase 1-like Serine/Threonine Kinases and of ...
26-270 6.30e-34

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: 132.03  E-value: 6.30e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLD-AVNLEKIyREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAkNGEI 104
Cdd:cd07835    7 IGEGTYGVVYKARDKLTGEIVALKKIRLETEDeGVPSTAI-REISLLKELNHPNIVRLLDVVHSENKLYLVFEFL-DLDL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGR--LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK------SGELLATW 176
Cdd:cd07835   85 KKYMDSSPLtgLDPPLIKSYLYQLLQGIAFCHSHRVLHRDLKPQNLLIDTEGALKLADFGLARAFGvpvrtyTHEVVTLW 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 cgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLV--------------------------------CGALPFDGPTLPI 224
Cdd:cd07835  165 -----YRAPEILLGSKHYSTPVDIWSVGCIFAEMVtrrplfpgdseidqlfrifrtlgtpdedvwpgVTSLPDYKPTFPK 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 929654453 225 LRQRVLEgrfRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07835  240 WARQDLS---KVVPSLDEDGLDLLSQMLVYDPAKRISAKAALQHPY 282
STKc_obscurin_rpt1 cd14107
Catalytic kinase domain, first repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
19-270 7.49e-34

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: 130.78  E-value: 7.49e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIdksQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14107    3 VYEVKEEIGRGTFGFVKRVTHKGNGECCAAKFI---PLRSSTRARAFQERDILARLSHRRLTCLLDQFETRKTLILILEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL--DNNMNIKIADFGFGNFFKSGELLATW 176
Cdd:cd14107   80 CSSEELLDRLFLKGVVTEAEVKLYIQQVLEGIGYLHGMNILHLDIKPDNILMvsPTREDIKICDFGFAQEITPSEHQFSK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEgQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGR--FRIPYF--MSEDCEHLIRRML 252
Cdd:cd14107  160 YGSPEFVAPEIVH-QEPVSAATDIWALGVIAYLSLTCHSPFAGENDRATLLNVAEGVvsWDTPEIthLSEDAKDFIKRVL 238
                        250
                 ....*....|....*...
gi 929654453 253 VLDPSKRLTIAQIKEHKW 270
Cdd:cd14107  239 QPDPEKRPSASECLSHEW 256
PKc_DYRK_like cd14133
Catalytic domain of Dual-specificity tYrosine-phosphorylated and -Regulated Kinase-like ...
20-271 1.17e-33

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: 130.47  E-value: 1.17e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKIyrEVQIMKML------DHPHIIKLYQVMETKSMLY 93
Cdd:cd14133    1 YEVLEVLGKGTFGQVVKCYDLLTGEEVALKII-KNNKDYLDQSLD--EIRLLELLnkkdkaDKYHIVRLKDVFYFKNHLC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTE--------YAKNgEIFDYLAnHGRLneseaRRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNN--MNIKIADFGF 163
Cdd:cd14133   78 IVFEllsqnlyeFLKQ-NKFQYLS-LPRI-----RKIAQQILEALVFLHSLGLIHCDLKPENILLASYsrCQIKIIDFGS 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 164 GNFfkSGELLATWCGSPPYAAPEVFEGQQYEGPqLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFM--- 240
Cdd:cd14133  151 SCF--LTQRLYSYIQSRYYRAPEVILGLPYDEK-IDMWSLGCILAELYTGEPLFPGASEVDQLARIIGTIGIPPAHMldq 227
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 929654453 241 ----SEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14133  228 gkadDELFVDFLKKLLEIDPKERPTASQALSHPWL 262
STKc_cPKC cd05587
Catalytic domain of the Serine/Threonine Kinase, Classical (or Conventional) Protein Kinase C; ...
26-268 1.34e-33

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: 132.13  E-value: 1.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKS---QLDAVNLEKIYREVqiMKMLDHPH-IIKLYQVMETKSMLYLVTEYAKN 101
Cdd:cd05587    4 LGKGSFGKVMLAERKGTDELYAIKILKKDviiQDDDVECTMVEKRV--LALSGKPPfLTQLHSCFQTMDRLYFVMEYVNG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF--GNFFkSGELLATWCGS 179
Cdd:cd05587   82 GDLMYHIQQVGKFKEPVAVFYAAEIAVGLFFLHSKGIIYRDLKLDNVMLDAEGHIKIADFGMckEGIF-GGKTTRTFCGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKR 259
Cdd:cd05587  161 PDYIAPEIIAYQPY-GKSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICKGLLTKHPAKR 239
                        250
                 ....*....|....
gi 929654453 260 LTI-----AQIKEH 268
Cdd:cd05587  240 LGCgptgeRDIKEH 253
STKc_cPKC_beta cd05616
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C beta; STKs ...
26-268 1.48e-33

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: 132.05  E-value: 1.48e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKS---QLDAVNLEKIYREVQIMKMlDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd05616    8 LGKGSFGKVMLAERKGTDELYAVKILKKDvviQDDDVECTMVEKRVLALSG-KPPFLTQLHSCFQTMDRLYFVMEYVNGG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF--GNFFkSGELLATWCGSP 180
Cdd:cd05616   87 DLMYHIQQVGRFKEPHAVFYAAEIAIGLFFLQSKGIIYRDLKLDNVMLDSEGHIKIADFGMckENIW-DGVTTKTFCGTP 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 181 PYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRL 260
Cdd:cd05616  166 DYIAPEIIAYQPY-GKSVDWWAFGVLLYEMLAGQAPFEGEDEDELFQSIMEHNVAYPKSMSKEAVAICKGLMTKHPGKRL 244
                        250
                 ....*....|...
gi 929654453 261 TIA-----QIKEH 268
Cdd:cd05616  245 GCGpegerDIKEH 257
STKc_aPKC cd05588
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C; STKs catalyze the ...
26-326 2.13e-33

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: 131.77  E-value: 2.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKII------DKSQLDAVNLEKIYREVQImkmlDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd05588    3 IGRGSYAKVLMVELKKTKRIYAMKVIkkelvnDDEDIDWVQTEKHVFETAS----NHPFLVGLHSCFQTESRLFFVIEFV 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCG 178
Cdd:cd05588   79 NGGDLMFHMQRQRRLPEEHARFYSAEISLALNFLHEKGIIYRDLKLDNVLLDSEGHIKLTDYGMcKEGLRPGDTTSTFCG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFD---------GPTLPILRQRVLEGRFRIPYFMSEDCEHLIR 249
Cdd:cd05588  159 TPNYIAPEILRGEDY-GFSVDWWALGVLMFEMLAGRSPFDivgssdnpdQNTEDYLFQVILEKPIRIPRSLSVKAASVLK 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 250 RMLVLDPSKRL------TIAQIKEHK------WMLIEVPVQRPVLYPQeQENEPSIGEFNEQVLRLMHSLGIDQQKTIES 317
Cdd:cd05588  238 GFLNKNPAERLgchpqtGFADIQSHPffrtidWEQLEQKQVTPPYKPR-IESERDLENFDPQFTNEPVQLTPDDPDVIEK 316

                 ....*....
gi 929654453 318 LQNKSYNHF 326
Cdd:cd05588  317 IDQSEFEGF 325
STKc_TAK1 cd14058
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Activated ...
26-265 2.15e-33

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: 129.48  E-value: 2.15e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRitKTEVAIKIIDKSQldavNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14058    1 VGRGSFGVVCKARWR--NQIVAVKIIESES----EKKAFEVEVRQLSRVDHPNIIKLYGACSNQKPVCLVMEYAEGGSLY 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLanHGRLNE-----SEARRKFWQILSAVDYCHG---RKIVHRDLKAENLLLDNN-MNIKIADFGfgnffksgellaTW 176
Cdd:cd14058   75 NVL--HGKEPKpiytaAHAMSWALQCAKGVAYLHSmkpKALIHRDLKPPNLLLTNGgTVLKICDFG------------TA 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 C----------GSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQ--RVLEGRfRIPyfMSEDC 244
Cdd:cd14058  141 CdisthmtnnkGSAAWMAPEVFEGSKYS-EKCDVFSWGIILWEVITRRKPFDHIGGPAFRImwAVHNGE-RPP--LIKNC 216
                        250       260
                 ....*....|....*....|....*
gi 929654453 245 ----EHLIRRMLVLDPSKRLTIAQI 265
Cdd:cd14058  217 pkpiESLMTRCWSKDPEKRPSMKEI 241
STKc_Nek5 cd08225
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
20-265 2.41e-33

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: 129.31  E-value: 2.41e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd08225    2 YEIIKKIGEGSFGKIYLAKAKSDSEHCVIKEIDLTKMPVKEKEASKKEVILLAKMKHPNIVTFFASFQENGRLFIVMEYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYL-ANHGRL-NESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNN-MNIKIADFGFGNFFK-SGELLAT 175
Cdd:cd08225   82 DGGDLMKRInRQRGVLfSEDQILSWFVQISLGLKHIHDRKILHRDIKSQNIFLSKNgMVAKLGDFGIARQLNdSMELAYT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFR--IPYFmSEDCEHLIRRMLV 253
Cdd:cd08225  162 CVGTPYYLSPEICQNRPYNN-KTDIWSLGCVLYELCTLKHPFEGNNLHQLVLKICQGYFApiSPNF-SRDLRSLISQLFK 239
                        250
                 ....*....|..
gi 929654453 254 LDPSKRLTIAQI 265
Cdd:cd08225  240 VSPRDRPSITSI 251
PKc_Pek1_like cd06621
Catalytic domain of fungal Pek1-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
24-274 2.55e-33

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: 130.24  E-value: 2.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  24 GTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLYQ--VMETKSMLYLVTEYAKN 101
Cdd:cd06621    7 SSLGEGAGGSVTKCRLRNTKTIFALKTITTDPNPDVQ-KQILRELEINKSCASPYIVKYYGafLDEQDSSIGIAMEYCEG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEI----FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFgnffkSGELL---- 173
Cdd:cd06621   86 GSLdsiyKKVKKKGGRIGEKVLGKIAESVLKGLSYLHSRKIIHRDIKPSNILLTRKGQVKLCDFGV-----SGELVnsla 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPF--DG--PTLPIlrqRVLEGRFRIPYFMSEDCE---- 245
Cdd:cd06621  161 GTFTGTSYYMAPERIQGGPYS-ITSDVWSLGLTLLEVAQNRFPFppEGepPLGPI---ELLSYIVNMPNPELKDEPengi 236
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 929654453 246 -------HLIRRMLVLDPSKRLTIAQIKEHKWMLIE 274
Cdd:cd06621  237 kwsesfkDFIEKCLEKDGTRRPGPWQMLAHPWIKAQ 272
STKc_RSK_N cd05582
N-terminal catalytic domain of the Serine/Threonine Kinase, 90 kDa ribosomal protein S6 kinase; ...
26-268 3.08e-33

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: 130.98  E-value: 3.08e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITK---TEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd05582    3 LGQGSFGKVFLVRKITGPdagTLYAMKVLKKATLKVRDRVRTKMERDILADVNHPFIVKLHYAFQTEGKLYLILDFLRGG 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGN-FFKSGELLATWCGSPP 181
Cdd:cd05582   83 DLFTRLSKEVMFTEEDVKFYLAELALALDHLHSLGIIYRDLKPENILLDEDGHIKLTDFGLSKeSIDHEKKAYSFCGTVE 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVFEgQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRL- 260
Cdd:cd05582  163 YMAPEVVN-RRGHTQSADWWSFGVLMFEMLTGSLPFQGKDRKETMTMILKAKLGMPQFLSPEAQSLLRALFKRNPANRLg 241
                        250
                 ....*....|..
gi 929654453 261 ----TIAQIKEH 268
Cdd:cd05582  242 agpdGVEEIKRH 253
STKc_MLCK3 cd14192
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 3; STKs catalyze ...
26-271 3.55e-33

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: 128.93  E-value: 3.55e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSqlDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14192   12 LGGGRFGQVHKCTELSTGLTLAAKIIKVK--GAKEREEVKNEINIMNQLNHVNLIQLYDAFESKTNLTLIMEYVDGGELF 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNM--NIKIADFGFGNFFKSGELLATWCGSPPY 182
Cdd:cd14192   90 DRITDESyQLTELDAILFTRQICEGVHYLHQHYILHLDLKPENILCVNSTgnQIKIIDFGLARRYKPREKLKVNFGTPEF 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGR--FRIPYF--MSEDCEHLIRRMLVLDPSK 258
Cdd:cd14192  170 LAPEVVNYDFVSFPT-DMWSVGVITYMLLSGLSPFLGETDAETMNNIVNCKwdFDAEAFenLSEEAKDFISRLLVKEKSC 248
                        250
                 ....*....|...
gi 929654453 259 RLTIAQIKEHKWM 271
Cdd:cd14192  249 RMSATQCLKHEWL 261
STKc_NDR_like cd05599
Catalytic domain of Nuclear Dbf2-Related kinase-like Protein Serine/Threonine Kinases; STKs ...
25-270 3.86e-33

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: 130.81  E-value: 3.86e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLdavnLEK-----IYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd05599    8 VIGRGAFGEVRLVRKKDTGHVYAMKKLRKSEM----LEKeqvahVRAERDILAEADNPWVVKLYYSFQDEENLYLIMEFL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGS 179
Cdd:cd05599   84 PGGDMMTLLMKKDTLTEEETRFYIAETVLAIESIHKLGYIHRDIKPDNLLLDARGHIKLSDFGLCTGLKKSHLAYSTVGT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGR--FRIPYFM--SEDCEHLIRRmLVLD 255
Cdd:cd05599  164 PDYIAPEVFLQKGY-GKECDWWSLGVIMYEMLIGYPPFCSDDPQETCRKIMNWRetLVFPPEVpiSPEAKDLIER-LLCD 241
                        250
                 ....*....|....*...
gi 929654453 256 PSKRL---TIAQIKEHKW 270
Cdd:cd05599  242 AEHRLganGVEEIKSHPF 259
STKc_BUR1 cd07866
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase (CDK), ...
20-270 4.34e-33

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: 130.13  E-value: 4.34e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIK-IIDKSQLDAVNLEKIyREVQIMKMLDHPHIIKLY--------QVMETKS 90
Cdd:cd07866   10 YEILGKLGEGTFGEVYKARQIKTGRVVALKkILMHNEKDGFPITAL-REIKILKKLKHPNVVPLIdmaverpdKSKRKRG 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  91 MLYLVTEYAKNgEIFDYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGfgnffks 169
Cdd:cd07866   89 SVYMVTPYMDH-DLSGLLENPSvKLTESQIKCYMLQLLEGINYLHENHILHRDIKAANILIDNQGILKIADFG------- 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 170 geLLATWCGSPP---------------------YAAPEVFEGQQYEGPQLDIWSMGVVLYVL------------------ 210
Cdd:cd07866  161 --LARPYDGPPPnpkggggggtrkytnlvvtrwYRPPELLLGERRYTTAVDIWGIGCVFAEMftrrpilqgksdidqlhl 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 929654453 211 ---VCG-----------ALP-----FDGPTlpilRQRVLEGRFRIpyfMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07866  239 ifkLCGtpteetwpgwrSLPgcegvHSFTN----YPRTLEERFGK---LGPEGLDLLSKLLSLDPYKRLTASDALEHPY 310
STKc_Pho85 cd07836
Catalytic domain of the Serine/Threonine Kinase, Fungal Cyclin-Dependent protein Kinase Pho85; ...
26-270 4.81e-33

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: 129.52  E-value: 4.81e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIdksQLDAVN--LEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNgE 103
Cdd:cd07836    8 LGEGTYATVYKGRNRTTGEIVALKEI---HLDAEEgtPSTAIREISLMKELKHENIVRLHDVIHTENKLMLVFEYMDK-D 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANHGR---LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK------SGELLA 174
Cdd:cd07836   84 LKKYMDTHGVrgaLDPNTVKSFTYQLLKGIAFCHENRVLHRDLKPQNLLINKRGELKLADFGLARAFGipvntfSNEVVT 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TWcgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPT-----LPILR-------------QRVLEGRFRI 236
Cdd:cd07836  164 LW-----YRAPDVLLGSRTYSTSIDIWSVGCIMAEMITGRPLFPGTNnedqlLKIFRimgtptestwpgiSQLPEYKPTF 238
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 237 PYFMSEDCEHLI-----------RRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07836  239 PRYPPQDLQQLFphadplgidllHRLLQLNPELRISAHDALQHPW 283
STKc_aPKC_iota cd05618
Catalytic domain of the Serine/Threonine Kinase, Atypical Protein Kinase C iota; STKs catalyze ...
8-334 7.06e-33

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: 131.31  E-value: 7.06e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   8 RHLQRGPVRVGF--YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-DAVNLEKIYREVQIMKML-DHPHIIKLY 83
Cdd:cd05618    8 RESGKASSSLGLqdFDLLRVIGRGSYAKVLLVRLKKTERIYAMKVVKKELVnDDEDIDWVQTEKHVFEQAsNHPFLVGLH 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  84 QVMETKSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF 163
Cdd:cd05618   88 SCFQTESRLFFVIEYVNGGDLMFHMQRQRKLPEEHARFYSAEISLALNYLHERGIIYRDLKLDNVLLDSEGHIKLTDYGM 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 164 -GNFFKSGELLATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPF------DGP---TLPILRQRVLEGR 233
Cdd:cd05618  168 cKEGLRPGDTTSTFCGTPNYIAPEILRGEDY-GFSVDWWALGVLMFEMMAGRSPFdivgssDNPdqnTEDYLFQVILEKQ 246
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 234 FRIPYFMSEDCEHLIRRMLVLDPSKRL------TIAQIKEHK------WMLIEVPVQRPVLYPQeQENEPSIGEFNEQVL 301
Cdd:cd05618  247 IRIPRSLSVKAASVLKSFLNKDPKERLgchpqtGFADIQGHPffrnvdWDLMEQKQVVPPFKPN-ISGEFGLDNFDSQFT 325
                        330       340       350
                 ....*....|....*....|....*....|...
gi 929654453 302 RLMHSLGIDQQKTIESLQNKSYNHFAAIYFLLV 334
Cdd:cd05618  326 NEPVQLTPDDDDIVRKIDQSEFEGFEYINPLLM 358
STKc_MLCK4 cd14193
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 4; STKs catalyze ...
19-271 1.13e-32

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: 127.72  E-value: 1.13e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGT--LGKGNFAVVKLGRHRITKTEVAIKIID-KSQLDAvnlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLV 95
Cdd:cd14193    3 YYNVNKEeiLGGGRFGQVHKCEEKSSGLKLAAKIIKaRSQKEK---EEVKNEIEVMNQLNHANLIQLYDAFESRNDIVLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNN--MNIKIADFGFGNFFKSGEL 172
Cdd:cd14193   80 MEYVDGGELFDRIIDENyNLTELDTILFIKQICEGIQYMHQMYILHLDLKPENILCVSReaNQVKIIDFGLARRYKPREK 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 LATWCGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPF----DGPTL-PILR-QRVLEG-RFRIpyfMSEDCE 245
Cdd:cd14193  160 LRVNFGTPEFLAPEVVNYEFVSFPT-DMWSLGVIAYMLLSGLSPFlgedDNETLnNILAcQWDFEDeEFAD---ISEEAK 235
                        250       260
                 ....*....|....*....|....*.
gi 929654453 246 HLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14193  236 DFISKLLIKEKSWRMSASEALKHPWL 261
STKc_Byr2_like cd06628
Catalytic domain of the Serine/Threonine Kinases, fungal Byr2-like Mitogen-Activated Protein ...
22-271 1.22e-32

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: 127.65  E-value: 1.22e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  22 IEGTL-GKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVN-------LEKIYREVQIMKMLDHPHIIKLYQVMETKSMLY 93
Cdd:cd06628    3 IKGALiGSGSFGSVYLGMNASSGELMAVKQVELPSVSAENkdrkksmLDALQREIALLRELQHENIVQYLGSSSDANHLN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELL 173
Cdd:cd06628   83 IFLEYVPGGSVATLLNNYGAFEESLVRNFVRQILKGLNYLHNRGIIHRDIKGANILVDNKGGIKISDFGISKKLEANSLS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPP-------YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFdgptlPILRQrvLEGRFRI--------PY 238
Cdd:cd06628  163 TKNNGARPslqgsvfWMAPEVVKQTSYT-RKADIWSLGCLVVEMLTGTHPF-----PDCTQ--MQAIFKIgenasptiPS 234
                        250       260       270
                 ....*....|....*....|....*....|...
gi 929654453 239 FMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd06628  235 NISSEARDFLEKTFEIDHNKRPTADELLKHPFL 267
STKc_PKN cd05589
Catalytic domain of the Serine/Threonine Kinase, Protein Kinase N; STKs catalyze the transfer ...
26-260 1.37e-32

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: 129.34  E-value: 1.37e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIK------IIDKSQLDAVNLEKiyREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd05589    7 LGRGHFGKVLLAEYKPTGELFAIKalkkgdIIARDEVESLMCEK--RIFETVNSARHPFLVNLFACFQTPEHVCFVMEYA 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNG--------EIFdylanhgrlneSEARRKFWQ--ILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF---GNF 166
Cdd:cd05589   85 AGGdlmmhiheDVF-----------SEPRAVFYAacVVLGLQFLHEHKIVYRDLKLDNLLLDTEGYVKIADFGLckeGMG 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 167 FksGELLATWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEH 246
Cdd:cd05589  154 F--GDRTSTFCGTPEFLAPEVLTDTSYT-RAVDWWGLGVLIYEMLVGESPFPGDDEEEVFDSIVNDEVRYPRFLSTEAIS 230
                        250
                 ....*....|....
gi 929654453 247 LIRRMLVLDPSKRL 260
Cdd:cd05589  231 IMRRLLRKNPERRL 244
STKc_MLCK1 cd14191
Catalytic domain of the Serine/Threonine Kinase, Myosin Light Chain Kinase 1; STKs catalyze ...
19-271 1.43e-32

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: 127.43  E-value: 1.43e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIdkSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14191    3 FYDIEERLGSGKFGQVFRLVEKKTKKVWAGKFF--KAYSAKEKENIRQEISIMNCLHHPKLVQCVDAFEEKANIVMVLEM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNM--NIKIADFGFGNFFKSGELLAT 175
Cdd:cd14191   81 VSGGELFERIIDEDfELTERECIKYMRQISEGVEYIHKQGIVHLDLKPENIMCVNKTgtKIKLIDFGLARRLENAGSLKV 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEV--FEGQQYEgpqLDIWSMGVVLYVLVCGALPF----DGPTLPILRQRVLEgrFRIPYF--MSEDCEHL 247
Cdd:cd14191  161 LFGTPEFVAPEVinYEPIGYA---TDMWSIGVICYILVSGLSPFmgdnDNETLANVTSATWD--FDDEAFdeISDDAKDF 235
                        250       260
                 ....*....|....*....|....
gi 929654453 248 IRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14191  236 ISNLLKKDMKARLTCTQCLQHPWL 259
STKc_PAK_II cd06648
Catalytic domain of the Serine/Threonine Kinase, Group II p21-activated kinase; STKs catalyze ...
26-272 2.33e-32

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: 126.79  E-value: 2.33e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIID--KSQldavNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd06648   15 IGEGSTGIVCIATDKSTGRQVAVKKMDlrKQQ----RRELLFNEVVIMRDYQHPNIVEMYSSYLVGDELWVVMEFLEGGA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDyLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGSPPY 182
Cdd:cd06648   91 LTD-IVTHTRMNEEQIATVCRAVLKALSFLHSQGVIHRDIKSDSILLTSDGRVKLSDFGFcAQVSKEVPRRKSLVGTPYW 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALP-FDGPTLPILRQ-RVLEG-RFRIPYFMSEDCEHLIRRMLVLDPSKR 259
Cdd:cd06648  170 MAPEVISRLPY-GTEVDIWSLGIMVIEMVDGEPPyFNEPPLQAMKRiRDNEPpKLKNLHKVSPRLRSFLDRMLVRDPAQR 248
                        250
                 ....*....|...
gi 929654453 260 LTIAQIKEHKWML 272
Cdd:cd06648  249 ATAAELLNHPFLA 261
STKc_Sck1_like cd05586
Catalytic domain of Suppressor of loss of cAMP-dependent protein kinase-like Serine/Threonine ...
26-299 2.33e-32

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: 128.84  E-value: 2.33e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVN-LEKIYREVQIMK---MLDHPHIIKLYQVMETKSMLYLVTEYAKN 101
Cdd:cd05586    1 IGKGTFGQVYQVRKKDTRRIYAMKVLSKKVIVAKKeVAHTIGERNILVrtaLDESPFIVGLKFSFQTPTDLYLVTDYMSG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNF-FKSGELLATWCGSP 180
Cdd:cd05586   81 GELFWHLQKEGRFSEDRAKFYIAELVLALEHLHKNDIVYRDLKPENILLDANGHIALCDFGLSKAdLTDNKTTNTFCGTT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 181 PYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPY-FMSEDCEHLIRRMLVLDPSKR 259
Cdd:cd05586  161 EYLAPEVLLDEKGYTKMVDFWSLGVLVFEMCCGWSPFYAEDTQQMYRNIAFGKVRFPKdVLSDEGRSFVKGLLNRNPKHR 240
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 929654453 260 L----TIAQIKEH------KWMLIEVPVQRPVLYPQEQeNEPSIGEFNEQ 299
Cdd:cd05586  241 LgahdDAVELKEHpffadiDWDLLSKKKITPPFKPIVD-SDTDVSNFDPE 289
STKc_cPKC_alpha cd05615
Catalytic domain of the Serine/Threonine Kinase, Classical Protein Kinase C alpha; STKs ...
15-268 2.58e-32

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: 128.96  E-value: 2.58e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  15 VRVGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKS---QLDAVNLEKIyrEVQIMKMLDHP-HIIKLYQVMETKS 90
Cdd:cd05615    7 VRLTDFNFLMVLGKGSFGKVMLAERKGSDELYAIKILKKDvviQDDDVECTMV--EKRVLALQDKPpFLTQLHSCFQTVD 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  91 MLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKS 169
Cdd:cd05615   85 RLYFVMEYVNGGDLMYHIQQVGKFKEPQAVFYAAEISVGLFFLHKKGIIYRDLKLDNVMLDSEGHIKIADFGMcKEHMVE 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 170 GELLATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIR 249
Cdd:cd05615  165 GVTTRTFCGTPDYIAPEIIAYQPY-GRSVDWWAYGVLLYEMLAGQPPFDGEDEDELFQSIMEHNVSYPKSLSKEAVSICK 243
                        250       260
                 ....*....|....*....|....
gi 929654453 250 RMLVLDPSKRLTIAQ-----IKEH 268
Cdd:cd05615  244 GLMTKHPAKRLGCGPegerdIREH 267
STKc_CDK1_euk cd07861
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 1 from higher ...
19-268 6.14e-32

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: 126.00  E-value: 6.14e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEgTLGKGNFAVVKLGRHRITKTEVAIKIID-KSQLDAVNLEKIyREVQIMKMLDHPHIIKLYQVMETKSMLYLVTE 97
Cdd:cd07861    2 YTKIE-KIGEGTYGVVYKGRNKKTGQIVAMKKIRlESEEEGVPSTAI-REISLLKELQHPNIVCLEDVLMQENRLYLVFE 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNG--EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK------S 169
Cdd:cd07861   80 FLSMDlkKYLDSLPKGKYMDAELVKSYLYQILQGILFCHSRRVLHRDLKPQNLLIDNKGVIKLADFGLARAFGipvrvyT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 170 GELLATWcgsppYAAPEVFEG-QQYEGPqLDIWSMGVVLYVLVCGALPFDG----------------------------- 219
Cdd:cd07861  160 HEVVTLW-----YRAPEVLLGsPRYSTP-VDIWSIGTIFAEMATKKPLFHGdseidqlfrifrilgtptediwpgvtslp 233
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 929654453 220 ---PTLPILRQRVLEGRFripYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd07861  234 dykNTFPKWKKGSLRTAV---KNLDEDGLDLLEKMLIYDPAKRISAKKALVH 282
STKc_SPEG_rpt2 cd14111
Catalytic kinase domain, second repeat, of Giant Serine/Threonine Kinase Striated muscle ...
20-271 6.62e-32

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: 125.32  E-value: 6.62e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIdksQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14111    5 YTFLDEKARGRFGVIRRCRENATGKNFPAKIV---PYQAEEKQGVLQEYEILKSLHHERIMALHEAYITPRYLVLIAEFC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL--LATWC 177
Cdd:cd14111   82 SGKELLHSLIDRFRYSEDDVVGYLVQILQGLEYLHGRRVLHLDIKPDNIMVTNLNAIKIVDFGSAQSFNPLSLrqLGRRT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 GSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRF---RIPYFMSEDCEHLIRRMLVL 254
Cdd:cd14111  162 GTLEYMAPEMVKGEPV-GPPADIWSIGVLTYIMLSGRSPFEDQDPQETEAKILVAKFdafKLYPNVSQSASLFLKKVLSS 240
                        250
                 ....*....|....*..
gi 929654453 255 DPSKRLTIAQIKEHKWM 271
Cdd:cd14111  241 YPWSRPTTKDCFAHAWL 257
STKc_MSK1_N cd05613
N-terminal catalytic domain of the Serine/Threonine Kinase, Mitogen and stress-activated ...
24-268 7.90e-32

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: 125.88  E-value: 7.90e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  24 GTLGKgNFAVVKLGRHRITKTeVAIKIIDKSQL--DAVNLEKIYREVQIMKMLDH-PHIIKLYQVMETKSMLYLVTEYAK 100
Cdd:cd05613   11 GAYGK-VFLVRKVSGHDAGKL-YAMKVLKKATIvqKAKTAEHTRTERQVLEHIRQsPFLVTLHYAFQTDTKLHLILDYIN 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFF--KSGELLATWCG 178
Cdd:cd05613   89 GGELFTHLSQRERFTENEVQIYIGEIVLALEHLHKLGIIYRDIKLENILLDSSGHVVLTDFGLSKEFllDENERAYSFCG 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFE-GQQYEGPQLDIWSMGVVLYVLVCGALPF--DGP--TLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLV 253
Cdd:cd05613  169 TIEYMAPEIVRgGDSGHDKAVDWWSLGVLMYELLTGASPFtvDGEknSQAEISRRILKSEPPYPQEMSALAKDIIQRLLM 248
                        250       260
                 ....*....|....*....|
gi 929654453 254 LDPSKRLTIA-----QIKEH 268
Cdd:cd05613  249 KDPKKRLGCGpngadEIKKH 268
STKc_Nek1 cd08218
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
20-267 8.60e-32

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: 124.92  E-value: 8.60e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd08218    2 YVRIKKIGEGSFGKALLVKSKEDGKQYVIKEINISKMSPKEREESRKEVAVLSKMKHPNIVQYQESFEENGNLYIVMDYC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYL-ANHGRL-NESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKS-GELLATW 176
Cdd:cd08218   82 DGGDLYKRInAQRGVLfPEDQILDWFVQLCLALKHVHDRKILHRDIKSQNIFLTKDGIIKLGDFGIARVLNStVELARTC 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRF-RIPYFMSEDCEHLIRRMLVLD 255
Cdd:cd08218  162 IGTPYYLSPEICENKPYNNKS-DIWALGCVLYEMCTLKHAFEAGNMKNLVLKIIRGSYpPVPSRYSYDLRSLVSQLFKRN 240
                        250
                 ....*....|..
gi 929654453 256 PSKRLTIAQIKE 267
Cdd:cd08218  241 PRDRPSINSILE 252
STKc_SGK1 cd05602
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
20-268 8.85e-32

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: 127.44  E-value: 8.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEK-IYREVQIM-KMLDHPHIIKLYQVMETKSMLYLVTE 97
Cdd:cd05602    9 FHFLKVIGKGSFGKVLLARHKSDEKFYAVKVLQKKAILKKKEEKhIMSERNVLlKNVKHPFLVGLHFSFQTTDKLYFVLD 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATW 176
Cdd:cd05602   89 YINGGELFYHLQRERCFLEPRARFYAAEIASALGYLHSLNIVYRDLKPENILLDSQGHIVLTDFGLcKENIEPNGTTSTF 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDP 256
Cdd:cd05602  169 CGTPEYLAPEVLHKQPYD-RTVDWWCLGAVLYEMLYGLPPFYSRNTAEMYDNILNKPLQLKPNITNSARHLLEGLLQKDR 247
                        250
                 ....*....|....*.
gi 929654453 257 SKRL----TIAQIKEH 268
Cdd:cd05602  248 TKRLgakdDFTEIKNH 263
STKc_MAPKAPK2 cd14170
Catalytic domain of the Serine/Threonine kinase, Mitogen-activated protein kinase-activated ...
63-281 1.18e-31

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: 125.92  E-value: 1.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  63 KIYREVQI-MKMLDHPHIIKLYQVME----TKSMLYLVTEYAKNGEIFDYLANHG--RLNESEARRKFWQILSAVDYCHG 135
Cdd:cd14170   40 KARREVELhWRASQCPHIVRIVDVYEnlyaGRKCLLIVMECLDGGELFSRIQDRGdqAFTEREASEIMKSIGEAIQYLHS 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 136 RKIVHRDLKAENLLLDN---NMNIKIADFGFGNFFKSGELLATWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC 212
Cdd:cd14170  120 INIAHRDVKPENLLYTSkrpNAILKLTDFGFAKETTSHNSLTTPCYTPYYVAPEVLGPEKYD-KSCDMWSLGVIMYILLC 198
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 929654453 213 GALPF---DGPTL-PILRQRVLEGRFRIP----YFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWML--IEVPvQRPV 281
Cdd:cd14170  199 GYPPFysnHGLAIsPGMKTRIRMGQYEFPnpewSEVSEEVKMLIRNLLKTEPTQRMTITEFMNHPWIMqsTKVP-QTPL 276
STKc_GRK cd05577
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase; STKs ...
26-260 1.18e-31

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: 125.33  E-value: 1.18e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKI-YREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05577    1 LGRGGFGEVCACQVKATGKMYACKKLDKKRIKKKKGETMaLNEKIILEKVSSPFIVSLAYAFETKDKLCLVLTLMNGGDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPY 182
Cdd:cd05577   81 KYHIYNVGTRGFSEARAIFYaaEIICGLEHLHNRFIVYRDLKPENILLDDHGHVRISDLGLAVEFKGGKKIKGRVGTHGY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPI----LRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSK 258
Cdd:cd05577  161 MAPEVLQKEVAYDFSVDWFALGCMLYEMIAGRSPFRQRKEKVdkeeLKRRTLEMAVEYPDSFSPEARSLCEGLLQKDPER 240

                 ..
gi 929654453 259 RL 260
Cdd:cd05577  241 RL 242
PKc_MAPKK cd06605
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein Kinase ...
21-270 1.71e-31

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: 124.38  E-value: 1.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  21 DIE--GTLGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd06605    2 DLEylGELGEGNGGVVSKVRHRPSGQIMAVKVI-RLEIDEALQKQILRELDVLHKCNSPYIVGFYGAFYSEGDISICMEY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCH-GRKIVHRDLKAENLLLDNNMNIKIADFGFgnffkSGELLA--- 174
Cdd:cd06605   81 MDGGSLDKILKEVGRIPERILGKIAVAVVKGLIYLHeKHKIIHRDVKPSNILVNSRGQVKLCDFGV-----SGQLVDsla 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 -TWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPT-------LPILRQRVLEGRFRIPYFM-SEDCE 245
Cdd:cd06605  156 kTFVGTRSYMAPERISGGKY-TVKSDIWSLGLSLVELATGRFPYPPPNakpsmmiFELLSYIVDEPPPLLPSGKfSPDFQ 234
                        250       260
                 ....*....|....*....|....*
gi 929654453 246 HLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd06605  235 DFVSQCLQKDPTERPSYKELMEHPF 259
STKc_MAPK cd07834
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase; STKs ...
20-271 1.71e-31

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: 126.10  E-value: 1.71e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSM-----LYL 94
Cdd:cd07834    2 YELLKPIGSGAYGVVCSAYDKRTGRKVAIKKISNVFDDLIDAKRILREIKILRHLKHENIIGLLDILRPPSPeefndVYI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAKNgeifDyLAN--HGRLNESEARRKF--WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG----FGNF 166
Cdd:cd07834   82 VTELMET----D-LHKviKSPQPLTDDHIQYflYQILRGLKYLHSAGVIHRDLKPSNILVNSNCDLKICDFGlargVDPD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 167 FKSGEL---LAT-WcgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPT--------------------- 221
Cdd:cd07834  157 EDKGFLteyVVTrW-----YRAPELLLSSKKYTKAIDIWSVGCIFAELLTRKPLFPGRDyidqlnlivevlgtpseedlk 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 222 ----------LPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd07834  232 fissekarnyLKSLPKKPKKPLSEVFPGASPEAIDLLEKMLVFNPKKRITADEALAHPYL 291
STKc_SGK2 cd05603
Catalytic domain of the Serine/Threonine Kinase, Serum- and Glucocorticoid-induced Kinase 2; ...
26-268 2.07e-31

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: 125.85  E-value: 2.07e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDK-SQLDAVNLEKIYREVQIM-KMLDHPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd05603    3 IGKGSFGKVLLAKRKCDGKFYAVKVLQKkTILKKKEQNHIMAERNVLlKNLKHPFLVGLHYSFQTSEKLYFVLDYVNGGE 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGfgnFFKSG----ELLATWCGS 179
Cdd:cd05603   83 LFFHLQRERCFLEPRARFYAAEVASAIGYLHSLNIIYRDLKPENILLDCQGHVVLTDFG---LCKEGmepeETTSTFCGT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKR 259
Cdd:cd05603  160 PEYLAPEVLRKEPYD-RTVDWWCLGAVLYEMLYGLPPFYSRDVSQMYDNILHKPLHLPGGKTVAACDLLQGLLHKDQRRR 238
                        250
                 ....*....|...
gi 929654453 260 L----TIAQIKEH 268
Cdd:cd05603  239 LgakaDFLEIKNH 251
STKc_IKK cd13989
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
26-217 2.56e-31

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: 124.48  E-value: 2.56e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAV--NLEKIYREVQIMKMLDHPHIIKLYQVME------TKSMLYLVTE 97
Cdd:cd13989    1 LGSGGFGYVTLWKHQDTGEYVAIKKC-RQELSPSdkNRERWCLEVQIMKKLNHPNVVSARDVPPeleklsPNDLPLLAME 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYL---ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFFKSGE 171
Cdd:cd13989   80 YCSGGDLRKVLnqpENCCGLKESEVRTLLSDISSAISYLHENRIIHRDLKPENIVLqqgGGRVIYKLIDLGYAKELDQGS 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 929654453 172 LLATWCGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPF 217
Cdd:cd13989  160 LCTSFVGTLQYLAPELFESKKYTC-TVDYWSFGTLAFECITGYRPF 204
STKc_DRAK2 cd14198
The catalytic domain of the Serine/Threonine Kinase, Death-associated protein kinase-Related ...
19-271 2.76e-31

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: 123.88  E-value: 2.76e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGT-LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKML-DHPHIIKLYQVMETKSMLYLVT 96
Cdd:cd14198    8 FYILTSKeLGRGKFAVVRQCISKSTGQEYAAKFLKKRRRGQDCRAEILHEIAVLELAkSNPRVVNLHEVYETTSEIILIL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNGEIFDYLAN--HGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNM---NIKIADFGFGNFFKSGE 171
Cdd:cd14198   88 EYAAGGEIFNLCVPdlAEMVSENDIIRLIRQILEGVYYLHQNNIVHLDLKPQNILLSSIYplgDIKIVDFGMSRKIGHAC 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 LLATWCGSPPYAAPEVFegqQYE--GPQLDIWSMGVVLYVLVCGALPFDG----PTLPILRQRVLEGRFRIPYFMSEDCE 245
Cdd:cd14198  168 ELREIMGTPEYLAPEIL---NYDpiTTATDMWNIGVIAYMLLTHESPFVGednqETFLNISQVNVDYSEETFSSVSQLAT 244
                        250       260
                 ....*....|....*....|....*.
gi 929654453 246 HLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14198  245 DFIQKLLVKNPEKRPTAEICLSHSWL 270
STKc_WNK cd13983
Catalytic domain of the Serine/Threonine kinase, With No Lysine (WNK) kinase; STKs catalyze ...
16-271 3.36e-31

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: 123.10  E-value: 3.36e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  16 RVGFYDIEgtLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSM--LY 93
Cdd:cd13983    1 RYLKFNEV--LGRGSFKTVYRAFDTEEGIEVAWNEIKLRKLPKAERQRFKQEIEILKSLKHPNIIKFYDSWESKSKkeVI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRK--IVHRDLKAENLLLD-NNMNIKIADFGFGNFFKSG 170
Cdd:cd13983   79 FITELMTSGTLKQYLKRFKRLKLKVIKSWCRQILEGLNYLHTRDppIIHRDLKCDNIFINgNTGEVKIGDLGLATLLRQS 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 EllATWC-GSPPYAAPEVFEgQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLP--ILRqRVLEGRF--RIPYFMSEDCE 245
Cdd:cd13983  159 F--AKSViGTPEFMAPEMYE-EHY-DEKVDIYAFGMCLLEMATGEYPYSECTNAaqIYK-KVTSGIKpeSLSKVKDPELK 233
                        250       260
                 ....*....|....*....|....*.
gi 929654453 246 HLIRRMLVlDPSKRLTIAQIKEHKWM 271
Cdd:cd13983  234 DFIEKCLK-PPDERPSARELLEHPFF 258
STKc_nPKC_epsilon cd05591
Catalytic domain of the Serine/Threonine Kinase, Novel Protein Kinase C epsilon; STKs catalyze ...
26-285 5.61e-31

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: 124.53  E-value: 5.61e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKS---QLDAVNLEKIYREVQIMKMlDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd05591    3 LGKGSFGKVMLAERKGTDEVYAIKVLKKDvilQDDDVDCTMTEKRILALAA-KHPFLTALHSCFQTKDRLFFVMEYVNGG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGSPP 181
Cdd:cd05591   82 DLMFQIQRARKFDEPRARFYAAEVTLALMFLHRHGVIYRDLKLDNILLDAEGHCKLADFGMcKEGILNGKTTTTFCGTPD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRL- 260
Cdd:cd05591  162 YIAPEILQELEY-GPSVDWWALGVLMYEMMAGQPPFEADNEDDLFESILHDDVLYPVWLSKEAVSILKAFMTKNPAKRLg 240
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 929654453 261 -TIAQ-----IKEH------KWMLIEVPVQRPVLYPQ 285
Cdd:cd05591  241 cVASQggedaIRQHpffreiDWEALEQRKVKPPFKPK 277
STKc_Kalirin_C cd14115
C-terminal kinase domain of the Large Serine/Threonine Kinase and Rho Guanine Nucleotide ...
26-270 1.35e-30

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: 121.22  E-value: 1.35e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAvnlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14115    1 IGRGRFSIVKKCLHKATRKDVAVKFVSKKMKKK---EQAAHEAALLQHLQHPQYITLHDTYESPTSYILVLELMDDGRLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNM---NIKIADFG----FGNFFKSGELLatwcG 178
Cdd:cd14115   78 DYLMNHDELMEEKVAFYIRDIMEALQYLHNCRVAHLDIKPENLLIDLRIpvpRVKLIDLEdavqISGHRHVHHLL----G 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPF--DGPTLPILRQRVLEGRFRIPYF--MSEDCEHLIRRMLVL 254
Cdd:cd14115  154 NPEFAAPEVIQGTPVS-LATDIWSIGVLTYVMLSGVSPFldESKEETCINVCRVDFSFPDEYFgdVSQAARDFINVILQE 232
                        250
                 ....*....|....*.
gi 929654453 255 DPSKRLTIAQIKEHKW 270
Cdd:cd14115  233 DPRRRPTAATCLQHPW 248
STKc_Sid2p_like cd05600
Catalytic domain of Fungal Sid2p-like Protein Serine/Threonine Kinases; STKs catalyze the ...
12-268 1.75e-30

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: 124.37  E-value: 1.75e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  12 RGPVRVGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKS---QLDAVNleKIYREVQIMKMLDHPHIIKLYQVMET 88
Cdd:cd05600    5 RTRLKLSDFQILTQVGQGGYGSVFLARKKDTGEICALKIMKKKvlfKLNEVN--HVLTERDILTTTNSPWLVKLLYAFQD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  89 KSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG------ 162
Cdd:cd05600   83 PENVYLAMEYVPGGDFRTLLNNSGILSEEHARFYIAEMFAAISSLHQLGYIHRDLKPENFLIDSSGHIKLTDFGlasgtl 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 163 -------------------------------FGNFFKSGELLATWC-GSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVL 210
Cdd:cd05600  163 spkkiesmkirleevkntafleltakerrniYRAMRKEDQNYANSVvGSPDYMAPEVLRGEGYD-LTVDYWSLGCILFEC 241
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 211 VCGALPFDGPTL-----------PILRQRVLEGRfRIPYFMSEDCEHLIRRMLVlDPSKRL-TIAQIKEH 268
Cdd:cd05600  242 LVGFPPFSGSTPnetwanlyhwkKTLQRPVYTDP-DLEFNLSDEAWDLITKLIT-DPQDRLqSPEQIKNH 309
STKc_CK2_alpha cd14132
Catalytic subunit (alpha) of the Serine/Threonine Kinase, Casein Kinase 2; STKs catalyze the ...
20-217 1.79e-30

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: 122.65  E-value: 1.79e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIidksqLDAVNLEKIYREVQIMKML-DHPHIIKLYQ-VMETKSMLY-LVT 96
Cdd:cd14132   20 YEIIRKIGRGKYSEVFEGINIGNNEKVVIKV-----LKPVKKKKIKREIKILQNLrGGPNIVKLLDvVKDPQSKTPsLIF 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNgEIFDYLanHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD-NNMNIKIADFGFGNFFKSGELLAT 175
Cdd:cd14132   95 EYVNN-TDFKTL--YPTLTDYDIRYYMYELLKALDYCHSKGIMHRDVKPHNIMIDhEKRKLRLIDWGLAEFYHPGQEYNV 171
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 929654453 176 WCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPF 217
Cdd:cd14132  172 RVASRYYKGPELLVDYQYYDYSLDMWSLGCMLASMIFRKEPF 213
STKc_GAK_like cd13985
Catalytic domain of cyclin G-Associated Kinase-like proteins; STKs catalyze the transfer of ...
20-265 1.84e-30

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: 121.67  E-value: 1.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKiidKSQLDAVN-LEKIYREVQIMKML-DHPHIIKLYQV----METKSMLY 93
Cdd:cd13985    2 YQVTKQLGEGGFSYVYLAHDVNTGRRYALK---RMYFNDEEqLRVAIKEIEIMKRLcGHPNIVQYYDSailsSEGRKEVL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKnGEIFDYLAN--HGRLNESEARRKFWQILSAVDYCH--GRKIVHRDLKAENLLLDNNMNIKIADFGFGNF-FK 168
Cdd:cd13985   79 LLMEYCP-GSLVDILEKspPSPLSEEEVLRIFYQICQAVGHLHsqSPPIIHRDIKIENILFSNTGRFKLCDFGSATTeHY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 SgelLATWCG------------SPPYAAPEVFEGQQYE--GPQLDIWSMGVVLYVLVCGALPFDGPTlpILrqRVLEGRF 234
Cdd:cd13985  158 P---LERAEEvniieeeiqkntTPMYRAPEMIDLYSKKpiGEKADIWALGCLLYKLCFFKLPFDESS--KL--AIVAGKY 230
                        250       260       270
                 ....*....|....*....|....*....|...
gi 929654453 235 RIPYF--MSEDCEHLIRRMLVLDPSKRLTIAQI 265
Cdd:cd13985  231 SIPEQprYSPELHDLIRHMLTPDPAERPDIFQV 263
PKc_Mps1 cd14131
Catalytic domain of the Dual-specificity Mitotic checkpoint protein kinase, Monopolar spindle ...
19-268 2.99e-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: 120.78  E-value: 2.99e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVklgrHRI---TKTEVAIKIIDKSQLDAVNLEKIYREVQIMKML-DHPHIIKL--YQVMETKSML 92
Cdd:cd14131    2 PYEILKQLGKGGSSKV----YKVlnpKKKIYALKRVDLEGADEQTLQSYKNEIELLKKLkGSDRIIQLydYEVTDEDDYL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  93 YLVTEYaknGEIfDyLAN--HGRLNE---SEARRKFW-QILSAVDYCHGRKIVHRDLKAENLLLDNNMnIKIADFGFGNF 166
Cdd:cd14131   78 YMVMEC---GEI-D-LATilKKKRPKpidPNFIRYYWkQMLEAVHTIHEEGIVHSDLKPANFLLVKGR-LKLIDFGIAKA 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 167 FKSGE---LLATWCGSPPYAAPE--------VFEGQQYE-GPQLDIWSMGVVLYVLVCGALPFDGPTLPILR-QRVLEGR 233
Cdd:cd14131  152 IQNDTtsiVRDSQVGTLNYMSPEaikdtsasGEGKPKSKiGRPSDVWSLGCILYQMVYGKTPFQHITNPIAKlQAIIDPN 231
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 929654453 234 FRIPY--FMSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14131  232 HEIEFpdIPNPDLIDVMKRCLQRDPKKRPSIPELLNH 268
STKc_MOK cd07831
Catalytic domain of the Serine/Threonine Kinase, MAPK/MAK/MRK Overlapping Kinase; STKs ...
20-268 3.02e-30

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: 121.22  E-value: 3.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDK--SQLDAVNLekiYREVQIMKML-DHPHIIKLYQVM--ETKSMLYL 94
Cdd:cd07831    1 YKILGKIGEGTFSEVLKAQSRKTGKYYAIKCMKKhfKSLEQVNN---LREIQALRRLsPHPNILRLIEVLfdRKTGRLAL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAkNGEIFDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNmNIKIADFGfgnffksgeLL 173
Cdd:cd07831   78 VFELM-DMNLYELIKGRKRpLPEKRVKNYMYQLLKSLDHMHRNGIFHRDIKPENILIKDD-ILKLADFG---------SC 146
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYA---------APEVFEGQQYEGPQLDIWSMGVVLYVLVC------GALPFD---------GPTLPILRQRV 229
Cdd:cd07831  147 RGIYSKPPYTeyistrwyrAPECLLTDGYYGPKMDIWAVGCVFFEILSlfplfpGTNELDqiakihdvlGTPDAEVLKKF 226
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 929654453 230 LEGRFRIPYF--------------MSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd07831  227 RKSRHMNYNFpskkgtglrkllpnASAEGLDLLKKLLAYDPDERITAKQALRH 279
STKc_obscurin_rpt2 cd14110
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Obscurin; STKs ...
20-271 3.02e-30

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: 120.41  E-value: 3.02e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAvnlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14110    5 YAFQTEINRGRFSVVRQCEEKRSGQMLAAKIIPYKPEDK---QLVLREYQVLRRLSHPRIAQLHSAYLSPRHLVLIEELC 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLAT-WCG 178
Cdd:cd14110   82 SGPELLYNLAERNSYSEAEVTDYLWQILSAVDYLHSRRILHLDLRSENMIITEKNLLKIVDLGNAQPFNQGKVLMTdKKG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 S-PPYAAPEVFEGQQyEGPQLDIWSMGVVLYVLVCGALPFDGpTLPILRQRVL-EGRFRIPYF---MSEDCEHLIRRMLV 253
Cdd:cd14110  162 DyVETMAPELLEGQG-AGPQTDIWAIGVTAFIMLSADYPVSS-DLNWERDRNIrKGKVQLSRCyagLSGGAVNFLKSTLC 239
                        250
                 ....*....|....*...
gi 929654453 254 LDPSKRLTIAQIKEHKWM 271
Cdd:cd14110  240 AKPWGRPTASECLQNPWL 257
STKc_CCRK cd07832
Catalytic domain of the Serine/Threonine Kinase, Cell Cycle-Related Kinase; STKs catalyze the ...
20-270 3.54e-30

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: 121.28  E-value: 3.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIK-IIDKSQLDAVNLEKIyREVQIMKML-DHPHIIKLYQVMETKSMLYLVTE 97
Cdd:cd07832    2 YKILGRIGEGAHGIVFKAKDRETGETVALKkVALRKLEGGIPNQAL-REIKALQACqGHPYVVKLRDVFPHGTGFVLVFE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGeIFDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE--LLA 174
Cdd:cd07832   81 YMLSS-LSEVLRDEERpLTEAQVKRYMRMLLKGVAYMHANRIMHRDLKPANLLISSTGVLKIADFGLARLFSEEDprLYS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG----------------PTL---PILRQRVLEGRFR 235
Cdd:cd07832  160 HQVATRWYRAPELLYGSRKYDEGVDLWAVGCIFAELLNGSPLFPGendieqlaivlrtlgtPNEktwPELTSLPDYNKIT 239
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 929654453 236 IPY---------FMSEDCE--HLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07832  240 FPEskgirleeiFPDCSPEaiDLLKGLLVYNPKKRLSAEEALRHPY 285
STKc_PCTAIRE3 cd07871
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-3 kinase; STKs catalyze the transfer ...
24-222 5.20e-30

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: 120.88  E-value: 5.20e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  24 GTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIyREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNgE 103
Cdd:cd07871   11 DKLGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI-REVSLLKNLKHANIVTLHDIIHTERCLTLVFEYLDS-D 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANHGRLNESEARRKF-WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK------SGELLATW 176
Cdd:cd07871   89 LKQYLDNCGNLMSMHNVKIFmFQLLRGLSYCHKRKILHRDLKPQNLLINEKGELKLADFGLARAKSvptktySNEVVTLW 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 929654453 177 cgsppYAAPEVFEGQ-QYEGPqLDIWSMGVVLYVLVCGALPFDGPTL 222
Cdd:cd07871  169 -----YRPPDVLLGStEYSTP-IDMWGVGCILYEMATGRPMFPGSTV 209
STKc_CDKL2_3 cd07846
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase Like 2 and 3; ...
20-268 5.54e-30

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: 120.60  E-value: 5.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVnLEKI-YREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd07846    3 YENLGLVGEGSYGMVMKCRHKETGQIVAIKKFLESEDDKM-VKKIaMREIKMLKQLRHENLVNLIEVFRRKKRWYLVFEF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNgEIFDYLANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKS-GELLATW 176
Cdd:cd07846   82 VDH-TVLDDLEKYpNGLDESRVRKYLFQILRGIDFCHSHNIIHRDIKPENILVSQSGVVKLCDFGFARTLAApGEVYTDY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYEGPQLDIWSMGVV-------------------LY--VLVCGAL------------PFDGPTLP 223
Cdd:cd07846  161 VATRWYRAPELLVGDTKYGKAVDVWAVGCLvtemltgeplfpgdsdidqLYhiIKCLGNLiprhqelfqknpLFAGVRLP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 929654453 224 ILRQRV-LEGRFriPYFmSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd07846  241 EVKEVEpLERRY--PKL-SGVVIDLAKKCLHIDPDKRPSCSELLHH 283
STKc_Nek3 cd08219
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
20-259 5.89e-30

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: 119.69  E-value: 5.89e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd08219    2 YNVLRVVGEGSFGRALLVQHVNSDQKYAMKEI-RLPKSSSAVEDSRKEAVLLAKMKHPNIVAFKESFEADGHLYIVMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANH-GRL-NESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKS-GELLATW 176
Cdd:cd08219   81 DGGDLMQKIKLQrGKLfPEDTILQWFVQMCLGVQHIHEKRVLHRDIKSKNIFLTQNGKVKLGDFGSARLLTSpGAYACTY 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFR-IPYFMSEDCEHLIRRMLVLD 255
Cdd:cd08219  161 VGTPYYVPPEIWENMPYNNKS-DIWSLGCILYELCTLKHPFQANSWKNLILKVCQGSYKpLPSHYSYELRSLIKQMFKRN 239

                 ....
gi 929654453 256 PSKR 259
Cdd:cd08219  240 PRSR 243
STKc_SLK_like cd06611
Catalytic domain of Ste20-Like Kinase-like Serine/Threonine Kinases; STKs catalyze the ...
19-270 6.55e-30

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: 120.23  E-value: 6.55e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSqlDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd06611    6 IWEIIGELGDGAFGKVYKAQHKETGLFAAAKIIQIE--SEEELEDFMVEIDILSECKHPNIVGLYEAYFYENKLWILIEF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSG-ELLATW 176
Cdd:cd06611   84 CDGGALDSIMLELERgLTEPQIRYVCRQMLEALNFLHSHKVIHRDLKAGNILLTLDGDVKLADFGVSAKNKSTlQKRDTF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEV-----FEGQQYEGpQLDIWSMGVVLYVLVCGALPfDGPTLPIlrqRVLegrFRI----------PYFMS 241
Cdd:cd06611  164 IGTPYWMAPEVvacetFKDNPYDY-KADIWSLGITLIELAQMEPP-HHELNPM---RVL---LKIlksepptldqPSKWS 235
                        250       260
                 ....*....|....*....|....*....
gi 929654453 242 EDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd06611  236 SSFNDFLKSCLVKDPDDRPTAAELLKHPF 264
PknB_PASTA_kin NF033483
Stk1 family PASTA domain-containing Ser/Thr kinase;
20-221 8.72e-30

Stk1 family PASTA domain-containing Ser/Thr kinase;


Pssm-ID: 468045 [Multi-domain]  Cd Length: 563  Bit Score: 125.29  E-value: 8.72e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIdKSQL--DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTE 97
Cdd:NF033483   9 YEIGERIGRGGMAEVYLAKDTRLDRDVAVKVL-RPDLarDPEFVARFRREAQSAASLSHPNIVSVYDVGEDGGIPYIVME 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKS------GE 171
Cdd:NF033483  88 YVDGRTLKDYIREHGPLSPEEAVEIMIQILSALEHAHRNGIVHRDIKPQNILITKDGRVKVTDFGIARALSSttmtqtNS 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 929654453 172 LLatwcGSPPYAAPEvfegqQYEG----PQLDIWSMGVVLYVLVCGALPFDGPT 221
Cdd:NF033483 168 VL----GTVHYLSPE-----QARGgtvdARSDIYSLGIVLYEMLTGRPPFDGDS 212
STKc_MAPK15-like cd07852
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein Kinase 15 and ...
20-270 9.78e-30

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: 121.13  E-value: 9.78e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIK-IID--KSQLDAvnlEKIYREVQIMKML-DHPHIIKLYQVMETKSM--LY 93
Cdd:cd07852    9 YEILKKLGKGAYGIVWKAIDKKTGEVVALKkIFDafRNATDA---QRTFREIMFLQELnDHPNIIKLLNVIRAENDkdIY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKNgeifDyLAN---HGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSG 170
Cdd:cd07852   86 LVFEYMET----D-LHAvirANILEDIHKQYIMYQLLKALKYLHSGGVIHRDLKPSNILLNSDCRVKLADFGLARSLSQL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 ----------ELLAT-WcgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG----------------PT-- 221
Cdd:cd07852  161 eeddenpvltDYVATrW-----YRAPEILLGSTRYTKGVDMWSVGCILGEMLLGKPLFPGtstlnqlekiievigrPSae 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 929654453 222 ----------------LPILRQRVLEGRFripYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07852  236 diesiqspfaatmlesLPPSRPKSLDELF---PKASPDALDLLKKLLVFNPNKRLTAEEALRHPY 297
PTZ00267 PTZ00267
NIMA-related protein kinase; Provisional
67-271 1.06e-29

NIMA-related protein kinase; Provisional


Pssm-ID: 140293 [Multi-domain]  Cd Length: 478  Bit Score: 123.97  E-value: 1.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  67 EVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG----EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRD 142
Cdd:PTZ00267 115 ELHCLAACDHFGIVKHFDDFKSDDKLLLIMEYGSGGdlnkQIKQRLKEHLPFQEYEVGLLFYQIVLALDEVHSRKMMHRD 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 143 LKAENLLLDNNMNIKIADFGFGNFFK---SGELLATWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDG 219
Cdd:PTZ00267 195 LKSANIFLMPTGIIKLGDFGFSKQYSdsvSLDVASSFCGTPYYLAPELWERKRYS-KKADMWSLGVILYELLTLHRPFKG 273
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 929654453 220 PTLPILRQRVLEGRFR-IPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:PTZ00267 274 PSQREIMQQVLYGKYDpFPCPVSSGMKALLDPLLSKNPALRPTTQQLLHTEFL 326
STKc_RIP cd13978
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein; STKs catalyze ...
26-251 1.17e-29

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: 119.09  E-value: 1.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd13978    1 LGSGGFGTVSKARHVSWFGMVAIKCLHSSPNCIEERKALLKEAEKMERARHSYVLPLLGVCVERRSLGLVMEYMENGSLK 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYL-ANHGRLNESEARRKFWQILSAVDYCHG--RKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPP- 181
Cdd:cd13978   81 SLLeREIQDVPWSLRFRIIHEIALGMNFLHNmdPPLLHHDLKPENILLDNHFHVKISDFGLSKLGMKSISANRRRGTENl 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 -----YAAPEVFEGQQYEGP-QLDIWSMGVVLYVLVCGALPFDGPTLPILR-QRVLEG-RFRIP----YFMSEDCEHLIR 249
Cdd:cd13978  161 ggtpiYMAPEAFDDFNKKPTsKSDVYSFAIVIWAVLTRKEPFENAINPLLImQIVSKGdRPSLDdigrLKQIENVQELIS 240

                 ..
gi 929654453 250 RM 251
Cdd:cd13978  241 LM 242
PKc_DYRK cd14210
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
20-271 1.38e-29

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: 119.96  E-value: 1.38e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFA-VVKLGRHRiTKTEVAIKII---DKSQLDAVNlekiyrEVQIMKML------DHPHIIKLYQVMETK 89
Cdd:cd14210   15 YEVLSVLGKGSFGqVVKCLDHK-TGQLVAIKIIrnkKRFHQQALV------EVKILKHLndndpdDKHNIVRYKDSFIFR 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  90 SMLYLVTEYA-KNgeIFDYLANHG--RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNN--MNIKIADFGFG 164
Cdd:cd14210   88 GHLCIVFELLsIN--LYELLKSNNfqGLSLSLIRKFAKQILQALQFLHKLNIIHCDLKPENILLKQPskSSIKVIDFGSS 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 165 NFfkSGELLATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDG----------------PTLPILRQ- 227
Cdd:cd14210  166 CF--EGEKVYTYIQSRFYRAPEVILGLPY-DTAIDMWSLGCILAELYTGYPLFPGeneeeqlacimevlgvPPKSLIDKa 242
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 929654453 228 ----------------RVLEGRFRIPYFMS------EDCEH---LIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14210  243 srrkkffdsngkprptTNSKGKKRRPGSKSlaqvlkCDDPSfldFLKKCLRWDPSERMTPEEALQHPWI 311
PTKc_Tec_like cd05059
Catalytic domain of Tec-like Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
26-237 1.55e-29

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: 118.32  E-value: 1.55e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRiTKTEVAIKIIDKSqldAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd05059   12 LGSGQFGVVHLGKWR-GKIDVAIKMIKEG---SMSEDDFIEEAKVMMKLSHPKLVQLYGVCTKQRPIFIVTEYMANGCLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYL-ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPP--Y 182
Cdd:cd05059   88 NYLrERRGKFQTEQLLEMCKDVCEAMEYLESNGFIHRDLAARNCLVGEQNVVKVSDFGLARYVLDDEYTSSVGTKFPvkW 167
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 929654453 183 AAPEVFEGQQYEGPQlDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEGrFRIP 237
Cdd:cd05059  168 SPPEVFMYSKFSSKS-DVWSFGVLMWeVFSEGKMPYERFSNSEVVEHISQG-YRLY 221
STKc_MEKK1 cd06630
Catalytic domain of the Protein Serine/Threonine Kinase, Mitogen-Activated Protein (MAP) ...
9-268 1.89e-29

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: 118.30  E-value: 1.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   9 HLQRGPVrvgfydiegtLGKGNFAVVKLGRHRITKTEVAIKII-----DKSQLDAVnLEKIYREVQIMKMLDHPHIIKLY 83
Cdd:cd06630    1 HWLKGPL----------LGTGAFSSCYQARDVKTGTLMAVKQVsfcrnSSSEQEEV-VEAIREEIRMMARLNHPNIVRML 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  84 QVMETKSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNN-MNIKIADFG 162
Cdd:cd06630   70 GATQHKSHFNIFVEWMAGGSVASLLSKYGAFSENVIINYTLQILRGLAYLHDNQIIHRDLKGANLLVDSTgQRLRIADFG 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 163 FGNFFKS-----GELLATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLP-----ILRQRVLEG 232
Cdd:cd06630  150 AAARLASkgtgaGEFQGQLLGTIAFMAPEVLRGEQY-GRSCDVWSVGCVIIEMATAKPPWNAEKISnhlalIFKIASATT 228
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 929654453 233 RFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd06630  229 PPPIPEHLSPGLRDVTLRCLELQPEDRPPARELLKH 264
PK_Unc-89_rpt1 cd14109
Pseudokinase domain, first repeat, of the Giant Serine/Threonine Kinase Uncoordinated protein ...
62-271 2.89e-29

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: 117.61  E-value: 2.89e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  62 EKIYREVQIMKMLDHPHIIKLYQVMETKSM-LYLVTEYAKNGEIF--DYLANHGRLNESEARRKFWQILSAVDYCHGRKI 138
Cdd:cd14109   41 PFLMREVDIHNSLDHPNIVQMHDAYDDEKLaVTVIDNLASTIELVrdNLLPGKDYYTERQVAVFVRQLLLALKHMHDLGI 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 139 VHRDLKAENLLLDNNmNIKIADFGFGNFFKSGELLATWCGSPPYAAPEVFEGqqyEGPQL--DIWSMGVVLYVLVCGALP 216
Cdd:cd14109  121 AHLDLRPEDILLQDD-KLKLADFGQSRRLLRGKLTTLIYGSPEFVSPEIVNS---YPVTLatDMWSVGVLTYVLLGGISP 196
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 929654453 217 F----DGPTLpilrQRVLEGRFR----IPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14109  197 FlgdnDRETL----TNVRSGKWSfdssPLGNISDDARDFIKKLLVYIPESRLTVDEALNHPWF 255
STKc_ROCK cd05596
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
20-269 3.17e-29

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: 120.17  E-value: 3.17e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKsqldavnLEKIYR--------EVQIMKMLDHPHIIKLYQVMETKSM 91
Cdd:cd05596   28 FDVIKVIGRGAFGEVQLVRHKSTKKVYAMKLLSK-------FEMIKRsdsaffweERDIMAHANSEWIVQLHYAFQDDKY 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  92 LYLVTEYAKNGEIFDYLANHgRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG-NFFKSG 170
Cdd:cd05596  101 LYMVMDYMPGGDLVNLMSNY-DVPEKWARFYTAEVVLALDAIHSMGFVHRDVKPDNMLLDASGHLKLADFGTCmKMDKDG 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 ELLA-TWCGSPPYAAPEVFEGQQ---YEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGR----FRIPYFMSE 242
Cdd:cd05596  180 LVRSdTAVGTPDYISPEVLKSQGgdgVYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYGKIMNHKnslqFPDDVEISK 259
                        250       260       270
                 ....*....|....*....|....*....|
gi 929654453 243 DCEHLIRRMLVlDPSKRL---TIAQIKEHK 269
Cdd:cd05596  260 DAKSLICAFLT-DREVRLgrnGIEEIKAHP 288
STKc_NAK1_like cd06917
Catalytic domain of Fungal Nak1-like Serine/Threonine Kinases; STKs catalyze the transfer of ...
26-271 3.21e-29

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: 117.96  E-value: 3.21e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQlDAVNLEKIYREVQIMKMLDH---PHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd06917    9 VGRGSYGAVYRGYHVKTGRVVALKVLNLDT-DDDDVSDIQKEVALLSQLKLgqpKNIIKYYGSYLKGPSLWIIMDYCEGG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIfDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL-LATWCGSPP 181
Cdd:cd06917   88 SI-RTLMRAGPIAERYIAVIMREVLVALKFIHKDGIIHRDIKAANILVTNTGNVKLCDFGVAASLNQNSSkRSTFVGTPY 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVF-EGQQYEgPQLDIWSMGVVLYVLVCGALPFDGptLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVL----DP 256
Cdd:cd06917  167 WMAPEVItEGKYYD-TKADIWSLGITTYEMATGNPPYSD--VDALRAVMLIPKSKPPRLEGNGYSPLLKEFVAAcldeEP 243
                        250
                 ....*....|....*
gi 929654453 257 SKRLTIAQIKEHKWM 271
Cdd:cd06917  244 KDRLSADELLKSKWI 258
PTZ00283 PTZ00283
serine/threonine protein kinase; Provisional
20-259 3.87e-29

serine/threonine protein kinase; Provisional


Pssm-ID: 240344 [Multi-domain]  Cd Length: 496  Bit Score: 122.67  E-value: 3.87e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVM--------ETKSM 91
Cdd:PTZ00283  34 YWISRVLGSGATGTVLCAKRVSDGEPFAVKVVDMEGMSEADKNRAQAEVCCLLNCDFFSIVKCHEDFakkdprnpENVLM 113
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  92 LYLVTEYAKNGEIFDYLANHGRLN----ESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFF 167
Cdd:PTZ00283 114 IALVLDYANAGDLRQEIKSRAKTNrtfrEHEAGLLFIQVLLAVHHVHSKHMIHRDIKSANILLCSNGLVKLGDFGFSKMY 193
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 168 K---SGELLATWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFR-IPYFMSED 243
Cdd:PTZ00283 194 AatvSDDVGRTFCGTPYYVAPEIWRRKPYS-KKADMFSLGVLLYELLTLKRPFDGENMEEVMHKTLAGRYDpLPPSISPE 272
                        250
                 ....*....|....*.
gi 929654453 244 CEHLIRRMLVLDPSKR 259
Cdd:PTZ00283 273 MQEIVTALLSSDPKRR 288
PTKc_Srm_Brk cd05148
Catalytic domain of the Protein Tyrosine Kinases, Src-related kinase lacking C-terminal ...
20-267 4.65e-29

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: 117.15  E-value: 4.65e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRiTKTEVAIKIIdkSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd05148    8 FTLERKLGSGYFGEVWEGLWK-NRVRVAIKIL--KSDDLLKQQDFQKEVQALKRLRHKHLISLFAVCSVGEPVYIITELM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLAN-HGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWC 177
Cdd:cd05148   85 EKGSLLAFLRSpEGQvLPVASLIDMACQVAEGMAYLEEQNSIHRDLAARNILVGEDLVCKVADFGLARLIKEDVYLSSDK 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 GSP-PYAAPEVFEGQQYEGPQlDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEGrFRIPyfMSEDCEHLIRRMLV-- 253
Cdd:cd05148  165 KIPyKWTAPEAASHGTFSTKS-DVWSFGILLYeMFTYGQVPYPGMNNHEVYDQITAG-YRMP--CPAKCPQEIYKIMLec 240
                        250
                 ....*....|....*.
gi 929654453 254 --LDPSKRLTIAQIKE 267
Cdd:cd05148  241 waAEPEDRPSFKALRE 256
PLN00009 PLN00009
cyclin-dependent kinase A; Provisional
20-270 4.82e-29

cyclin-dependent kinase A; Provisional


Pssm-ID: 177649 [Multi-domain]  Cd Length: 294  Bit Score: 118.00  E-value: 4.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY- 98
Cdd:PLN00009   4 YEKVEKIGEGTYGVVYKARDRVTNETIALKKIRLEQEDEGVPSTAIREISLLKEMQHGNIVRLQDVVHSEKRLYLVFEYl 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 ----AKNGEIFDYLANHGRLNESearrKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMN-IKIADFGFGNFFK----- 168
Cdd:PLN00009  84 dldlKKHMDSSPDFAKNPRLIKT----YLYQILRGIAYCHSHRVLHRDLKPQNLLIDRRTNaLKLADFGLARAFGipvrt 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 -SGELLATWcgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLV--------------------------------CGAL 215
Cdd:PLN00009 160 fTHEVVTLW-----YRAPEILLGSRHYSTPVDIWSVGCIFAEMVnqkplfpgdseidelfkifrilgtpneetwpgVTSL 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 929654453 216 PFDGPTLPILRQRVLEGrfRIPYFMSEDCEhLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:PLN00009 235 PDYKSAFPKWPPKDLAT--VVPTLEPAGVD-LLSKMLRLDPSKRITARAALEHEY 286
STKc_LATS cd05598
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor; STKs catalyze the ...
25-270 5.82e-29

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: 118.96  E-value: 5.82e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLGRHRITKTEVAIKIIDKS------QLDAVNLEKiyrevQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd05598    8 TIGVGAFGEVSLVRKKDTNALYAMKTLRKKdvlkrnQVAHVKAER-----DILAEADNEWVVKLYYSFQDKENLYFVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK----SGELLA 174
Cdd:cd05598   83 IPGGDLMSLLIKKGIFEEDLARFYIAELVCAIESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLCTGFRwthdSKYYLA 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 -TWCGSPPYAAPEVFEGQQYEgpQL-DIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGR--FRIPYF--MSEDCEHLI 248
Cdd:cd05598  163 hSLVGTPNYIAPEVLLRTGYT--QLcDWWSVGVILYEMLVGQPPFLAQTPAETQLKVINWRttLKIPHEanLSPEAKDLI 240
                        250       260
                 ....*....|....*....|....*
gi 929654453 249 RRMLVlDPSKRL---TIAQIKEHKW 270
Cdd:cd05598  241 LRLCC-DAEDRLgrnGADEIKAHPF 264
STKc_CRIK cd05601
Catalytic domain of the Serine/Threonine Kinase, Citron Rho-interacting kinase; STKs catalyze ...
20-269 6.10e-29

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: 118.57  E-value: 6.10e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDA----VNLEKiyrEVQIMKMLDHPHIIKLYQVMETKSMLYLV 95
Cdd:cd05601    3 FEVKNVIGRGHFGEVQVVKEKATGDIYAMKVLKKSETLAqeevSFFEE---ERDIMAKANSPWITKLQYAFQDSENLYLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA 174
Cdd:cd05601   80 MEYHPGGDLLSLLSRYdDIFEESMARFYLAELVLAIHSLHSMGYVHRDIKPENILIDRTGHIKLADFGSAAKLSSDKTVT 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TW--CGSPPYAAPEVF-----EGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYF----MSED 243
Cdd:cd05601  160 SKmpVGTPDYIAPEVLtsmngGSKGTYGVECDWWSLGIVAYEMLYGKTPFTEDTVIKTYSNIMNFKKFLKFPedpkVSES 239
                        250       260
                 ....*....|....*....|....*.
gi 929654453 244 CEHLIRRmLVLDPSKRLTIAQIKEHK 269
Cdd:cd05601  240 AVDLIKG-LLTDAKERLGYEGLCCHP 264
STKc_NAK_like cd14037
Catalytic domain of Numb-Associated Kinase (NAK)-like Serine/Threonine kinases; STKs catalyze ...
22-268 7.86e-29

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: 117.00  E-value: 7.86e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  22 IEGTLGKGNFAVVKLGRHRITKTEVAIKII---DKSQLDAVNlekiyREVQIMKML-DHPHIIKLYQVMETKSM-----L 92
Cdd:cd14037    7 IEKYLAEGGFAHVYLVKTSNGGNRAALKRVyvnDEHDLNVCK-----REIEIMKRLsGHKNIVGYIDSSANRSGngvyeV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  93 YLVTEYAKNGEIFDYLAN--HGRLNESEARRKFWQILSAVDYCHGRK--IVHRDLKAENLLLDNNMNIKIADFG-----F 163
Cdd:cd14037   82 LLLMEYCKGGGVIDLMNQrlQTGLTESEILKIFCDVCEAVAAMHYLKppLIHRDLKVENVLISDSGNYKLCDFGsattkI 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 164 GNFFKSGELLA--------TwcgSPPYAAPEVFEgqQYEGPQL----DIWSMGVVLYVLVCGALPF-DGPTLPIlrqrvL 230
Cdd:cd14037  162 LPPQTKQGVTYveedikkyT---TLQYRAPEMID--LYRGKPIteksDIWALGCLLYKLCFYTTPFeESGQLAI-----L 231
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 929654453 231 EGRFRIPYF--MSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14037  232 NGNFTFPDNsrYSKRLHKLIRYMLEEDPEKRPNIYQVSYE 271
STKc_CDK2_3 cd07860
Catalytic domain of the Serine/Threonine Kinases, Cyclin-Dependent protein Kinase 2 and 3; ...
26-261 1.47e-28

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: 116.45  E-value: 1.47e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIID-KSQLDAVNLEKIyREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAkNGEI 104
Cdd:cd07860    8 IGEGTYGVVYKARNKLTGEVVALKKIRlDTETEGVPSTAI-REISLLKELNHPNIVKLLDVIHTENKLYLVFEFL-HQDL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYL--ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK------SGELLATW 176
Cdd:cd07860   86 KKFMdaSALTGIPLPLIKSYLFQLLQGLAFCHSHRVLHRDLKPQNLLINTEGAIKLADFGLARAFGvpvrtyTHEVVTLW 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 cgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGP-----------TLPILRQRVLEGRFRIPYF------ 239
Cdd:cd07860  166 -----YRAPEILLGCKYYSTAVDIWSLGCIFAEMVTRRALFPGDseidqlfrifrTLGTPDEVVWPGVTSMPDYkpsfpk 240
                        250       260       270
                 ....*....|....*....|....*....|....
gi 929654453 240 ------------MSEDCEHLIRRMLVLDPSKRLT 261
Cdd:cd07860  241 warqdfskvvppLDEDGRDLLSQMLHYDPNKRIS 274
STKc_TLK cd13990
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase; STKs catalyze the ...
26-268 2.00e-28

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: 115.88  E-value: 2.00e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIidkSQLD--------AVNLEKIYREVQIMKMLDHPHIIKLYQVMET-KSMLYLVT 96
Cdd:cd13990    8 LGKGGFSEVYKAFDLVEQRYVACKI---HQLNkdwseekkQNYIKHALREYEIHKSLDHPRIVKLYDVFEIdTDSFCTVL 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRK--IVHRDLKAENLLLDNNM---NIKIADFGF------GN 165
Cdd:cd13990   85 EYCDGNDLDFYLKQHKSIPEREARSIIMQVVSALKYLNEIKppIIHYDLKPGNILLHSGNvsgEIKITDFGLskimddES 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 166 FFKSG-ELLATWCGSPPYAAPEVFEGQQyEGP----QLDIWSMGVVLYVLVCGALPF--DGPTLPILRQ----RVLEGRF 234
Cdd:cd13990  165 YNSDGmELTSQGAGTYWYLPPECFVVGK-TPPkissKVDVWSVGVIFYQMLYGRKPFghNQSQEAILEEntilKATEVEF 243
                        250       260       270
                 ....*....|....*....|....*....|....
gi 929654453 235 RIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd13990  244 PSKPVVSSEAKDFIRRCLTYRKEDRPDVLQLAND 277
STKc_SGK3 cd05604
Catalytic domain of the Protein Serine/Threonine Kinase, Serum- and Glucocorticoid-induced ...
26-270 2.15e-28

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: 116.99  E-value: 2.15e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQ-LDAVNLEKIYREVQIM-KMLDHPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd05604    4 IGKGSFGKVLLAKRKRDGKYYAVKVLQKKViLNRKEQKHIMAERNVLlKNVKHPFLVGLHYSFQTTDKLYFVLDFVNGGE 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGSPPY 182
Cdd:cd05604   84 LFFHLQRERSFPEPRARFYAAEIASALGYLHSINIVYRDLKPENILLDSQGHIVLTDFGLcKEGISNSDTTTTFCGTPEY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTI 262
Cdd:cd05604  164 LAPEVIRKQPYDN-TVDWWCLGSVLYEMLYGLPPFYCRDTAEMYENILHKPLVLRPGISLTAWSILEELLEKDRQLRLGA 242
                        250
                 ....*....|..
gi 929654453 263 A----QIKEHKW 270
Cdd:cd05604  243 KedflEIKNHPF 254
STKc_16 cd13986
Catalytic domain of Serine/Threonine Kinase 16; STKs catalyze the transfer of the ...
20-268 2.18e-28

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: 115.86  E-value: 2.18e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIK-IIDKSQLDavnLEKIYREVQIMKMLDHPHIIKL--YQVME---TKSMLY 93
Cdd:cd13986    2 YRIQRLLGEGGFSFVYLVEDLSTGRLYALKkILCHSKED---VKEAMREIENYRLFNHPNILRLldSQIVKeagGKKEVY 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKNGEIFDYL----ANHGRLNESEARRKFWQILSAVDYCH---GRKIVHRDLKAENLLLDNNMNIKIADFG---- 162
Cdd:cd13986   79 LLLPYYKRGSLQDEIerrlVKGTFFPEDRILHIFLGICRGLKAMHepeLVPYAHRDIKPGNVLLSEDDEPILMDLGsmnp 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 163 ---FGNFFKSGELLATWC---GSPPYAAPEVF--EGQQYEGPQLDIWSMGVVLYVLVCGALPFD------GPtlpiLRQR 228
Cdd:cd13986  159 ariEIEGRREALALQDWAaehCTMPYRAPELFdvKSHCTIDEKTDIWSLGCTLYALMYGESPFErifqkgDS----LALA 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 929654453 229 VLEGRFRIP----YfmSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd13986  235 VLSGNYSFPdnsrY--SEELHQLVKSMLVVNPAERPSIDDLLSR 276
STKc_Nek4 cd08223
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
20-271 2.35e-28

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: 114.84  E-value: 2.35e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKS-MLYLVTEY 98
Cdd:cd08223    2 YQFLRVIGKGSYGEVWLVRHKRDRKQYVIKKLNLKNASKRERKAAEQEAKLLSKLKHPNIVSYKESFEGEDgFLYIVMGF 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHG--RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA-T 175
Cdd:cd08223   82 CEGGDLYTRLKEQKgvLLEERQVVEWFVQIAMALQYMHERNILHRDLKTQNIFLTKSNIIKVGDLGIARVLESSSDMAtT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRF-RIPYFMSEDCEHLIRRMLVL 254
Cdd:cd08223  162 LIGTPYYMSPELFSNKPYNH-KSDVWALGCCVYEMATLKHAFNAKDMNSLVYKILEGKLpPMPKQYSPELGELIKAMLHQ 240
                        250
                 ....*....|....*..
gi 929654453 255 DPSKRLTIAQIKEHKWM 271
Cdd:cd08223  241 DPEKRPSVKRILRQPYI 257
STKc_EIF2AK4_GCN2_rpt2 cd14046
Catalytic domain, repeat 2, of the Serine/Threonine kinase, eukaryotic translation Initiation ...
26-268 2.77e-28

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: 115.16  E-value: 2.77e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNF-AVVKLgRHRITKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd14046   14 LGKGAFgQVVKV-RNKLDGRYYAIKKI-KLRSESKNNSRILREVMLLSRLNHQHVVRYYQAWIERANLYIQMEYCEKSTL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPYAA 184
Cdd:cd14046   92 RDLIDSGLFQDTDRLWRLFRQILEGLAYIHSQGIIHRDLKPVNIFLDSNGNVKIGDFGLATSNKLNVELATQDINKSTSA 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 185 PEVFEGQQ--------YEGPQL------------DIWSMGVVLYVLvcgALPFDGP-----TLPILRQRVLEgrfrIPYF 239
Cdd:cd14046  172 ALGSSGDLtgnvgtalYVAPEVqsgtkstynekvDMYSLGIIFFEM---CYPFSTGmervqILTALRSVSIE----FPPD 244
                        250       260       270
                 ....*....|....*....|....*....|....
gi 929654453 240 MsEDCEH-----LIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14046  245 F-DDNKHskqakLIRWLLNHDPAKRPSAQELLKS 277
STKc_CDC2L1 cd07843
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 2-like 1; STKs catalyze ...
23-270 5.25e-28

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: 115.01  E-value: 5.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  23 EGTLGkgnfaVVKLGRHRITKTEVAIK-IIDKSQLDAVNLEKIyREVQIMKMLDHPHIIKLYQVMETKSM--LYLVTEYA 99
Cdd:cd07843   15 EGTYG-----VVYRARDKKTGEIVALKkLKMEKEKEGFPITSL-REINILLKLQHPNIVTVKEVVVGSNLdkIYMVMEYV 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNgEIFDYLAN-HGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGfgnffksgelLATWCG 178
Cdd:cd07843   89 EH-DLKSLMETmKQPFLQSEVKCLMLQLLSGVAHLHDNWILHRDLKTSNLLLNNRGILKICDFG----------LAREYG 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPP-----------YAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG----------------PT---------L 222
Cdd:cd07843  158 SPLkpytqlvvtlwYRAPELLLGAKEYSTAIDMWSVGCIFAELLTKKPLFPGkseidqlnkifkllgtPTekiwpgfseL 237
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 929654453 223 PILRQRV--------LEGRFRiPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07843  238 PGAKKKTftkypynqLRKKFP-ALSLSDNGFDLLNRLLTYDPAKRISAEDALKHPY 292
STKc_PCTAIRE_like cd07844
Catalytic domain of PCTAIRE-like Serine/Threonine Kinases; STKs catalyze the transfer of the ...
26-221 8.33e-28

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: 114.02  E-value: 8.33e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIyREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNgEIF 105
Cdd:cd07844    8 LGEGSYATVYKGRSKLTGQLVALKEIRLEHEEGAPFTAI-REASLLKDLKHANIVTLHDIIHTKKTLTLVFEYLDT-DLK 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK------SGELLATWcg 178
Cdd:cd07844   86 QYMDDCGGgLSMHNVRLFLFQLLRGLAYCHQRRVLHRDLKPQNLLISERGELKLADFGLARAKSvpsktySNEVVTLW-- 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 929654453 179 sppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPT 221
Cdd:cd07844  164 ---YRPPDVLLGSTEYSTSLDMWGVGCIFYEMATGRPLFPGST 203
STKc_Bck1_like cd06629
Catalytic domain of the Serine/Threonine Kinases, fungal Bck1-like Mitogen-Activated Protein ...
26-271 8.36e-28

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: 113.63  E-value: 8.36e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKII----------DKSQLDAVnlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLV 95
Cdd:cd06629    9 IGKGTYGRVYLAMNATTGEMLAVKQVelpktssdraDSRQKTVV--DALKSEIDTLKDLDHPNIVQYLGFEETEDYFSIF 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG--------FGNFF 167
Cdd:cd06629   87 LEYVPGGSIGSCLRKYGKFEEDLVRFFTRQILDGLAYLHSKGILHRDLKADNILVDLEGICKISDFGiskksddiYGNNG 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 168 KSgellaTWCGSPPYAAPEVFE--GQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPY----FMS 241
Cdd:cd06629  167 AT-----SMQGSVFWMAPEVIHsqGQGY-SAKVDIWSLGCVVLEMLAGRRPWSDDEAIAAMFKLGNKRSAPPVpedvNLS 240
                        250       260       270
                 ....*....|....*....|....*....|
gi 929654453 242 EDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd06629  241 PEALDFLNACFAIDPRDRPTAAELLSHPFL 270
PTKc_Jak_rpt2 cd05038
Catalytic (repeat 2) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily ...
26-260 1.08e-27

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: 113.63  E-value: 1.08e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRI----TKTEVAIKIIDKSQLDAVnLEKIYREVQIMKMLDHPHIIKLYQVMET---KSMLyLVTEY 98
Cdd:cd05038   12 LGEGHFGSVELCRYDPlgdnTGEQVAVKSLQPSGEEQH-MSDFKREIEILRTLDHEYIVKYKGVCESpgrRSLR-LIMEY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKS-------- 169
Cdd:cd05038   90 LPSGSLRDYLQRHrDQIDLKRLLLFASQICKGMEYLGSQRYIHRDLAARNILVESEDLVKISDFGLAKVLPEdkeyyyvk 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 170 --GELLATWcgsppYaAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIpyfmsedCEHL 247
Cdd:cd05038  170 epGESPIFW-----Y-APECLRESRFSS-ASDVWSFGVTLYELFTYGDPSQSPPALFLRMIGIAQGQMI-------VTRL 235
                        250
                 ....*....|...
gi 929654453 248 IRRmlvLDPSKRL 260
Cdd:cd05038  236 LEL---LKSGERL 245
STKc_IKK_alpha cd14039
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
26-217 1.32e-27

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: 113.86  E-value: 1.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSML-----YLVTEYAK 100
Cdd:cd14039    1 LGTGGFGNVCLYQNQETGEKIAIKSC-RLELSVKNKDRWCHEIQIMKKLNHPNVVKACDVPEEMNFLvndvpLLAMEYCS 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLA---NHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL-DNNMNI--KIADFGFGNFFKSGELLA 174
Cdd:cd14039   80 GGDLRKLLNkpeNCCGLKESQVLSLLSDIGSGIQYLHENKIIHRDLKPENIVLqEINGKIvhKIIDLGYAKDLDQGSLCT 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 929654453 175 TWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPF 217
Cdd:cd14039  160 SFVGTLQYLAPELFENKSYT-VTVDYWSFGTMVFECIAGFRPF 201
STKc_PCTAIRE1 cd07873
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-1 kinase; STKs catalyze the transfer ...
26-222 1.44e-27

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: 113.94  E-value: 1.44e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIyREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAkNGEIF 105
Cdd:cd07873   10 LGEGTYATVYKGRSKLTDNLVALKEIRLEHEEGAPCTAI-REVSLLKDLKHANIVTLHDIIHTEKSLTLVFEYL-DKDLK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRL-NESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK------SGELLATWcg 178
Cdd:cd07873   88 QYLDDCGNSiNMHNVKLFLFQLLRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSiptktySNEVVTLW-- 165
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 929654453 179 sppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTL 222
Cdd:cd07873  166 ---YRPPDILLGSTDYSTQIDMWGVGCIFYEMSTGRPLFPGSTV 206
STKc_SHIK cd13974
Catalytic domain of the Serine/Threonine kinase, SINK-homologous inhibitory kinase; STKs ...
113-268 1.51e-27

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: 113.65  E-value: 1.51e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 113 RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMN-IKIADFGFGNFFKS-GELLATWCGSPPYAAPEVFEG 190
Cdd:cd13974  128 RLSEREALVIFYDVVRVVEALHKKNIVHRDLKLGNMVLNKRTRkITITNFCLGKHLVSeDDLLKDQRGSPAYISPDVLSG 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 191 QQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIP--YFMSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd13974  208 KPYLGKPSDMWALGVVLFTMLYGQFPFYDSIPQELFRKIKAAEYTIPedGRVSENTVCLIRKLLVLNPQKRLTASEVLDS 287
STKc_GRK7 cd05607
Catalytic domain of the Protein Serine/Threonine Kinase, G protein-coupled Receptor Kinase 7; ...
19-260 2.26e-27

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: 113.08  E-value: 2.26e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEgTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKI-YREVQIMKMLDHPHIIKLYQVMETKSMLYLVTE 97
Cdd:cd05607    4 FYEFR-VLGKGGFGEVCAVQVKNTGQMYACKKLDKKRLKKKSGEKMaLLEKEILEKVNSPFIVSLAYAFETKTHLCLVMS 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHGRLNESEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLAT 175
Cdd:cd05607   83 LMNGGDLKYHIYNVGERGIEMERVIFYsaQITCGILHLHSLKIVYRDMKPENVLLDDNGNCRLSDLGLAVEVKEGKPITQ 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYEGPqLDIWSMGVVLYVLVCGALPFDGPTLPI----LRQRVLEG--RFRIPYFmSEDCEHLIR 249
Cdd:cd05607  163 RAGTNGYMAPEILKEESYSYP-VDWFAMGCSIYEMVAGRTPFRDHKEKVskeeLKRRTLEDevKFEHQNF-TEEAKDICR 240
                        250
                 ....*....|.
gi 929654453 250 RMLVLDPSKRL 260
Cdd:cd05607  241 LFLAKKPENRL 251
STKc_ASK cd06624
Catalytic domain of the Serine/Threonine Kinase, Apoptosis signal-regulating kinase; STKs ...
26-271 4.32e-27

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: 111.73  E-value: 4.32e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSqlDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06624   16 LGKGTFGVVYAARDLSTQVRIAIKEIPER--DSREVQPLHEEIALHSRLSHKNIVQYLGSVSEDGFFKIFMEQVPGGSLS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANH-GRLNESEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDN-NMNIKIADFGfgnffkSGELLA------- 174
Cdd:cd06624   94 ALLRSKwGPLKDNENTIGYYtkQILEGLKYLHDNKIVHRDIKGDNVLVNTySGVVKISDFG------TSKRLAginpcte 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TWCGSPPYAAPEVFE-GQQYEGPQLDIWSMGVVLYVLVCGALPF---DGPTLPILRQrvleGRFR----IPYFMSEDCEH 246
Cdd:cd06624  168 TFTGTLQYMAPEVIDkGQRGYGPPADIWSLGCTIIEMATGKPPFielGEPQAAMFKV----GMFKihpeIPESLSEEAKS 243
                        250       260
                 ....*....|....*....|....*
gi 929654453 247 LIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd06624  244 FILRCFEPDPDKRATASDLLQDPFL 268
PKc_Wee1_like cd13997
Catalytic domain of the Wee1-like Protein Kinases; PKs catalyze the transfer of the ...
26-268 5.28e-27

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: 110.94  E-value: 5.28e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQI-MKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd13997    8 IGSGSFSEVFKVRSKVDGCLYAVKKSKKPFRGPKERARALREVEAhAALGQHPNIVRYYSSWEEGGHLYIQMELCENGSL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHG---RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG----FGNFFKSGEllatwc 177
Cdd:cd13997   88 QDALEELSpisKLSEAEVWDLLLQVALGLAFIHSKGIVHLDIKPDNIFISNKGTCKIGDFGlatrLETSGDVEE------ 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 GSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCG-ALPFDGPTLPILRQRVLEGRFRIPYfmSEDCEHLIRRMLVLDP 256
Cdd:cd13997  162 GDSRYLAPELLNENYTHLPKADIFSLGVTVYEAATGePLPRNGQQWQQLRQGKLPLPPGLVL--SQELTRLLKVMLDPDP 239
                        250
                 ....*....|..
gi 929654453 257 SKRLTIAQIKEH 268
Cdd:cd13997  240 TRRPTADQLLAH 251
STKc_MST4 cd06640
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 4; STKs ...
26-272 5.30e-27

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: 111.68  E-value: 5.30e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAvNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06640   12 IGKGSFGEVFKGIDNRTQQVVAIKIIDLEEAED-EIEDIQQEITVLSQCDSPYVTKYYGSYLKGTKLWIIMEYLGGGSAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLaNHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL-LATWCGSPPYAA 184
Cdd:cd06640   91 DLL-RAGPFDEFQIATMLKEILKGLDYLHSEKKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIkRNTFVGTPFWMA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 185 PEVFEGQQYEGpQLDIWSMGVVLYVLVCGalpfDGPTLPILRQRVLegrFRIPYF--------MSEDCEHLIRRMLVLDP 256
Cdd:cd06640  170 PEVIQQSAYDS-KADIWSLGITAIELAKG----EPPNSDMHPMRVL---FLIPKNnpptlvgdFSKPFKEFIDACLNKDP 241
                        250
                 ....*....|....*.
gi 929654453 257 SKRLTIAQIKEHKWML 272
Cdd:cd06640  242 SFRPTAKELLKHKFIV 257
PTKc_Frk_like cd05068
Catalytic domain of Fyn-related kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
26-237 8.15e-27

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: 110.57  E-value: 8.15e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITkTEVAIKIIDKSQLDAvnlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd05068   16 LGSGQFGEVWEGLWNNT-TPVAVKTLKPGTMDP---EDFLREAQIMKKLRHPKLIQLYAVCTLEEPIYIITELMKHGSLL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSP---P 181
Cdd:cd05068   92 EYLQGKGRsLQLPQLIDMAAQVASGMAYLESQNYIHRDLAARNVLVGENNICKVADFGLARVIKVEDEYEAREGAKfpiK 171
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 929654453 182 YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLPILRQRVLEGrFRIP 237
Cdd:cd05068  172 WTAPEAANYNRFS-IKSDVWSFGILLTEIVTyGRIPYPGMTNAEVLQQVERG-YRMP 226
STKc_CDK9 cd07865
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 9; STKs ...
17-270 8.82e-27

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: 111.69  E-value: 8.82e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  17 VGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIdksqldAVNLEK------IYREVQIMKMLDHPHIIKLYQVMET-- 88
Cdd:cd07865   11 VSKYEKLAKIGQGTFGEVFKARHRKTGQIVALKKV------LMENEKegfpitALREIKILQLLKHENVVNLIEICRTka 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  89 ------KSMLYLVTEYAKNgEIFDYLAN-HGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADF 161
Cdd:cd07865   85 tpynryKGSIYLVFEFCEH-DLAGLLSNkNVKFTLSEIKKVMKMLLNGLYYIHRNKILHRDMKAANILITKDGVLKLADF 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 162 GFGNFFK----------SGELLATWcgsppYAAPEVFEGQQYEGPQLDIWSMGVV---------------------LYVL 210
Cdd:cd07865  164 GLARAFSlaknsqpnryTNRVVTLW-----YRPPELLLGERDYGPPIDMWGAGCImaemwtrspimqgnteqhqltLISQ 238
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 929654453 211 VCGAL-----P-------FDGPTLPILRQRVLEGRFRiPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07865  239 LCGSItpevwPgvdklelFKKMELPQGQKRKVKERLK-PYVKDPYALDLIDKLLVLDPAKRIDADTALNHDF 309
STKc_Titin cd14104
Catalytic domain of the Giant Serine/Threonine Kinase Titin; STKs catalyze the transfer of the ...
20-271 1.19e-26

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: 110.72  E-value: 1.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKiyrEVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14104    2 YMIAEELGRGQFGIVHRCVETSSKKTYMAKFVKVKGADQVLVKK---EISILNIARHRNILRLHESFESHEELVMIFEFI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNM--NIKIADFGFGNFFKSGELLATW 176
Cdd:cd14104   79 SGVDIFERITTARfELNEREIVSYVRQVCEALEFLHSKNIGHFDIRPENIIYCTRRgsYIKIIEFGQSRQLKPGDKFRLQ 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGR--FRIPYF--MSEDCEHLIRRML 252
Cdd:cd14104  159 YTSAEFYAPEVHQHESV-STATDMWSLGCLVYVLLSGINPFEAETNQQTIENIRNAEyaFDDEAFknISIEALDFVDRLL 237
                        250
                 ....*....|....*....
gi 929654453 253 VLDPSKRLTIAQIKEHKWM 271
Cdd:cd14104  238 VKERKSRMTAQEALNHPWL 256
STKc_GRK6 cd05630
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 6; STKs ...
26-268 1.19e-26

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: 110.88  E-value: 1.19e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKI-YREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05630    8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMaLNEKQILEKVNSRFVVSLAYAYETKDALCLVLTLMNGGDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPY 182
Cdd:cd05630   88 KFHIYHMGQAGFPEARAVFYaaEICCGLEDLHRERIVYRDLKPENILLDDHGHIRISDLGLAVHVPEGQTIKGRVGTVGY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYE-GPqlDIWSMGVVLYVLVCGALPFDGPTLPILRQR----VLEGRFRIPYFMSEDCEHLIRRMLVLDPS 257
Cdd:cd05630  168 MAPEVVKNERYTfSP--DWWALGCLLYEMIAGQSPFQQRKKKIKREEverlVKEVPEEYSEKFSPQARSLCSMLLCKDPA 245
                        250
                 ....*....|....*.
gi 929654453 258 KRL-----TIAQIKEH 268
Cdd:cd05630  246 ERLgcrggGAREVKEH 261
STKc_MEKK3_like_u1 cd06653
Catalytic domain of an Uncharacterized subfamily of Mitogen-Activated Protein (MAP) ...
26-253 1.22e-26

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: 110.11  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIID---KSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVME--TKSMLYLVTEYAK 100
Cdd:cd06653   10 LGRGAFGEVYLCYDADTGRELAVKQVPfdpDSQETSKEVNALECEIQLLKNLRHDRIVQYYGCLRdpEEKKLSIFVEYMP 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG----FGNFFKSGELLATW 176
Cdd:cd06653   90 GGSVKDQLKAYGALTENVTRRYTRQILQGVSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGaskrIQTICMSGTGIKSV 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 929654453 177 CGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFD--GPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLV 253
Cdd:cd06653  170 TGTPYWMSPEVISGEGY-GRKADVWSVACTVVEMLTEKPPWAeyEAMAAIFKIATQPTKPQLPDGVSDACRDFLRQIFV 247
PKc_Byr1_like cd06620
Catalytic domain of fungal Byr1-like dual-specificity Mitogen-activated protein Kinase Kinases; ...
26-278 1.37e-26

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: 110.61  E-value: 1.37e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLYQVMETKS-MLYLVTEYAKNGEI 104
Cdd:cd06620   13 LGAGNGGSVSKVLHIPTGTIMAKKVIHIDAKSSVR-KQILRELQILHECHSPYIVSFYGAFLNENnNIIICMEYMDCGSL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGR-KIVHRDLKAENLLLDNNMNIKIADFGFgnffkSGELL----ATWCGS 179
Cdd:cd06620   92 DKILKKKGPFPEEVLGKIAVAVLEGLTYLYNVhRIIHRDIKPSNILVNSKGQIKLCDFGV-----SGELInsiaDTFVGT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPT------------LPILRQRVLEGRFRIP--YFMSEDCE 245
Cdd:cd06620  167 STYMSPERIQGGKY-SVKSDVWSLGLSIIELALGEFPFAGSNddddgyngpmgiLDLLQRIVNEPPPRLPkdRIFPKDLR 245
                        250       260       270
                 ....*....|....*....|....*....|....
gi 929654453 246 HLIRRMLVLDPSKRLTIAQIKEHK-WMLIEVPVQ 278
Cdd:cd06620  246 DFVDRCLLKDPRERPSPQLLLDHDpFIQAVRASD 279
PTKc_FAK cd05056
Catalytic domain of the Protein Tyrosine Kinase, Focal Adhesion Kinase; PTKs catalyze the ...
25-267 1.68e-26

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: 109.82  E-value: 1.68e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLG---RHRITKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMlYLVTEYAKN 101
Cdd:cd05056   13 CIGEGQFGDVYQGvymSPENEKIAVAVKTC-KNCTSPSVREKFLQEAYIMRQFDHPHIVKLIGVITENPV-WIVMELAPL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLANHGRLNESEARRKF-WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSP 180
Cdd:cd05056   91 GELRSYLQVNKYSLDLASLILYaYQLSTALAYLESKRFVHRDIAARNVLVSSPDCVKLGDFGLSRYMEDESYYKASKGKL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 181 P--YAAPEVFEGQQYEGPQlDIWSMGVVLY-VLVCGALPFDGPTLP--ILRqrvLEGRFRIPyfMSEDCE----HLIRRM 251
Cdd:cd05056  171 PikWMAPESINFRRFTSAS-DVWMFGVCMWeILMLGVKPFQGVKNNdvIGR---IENGERLP--MPPNCPptlySLMTKC 244
                        250
                 ....*....|....*.
gi 929654453 252 LVLDPSKRLTIAQIKE 267
Cdd:cd05056  245 WAYDPSKRPRFTELKA 260
PTKc_Syk_like cd05060
Catalytic domain of Spleen Tyrosine Kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
26-267 1.91e-26

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: 109.36  E-value: 1.91e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKT---EVAIKIIDKSQLDAvNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLyLVTEYAKNG 102
Cdd:cd05060    3 LGHGNFGSVRKGVYLMKSGkevEVAVKTLKQEHEKA-GKKEFLREASVMAQLDHPCIVRLIGVCKGEPLM-LVMELAPLG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE--LLATWCGSP 180
Cdd:cd05060   81 PLLKYLKKRREIPVSDLKELAHQVAMGMAYLESKHFVHRDLAARNVLLVNRHQAKISDFGMSRALGAGSdyYRATTAGRW 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 181 P--YAAPEVFEGQQYEGPQlDIWSMGVVLY-VLVCGALPFDGPTLP-ILRQrvLEGRFRIPyfMSEDC-EHLIRRML--- 252
Cdd:cd05060  161 PlkWYAPECINYGKFSSKS-DVWSYGVTLWeAFSYGAKPYGEMKGPeVIAM--LESGERLP--RPEECpQEIYSIMLscw 235
                        250
                 ....*....|....*
gi 929654453 253 VLDPSKRLTIAQIKE 267
Cdd:cd05060  236 KYRPEDRPTFSELES 250
STKc_GRK1 cd05608
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 1; STKs ...
26-268 2.07e-26

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: 110.36  E-value: 2.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVN-LEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05608    9 LGKGGFGEVSACQMRATGKLYACKKLNKKRLKKRKgYEGAMVEKRILAKVHSRFIVSLAYAFQTKTDLCLVMTIMNGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNE--SEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSG-ELLATWCGS 179
Cdd:cd05608   89 RYHIYNVDEENPgfQEPRACFYtaQIISGLEHLHQRRIIYRDLKPENVLLDDDGNVRISDLGLAVELKDGqTKTKGYAGT 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPI----LRQRVLEGRFRIPYFMSEDCEHLIRRMLVLD 255
Cdd:cd05608  169 PGFMAPELLLGEEYD-YSVDYFTLGVTLYEMIAARGPFRARGEKVenkeLKQRILNDSVTYSEKFSPASKSICEALLAKD 247
                        250
                 ....*....|....*...
gi 929654453 256 PSKRL-----TIAQIKEH 268
Cdd:cd05608  248 PEKRLgfrdgNCDGLRTH 265
STKc_EIF2AK2_PKR cd14047
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
16-268 2.28e-26

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: 109.50  E-value: 2.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  16 RVGFYDIEgTLGKGNFAVVKLGRHRITKTEVAIKIIDksqldaVNLEKIYREVQIMKMLDHPHIIKLY-------QVMET 88
Cdd:cd14047    5 RQDFKEIE-LIGSGGFGQVFKAKHRIDGKTYAIKRVK------LNNEKAEREVKALAKLDHPNIVRYNgcwdgfdYDPET 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  89 KSM---------LYLVTEYAKNGEIFDYLA--NHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIK 157
Cdd:cd14047   78 SSSnssrsktkcLFIQMEFCEKGTLESWIEkrNGEKLDKVLALEIFEQITKGVEYIHSKKLIHRDLKPSNIFLVDTGKVK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 158 IADFGFGNFFKSGELLATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVL--VCGALPFDGPTLPILRQRVLEGRFR 235
Cdd:cd14047  158 IGDFGLVTSLKNDGKRTKSKGTLSYMSPEQISSQDY-GKEVDIYALGLILFELlhVCDSAFEKSKFWTDLRNGILPDIFD 236
                        250       260       270
                 ....*....|....*....|....*....|...
gi 929654453 236 IPYFMSEDcehLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14047  237 KRYKIEKT---IIKKMLSKKPEDRPNASEILRT 266
STKc_MAP4K3_like cd06613
Catalytic domain of Mitogen-activated protein kinase kinase kinase kinase (MAP4K) 3-like ...
20-269 2.72e-26

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: 108.93  E-value: 2.72e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDavNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd06613    2 YELIQRIGSGTYGDVYKARNIATGELAAVKVIKLEPGD--DFEIIQQEISMLKECRHPNIVAYFGSYLRRDKLWIVMEYC 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFgnffkSGELLAT---- 175
Cdd:cd06613   80 GGGSLQDIYQVTGPLSELQIAYVCRETLKGLAYLHSTGKIHRDIKGANILLTEDGDVKLADFGV-----SAQLTATiakr 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 --WCGSPPYAAPEVFEGQQYEG--PQLDIWSMGVVLYVLVCGALP-FDgpTLPIlrqRVLegrFRIPYFM---------- 240
Cdd:cd06613  155 ksFIGTPYWMAPEVAAVERKGGydGKCDIWALGITAIELAELQPPmFD--LHPM---RAL---FLIPKSNfdppklkdke 226
                        250       260       270
                 ....*....|....*....|....*....|.
gi 929654453 241 --SEDCEHLIRRMLVLDPSKRLTIAQIKEHK 269
Cdd:cd06613  227 kwSPDFHDFIKKCLTKNPKKRPTATKLLQHP 257
pk1 PHA03390
serine/threonine-protein kinase 1; Provisional
29-273 2.73e-26

serine/threonine-protein kinase 1; Provisional


Pssm-ID: 223069 [Multi-domain]  Cd Length: 267  Bit Score: 109.18  E-value: 2.73e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  29 GNFAVVKLGRHRITKTEVAIKIIDKSQLDAVnlekiyrEV---QIMKmlDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:PHA03390  27 GKFGKVSVLKHKPTQKLFVQKIIKAKNFNAI-------EPmvhQLMK--DNPNFIKLYYSVTTLKGHVLIMDYIKDGDLF 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMN-IKIADFGfgnffksgelLATWCGSPP--- 181
Cdd:PHA03390  98 DLLKKEGKLSEAEVKKIIRQLVEALNDLHKHNIIHNDIKLENVLYDRAKDrIYLCDYG----------LCKIIGTPScyd 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 ----YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGP-----TLPILRQRvLEGRFRIPYFMSEDCEHLIRRML 252
Cdd:PHA03390 168 gtldYFSPEKIKGHNYD-VSFDWWAVGVLTYELLTGKHPFKEDedeelDLESLLKR-QQKKLPFIKNVSKNANDFVQSML 245
                        250       260
                 ....*....|....*....|..
gi 929654453 253 VLDPSKRL-TIAQIKEHKWMLI 273
Cdd:PHA03390 246 KYNINYRLtNYNEIIKHPFLKI 267
PTKc_Src_like cd05034
Catalytic domain of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
26-267 2.82e-26

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: 108.52  E-value: 2.82e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITkTEVAIKIIDKSQLDAvnlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd05034    3 LGAGQFGEVWMGVWNGT-TKVAVKTLKPGTMSP---EAFLQEAQIMKKLRHDKLVQLYAVCSDEEPIYIVTELMSKGSLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLAN-HGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPP-- 181
Cdd:cd05034   79 DYLRTgEGRaLRLPQLIDMAAQIASGMAYLESRNYIHRDLAARNILVGENNVCKVADFGLARLIEDDEYTAREGAKFPik 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLP-ILRQrvLEGRFRIPyfMSEDCEHLIRRMLVL----D 255
Cdd:cd05034  159 WTAPEAALYGRFT-IKSDVWSFGILLYEIVTyGRVPYPGMTNReVLEQ--VERGYRMP--KPPGCPDELYDIMLQcwkkE 233
                        250
                 ....*....|..
gi 929654453 256 PSKRLTIAQIKE 267
Cdd:cd05034  234 PEERPTFEYLQS 245
PK_TRB2 cd14022
Pseudokinase domain of Tribbles Homolog 2; The pseudokinase domain shows similarity to protein ...
76-270 3.22e-26

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: 108.20  E-value: 3.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  76 HPHIIKLYQVM--ETKSMLYLVTEYaknGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNN 153
Cdd:cd14022   44 HSNINQITEIIlgETKAYVFFERSY---GDMHSFVRTCKKLREEEAARLFYQIASAVAHCHDGGLVLRDLKLRKFVFKDE 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 154 MNIKIADFGFGNFF---KSGELLATWCGSPPYAAPEVFEGQ-QYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRV 229
Cdd:cd14022  121 ERTRVKLESLEDAYilrGHDDSLSDKHGCPAYVSPEILNTSgSYSGKAADVWSLGVMLYTMLVGRYPFHDIEPSSLFSKI 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 929654453 230 LEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd14022  201 RRGQFNIPETLSPKAKCLIRSILRREPSERLTSQEILDHPW 241
PKc_Myt1 cd14050
Catalytic domain of the Dual-specificity protein kinase, Myt1; Dual-specificity PKs catalyze ...
20-268 3.24e-26

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: 108.55  E-value: 3.24e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREV-QIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd14050    3 FTILSKLGEGSFGEVFKVRSREDGKLYAVKRSRSRFRGEKDRKRKLEEVeRHEKLGEHPNCVRFIKAWEEKGILYIQTEL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AkNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCG 178
Cdd:cd14050   83 C-DTSLQQYCEETHSLPESEVWNILLDLLKGLKHLHDHGLIHLDIKPANIFLSKDGVCKLGDFGLVVELDKEDIHDAQEG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQyeGPQLDIWSMGVVLYVLVCG-ALPFDGPTLPILRQRVLEGRFRIPyfMSEDCEHLIRRMLVLDPS 257
Cdd:cd14050  162 DPRYMAPELLQGSF--TKAADIFSLGITILELACNlELPSGGDGWHQLRQGYLPEEFTAG--LSPELRSIIKLMMDPDPE 237
                        250
                 ....*....|.
gi 929654453 258 KRLTIAQIKEH 268
Cdd:cd14050  238 RRPTAEDLLAL 248
STKc_CDK4_6_like cd07838
Catalytic domain of Cyclin-Dependent protein Kinase 4 and 6-like Serine/Threonine Kinases; ...
20-270 3.44e-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: 109.29  E-value: 3.44e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIdKSQL--DAVNLEKIyREVQIMKMLD---HPHIIKLYQV-----METK 89
Cdd:cd07838    1 YEEVAEIGEGAYGTVYKARDLQDGRFVALKKV-RVPLseEGIPLSTI-REIALLKQLEsfeHPNVVRLLDVchgprTDRE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  90 SMLYLVTEYAKNgEIFDYLANHGR--LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFF 167
Cdd:cd07838   79 LKLTLVFEHVDQ-DLATYLDKCPKpgLPPETIKDLMRQLLRGLDFLHSHRIVHRDLKPQNILVTSDGQVKLADFGLARIY 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 168 KSGELLAT-----WcgsppYAAPEVFEGQQYEGPqLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLE----------- 231
Cdd:cd07838  158 SFEMALTSvvvtlW-----YRAPEVLLQSSYATP-VDMWSVGCIFAELFNRRPLFRGSSEADQLGKIFDviglpseeewp 231
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 929654453 232 -----------GRFRIPY--FMSEDCE---HLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07838  232 rnsalprssfpSYTPRPFksFVPEIDEeglDLLKKMLTFNPHKRISAFEALQHPY 286
STKc_ROCK2 cd05621
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
8-222 4.08e-26

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: 111.63  E-value: 4.08e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   8 RHLQRGPVRVGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLDHPHIIKLYQVM 86
Cdd:cd05621   42 NKIRELQMKAEDYDVVKVIGRGAFGEVQLVRHKASQKVYAMKLLSKFEMiKRSDSAFFWEERDIMAFANSPWVVQLFCAF 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  87 ETKSMLYLVTEYAKNGEIFDYLANHgrlNESEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADfgFG 164
Cdd:cd05621  122 QDDKYLYMVMEYMPGGDLVNLMSNY---DVPEKWAKFYtaEVVLALDAIHSMGLIHRDVKPDNMLLDKYGHLKLAD--FG 196
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 929654453 165 NFFKSGELLATWC----GSPPYAAPEVFE---GQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTL 222
Cdd:cd05621  197 TCMKMDETGMVHCdtavGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLFEMLVGDTPFYADSL 261
STKc_ROCK1 cd05622
Catalytic domain of the Serine/Threonine Kinase, Rho-associated coiled-coil containing protein ...
20-268 4.61e-26

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: 111.64  E-value: 4.61e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd05622   75 YEVVKVIGRGAFGEVQLVRHKSTRKVYAMKLLSKFEMiKRSDSAFFWEERDIMAFANSPWVVQLFYAFQDDRYLYMVMEY 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGrLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG-NFFKSGELLA-TW 176
Cdd:cd05622  155 MPGGDLVNLMSNYD-VPEKWARFYTAEVVLALDAIHSMGFIHRDVKPDNMLLDKSGHLKLADFGTCmKMNKEGMVRCdTA 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFE---GQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPY----FMSEDCEHLIR 249
Cdd:cd05622  234 VGTPDYISPEVLKsqgGDGYYGRECDWWSVGVFLYEMLVGDTPFYADSLVGTYSKIMNHKNSLTFpddnDISKEAKNLIC 313
                        250       260
                 ....*....|....*....|..
gi 929654453 250 RMLVlDPSKRL---TIAQIKEH 268
Cdd:cd05622  314 AFLT-DREVRLgrnGVEEIKRH 334
STKc_DMPK_like cd05597
Catalytic domain of Myotonic Dystrophy protein kinase (DMPK)-like Serine/Threonine Kinases; ...
20-270 5.46e-26

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: 110.13  E-value: 5.46e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQ-IMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd05597    3 FEILKVIGRGAFGEVAVVKLKSTEKVYAMKILNKWEMLKRAETACFREERdVLVNGDRRWITKLHYAFQDENYLYLVMDY 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADfgFGNFFKSGELLATWC 177
Cdd:cd05597   83 YCGGDLLTLLSKFEdRLPEEMARFYLAEMVLAIDSIHQLGYVHRDIKPDNVLLDRNGHIRLAD--FGSCLKLREDGTVQS 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 ----GSPPYAAPEVF----EGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVL--EGRFRIPYF---MSEDC 244
Cdd:cd05597  161 svavGTPDYISPEILqameDGKGRYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhKEHFSFPDDeddVSEEA 240
                        250       260
                 ....*....|....*....|....*....
gi 929654453 245 EHLIRRmLVLDPSKRL---TIAQIKEHKW 270
Cdd:cd05597  241 KDLIRR-LICSRERRLgqnGIDDFKKHPF 268
STKc_MST3 cd06641
Catalytic domain of the Serine/Threonine Kinase, Mammalian Ste20-like protein kinase 3; STKs ...
26-272 5.52e-26

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: 108.62  E-value: 5.52e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAvNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06641   12 IGKGSFGEVFKGIDNRTQKVVAIKIIDLEEAED-EIEDIQQEITVLSQCDSPYVTKYYGSYLKDTKLWIIMEYLGGGSAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLaNHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFgnffkSGELLAT------WCGS 179
Cdd:cd06641   91 DLL-EPGPLDETQIATILREILKGLDYLHSEKKIHRDIKAANVLLSEHGEVKLADFGV-----AGQLTDTqikrn*FVGT 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFD--GPT-----LPILRQRVLEGRFripyfmSEDCEHLIRRML 252
Cdd:cd06641  165 PFWMAPEVIKQSAYDS-KADIWSLGITAIELARGEPPHSelHPMkvlflIPKNNPPTLEGNY------SKPLKEFVEACL 237
                        250       260
                 ....*....|....*....|
gi 929654453 253 VLDPSKRLTIAQIKEHKWML 272
Cdd:cd06641  238 NKEPSFRPTAKELLKHKFIL 257
STKc_CDK12 cd07864
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 12; STKs ...
17-271 5.62e-26

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: 109.12  E-value: 5.62e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  17 VGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKiidKSQLDAvnlEK------IYREVQIMKMLDHPHIIKLYQVM---- 86
Cdd:cd07864    6 VDKFDIIGIIGEGTYGQVYKAKDKDTGELVALK---KVRLDN---EKegfpitAIREIKILRQLNHRSVVNLKEIVtdkq 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  87 ------ETKSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIAD 160
Cdd:cd07864   80 daldfkKDKGAFYLVFEYMDHDLMGLLESGLVHFSEDHIKSFMKQLLEGLNYCHKKNFLHRDIKCSNILLNNKGQIKLAD 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 161 FGFGNFFKSGE-------LLATWcgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVL---------------------VC 212
Cdd:cd07864  160 FGLARLYNSEEsrpytnkVITLW-----YRPPELLLGEERYGPAIDVWSCGCILGELftkkpifqanqelaqlelisrLC 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 929654453 213 GA-LPFDGPT---LPILR----QRVLEGRFRIPY-FMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd07864  235 GSpCPAVWPDvikLPYFNtmkpKKQYRRRLREEFsFIPTPALDLLDHMLTLDPSKRCTAEQALNSPWL 302
STKc_GRK5 cd05632
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 5; STKs ...
26-271 6.76e-26

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: 109.29  E-value: 6.76e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKI-YREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05632   10 LGKGGFGEVCACQVRATGKMYACKRLEKKRIKKRKGESMaLNEKQILEKVNSQFVVNLAYAYETKDALCLVLTIMNGGDL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPY 182
Cdd:cd05632   90 KFHIYNMGNPGFEEERALFYaaEILCGLEDLHRENTVYRDLKPENILLDDYGHIRISDLGLAVKIPEGESIRGRVGTVGY 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQ----RVLEGRFRIPYFMSEDCEHLIRRMLVLDPSK 258
Cdd:cd05632  170 MAPEVLNNQRY-TLSPDYWGLGCLIYEMIEGQSPFRGRKEKVKREevdrRVLETEEVYSAKFSEEAKSICKMLLTKDPKQ 248
                        250
                 ....*....|....*...
gi 929654453 259 RLTI-----AQIKEHKWM 271
Cdd:cd05632  249 RLGCqeegaGEVKRHPFF 266
STKc_PFTAIRE2 cd07870
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-2 kinase; STKs catalyze the transfer ...
26-219 7.51e-26

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: 108.51  E-value: 7.51e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIyREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNgEIF 105
Cdd:cd07870    8 LGEGSYATVYKGISRINGQLVALKVISMKTEEGVPFTAI-REASLLKGLKHANIVLLHDIIHTKETLTFVFEYMHT-DLA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK------SGELLATWcg 178
Cdd:cd07870   86 QYMIQHpGGLHPYNVRLFMFQLLRGLAYIHGQHILHRDLKPQNLLISYLGELKLADFGLARAKSipsqtySSEVVTLW-- 163
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 929654453 179 sppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG 219
Cdd:cd07870  164 ---YRPPDVLLGATDYSSALDIWGAGCIFIEMLQGQPAFPG 201
PTKc_Btk_Bmx cd05113
Catalytic domain of the Protein Tyrosine Kinases, Bruton's tyrosine kinase and Bone marrow ...
26-242 7.94e-26

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: 107.66  E-value: 7.94e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRiTKTEVAIKIIDKSQLDAvnlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd05113   12 LGTGQFGVVKYGKWR-GQYDVAIKMIKEGSMSE---DEFIEEAKVMMNLSHEKLVQLYGVCTKQRPIFIITEYMANGCLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPP--Y 182
Cdd:cd05113   88 NYLREMRkRFQTQQLLEMCKDVCEAMEYLESKQFLHRDLAARNCLVNDQGVVKVSDFGLSRYVLDDEYTSSVGSKFPvrW 167
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 929654453 183 AAPEVFEGQQYEGPQlDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEG-RFRIPYFMSE 242
Cdd:cd05113  168 SPPEVLMYSKFSSKS-DVWAFGVLMWeVYSLGKMPYERFTNSETVEHVSQGlRLYRPHLASE 228
STKc_SLK cd06643
Catalytic domain of the Serine/Threonine Kinase, Ste20-Like Kinase; STKs catalyze the transfer ...
19-207 8.22e-26

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: 108.19  E-value: 8.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDavNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd06643    6 FWEIVGELGDGAFGKVYKAQNKETGILAAAKVIDTKSEE--ELEDYMVEIDILASCDHPNIVKLLDAFYYENNLWILIEF 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATW 176
Cdd:cd06643   84 CAGGAVDAVMLELERpLTEPQIRVVCKQTLEALVYLHENKIIHRDLKAGNILFTLDGDIKLADFGVsAKNTRTLQRRDSF 163
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 929654453 177 CGSPPYAAPEVF-----EGQQYEGpQLDIWSMGVVL 207
Cdd:cd06643  164 IGTPYWMAPEVVmcetsKDRPYDY-KADVWSLGVTL 198
STKc_IRAK cd14066
Catalytic domain of the Serine/Threonine kinases, Interleukin-1 Receptor Associated Kinases ...
26-259 8.93e-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: 107.74  E-value: 8.93e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRiTKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQ-VMETKSMLyLVTEYAKNGEI 104
Cdd:cd14066    1 IGSGGFGTVYKGVLE-NGTVVAVKRL-NEMNCAASKKEFLTELEMLGRLRHPNLVRLLGyCLESDEKL-LVYEYMPNGSL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDylanhgRLNESEARRKF-WQ--------ILSAVDYCHG---RKIVHRDLKAENLLLDNNMNIKIADFGF---GNFFKS 169
Cdd:cd14066   78 ED------RLHCHKGSPPLpWPqrlkiakgIARGLEYLHEecpPPIIHGDIKSSNILLDEDFEPKLTDFGLarlIPPSES 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 170 GELLATWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEgrfripYFMS---EDCEH 246
Cdd:cd14066  152 VSKTSAVKGTIGYLAPEYIRTGRVS-TKSDVYSFGVVLLELLTGKPAVDENRENASRKDLVE------WVESkgkEELED 224
                        250
                 ....*....|...
gi 929654453 247 LIRRMLVLDPSKR 259
Cdd:cd14066  225 ILDKRLVDDDGVE 237
STKc_PAK6 cd06659
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 6; STKs catalyze the ...
1-272 9.01e-26

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: 108.53  E-value: 9.01e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   1 MVMADG-PRHLQRGPVRVGfydiEGTLGkgnfaVVKLGRHRITKTEVAIKIID--KSQldavNLEKIYREVQIMKMLDHP 77
Cdd:cd06659   12 MVVDQGdPRQLLENYVKIG----EGSTG-----VVCIAREKHSGRQVAVKMMDlrKQQ----RRELLFNEVVIMRDYQHP 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  78 HIIKLYQVMETKSMLYLVTEYAKNGEIFDyLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIK 157
Cdd:cd06659   79 NVVEMYKSYLVGEELWVLMEYLQGGALTD-IVSQTRLNEEQIATVCEAVLQALAYLHSQGVIHRDIKSDSILLTLDGRVK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 158 IADFGF-GNFFKSGELLATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPF--DGPTLPILRQR-VLEGR 233
Cdd:cd06659  158 LSDFGFcAQISKDVPKRKSLVGTPYWMAPEVISRCPY-GTEVDIWSLGIMVIEMVDGEPPYfsDSPVQAMKRLRdSPPPK 236
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 929654453 234 FRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWML 272
Cdd:cd06659  237 LKNSHKASPVLRDFLERMLVRDPQERATAQELLDHPFLL 275
PK_TRB1 cd14023
Pseudokinase domain of Tribbles Homolog 1; The pseudokinase domain shows similarity to protein ...
76-270 9.32e-26

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: 107.06  E-value: 9.32e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  76 HPHIIKLYQVM--ETKSMLYLVTEYaknGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNN 153
Cdd:cd14023   44 HRNITGIVEVIlgDTKAYVFFEKDF---GDMHSYVRSCKRLREEEAARLFKQIVSAVAHCHQSAIVLGDLKLRKFVFSDE 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 154 --MNIKIADFGFGNFFK-SGELLATWCGSPPYAAPEVFEGQ-QYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRV 229
Cdd:cd14023  121 erTQLRLESLEDTHIMKgEDDALSDKHGCPAYVSPEILNTTgTYSGKSADVWSLGVMLYTLLVGRYPFHDSDPSALFSKI 200
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 929654453 230 LEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd14023  201 RRGQFCIPDHVSPKARCLIRSLLRREPSERLTAPEILLHPW 241
STKc_GRK4_like cd05605
Catalytic domain of G protein-coupled Receptor Kinase 4-like Serine/Threonine Kinases; STKs ...
26-270 1.01e-25

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: 108.21  E-value: 1.01e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKI-YREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05605    8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMaLNEKQILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPY 182
Cdd:cd05605   88 KFHIYNMGNPGFEEERAVFYaaEITCGLEHLHSERIVYRDLKPENILLDDHGHVRISDLGLAVEIPEGETIRGRVGTVGY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYE-GPqlDIWSMGVVLYVLVCGALPFDGPTLPILR----QRVLEGRFRIPYFMSEDCEHLIRRMLVLDPS 257
Cdd:cd05605  168 MAPEVVKNERYTfSP--DWWGLGCLIYEMIEGQAPFRARKEKVKReevdRRVKEDQEEYSEKFSEEAKSICSQLLQKDPK 245
                        250
                 ....*....|....*...
gi 929654453 258 KRL-----TIAQIKEHKW 270
Cdd:cd05605  246 TRLgcrgeGAEDVKSHPF 263
STKc_CDKL5 cd07848
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase Like 5; STKs ...
20-221 1.05e-25

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: 108.16  E-value: 1.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd07848    3 FEVLGVVGEGAYGVVLKCRHKETKEIVAIKKFKDSEENEEVKETTLRELKMLRTLKQENIVELKEAFRRRGKLYLVFEYV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNG--EIFDYLANhGRLNEsEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSG------E 171
Cdd:cd07848   83 EKNmlELLEEMPN-GVPPE-KVRSYIYQLIKAIHWCHKNDIVHRDIKPENLLISHNDVLKLCDFGFARNLSEGsnanytE 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 929654453 172 LLAT-WcgsppYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPT 221
Cdd:cd07848  161 YVATrW-----YRSPELLLGAPY-GKAVDMWSVGCILGELSDGQPLFPGES 205
STKc_STK25 cd06642
Catalytic domain of Serine/Threonine Kinase 25 (also called Yeast Sps1/Ste20-related kinase 1); ...
26-272 1.10e-25

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: 107.84  E-value: 1.10e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAvNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06642   12 IGKGSFGEVYKGIDNRTKEVVAIKIIDLEEAED-EIEDIQQEITVLSQCDSPYITRYYGSYLKGTKLWIIMEYLGGGSAL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLaNHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL-LATWCGSPPYAA 184
Cdd:cd06642   91 DLL-KPGPLEETYIATILREILKGLDYLHSERKIHRDIKAANVLLSEQGDVKLADFGVAGQLTDTQIkRNTFVGTPFWMA 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 185 PEVFEGQQYEGpQLDIWSMGVVLYVLVCGALPFDG--PT-----LPILRQRVLEGRFRIPYfmsedcEHLIRRMLVLDPS 257
Cdd:cd06642  170 PEVIKQSAYDF-KADIWSLGITAIELAKGEPPNSDlhPMrvlflIPKNSPPTLEGQHSKPF------KEFVEACLNKDPR 242
                        250
                 ....*....|....*
gi 929654453 258 KRLTIAQIKEHKWML 272
Cdd:cd06642  243 FRPTAKELLKHKFIT 257
STKc_MRCK_beta cd05624
Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control ...
20-269 1.45e-25

Catalytic domain of the Protein Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) beta; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-beta is expressed ubiquitously in many tissues. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-beta subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270774 [Multi-domain]  Cd Length: 409  Bit Score: 110.48  E-value: 1.45e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQ-IMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd05624   74 FEIIKVIGRGAFGEVAVVKMKNTERIYAMKILNKWEMLKRAETACFREERnVLVNGDCQWITTLHYAFQDENYLYLVMDY 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLAN-HGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG-NFFKSGELLATW 176
Cdd:cd05624  154 YVGGDLLTLLSKfEDKLPEDMARFYIGEMVLAIHSIHQLHYVHRDIKPDNVLLDMNGHIRLADFGSClKMNDDGTVQSSV 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 C-GSPPYAAPEVFE----GQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVL--EGRFRIPYFM---SEDCEH 246
Cdd:cd05624  234 AvGTPDYISPEILQamedGMGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhEERFQFPSHVtdvSEEAKD 313
                        250       260
                 ....*....|....*....|...
gi 929654453 247 LIRRmLVLDPSKRLTIAQIKEHK 269
Cdd:cd05624  314 LIQR-LICSRERRLGQNGIEDFK 335
STKc_IKK_beta cd14038
Catalytic domain of the Serine/Threonine kinase, Inhibitor of Nuclear Factor-KappaB Kinase ...
26-285 2.52e-25

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: 106.97  E-value: 2.52e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVME------TKSMLYLVTEYA 99
Cdd:cd14038    2 LGTGGFGNVLRWINQETGEQVAIKQC-RQELSPKNRERWCLEIQIMKRLNHPNVVAARDVPEglqklaPNDLPLLAMEYC 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYL---ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFFKSGELL 173
Cdd:cd14038   81 QGGDLRKYLnqfENCCGLREGAILTLLSDISSALRYLHENRIIHRDLKPENIVLqqgEQRLIHKIIDLGYAKELDQGSLC 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLV 253
Cdd:cd14038  161 TSFVGTLQYLAPELLEQQKYT-VTVDYWSFGTLAFECITGFRPFLPNWQPVQWHGKVRQKSNEDIVVYEDLTGAVKFSSV 239
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 929654453 254 L-DPSKRLTIAQIKEHKW---MLIEVPVQRPVLYPQ 285
Cdd:cd14038  240 LpTPNNLNGILAGKLERWlqcMLMWHPRQRGTDPPQ 275
STKc_PCTAIRE2 cd07872
Catalytic domain of the Serine/Threonine Kinase, PCTAIRE-2 kinase; STKs catalyze the transfer ...
26-252 2.59e-25

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: 107.39  E-value: 2.59e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIyREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAkNGEIF 105
Cdd:cd07872   14 LGEGTYATVFKGRSKLTENLVALKEIRLEHEEGAPCTAI-REVSLLKDLKHANIVTLHDIVHTDKSLTLVFEYL-DKDLK 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKF-WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK------SGELLATWcg 178
Cdd:cd07872   92 QYMDDCGNIMSMHNVKIFlYQILRGLAYCHRRKVLHRDLKPQNLLINERGELKLADFGLARAKSvptktySNEVVTLW-- 169
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 929654453 179 sppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLpilrqrvlegrfripyfmsEDCEHLIRRML 252
Cdd:cd07872  170 ---YRPPDVLLGSSEYSTQIDMWGVGCIFFEMASGRPLFPGSTV-------------------EDELHLIFRLL 221
PTKc_Ack_like cd05040
Catalytic domain of the Protein Tyrosine Kinase, Activated Cdc42-associated kinase; PTKs ...
26-267 3.30e-25

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: 105.89  E-value: 3.30e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRI---TKTEVAIKIIDKSQLDAVN-LEKIYREVQIMKMLDHPHIIKLYQVMETKSMLyLVTEYAKN 101
Cdd:cd05040    3 LGDGSFGVVRRGEWTTpsgKVIQVAVKCLKSDVLSQPNaMDDFLKEVNAMHSLDHPNLIRLYGVVLSSPLM-MVTELAPL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYL-ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE--------- 171
Cdd:cd05040   82 GSLLDRLrKDQGHFLISTLCDYAVQIANGMAYLESKRFIHRDLAARNILLASKDKVKIGDFGLMRALPQNEdhyvmqehr 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 -LLATWCgsppyaAPEVFEGQQYEGPQlDIWSMGVVLY-VLVCGALPFDGPT-LPILRQRVLEG-RFRIPYFMSEDCEHL 247
Cdd:cd05040  162 kVPFAWC------APESLKTRKFSHAS-DVWMFGVTLWeMFTYGEEPWLGLNgSQILEKIDKEGeRLERPDDCPQDIYNV 234
                        250       260
                 ....*....|....*....|
gi 929654453 248 IRRMLVLDPSKRLTIAQIKE 267
Cdd:cd05040  235 MLQCWAHKPADRPTFVALRD 254
STKc_MEKK2 cd06652
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
26-253 3.61e-25

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: 105.90  E-value: 3.61e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIdksQLDAVNLEK------IYREVQIMKMLDHPHIIKLYQVME--TKSMLYLVTE 97
Cdd:cd06652   10 LGQGAFGRVYLCYDADTGRELAVKQV---QFDPESPETskevnaLECEIQLLKNLLHERIVQYYGCLRdpQERTLSIFME 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK----SGELL 173
Cdd:cd06652   87 YMPGGSIKDQLKSYGALTENVTRKYTRQILEGVHYLHSNMIVHRDIKGANILRDSVGNVKLGDFGASKRLQticlSGTGM 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALP---FDG----------PTLPILrqrvlegrfriPYFM 240
Cdd:cd06652  167 KSVTGTPYWMSPEVISGEGY-GRKADIWSVGCTVVEMLTEKPPwaeFEAmaaifkiatqPTNPQL-----------PAHV 234
                        250
                 ....*....|...
gi 929654453 241 SEDCEHLIRRMLV 253
Cdd:cd06652  235 SDHCRDFLKRIFV 247
STKc_Nek9 cd08221
Catalytic domain of the Protein Serine/Threonine Kinase, Never In Mitosis gene A (NIMA) ...
14-265 4.78e-25

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: 105.20  E-value: 4.78e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  14 PVRVgfydiegtLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLY 93
Cdd:cd08221    4 PVRV--------LGRGAFGEAVLYRKTEDNSLVVWKEVNLSRLSEKERRDALNEIDILSLLNHDNIITYYNHFLDGESLF 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKNGEIFDYLANHGR--LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE 171
Cdd:cd08221   76 IEMEYCNGGNLHDKIAQQKNqlFPEEVVLWYLYQIVSAVSHIHKAGILHRDIKTLNIFLTKADLVKLGDFGISKVLDSES 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 LLATWC-GSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFR-IPYFMSEDCEHLIR 249
Cdd:cd08221  156 SMAESIvGTPYYMSPELVQGVKYN-FKSDIWAVGCVLYELLTLKRTFDATNPLRLAVKIVQGEYEdIDEQYSEEIIQLVH 234
                        250
                 ....*....|....*.
gi 929654453 250 RMLVLDPSKRLTIAQI 265
Cdd:cd08221  235 DCLHQDPEDRPTAEEL 250
STKc_STK10 cd06644
Catalytic domain of the Serine/Threonine Kinase, STK10 (also called Lymphocyte-Oriented Kinase ...
9-271 7.42e-25

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: 105.88  E-value: 7.42e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   9 HLQRGPVRVGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDavNLEKIYREVQIMKMLDHPHIIKLYQVMET 88
Cdd:cd06644    3 HVRRDLDPNEVWEIIGELGDGAFGKVYKAKNKETGALAAAKVIETKSEE--ELEDYMVEIEILATCNHPYIVKLLGAFYW 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  89 KSMLYLVTEYAKNGEIFDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNF 166
Cdd:cd06644   81 DGKLWIMIEFCPGGAVDAIMLELDRgLTEPQIQVICRQMLEALQYLHSMKIIHRDLKAGNVLLTLDGDIKLADFGVsAKN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 167 FKSGELLATWCGSPPYAAPEVFEGQQY-EGP---QLDIWSMGVVLYVLVcgalPFDGPTLPILRQRVLegrFRI------ 236
Cdd:cd06644  161 VKTLQRRDSFIGTPYWMAPEVVMCETMkDTPydyKADIWSLGITLIEMA----QIEPPHHELNPMRVL---LKIaksepp 233
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 929654453 237 ----PYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd06644  234 tlsqPSKWSMEFRDFLKTALDKHPETRPSAAQLLEHPFV 272
PTKc_Fes cd05084
Catalytic domain of the Protein Tyrosine Kinase, Fes; PTKs catalyze the transfer of the ...
26-267 7.74e-25

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: 104.63  E-value: 7.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd05084    4 IGRGNFGEVFSGRLRADNTPVAVKSC-RETLPPDLKAKFLQEARILKQYSHPNIVRLIGVCTQKQPIYIVMELVQGGDFL 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLAT--------- 175
Cdd:cd05084   83 TFLRTEGpRLKVKELIRMVENAAAGMEYLESKHCIHRDLAARNCLVTEKNVLKISDFGMSREEEDGVYAATggmkqipvk 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WcgsppyAAPEVFEGQQYEGpQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEG-RFRIPYFMSEDCEHLIRRMLV 253
Cdd:cd05084  163 W------TAPEALNYGRYSS-ESDVWSFGILLWeTFSLGAVPYANLSNQQTREAVEQGvRLPCPENCPDEVYRLMEQCWE 235
                        250
                 ....*....|....
gi 929654453 254 LDPSKRLTIAQIKE 267
Cdd:cd05084  236 YDPRKRPSFSTVHQ 249
PTKc_Fes_like cd05041
Catalytic domain of Fes-like Protein Tyrosine Kinases; Protein Tyrosine Kinase (PTK) family; ...
26-267 1.29e-24

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: 104.06  E-value: 1.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd05041    3 IGRGNFGDVYRGVLKPDNTEVAVKTC-RETLPPDLKRKFLQEARILKQYDHPNIVKLIGVCVQKQPIMIVMELVPGGSLL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE-LLATWCGSPP-- 181
Cdd:cd05041   82 TFLRKKGaRLTVKQLLQMCLDAAAGMEYLESKNCIHRDLAARNCLVGENNVLKISDFGMSREEEDGEyTVSDGLKQIPik 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVFEGQQYEGpQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEGrFRIPyfMSEDCEHLIRRMLVL----DP 256
Cdd:cd05041  162 WTAPEALNYGRYTS-ESDVWSFGILLWeIFSLGATPYPGMSNQQTREQIESG-YRMP--APELCPEAVYRLMLQcwayDP 237
                        250
                 ....*....|.
gi 929654453 257 SKRLTIAQIKE 267
Cdd:cd05041  238 ENRPSFSEIYN 248
STKc_MASTL cd05610
Catalytic domain of the Serine/Threonine Kinase, Microtubule-associated serine/threonine-like ...
26-268 1.35e-24

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: 106.50  E-value: 1.35e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNL-EKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05610   12 ISRGAFGKVYLGRKKNNSKLYAVKVVKKADMINKNMvHQVQAERDALALSKSPFIVHLYYSLQSANNVYLVMEYLIGGDV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG-------------------- 164
Cdd:cd05610   92 KSLLHIYGYFDEEMAVKYISEVALALDYLHRHGIIHRDLKPDNMLISNEGHIKLTDFGLSkvtlnrelnmmdilttpsma 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 165 -----NFFKSGELL-----------------------------ATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVL 210
Cdd:cd05610  172 kpkndYSRTPGQVLslisslgfntptpyrtpksvrrgaarvegERILGTPDYLAPELLLGKPH-GPAVDWWALGVCLFEF 250
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929654453 211 VCGALPFDGPTLPILRQRVLEGRFRIP---YFMSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd05610  251 LTGIPPFNDETPQQVFQNILNRDIPWPegeEELSVNAQNAIEILLTMDPTKRAGLKELKQH 311
PTKc_Itk cd05112
Catalytic domain of the Protein Tyrosine Kinase, Interleukin-2-inducible T-cell Kinase; PTKs ...
26-218 1.63e-24

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: 103.88  E-value: 1.63e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGrHRITKTEVAIKIIDKSqldAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd05112   12 IGSGQFGLVHLG-YWLNKDKVAIKTIREG---AMSEEDFIEEAEVMMKLSHPKLVQLYGVCLEQAPICLVFEFMEHGCLS 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYL-ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPP--Y 182
Cdd:cd05112   88 DYLrTQRGLFSAETLLGMCLDVCEGMAYLEEASVIHRDLAARNCLVGENQVVKVSDFGMTRFVLDDQYTSSTGTKFPvkW 167
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 929654453 183 AAPEVFEGQQYEGPQlDIWSMGVVLY-VLVCGALPFD 218
Cdd:cd05112  168 SSPEVFSFSRYSSKS-DVWSFGVLMWeVFSEGKIPYE 203
STKc_PAK5 cd06658
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 5; STKs catalyze the ...
26-276 1.82e-24

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: 104.74  E-value: 1.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDavNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06658   30 IGEGSTGIVCIATEKHTGKQVAVKKMDLRKQQ--RRELLFNEVVIMRDYHHENVVDMYNSYLVGDELWVVMEFLEGGALT 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DyLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGSPPYAA 184
Cdd:cd06658  108 D-IVTHTRMNEEQIATVCLSVLRALSYLHNQGVIHRDIKSDSILLTSDGRIKLSDFGFcAQVSKEVPKRKSLVGTPYWMA 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 185 PEVFEGQQYeGPQLDIWSMGVVLYVLVCGALP-FDGPTLPILR--QRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLT 261
Cdd:cd06658  187 PEVISRLPY-GTEVDIWSLGIMVIEMIDGEPPyFNEPPLQAMRriRDNLPPRVKDSHKVSSVLRGFLDLMLVREPSQRAT 265
                        250
                 ....*....|....*
gi 929654453 262 IAQIKEHKWMLIEVP 276
Cdd:cd06658  266 AQELLQHPFLKLAGP 280
STKc_GRK4 cd05631
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 4; STKs ...
26-268 2.38e-24

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: 103.92  E-value: 2.38e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKI-YREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05631    8 LGKGGFGEVCACQVRATGKMYACKKLEKKRIKKRKGEAMaLNEKRILEKVNSRFVVSLAYAYETKDALCLVLTIMNGGDL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPY 182
Cdd:cd05631   88 KFHIYNMGNPGFDEQRAIFYaaELCCGLEDLQRERIVYRDLKPENILLDDRGHIRISDLGLAVQIPEGETVRGRVGTVGY 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYE-GPqlDIWSMGVVLYVLVCGALPFDGPTLPILR----QRVLEGRFRIPYFMSEDCEHLIRRMLVLDPS 257
Cdd:cd05631  168 MAPEVINNEKYTfSP--DWWGLGCLIYEMIQGQSPFRKRKERVKReevdRRVKEDQEEYSEKFSEDAKSICRMLLTKNPK 245
                        250
                 ....*....|....*.
gi 929654453 258 KRLTI-----AQIKEH 268
Cdd:cd05631  246 ERLGCrgngaAGVKQH 261
PK_TRB cd13976
Pseudokinase domain of Tribbles Homolog proteins; The pseudokinase domain shows similarity to ...
42-271 2.48e-24

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: 102.89  E-value: 2.48e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  42 TKTEVAIKIIDKSQLDAVnLEKIYRevqimkMLDHPHIIKLYQVMETKSMLYLVTEYAkNGEIFDYLANHGRLNESEARR 121
Cdd:cd13976   17 TGEELVCKVVPVPECHAV-LRAYFR------LPSHPNISGVHEVIAGETKAYVFFERD-HGDLHSYVRSRKRLREPEAAR 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 122 KFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATW--CGSPPYAAPEVFE-GQQYEGPQ 197
Cdd:cd13976   89 LFRQIASAVAHCHRNGIVLRDLKLRKFVFADEERTKLRLESLeDAVILEGEDDSLSdkHGCPAYVSPEILNsGATYSGKA 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 929654453 198 LDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd13976  169 ADVWSLGVILYTMLVGRYPFHDSEPASLFAKIRRGQFAIPETLSPRARCLIRSLLRREPSERLTAEDILLHPWL 242
PK_eIF2AK_GCN2_rpt1 cd14012
Pseudokinase domain, repeat 1, of eukaryotic translation Initiation Factor 2-Alpha Kinase 4 or ...
60-269 3.69e-24

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: 102.82  E-value: 3.69e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  60 NLEKiyrEVQIMKMLDHPHIIKLYQVMETKSM------LYLVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYC 133
Cdd:cd14012   44 LLEK---ELESLKKLRHPNLVSYLAFSIERRGrsdgwkVYLLTEYAPGGSLSELLDSVGSVPLDTARRWTLQLLEALEYL 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 134 HGRKIVHRDLKAENLLLDNNM---NIKIADFGFGNffksgeLLATWCG--------SPPYAAPEVFEGQQYEGPQLDIWS 202
Cdd:cd14012  121 HRNGVVHKSLHAGNVLLDRDAgtgIVKLTDYSLGK------TLLDMCSrgsldefkQTYWLPPELAQGSKSPTRKTDVWD 194
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 929654453 203 MGVVLYVLVCGALPFDGPTLPILrqrvlegrFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHK 269
Cdd:cd14012  195 LGLLFLQMLFGLDVLEKYTSPNP--------VLVSLDLSASLQDFLSKCLSLDPKKRPTALELLPHE 253
STKc_Nek10 cd08528
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
20-265 4.30e-24

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: 102.97  E-value: 4.30e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFA-VVKLGRHRITKTEVAIKIIDKSQLDAVNLEK--------IYREVQIMK-MLDHPHIIKLYQVMETK 89
Cdd:cd08528    2 YAVLELLGSGAFGcVYKVRKKSNGQTLLALKEINMTNPAFGRTEQerdksvgdIISEVNIIKeQLRHPNIVRYYKTFLEN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  90 SMLYLVTEY---AKNGEIFDYLA-NHGRLNESEARRKFWQILSAVDYCHG-RKIVHRDLKAENLLLDNNMNIKIADFGFG 164
Cdd:cd08528   82 DRLYIVMELiegAPLGEHFSSLKeKNEHFTEDRIWNIFVQMVLALRYLHKeKQIVHRDLKPNNIMLGEDDKVTITDFGLA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 165 NFFKSGEL-LATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGRFR-IPYFM-S 241
Cdd:cd08528  162 KQKGPESSkMTSVVGTILYSCPEIVQNEPY-GEKADIWALGCILYQMCTLQPPFYSTNMLTLATKIVEAEYEpLPEGMyS 240
                        250       260
                 ....*....|....*....|....
gi 929654453 242 EDCEHLIRRMLVLDPSKRLTIAQI 265
Cdd:cd08528  241 DDITFVIRSCLTPDPEARPDIVEV 264
STKc_CDK8_like cd07842
Catalytic domain of Cyclin-Dependent protein Kinase 8-like Serine/Threonine Kinases; STKs ...
19-270 4.68e-24

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: 103.90  E-value: 4.68e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNF-----AVVKLGRhriTKTEVAIKII--DKSQLDAVNLEKIyREVQIMKMLDHPHIIKLYQVM---ET 88
Cdd:cd07842    1 KYEIEGCIGRGTYgrvykAKRKNGK---DGKEYAIKKFkgDKEQYTGISQSAC-REIALLRELKHENVVSLVEVFlehAD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  89 KSmLYLVTEYAKN--GEIFDYLANHGR--LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL--DNNMN--IKIAD 160
Cdd:cd07842   77 KS-VYLLFDYAEHdlWQIIKFHRQAKRvsIPPSMVKSLLWQILNGIHYLHSNWVLHRDLKPANILVmgEGPERgvVKIGD 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 161 FGFGNFFKSgELLATWCGSPP-----YAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG---------------- 219
Cdd:cd07842  156 LGLARLFNA-PLKPLADLDPVvvtiwYRAPELLLGARHYTKAIDIWAIGCIFAELLTLEPIFKGreakikksnpfqrdql 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 220 ---------PT---------LPILRQ------------RVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHK 269
Cdd:cd07842  235 erifevlgtPTekdwpdikkMPEYDTlksdtkastypnSLLAKWMHKHKKPDSQGFDLLRKLLEYDPTKRITAEEALEHP 314

                 .
gi 929654453 270 W 270
Cdd:cd07842  315 Y 315
PTKc_EphR cd05033
Catalytic domain of Ephrin Receptor Protein Tyrosine Kinases; PTKs catalyze the transfer of ...
22-265 5.27e-24

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: 102.45  E-value: 5.27e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  22 IEGTLGKGNFAVVKLGRHRITKTE---VAIKII-----DKSQLDavnlekIYREVQIMKMLDHPHIIKLYQVMETKSMLY 93
Cdd:cd05033    8 IEKVIGGGEFGEVCSGSLKLPGKKeidVAIKTLksgysDKQRLD------FLTEASIMGQFDHPNVIRLEGVVTKSRPVM 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKNGEIFDYLANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE- 171
Cdd:cd05033   82 IVTEYMENGSLDKFLRENdGKFTVTQLVGMLRGIASGMKYLSEMNYVHRDLAARNILVNSDLVCKVSDFGLSRRLEDSEa 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 LLATWCGSPP--YAAPEVFEGQQYEgPQLDIWSMGVVLY-VLVCGALPFDGPTlpilRQRVL---EGRFRIPYFMseDCE 245
Cdd:cd05033  162 TYTTKGGKIPirWTAPEAIAYRKFT-SASDVWSFGIVMWeVMSYGERPYWDMS----NQDVIkavEDGYRLPPPM--DCP 234
                        250       260
                 ....*....|....*....|....
gi 929654453 246 HLIRRMLV----LDPSKRLTIAQI 265
Cdd:cd05033  235 SALYQLMLdcwqKDRNERPTFSQI 258
STKc_PAK4 cd06657
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 4; STKs catalyze the ...
26-271 5.76e-24

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: 103.18  E-value: 5.76e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDavNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06657   28 IGEGSTGIVCIATVKSSGKLVAVKKMDLRKQQ--RRELLFNEVVIMRDYQHENVVEMYNSYLVGDELWVVMEFLEGGALT 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DyLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGSPPYAA 184
Cdd:cd06657  106 D-IVTHTRMNEEQIAAVCLAVLKALSVLHAQGVIHRDIKSDSILLTHDGRVKLSDFGFcAQVSKEVPRRKSLVGTPYWMA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 185 PEVFEGQQYeGPQLDIWSMGVVLYVLVCGALP-FDGPTLPILR--QRVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLT 261
Cdd:cd06657  185 PELISRLPY-GPEVDIWSLGIMVIEMVDGEPPyFNEPPLKAMKmiRDNLPPKLKNLHKVSPSLKGFLDRLLVRDPAQRAT 263
                        250
                 ....*....|
gi 929654453 262 IAQIKEHKWM 271
Cdd:cd06657  264 AAELLKHPFL 273
STKc_Unc-89_rpt2 cd14112
Catalytic kinase domain, second repeat, of the Giant Serine/Threonine Kinase Uncoordinated ...
20-271 6.47e-24

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: 102.22  E-value: 6.47e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTE--VAIKIIDKSQldavNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTE 97
Cdd:cd14112    5 FSFGSEIFRGRFSVIVKAVDSTTETDahCAVKIFEVSD----EASEAVREFESLRTLQHENVQRLIAAFKPSNFAYLVME 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKnGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDN--NMNIKIADFGFGNFFkSGELLAT 175
Cdd:cd14112   81 KLQ-EDVFTRFSSNDYYSEEQVATTVRQILDALHYLHFKGIAHLDVQPDNIMFQSvrSWQVKLVDFGRAQKV-SKLGKVP 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 WCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPF--DGPTLPILRQRVLEGRFR---IPYFMSEDCEHLIRR 250
Cdd:cd14112  159 VDGDTDWASPEFHNPETPITVQSDIWGLGVLTFCLLSGFHPFtsEYDDEEETKENVIFVKCRpnlIFVEATQEALRFATW 238
                        250       260
                 ....*....|....*....|.
gi 929654453 251 MLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14112  239 ALKKSPTRRMRTDEALEHRWL 259
PLN00034 PLN00034
mitogen-activated protein kinase kinase; Provisional
26-280 7.86e-24

mitogen-activated protein kinase kinase; Provisional


Pssm-ID: 215036 [Multi-domain]  Cd Length: 353  Bit Score: 104.14  E-value: 7.86e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVnLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:PLN00034  82 IGSGAGGTVYKVIHRPTGRLYALKVIYGNHEDTV-RRQICREIEILRDVNHPNVVKCHDMFDHNGEIQVLLEFMDGGSLE 160
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARrkfwQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFF-KSGELLATWCGSPPYAA 184
Cdd:PLN00034 161 GTHIADEQFLADVAR----QILSGIAYLHRRHIVHRDIKPSNLLINSAKNVKIADFGVSRILaQTMDPCNSSVGTIAYMS 236
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 185 PEVFEGQ----QYEGPQLDIWSMGVVLYVLVCGALPF----DGPTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLDP 256
Cdd:PLN00034 237 PERINTDlnhgAYDGYAGDIWSLGVSILEFYLGRFPFgvgrQGDWASLMCAICMSQPPEAPATASREFRHFISCCLQREP 316
                        250       260
                 ....*....|....*....|....
gi 929654453 257 SKRLTIAQIKEHKWMLIEVPVQRP 280
Cdd:PLN00034 317 AKRWSAMQLLQHPFILRAQPGQGQ 340
STKc_MRCK_alpha cd05623
Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 ...
20-252 9.59e-24

Catalytic domain of the Serine/Threonine Kinase, DMPK-related cell division control protein 42 binding kinase (MRCK) alpha; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MRCK-alpha is expressed ubiquitously in many tissues. It plays a role in the regulation of peripheral actin reorganization and neurite outgrowth. It may also play a role in the transferrin iron uptake pathway. MRCK is activated via interaction with the small GTPase Cdc42. MRCK/Cdc42 signaling mediates myosin-dependent cell motility. The MRCK-alpha subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase. This alignment model includes the dimerization domain.


Pssm-ID: 270773 [Multi-domain]  Cd Length: 409  Bit Score: 105.10  E-value: 9.59e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQ-IMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd05623   74 FEILKVIGRGAFGEVAVVKLKNADKVFAMKILNKWEMLKRAETACFREERdVLVNGDSQWITTLHYAFQDDNNLYLVMDY 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLAN-HGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG-NFFKSGELLATW 176
Cdd:cd05623  154 YVGGDLLTLLSKfEDRLPEDMARFYLAEMVLAIDSVHQLHYVHRDIKPDNILMDMNGHIRLADFGSClKLMEDGTVQSSV 233
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 C-GSPPYAAPEVFE----GQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVL--EGRFRIPYFM---SEDCEH 246
Cdd:cd05623  234 AvGTPDYISPEILQamedGKGKYGPECDWWSLGVCMYEMLYGETPFYAESLVETYGKIMnhKERFQFPTQVtdvSENAKD 313

                 ....*.
gi 929654453 247 LIRRML 252
Cdd:cd05623  314 LIRRLI 319
STKc_p38 cd07851
Catalytic domain of the Serine/Threonine Kinase, p38 Mitogen-Activated Protein Kinase; STKs ...
14-271 1.42e-23

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: 103.14  E-value: 1.42e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  14 PVRvgfYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQV------ME 87
Cdd:cd07851   14 PDR---YQNLSPVGSGAYGQVCSAFDTKTGRKVAIKKLSRPFQSAIHAKRTYRELRLLKHMKHENVIGLLDVftpassLE 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  88 TKSMLYLVTEYAknGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNff 167
Cdd:cd07851   91 DFQDVYLVTHLM--GADLNNIVKCQKLSDDHIQFLVYQILRGLKYIHSAGIIHRDLKPSNLAVNEDCELKILDFGLAR-- 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 168 KSGELLATWCGSPPYAAPEV-FEGQQYEgpQL-DIWSMGVVLYVLVCGALPFDG----------------PT-------- 221
Cdd:cd07851  167 HTDDEMTGYVATRWYRAPEImLNWMHYN--QTvDIWSVGCIMAELLTGKTLFPGsdhidqlkrimnlvgtPDeellkkis 244
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 222 ----------LPILRQRVLEGRFRipyFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd07851  245 sesarnyiqsLPQMPKKDFKEVFS---GANPLAIDLLEKMLVLDPDKRITAAEALAHPYL 301
STKc_myosinIII_N_like cd06608
N-terminal Catalytic domain of Class III myosin-like Serine/Threonine Kinases; STKs catalyze ...
17-271 1.68e-23

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: 101.22  E-value: 1.68e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  17 VGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDksqLDAVNLEKIYREVQIMKML-DHPHIIKLYQVMETKS----- 90
Cdd:cd06608    5 AGIFELVEVIGEGTYGKVYKARHKKTGQLAAIKIMD---IIEDEEEEIKLEINILRKFsNHPNIATFYGAFIKKDppggd 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  91 -MLYLVTEYAKNGEIFDyLANhGRLNESEARRKFW------QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF 163
Cdd:cd06608   82 dQLWLVMEYCGGGSVTD-LVK-GLRKKGKRLKEEWiayilrETLRGLAYLHENKVIHRDIKGQNILLTEEAEVKLVDFGV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 164 gnffkSGELLA------TWCGSPPYAAPEVFEGQQYEGP----QLDIWSMGVVLYVLVCGALPF-DGPTLPILRQ--RVL 230
Cdd:cd06608  160 -----SAQLDStlgrrnTFIGTPYWMAPEVIACDQQPDAsydaRCDVWSLGITAIELADGKPPLcDMHPMRALFKipRNP 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 929654453 231 EGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd06608  235 PPTLKSPEKWSKEFNDFISECLIKNYEQRPFTEELLEHPFI 275
PTKc_Csk_like cd05039
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
25-267 1.83e-23

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: 100.50  E-value: 1.83e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLGRHRITKteVAIKIIdKSQLDAVNleKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05039   13 LIGKGEFGDVMLGDYRGQK--VAVKCL-KDDSTAAQ--AFLAEASVMTTLRHPNLVQLLGVVLEGNGLYIVTEYMAKGSL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGR-LNESEARRKF-WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNF----FKSGELLATWcg 178
Cdd:cd05039   88 VDYLRSRGRaVITRKDQLGFaLDVCEGMEYLESKKFVHRDLAARNVLVSEDNVAKVSDFGLAKEassnQDGGKLPIKW-- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 sppyAAPEVFEGQQYEGpQLDIWSMGVVLY-VLVCGALPFdgPTLPI--LRQRVLEGrfripYFMS--EDCE----HLIR 249
Cdd:cd05039  166 ----TAPEALREKKFST-KSDVWSFGILLWeIYSFGRVPY--PRIPLkdVVPHVEKG-----YRMEapEGCPpevyKVMK 233
                        250
                 ....*....|....*...
gi 929654453 250 RMLVLDPSKRLTIAQIKE 267
Cdd:cd05039  234 NCWELDPAKRPTFKQLRE 251
PTKc_Wee1_fungi cd14052
Catalytic domain of the Protein Tyrosine Kinases, Fungal Wee1 proteins; PTKs catalyze the ...
20-268 2.18e-23

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: 100.96  E-value: 2.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEV-AIKIIDKSQLDAVNLEKIYREVQIMKMLD---HPHIIKLYQVMETKSMLYLV 95
Cdd:cd14052    2 FANVELIGSGEFSQVYKVSERVPTGKVyAVKKLKPNYAGAKDRLRRLEEVSILRELTldgHDNIVQLIDSWEYHGHLYIQ 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLANHGRLNESEARRkFWQIL----SAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGfgnffksge 171
Cdd:cd14052   82 TELCENGSLDVFLSELGLLGRLDEFR-VWKILvelsLGLRFIHDHHFVHLDLKPANVLITFEGTLKIGDFG--------- 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 lLATWCGSP---------PYAAPEVFEGQQYEGPQlDIWSMGVVLY------VLVCGALPF---------DGPTLPILR- 226
Cdd:cd14052  152 -MATVWPLIrgieregdrEYIAPEILSEHMYDKPA-DIFSLGLILLeaaanvVLPDNGDAWqklrsgdlsDAPRLSSTDl 229
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 929654453 227 -QRVLEGRFRIPYFM-----SEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14052  230 hSASSPSSNPPPDPPnmpilSGSLDRVVRWMLSPEPDRRPTADDVLAT 277
STKc_MAP3K12_13 cd14059
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase Kinase ...
26-217 2.21e-23

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: 99.88  E-value: 2.21e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRitKTEVAIKII-DKSQLDAVNLEKiyrevqimkmLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd14059    1 LGSGAQGAVFLGKFR--GEEVAVKKVrDEKETDIKHLRK----------LNHPNIIKFKGVCTQAPCYCILMEYCPYGQL 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLanHGRLNESEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPY 182
Cdd:cd14059   69 YEVL--RAGREITPSLLVDWskQIASGMNYLHLHKIIHRDLKSPNVLVTYNDVLKISDFGTSKELSEKSTKMSFAGTVAW 146
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 929654453 183 AAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPF 217
Cdd:cd14059  147 MAPEVIRNEPCS-EKVDIWSFGVVLWELLTGEIPY 180
STKc_TGFbR_I cd14056
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta family Type ...
24-266 2.27e-23

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: 101.19  E-value: 2.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  24 GTLGKGNFAVVKLGRHRitKTEVAIKIIDKSQLDAVNLE-KIYREVqimkMLDHPHIIKlYQVMETKSM-----LYLVTE 97
Cdd:cd14056    1 KTIGKGRYGEVWLGKYR--GEKVAVKIFSSRDEDSWFREtEIYQTV----MLRHENILG-FIAADIKSTgswtqLWLITE 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHgRLNESEARRKFWQILSAVDYCH----GRK----IVHRDLKAENLLLDNNMNIKIADFGFGNFFKS 169
Cdd:cd14056   74 YHEHGSLYDYLQRN-TLDTEEALRLAYSAASGLAHLHteivGTQgkpaIAHRDLKSKNILVKRDGTCCIADLGLAVRYDS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 170 G-----ELLATWCGSPPYAAPEVFEGQ-------QYEgpQLDIWSMGVVLY-VL---VCG------ALPFDG-----PTL 222
Cdd:cd14056  153 DtntidIPPNPRVGTKRYMAPEVLDDSinpksfeSFK--MADIYSFGLVLWeIArrcEIGgiaeeyQLPYFGmvpsdPSF 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 929654453 223 PILRQRVLEGRFRIPY--------FMSEDCEhLIRRMLVLDPSKRLTIAQIK 266
Cdd:cd14056  231 EEMRKVVCVEKLRPPIpnrwksdpVLRSMVK-LMQECWSENPHARLTALRVK 281
STKc_Nek6 cd08228
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
20-225 2.37e-23

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: 100.87  E-value: 2.37e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd08228    4 FQIEKKIGRGQFSEVYRATCLLDRKPVALKKVQIFEMmDAKARQDCVKEIDLLKQLNHPNVIKYLDSFIEDNELNIVLEL 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEI---FDYLANHGRL-NESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA 174
Cdd:cd08228   84 ADAGDLsqmIKYFKKQKRLiPERTVWKYFVQLCSAVEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAA 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 929654453 175 -TWCGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPFDGPTLPIL 225
Cdd:cd08228  164 hSLVGTPYYMSPERIHENGYNFKS-DIWSLGCLLYEMAALQSPFYGDKMNLF 214
PKc_PBS2_like cd06622
Catalytic domain of fungal PBS2-like dual-specificity Mitogen-Activated Protein Kinase Kinases; ...
24-272 2.85e-23

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: 101.08  E-value: 2.85e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  24 GTLGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG- 102
Cdd:cd06622    7 DELGKGNYGSVYKVLHRPTGVTMAMKEI-RLELDESKFNQIIMELDILHKAVSPYIVDFYGAFFIEGAVYMCMEYMDAGs 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 --EIFDYLANHGRLNESEARRkfwqILSAVdyCHGRK-------IVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSgeL 172
Cdd:cd06622   86 ldKLYAGGVATEGIPEDVLRR----ITYAV--VKGLKflkeehnIIHRDVKPTNVLVNGNGQVKLCDFGVsGNLVAS--L 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 LATWCGSPPYAAPEVFEGqqyEGP--------QLDIWSMGVVLYVLVCGALPFDGPTLP-ILRQ--RVLEGR-FRIPYFM 240
Cdd:cd06622  158 AKTNIGCQSYMAPERIKS---GGPnqnptytvQSDVWSLGLSILEMALGRYPYPPETYAnIFAQlsAIVDGDpPTLPSGY 234
                        250       260       270
                 ....*....|....*....|....*....|..
gi 929654453 241 SEDCEHLIRRMLVLDPSKRLTIAQIKEHKWML 272
Cdd:cd06622  235 SDDAQDFVAKCLNKIPNRRPTYAQLLEHPWLV 266
STKc_CDK5 cd07839
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 5; STKs ...
20-270 3.13e-23

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: 100.59  E-value: 3.13e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKiidKSQLDAVNlEKI----YREVQIMKMLDHPHIIKLYQVMETKSMLYLV 95
Cdd:cd07839    2 YEKLEKIGEGTYGTVFKAKNRETHEIVALK---RVRLDDDD-EGVpssaLREICLLKELKHKNIVRLYDVLHSDKKLTLV 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNG--EIFDYLanHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK----- 168
Cdd:cd07839   78 FEYCDQDlkKYFDSC--NGDIDPEIVKSFMFQLLKGLAFCHSHNVLHRDLKPQNLLINKNGELKLADFGLARAFGipvrc 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 -SGELLATWcgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPF------------------------------ 217
Cdd:cd07839  156 ySAEVVTLW-----YRPPDVLFGAKLYSTSIDMWSAGCIFAELANAGRPLfpgndvddqlkrifrllgtpteeswpgvsk 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 929654453 218 --DGPTLPILRQRVLEGRFrIPYFMSEDCEhLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07839  231 lpDYKPYPMYPATTSLVNV-VPKLNSTGRD-LLQNLLVCNPVQRISAEEALQHPY 283
STKc_SPEG_rpt1 cd14108
Catalytic kinase domain, first repeat, of Giant Serine/Threonine Kinase Striated muscle ...
19-270 3.18e-23

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: 99.98  E-value: 3.18e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIID---KSQLDAVnlekiyREVQIMKMLDHPHIIKLYQVMETKSMLYLV 95
Cdd:cd14108    3 YYDIHKEIGRGAFSYLRRVKEKSSDLSFAAKFIPvraKKKTSAR------RELALLAELDHKSIVRFHDAFEKRRVVIIV 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDyLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL--DNNMNIKIADFGFGNFFKSGELL 173
Cdd:cd14108   77 TELCHEELLER-ITKRPTVCESEVRSYMRQLLEGIEYLHQNDVLHLDLKPENLLMadQKTDQVRICDFGNAQELTPNEPQ 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPPYAAPEVFEgQQYEGPQLDIWSMGVVLYVLVCGALPF----DGPTLPILRQRVLEGRFRIPYFMSEDCEHLIR 249
Cdd:cd14108  156 YCKYGTPEFVAPEIVN-QSPVSKVTDIWPVGVIAYLCLTGISPFvgenDRTTLMNIRNYNVAFEESMFKDLCREAKGFII 234
                        250       260
                 ....*....|....*....|.
gi 929654453 250 RMLVLDpSKRLTIAQIKEHKW 270
Cdd:cd14108  235 KVLVSD-RLRPDAEETLEHPW 254
PK_TRB3 cd14024
Pseudokinase domain of Tribbles Homolog 3; The pseudokinase domain shows similarity to protein ...
72-271 4.17e-23

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


Pssm-ID: 270926 [Multi-domain]  Cd Length: 242  Bit Score: 99.18  E-value: 4.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  72 KMLDHPHIIKLYQVMETKSMLYLVTEyAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD 151
Cdd:cd14024   40 RLGPHEGVCSVLEVVIGQDRAYAFFS-RHYGDMHSHVRRRRRLSEDEARGLFTQMARAVAHCHQHGVILRDLKLRRFVFT 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 152 NNMNIKIADFGFGNFF---KSGELLATWCGSPPYAAPEVF-EGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQ 227
Cdd:cd14024  119 DELRTKLVLVNLEDSCplnGDDDSLTDKHGCPAYVGPEILsSRRSYSGKAADVWSLGVCLYTMLLGRYPFQDTEPAALFA 198
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 929654453 228 RVLEGRFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14024  199 KIRRGAFSLPAWLSPGARCLVSCMLRRSPAERLKASEILLHPWL 242
PTKc_Csk cd05082
Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the ...
25-267 4.99e-23

Catalytic domain of the Protein Tyrosine Kinase, C-terminal Src kinase; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk catalyzes the tyr phosphorylation of the regulatory C-terminal tail of Src kinases, resulting in their inactivation. Csk is expressed in a wide variety of tissues. As a negative regulator of Src, Csk plays a role in cell proliferation, survival, and differentiation, and consequently, in cancer development and progression. Csk is a cytoplasmic (or nonreceptor) PTK containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. To inhibit Src kinases, Csk is translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. In addition, Csk also shows Src-independent functions. It is a critical component in G-protein signaling, and plays a role in cytoskeletal reorganization and cell migration. The Csk 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: 133213 [Multi-domain]  Cd Length: 256  Bit Score: 99.29  E-value: 4.99e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLGRHRITKteVAIKIIDKsqlDAVnLEKIYREVQIMKMLDHPHIIKLYQVM-ETKSMLYLVTEYAKNGE 103
Cdd:cd05082   13 TIGKGEFGDVMLGDYRGNK--VAVKCIKN---DAT-AQAFLAEASVMTQLRHSNLVQLLGVIvEEKGGLYIVTEYMAKGS 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANHGR-LNESEARRKF-WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKS----GELLATWc 177
Cdd:cd05082   87 LVDYLRSRGRsVLGGDCLLKFsLDVCEAMEYLEGNNFVHRDLAARNVLVSEDNVAKVSDFGLTKEASStqdtGKLPVKW- 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 gsppyAAPEVFEGQQYEgPQLDIWSMGVVLY-VLVCGALPFdgPTLPI--LRQRVLEG-RFRIPYFMSEDCEHLIRRMLV 253
Cdd:cd05082  166 -----TAPEALREKKFS-TKSDVWSFGILLWeIYSFGRVPY--PRIPLkdVVPRVEKGyKMDAPDGCPPAVYDVMKNCWH 237
                        250
                 ....*....|....
gi 929654453 254 LDPSKRLTIAQIKE 267
Cdd:cd05082  238 LDAAMRPSFLQLRE 251
PTKc_Lyn cd05072
Catalytic domain of the Protein Tyrosine Kinase, Lyn; PTKs catalyze the transfer of the ...
26-244 6.57e-23

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: 99.73  E-value: 6.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRiTKTEVAIKIIDKSQLdavNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd05072   15 LGAGQFGEVWMGYYN-NSTKVAVKTLKPGTM---SVQAFLEEANLMKTLQHDKLVRLYAVVTKEEPIYIITEYMAKGSLL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANH--GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPP-- 181
Cdd:cd05072   91 DFLKSDegGKVLLPKLIDFSAQIAEGMAYIERKNYIHRDLRAANVLVSESLMCKIADFGLARVIEDNEYTAREGAKFPik 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 929654453 182 YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLPILRQRVLEGrFRIPYFmsEDC 244
Cdd:cd05072  171 WTAPEAINFGSFT-IKSDVWSFGILLYEIVTyGKIPYPGMSNSDVMSALQRG-YRMPRM--ENC 230
PTKc_Lck_Blk cd05067
Catalytic domain of the Protein Tyrosine Kinases, Lymphocyte-specific kinase and Blk; PTKs ...
26-237 7.50e-23

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: 99.19  E-value: 7.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRiTKTEVAIKIIDKSQLDAvnlEKIYREVQIMKMLDHPHIIKLYQVMeTKSMLYLVTEYAKNGEIF 105
Cdd:cd05067   15 LGAGQFGEVWMGYYN-GHTKVAIKSLKQGSMSP---DAFLAEANLMKQLQHQRLVRLYAVV-TQEPIYIITEYMENGSLV 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHG--RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPP-- 181
Cdd:cd05067   90 DFLKTPSgiKLTINKLLDMAAQIAEGMAFIEERNYIHRDLRAANILVSDTLSCKIADFGLARLIEDNEYTAREGAKFPik 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 929654453 182 YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLPILRQRvLEGRFRIP 237
Cdd:cd05067  170 WTAPEAINYGTFT-IKSDVWSFGILLTEIVThGRIPYPGMTNPEVIQN-LERGYRMP 224
STKc_IRE1 cd13982
Catalytic domain of the Serine/Threonine kinase, Inositol-requiring protein 1; STKs catalyze ...
66-268 7.60e-23

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: 99.27  E-value: 7.60e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  66 REVQIMKMLD-HPHIIKLYQVMETKSMLYLVTE--------YAKNGEIFDYLANHGRlnesEARRKFWQILSAVDYCHGR 136
Cdd:cd13982   43 REVQLLRESDeHPNVIRYFCTEKDRQFLYIALElcaaslqdLVESPRESKLFLRPGL----EPVRLLRQIASGLAHLHSL 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 137 KIVHRDLKAENLLLD-----NNMNIKIADFGFGNFFKSGE----LLATWCGSPPYAAPEVFEGQQYEGPQ--LDIWSMG- 204
Cdd:cd13982  119 NIVHRDLKPQNILIStpnahGNVRAMISDFGLCKKLDVGRssfsRRSGVAGTSGWIAPEMLSGSTKRRQTraVDIFSLGc 198
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 205 VVLYVLVCGALPFDGptlPILRQR-VLEGRFRIPYFMSE-----DCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd13982  199 VFYYVLSGGSHPFGD---KLEREAnILKGKYSLDKLLSLgehgpEAQDLIERMIDFDPEKRPSAEEVLNH 265
PTKc_EGFR_like cd05057
Catalytic domain of Epidermal Growth Factor Receptor-like Protein Tyrosine Kinases; PTKs ...
26-265 9.01e-23

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: 99.41  E-value: 9.01e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLG----RHRITKTEVAIKIIDKSQlDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLyLVTEYAKN 101
Cdd:cd05057   15 LGSGAFGTVYKGvwipEGEKVKIPVAIKVLREET-GPKANEEILDEAYVMASVDHPHLVRLLGICLSSQVQ-LITQLMPL 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE--LLATWCG 178
Cdd:cd05057   93 GCLLDYVRNHrDNIGSQLLLNWCVQIAKGMSYLEEKRLVHRDLAARNVLVKTPNHVKITDFGLAKLLDVDEkeYHAEGGK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SP-PYAAPEVFEGQQYEGpQLDIWSMGVVLY-VLVCGALPFDG-PTLPILRQRVLEGRFRIPYFMSEDCEHLIRRMLVLD 255
Cdd:cd05057  173 VPiKWMALESIQYRIYTH-KSDVWSYGVTVWeLMTFGAKPYEGiPAVEIPDLLEKGERLPQPPICTIDVYMVLVKCWMID 251
                        250
                 ....*....|
gi 929654453 256 PSKRLTIAQI 265
Cdd:cd05057  252 AESRPTFKEL 261
STKc_MLTK cd14060
Catalytic domain of the Serine/Threonine Kinase, Mixed lineage kinase-Like mitogen-activated ...
27-265 9.50e-23

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: 98.11  E-value: 9.50e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  27 GKGNFAVVKLGRHRITKTEVAIKiidksqldavNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFD 106
Cdd:cd14060    2 GGGSFGSVYRAIWVSQDKEVAVK----------KLLKIEKEAEILSVLSHRNIIQFYGAILEAPNYGIVTEYASYGSLFD 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 107 YLANhgrlNESEaRRKFWQILS-------AVDYCHGR---KIVHRDLKAENLLLDNNMNIKIADFGFGNFFkSGELLATW 176
Cdd:cd14060   72 YLNS----NESE-EMDMDQIMTwatdiakGMHYLHMEapvKVIHRDLKSRNVVIAADGVLKICDFGASRFH-SHTTHMSL 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 CGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEG--RFRIPYFMSEDCEHLIRRMLVL 254
Cdd:cd14060  146 VGTFPWMAPEVIQSLPVS-ETCDTYSYGVVLWEMLTREVPFKGLEGLQVAWLVVEKneRPTIPSSCPRSFAELMRRCWEA 224
                        250
                 ....*....|.
gi 929654453 255 DPSKRLTIAQI 265
Cdd:cd14060  225 DVKERPSFKQI 235
PKc_LIMK_like cd14065
Catalytic domain of the LIM domain kinase-like protein kinases; PKs catalyze the transfer of ...
26-268 1.20e-22

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: 98.33  E-value: 1.20e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIidksQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14065    1 LGKGFFGEVYKVTHRETGKVMVMKE----LKRFDEQRSFLKEVKLMRRLSHPNILRFIGVCVKDNKLNFITEYVNGGTLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFG--------NFFKSGELL 173
Cdd:cd14065   77 ELLKSMDeQLPWSQRVSLAKDIASGMAYLHSKNIIHRDLNSKNCLVreaNRGRNAVVADFGLArempdektKKPDRKKRL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATwCGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVcGALPFDGPTLPilrqRVLEGRFRIPYFMS---EDCE----H 246
Cdd:cd14065  157 TV-VGSPYWMAPEMLRGESYDE-KVDVFSFGIVLCEII-GRVPADPDYLP----RTMDFGLDVRAFRTlyvPDCPpsflP 229
                        250       260
                 ....*....|....*....|..
gi 929654453 247 LIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14065  230 LAIRCCQLDPEKRPSFVELEHH 251
PTKc_Tec_Rlk cd05114
Catalytic domain of the Protein Tyrosine Kinases, Tyrosine kinase expressed in hepatocellular ...
26-218 1.22e-22

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: 98.40  E-value: 1.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRiTKTEVAIKIIDKSqldAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd05114   12 LGSGLFGVVRLGKWR-AQYKVAIKAIREG---AMSEEDFIEEAKVMMKLTHPKLVQLYGVCTQQKPIYIVTEFMENGCLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYL-ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPP--Y 182
Cdd:cd05114   88 NYLrQRRGKLSRDMLLSMCQDVCEGMEYLERNNFIHRDLAARNCLVNDTGVVKVSDFGMTRYVLDDQYTSSSGAKFPvkW 167
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 929654453 183 AAPEVFEGQQYEGPQlDIWSMGVVLY-VLVCGALPFD 218
Cdd:cd05114  168 SPPEVFNYSKFSSKS-DVWSFGVLMWeVFTEGKMPFE 203
PTKc_RET cd05045
Catalytic domain of the Protein Tyrosine Kinase, REarranged during Transfection protein; PTKs ...
25-274 1.53e-22

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: 98.88  E-value: 1.53e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFA-VVKLGRHRITK----TEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd05045    7 TLGEGEFGkVVKATAFRLKGragyTTVAVKML-KENASSSELRDLLSEFNLLKQVNHPHVIKLYGACSQDGPLLLIVEYA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYL----------------ANHGRLNESEARR-------KF-WQILSAVDYCHGRKIVHRDLKAENLLLDNNMN 155
Cdd:cd05045   86 KYGSLRSFLresrkvgpsylgsdgnRNSSYLDNPDERAltmgdliSFaWQISRGMQYLAEMKLVHRDLAARNVLVAEGRK 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 156 IKIADFGFG-NFFKSGELLATWCGSPP--YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGptlpILRQR--- 228
Cdd:cd05045  166 MKISDFGLSrDVYEEDSYVKRSKGRIPvkWMAIESLFDHIYT-TQSDVWSFGVLLWEIVTlGGNPYPG----IAPERlfn 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 929654453 229 VLEGRFRI--PYFMSEDCEHLIRRMLVLDPSKRLTIAQI-KEHKWMLIE 274
Cdd:cd05045  241 LLKTGYRMerPENCSEEMYNLMLTCWKQEPDKRPTFADIsKELEKMMVK 289
PTKc_FGFR cd05053
Catalytic domain of the Protein Tyrosine Kinases, Fibroblast Growth Factor Receptors; PTKs ...
24-272 1.79e-22

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: 98.64  E-value: 1.79e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  24 GTLGKGNFA-VVK-----LGRHRITKTEVAIKIIDKSQLDAvNLEKIYREVQIMKML-DHPHIIKLYQVMETKSMLYLVT 96
Cdd:cd05053   18 KPLGEGAFGqVVKaeavgLDNKPNEVVTVAVKMLKDDATEK-DLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVVV 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNGEIFDYL---------ANHGRLNESEARRKF-------WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIAD 160
Cdd:cd05053   97 EYASKGNLREFLrarrppgeeASPDDPRVPEEQLTQkdlvsfaYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIAD 176
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 161 FGFG------NFFK---SGELLATWcgsppyAAPEVFEGQQYEgPQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVL 230
Cdd:cd05053  177 FGLArdihhiDYYRkttNGRLPVKW------MAPEALFDRVYT-HQSDVWSFGVLLWeIFTLGGSPYPGIPVEELFKLLK 249
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 929654453 231 EG-RFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEH-KWML 272
Cdd:cd05053  250 EGhRMEKPQNCTQELYMLMRDCWHEVPSQRPTFKQLVEDlDRIL 293
STKc_PFTAIRE1 cd07869
Catalytic domain of the Serine/Threonine Kinase, PFTAIRE-1 kinase; STKs catalyze the transfer ...
26-219 1.80e-22

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: 99.00  E-value: 1.80e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIyREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNgEIF 105
Cdd:cd07869   13 LGEGSYATVYKGKSKVNGKLVALKVIRLQEEEGTPFTAI-REASLLKGLKHANIVLLHDIIHTKETLTLVFEYVHT-DLC 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG------NFFKSGELLATWcg 178
Cdd:cd07869   91 QYMDKHpGGLHPENVKLFLFQLLRGLSYIHQRYILHRDLKPQNLLISDTGELKLADFGLAraksvpSHTYSNEVVTLW-- 168
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 929654453 179 sppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG 219
Cdd:cd07869  169 ---YRPPDVLLGSTEYSTCLDMWGVGCIFVEMIQGVAAFPG 206
STKc_myosinIIIA_N cd06638
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIA myosin; STKs catalyze ...
20-271 3.14e-22

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: 97.77  E-value: 3.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDK-SQLDavnlEKIYREVQIMKML-DHPHIIKLYQVMETKSM-----L 92
Cdd:cd06638   20 WEIIETIGKGTYGKVFKVLNKKNGSKAAVKILDPiHDID----EEIEAEYNILKALsDHPNVVKFYGMYYKKDVkngdqL 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  93 YLVTEYAKNGEIFD----YLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK 168
Cdd:cd06638   96 WLVLELCNGGSVTDlvkgFLKRGERMEEPIIAYILHEALMGLQHLHVNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLT 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 SGELLA-TWCGSPPYAAPEVFEGQQ-----YEGpQLDIWSMGVVLYVLVCGalpfDGPTLPILRQRVLegrFRIPY---- 238
Cdd:cd06638  176 STRLRRnTSVGTPFWMAPEVIACEQqldstYDA-RCDVWSLGITAIELGDG----DPPLADLHPMRAL---FKIPRnppp 247
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 929654453 239 ------FMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd06638  248 tlhqpeLWSNEFNDFIRKCLTKDYEKRPTVSDLLQHVFI 286
PTKc_Fer cd05085
Catalytic domain of the Protein Tyrosine Kinase, Fer; Protein Tyrosine Kinase (PTK) family; ...
26-267 4.08e-22

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: 96.61  E-value: 4.08e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRiTKTEVAIKIIDKSQLDAVNLeKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd05085    4 LGKGNFGEVYKGTLK-DKTPVAVKTCKEDLPQELKI-KFLSEARILKQYDHPNIVKLIGVCTQRQPIYIVMELVPGGDFL 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLanhgRLNESEARRKfwQIL-------SAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCG 178
Cdd:cd05085   82 SFL----RKKKDELKTK--QLVkfsldaaAGMAYLESKNCIHRDLAARNCLVGENNALKISDFGMSRQEDDGVYSSSGLK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPP--YAAPEVFEGQQYEGpQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEG-RFRIPYFMSEDCEHLIRRMLVL 254
Cdd:cd05085  156 QIPikWTAPEALNYGRYSS-ESDVWSFGILLWeTFSLGVCPYPGMTNQQAREQVEKGyRMSAPQRCPEDIYKIMQRCWDY 234
                        250
                 ....*....|...
gi 929654453 255 DPSKRLTIAQIKE 267
Cdd:cd05085  235 NPENRPKFSELQK 247
STKc_YSK4 cd06631
Catalytic domain of the Serine/Threonine Kinase, Yeast Sps1/Ste20-related Kinase 4; STKs ...
26-271 5.86e-22

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: 96.74  E-value: 5.86e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGrhrITKTE--VAIKIIDKSQLDAVNLEKIY----REVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd06631    9 LGKGAYGTVYCG---LTSTGqlIAVKQVELDTSDKEKAEKEYeklqEEVDLLKTLKHVNIVGYLGTCLEDNVVSIFMEFV 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG-------FGNFFKSGEL 172
Cdd:cd06631   86 PGGSIASILARFGALEEPVFCRYTKQILEGVAYLHNNNVIHRDIKGNNIMLMPNGVIKLIDFGcakrlciNLSSGSQSQL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 LATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPF-DGPTLPIL------RQRVLegrfRIPYFMSEDCE 245
Cdd:cd06631  166 LKSMRGTPYWMAPEVINETGH-GRKSDIWSIGCTVFEMATGKPPWaDMNPMAAIfaigsgRKPVP----RLPDKFSPEAR 240
                        250       260
                 ....*....|....*....|....*.
gi 929654453 246 HLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd06631  241 DFVHACLTRDQDERPSAEQLLKHPFI 266
STKc_EIF2AK3_PERK cd14048
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
26-269 7.07e-22

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: 96.87  E-value: 7.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLY-----------QVMETKSMLYL 94
Cdd:cd14048   14 LGRGGFGVVFEAKNKVDDCNYAVKRIRLPNNELAR-EKVLREVRALAKLDHPGIVRYFnawlerppegwQEKMDEVYLYI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAKNGEIFDYLANHGRLNESE---ARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE 171
Cdd:cd14048   93 QMQLCRKENLKDWMNRRCTMESRElfvCLNIFKQIASAVEYLHSKGLIHRDLKPSNVFFSLDDVVKVGDFGLVTAMDQGE 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 LLATWCGSPP-------------YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVcgaLPFDGPTLPILR-QRVLEGRFRIP 237
Cdd:cd14048  173 PEQTVLTPMPayakhtgqvgtrlYMSPEQIHGNQYS-EKVDIFALGLILFELI---YSFSTQMERIRTlTDVRKLKFPAL 248
                        250       260       270
                 ....*....|....*....|....*....|...
gi 929654453 238 YFMSEDCEH-LIRRMLVLDPSKRLTIAQIKEHK 269
Cdd:cd14048  249 FTNKYPEERdMVQQMLSPSPSERPEAHEVIEHA 281
STKc_CdkB_plant cd07837
Catalytic domain of the Serine/Threonine Kinase, Plant B-type Cyclin-Dependent protein Kinase; ...
26-270 8.37e-22

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: 96.83  E-value: 8.37e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKiidKSQLDaVNLEKI----YREVQIMKMLDH-PHIIKLYQVMET----KSMLYLVT 96
Cdd:cd07837    9 IGEGTYGKVYKARDKNTGKLVALK---KTRLE-MEEEGVpstaLREVSLLQMLSQsIYIVRLLDVEHVeengKPLLYLVF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAkNGEIFDYLANHGR-----LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNI-KIADFGFGNFFK-- 168
Cdd:cd07837   85 EYL-DTDLKKFIDSYGRgphnpLPAKTIQSFMYQLCKGVAHCHSHGVMHRDLKPQNLLVDKQKGLlKIADLGLGRAFTip 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 ----SGELLATWcgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPT-----LPILR------QRVLEGR 233
Cdd:cd07837  164 iksyTHEIVTLW-----YRAPEVLLGSTHYSTPVDMWSVGCIFAEMSRKQPLFPGDSelqqlLHIFRllgtpnEEVWPGV 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 929654453 234 FRI------PYFMSEDCEH-----------LIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07837  239 SKLrdwheyPQWKPQDLSRavpdlepegvdLLTKMLAYDPAKRISAKAALQHPY 292
STKc_CDK10 cd07845
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 10; STKs ...
26-270 8.41e-22

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: 97.05  E-value: 8.41e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKII--DKSQlDAVNLEKIyREVQIMKMLDHPHIIKLYQVMETKSM--LYLVTEYAKN 101
Cdd:cd07845   15 IGEGTYGIVYRARDTTSGEIVALKKVrmDNER-DGIPISSL-REITLLLNLRHPNIVELKEVVVGKHLdsIFLVMEYCEQ 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 gEIFDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGfgnffksgelLATWCGSP 180
Cdd:cd07845   93 -DLASLLDNMPTpFSESQVKCLMLQLLRGLQYLHENFIIHRDLKVSNLLLTDKGCLKIADFG----------LARTYGLP 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 181 P-----------YAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPT-------------------------LPI 224
Cdd:cd07845  162 AkpmtpkvvtlwYRAPELLLGCTTYTTAIDMWAVGCILAELLAHKPLLPGKSeieqldliiqllgtpnesiwpgfsdLPL 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 929654453 225 LRQRVLEGRfriPY--------FMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07845  242 VGKFTLPKQ---PYnnlkhkfpWLSEAGLRLLNFLLMYDPKKRATAEEALESSY 292
UBA_SIK2 cd14409
UBA domain found in salt-inducible kinase 2 (SIK2); SIK2, also called Qin-induced kinase or ...
297-341 9.71e-22

UBA domain found in salt-inducible kinase 2 (SIK2); SIK2, also called Qin-induced kinase or serine/threonine-protein kinase SNF1-like kinase 2 (SNF1LK2), is a serine/threonine kinase highly expressed in adipocytes. It belongs to the AMP-activated protein kinases (AMPK) family involved in the regulation of metabolism during energy stress. It plays an important role in the insulin-signaling pathway during adipocyte differentiation, as well as in autophagy progression. Moreover, SIK2 plays a critical role in neuronal survival and modulates cAMP responsive element binding protein (CREB)-mediated gene expression in response to hormones and nutrients. SIK2 acts as a critical determinant in autophagy progression. In addition, SIK2 localizes at the centrosome and functions as a centrosome kinase required for bipolar mitotic spindle formation. It is involved in the initiation of mitosis, and regulates the localization of the centrosome linker protein, C-Nap1, through S2392 phosphorylation. SIK2 contains an N-terminal protein kinase catalytic domain followed by an ubiquitin-associated (UBA) domain.


Pssm-ID: 270592  Cd Length: 45  Bit Score: 88.92  E-value: 9.71e-22
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 297 NEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAIYFLLVERLKSHR 341
Cdd:cd14409    1 NEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAIYYLLVERLKSHR 45
STKc_PAK_I cd06647
Catalytic domain of the Serine/Threonine Kinase, Group I p21-activated kinase; STKs catalyze ...
26-217 1.21e-21

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: 95.38  E-value: 1.21e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLekIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06647   15 IGQGASGTVYTAIDVATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DyLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGSPPYAA 184
Cdd:cd06647   93 D-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKRSTMVGTPYWMA 171
                        170       180       190
                 ....*....|....*....|....*....|...
gi 929654453 185 PEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPF 217
Cdd:cd06647  172 PEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPY 203
STKc_TAO cd06607
Catalytic domain of the Serine/Threonine Kinases, Thousand-and-One Amino acids proteins; STKs ...
19-205 1.39e-21

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: 95.21  E-value: 1.39e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEgTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVnlEK---IYREVQIMKMLDHPHIIKLYQVMETKSMLYLV 95
Cdd:cd06607    3 FEDLR-EIGHGSFGAVYYARNKRTSEVVAIKKMSYSGKQST--EKwqdIIKEVKFLRQLRHPNTIEYKGCYLREHTAWLV 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKnGEIFDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGfgnffkSGELLA 174
Cdd:cd06607   80 MEYCL-GSASDIVEVHKKpLQEVEIAAICHGALQGLAYLHSHNRIHRDVKAGNILLTEPGTVKLADFG------SASLVC 152
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 929654453 175 ---TWCGSPPYAAPEVF----EGqQYEGpQLDIWSMGV 205
Cdd:cd06607  153 panSFVGTPYWMAPEVIlamdEG-QYDG-KVDVWSLGI 188
STKc_TBK1 cd13988
Catalytic domain of the Serine/Threonine kinase, TANK Binding Kinase 1; STKs catalyze the ...
26-217 1.93e-21

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: 96.41  E-value: 1.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDK-SQLDAVNLEKiyREVQIMKMLDHPHIIKLYQV---METKSMLyLVTEYAKN 101
Cdd:cd13988    1 LGQGATANVFRGRHKKTGDLYAVKVFNNlSFMRPLDVQM--REFEVLKKLNHKNIVKLFAIeeeLTTRHKV-LVMELCPC 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYL---ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL----DNNMNIKIADFGFGNFFKSGELLA 174
Cdd:cd13988   78 GSLYTVLeepSNAYGLPESEFLIVLRDVVAGMNHLRENGIVHRDIKPGNIMRvigeDGQSVYKLTDFGAARELEDDEQFV 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TWCGSPPYAAPEVFE-------GQQYEGPQLDIWSMGVVLYVLVCGALPF 217
Cdd:cd13988  158 SLYGTEEYLHPDMYEravlrkdHQKKYGATVDLWSIGVTFYHAATGSLPF 207
STKc_GAK cd14036
Catalytic domain of the Serine/Threonine protein kinase, cyclin G-Associated Kinase; STKs ...
22-267 2.44e-21

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: 95.27  E-value: 2.44e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  22 IEGTLGKGNFAVVKLGRHRITKTEVAIKiidksQLDAVNLEK---IYREVQIMKMLD-HPHIIKLYQVMET--------K 89
Cdd:cd14036    4 IKRVIAEGGFAFVYEAQDVGTGKEYALK-----RLLSNEEEKnkaIIQEINFMKKLSgHPNIVQFCSAASIgkeesdqgQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  90 SMLYLVTEYAKNG--EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRK--IVHRDLKAENLLLDNNMNIKIADFGfgn 165
Cdd:cd14036   79 AEYLLLTELCKGQlvDFVKKVEAPGPFSPDTVLKIFYQTCRAVQHMHKQSppIIHRDLKIENLLIGNQGQIKLCDFG--- 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 166 ffkSGELLA-----TWCG--------------SPPYAAPEVFEgqQYE----GPQLDIWSMGVVLYVLVCGALPF-DGPT 221
Cdd:cd14036  156 ---SATTEAhypdySWSAqkrslvedeitrntTPMYRTPEMID--LYSnypiGEKQDIWALGCILYLLCFRKHPFeDGAK 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 929654453 222 LpilrqRVLEGRFRIP-----YFMSEDcehLIRRMLVLDPSKRLTIAQIKE 267
Cdd:cd14036  231 L-----RIINAKYTIPpndtqYTVFHD---LIRSTLKVNPEERLSITEIVE 273
PTKc_Syk cd05116
Catalytic domain of the Protein Tyrosine Kinase, Spleen tyrosine kinase; PTKs catalyze the ...
24-208 3.75e-21

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: 93.87  E-value: 3.75e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  24 GTLGKGNFAVVKLGRHRITKTE--VAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLyLVTEYAKN 101
Cdd:cd05116    1 GELGSGNFGTVKKGYYQMKKVVktVAVKILKNEANDPALKDELLREANVMQQLDNPYIVRMIGICEAESWM-LVMEMAEL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE--LLATWCGS 179
Cdd:cd05116   80 GPLNKFLQKNRHVTEKNITELVHQVSMGMKYLEESNFVHRDLAARNVLLVTQHYAKISDFGLSKALRADEnyYKAQTHGK 159
                        170       180       190
                 ....*....|....*....|....*....|.
gi 929654453 180 PP--YAAPEVFEGQQYEGPQlDIWSMGVVLY 208
Cdd:cd05116  160 WPvkWYAPECMNYYKFSSKS-DVWSFGVLMW 189
STKc_MEKK3 cd06651
Catalytic domain of the Serine/Threonine Kinase, Mitogen-Activated Protein (MAP)/Extracellular ...
26-217 4.43e-21

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: 93.99  E-value: 4.43e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIID---KSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKS--MLYLVTEYAK 100
Cdd:cd06651   15 LGQGAFGRVYLCYDVDTGRELAAKQVQfdpESPETSKEVSALECEIQLLKNLQHERIVQYYGCLRDRAekTLTIFMEYMP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK----SGELLATW 176
Cdd:cd06651   95 GGSVKDQLKAYGALTESVTRKYTRQILEGMSYLHSNMIVHRDIKGANILRDSAGNVKLGDFGASKRLQticmSGTGIRSV 174
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 929654453 177 CGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPF 217
Cdd:cd06651  175 TGTPYWMSPEVISGEGY-GRKADVWSLGCTVVEMLTEKPPW 214
STKc_beta_ARK cd05606
Catalytic domain of the Serine/Threonine Kinase, beta-adrenergic receptor kinase; STKs ...
26-270 4.78e-21

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: 94.04  E-value: 4.78e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKML-----DHPHIIKLYQVMETKSMLYLVTEYAK 100
Cdd:cd05606    2 IGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstggDCPFIVCMTYAFQTPDKLCFILDLMN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATwCGSP 180
Cdd:cd05606   82 GGDLHYHLSQHGVFSEAEMRFYAAEVILGLEHMHNRFIVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHAS-VGTH 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 181 PYAAPEVF-EGQQYEGPQlDIWSMGVVLYVLVCGALPFdgptlpilRQ-----------RVLEGRFRIPYFMSEDCEHLI 248
Cdd:cd05606  161 GYMAPEVLqKGVAYDSSA-DWFSLGCMLYKLLKGHSPF--------RQhktkdkheidrMTLTMNVELPDSFSPELKSLL 231
                        250       260
                 ....*....|....*....|....*..
gi 929654453 249 RRMLVLDPSKRL-----TIAQIKEHKW 270
Cdd:cd05606  232 EGLLQRDVSKRLgclgrGATEVKEHPF 258
STKc_Sty1_Hog1 cd07856
Catalytic domain of the Serine/Threonine Kinases, Fungal Mitogen-Activated Protein Kinases ...
26-271 5.96e-21

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: 94.95  E-value: 5.96e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSM-LYLVTEYAknGEI 104
Cdd:cd07856   18 VGMGAFGLVCSARDQLTGQNVAVKKIMKPFSTPVLAKRTYRELKLLKHLRHENIISLSDIFISPLEdIYFVTELL--GTD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGelLATWCGSPPYAA 184
Cdd:cd07856   96 LHRLLTSRPLEKQFIQYFLYQILRGLKYVHSAGVIHRDLKPSNILVNENCDLKICDFGLARIQDPQ--MTGYVSTRYYRA 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 185 PEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG----------------PTLPILRQ----------RVLEGRFRIPY 238
Cdd:cd07856  174 PEIMLTWQKYDVEVDIWSAGCIFAEMLEGKPLFPGkdhvnqfsiitellgtPPDDVINTicsentlrfvQSLPKRERVPF 253
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 929654453 239 ---FMSEDCE--HLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd07856  254 sekFKNADPDaiDLLEKMLVFDPKKRISAAEALAHPYL 291
PTKc_InsR_like cd05032
Catalytic domain of Insulin Receptor-like Protein Tyrosine Kinases; PTKs catalyze the transfer ...
26-265 6.46e-21

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: 93.95  E-value: 6.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLG-RHRI----TKTEVAIKIIDKSQLDAVNLEkIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAK 100
Cdd:cd05032   14 LGQGSFGMVYEGlAKGVvkgePETRVAIKTVNENASMRERIE-FLNEASVMKEFNCHHVVRLLGVVSTGQPTLVVMELMA 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLANHgRLNESEA-------RRKF--W--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG----- 164
Cdd:cd05032   93 KGDLKSYLRSR-RPEAENNpglgpptLQKFiqMaaEIADGMAYLAAKKFVHRDLAARNCMVAEDLTVKIGDFGMTrdiye 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 165 -NFFK---SGELLATWcgsppyAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTlpilRQRVLE-----GRF 234
Cdd:cd05032  172 tDYYRkggKGLLPVRW------MAPESLKDGVFT-TKSDVWSFGVVLWEMATlAEQPYQGLS----NEEVLKfvidgGHL 240
                        250       260       270
                 ....*....|....*....|....*....|.
gi 929654453 235 RIPYFMSEDCEHLIRRMLVLDPSKRLTIAQI 265
Cdd:cd05032  241 DLPENCPDKLLELMRMCWQYNPKMRPTFLEI 271
STKc_NDR_like_fungal cd05629
Catalytic domain of Fungal Nuclear Dbf2-Related kinase-like Serine/Threonine Kinases; STKs ...
26-268 6.85e-21

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: 95.69  E-value: 6.85e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05629    9 IGKGAFGEVRLVQKKDTGKIYAMKTLLKSEMfKKDQLAHVKAERDVLAESDSPWVVSLYYSFQDAQYLYLIMEFLPGGDL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFF----------------- 167
Cdd:cd05629   89 MTMLIKYDTFSEDVTRFYMAECVLAIEAVHKLGFIHRDIKPDNILIDRGGHIKLSDFGLSTGFhkqhdsayyqkllqgks 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 168 --------------------KSGELLATW-----------CGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALP 216
Cdd:cd05629  169 nknridnrnsvavdsinltmSSKDQIATWkknrrlmaystVGTPDYIAPEIFLQQGY-GQECDWWSLGAIMFECLIGWPP 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 217 FDGPTLPILRQRVLEGRFRIpYF-----MSEDCEHLIRRmLVLDPSKRL---TIAQIKEH 268
Cdd:cd05629  248 FCSENSHETYRKIINWRETL-YFpddihLSVEAEDLIRR-LITNAENRLgrgGAHEIKSH 305
PTKc_Src_Fyn_like cd14203
Catalytic domain of a subset of Src kinase-like Protein Tyrosine Kinases; PTKs catalyze the ...
26-261 6.99e-21

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: 93.06  E-value: 6.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITkTEVAIKIIDKSQLDAvnlEKIYREVQIMKMLDHPHIIKLYQVMeTKSMLYLVTEYAKNGEIF 105
Cdd:cd14203    3 LGQGCFGEVWMGTWNGT-TKVAIKTLKPGTMSP---EAFLEEAQIMKKLRHDKLVQLYAVV-SEEPIYIVTEFMSKGSLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLAN-HGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPP-- 181
Cdd:cd14203   78 DFLKDgEGKyLKLPQLVDMAAQIASGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAKFPik 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLPILRQRVLEG-RFRIPYFMSEDCEHLIRRMLVLDPSKR 259
Cdd:cd14203  158 WTAPEAALYGRFT-IKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERGyRMPCPPGCPESLHELMCQCWRKDPEER 236

                 ..
gi 929654453 260 LT 261
Cdd:cd14203  237 PT 238
PK_GC cd13992
Pseudokinase domain of membrane Guanylate Cyclase receptors; The pseudokinase domain shows ...
28-266 1.06e-20

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: 92.84  E-value: 1.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  28 KGNFAVVKLGRHRITKTE-------VAIKIIDKSqldAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAK 100
Cdd:cd13992    3 CGSGASSHTGEPKYVKKVgvyggrtVAIKHITFS---RTEKRTILQELNQLKELVHDNLNKFIGICINPPNIAVVTEYCT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLANHGRLNESEARRKF-WQILSAVDYCHGRKI-VHRDLKAENLLLDNNMNIKIADFGFGNfFKSGELLATWCG 178
Cdd:cd13992   80 RGSLQDVLLNREIKMDWMFKSSFiKDIVKGMNYLHSSSIgYHGRLKSSNCLVDSRWVVKLTDFGLRN-LLEEQTNHQLDE 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPP-----YAAPEVFegQQYEGPQL-----DIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGR---FRIPYFMS---- 241
Cdd:cd13992  159 DAQhkkllWTAPELL--RGSLLEVRgtqkgDVYSFAIILYEILFRSDPFALEREVAIVEKVISGGnkpFRPELAVLldef 236
                        250       260
                 ....*....|....*....|....*.
gi 929654453 242 -EDCEHLIRRMLVLDPSKRLTIAQIK 266
Cdd:cd13992  237 pPRLVLLVKQCWAENPEKRPSFKQIK 262
STKc_p38alpha cd07877
Catalytic domain of the Serine/Threonine Kinase, p38alpha Mitogen-Activated Protein Kinase ...
26-290 1.19e-20

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: 94.34  E-value: 1.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQV------METKSMLYLVTEYA 99
Cdd:cd07877   25 VGSGAYGSVCAAFDTKTGLRVAVKKLSRPFQSIIHAKRTYRELRLLKHMKHENVIGLLDVftparsLEEFNDVYLVTHLM 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 knGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNffKSGELLATWCGS 179
Cdd:cd07877  105 --GADLNNIVKCQKLTDDHVQFLIYQILRGLKYIHSADIIHRDLKPSNLAVNEDCELKILDFGLAR--HTDDEMTGYVAT 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG----------------PTlPILRQRVLEGRFR-----IPY 238
Cdd:cd07877  181 RWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLTGRTLFPGtdhidqlklilrlvgtPG-AELLKKISSESARnyiqsLTQ 259
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 929654453 239 FMSEDCEH-----------LIRRMLVLDPSKRLTIAQIKEHKWML-IEVPVQRPVLYPQEQENE 290
Cdd:cd07877  260 MPKMNFANvfiganplavdLLEKMLVLDSDKRITAAQALAHAYFAqYHDPDDEPVADPYDQSFE 323
PTKc_Zap-70 cd05115
Catalytic domain of the Protein Tyrosine Kinase, Zeta-chain-associated protein of 70kDa; PTKs ...
21-208 1.63e-20

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: 92.32  E-value: 1.63e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  21 DIEgtLGKGNFAVVKLGRHRITKTE--VAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLyLVTEY 98
Cdd:cd05115    9 EVE--LGSGNFGCVKKGVYKMRKKQidVAIKVL-KQGNEKAVRDEMMREAQIMHQLDNPYIVRMIGVCEAEALM-LVMEM 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYL-ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG-------NFFKsg 170
Cdd:cd05115   85 ASGGPLNKFLsGKKDEITVSNVVELMHQVSMGMKYLEEKNFVHRDLAARNVLLVNQHYAKISDFGLSkalgaddSYYK-- 162
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 929654453 171 ellATWCGSPP--YAAPEVFEGQQYEGpQLDIWSMGVVLY 208
Cdd:cd05115  163 ---ARSAGKWPlkWYAPECINFRKFSS-RSDVWSYGVTMW 198
STKc_MLK4 cd14146
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 4; STKs catalyze the ...
26-219 1.72e-20

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: 92.41  E-value: 1.72e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITktEVAIKII--DKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd14146    2 IGVGGFGKVYRATWKGQ--EVAVKAArqDPDEDIKATAESVRQEAKLFSMLRHPNIIKLEGVCLEEPNLCLVMEFARGGT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANHGRLNESEARRKF-------W--QILSAVDYCHGRKIV---HRDLKAENLLL------DN--NMNIKIADFGF 163
Cdd:cd14146   80 LNRALAAANAAPGPRRARRIpphilvnWavQIARGMLYLHEEAVVpilHRDLKSSNILLlekiehDDicNKTLKITDFGL 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 929654453 164 GNFFKSGELLATwCGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPFDG 219
Cdd:cd14146  160 AREWHRTTKMSA-AGTYAWMAPEVIKSSLFSKGS-DIWSYGVLLWELLTGEVPYRG 213
STKc_LRRK2 cd14068
Catalytic domain of the Serine/Threonine Kinase, Leucine-Rich Repeat Kinase 2; STKs catalyze ...
26-267 2.13e-20

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: 91.55  E-value: 2.13e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRitKTEVAIKIIDKSqldaVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLylVTEYAKNGEIf 105
Cdd:cd14068    2 LGDGGFGSVYRAVYR--GEDVAVKIFNKH----TSFRLLRQELVVLSHLHHPSLVALLAAGTAPRML--VMELAPKGSL- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANH--GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL-----DNNMNIKIADFGFGNFFKSGELlATWCG 178
Cdd:cd14068   73 DALLQQdnASLTRTLQHRIALHVADGLRYLHSAMIIYRDLKPHNVLLftlypNCAIIAKIADYGIAQYCCRMGI-KTSEG 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYEGPQLDIWSMGVVLY-VLVCGALPFDGPTLPI-LRQRVLEGRFRIPyFMSEDC------EHLIRR 250
Cdd:cd14068  152 TPGFRAPEVARGNVIYNQQADVYSFGLLLYdILTCGERIVEGLKFPNeFDELAIQGKLPDP-VKEYGCapwpgvEALIKD 230
                        250
                 ....*....|....*..
gi 929654453 251 MLVLDPSKRLTIAQIKE 267
Cdd:cd14068  231 CLKENPQCRPTSAQVFD 247
PTZ00024 PTZ00024
cyclin-dependent protein kinase; Provisional
26-270 2.30e-20

cyclin-dependent protein kinase; Provisional


Pssm-ID: 240233 [Multi-domain]  Cd Length: 335  Bit Score: 93.29  E-value: 2.30e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIK---IIDKSQLDAVNLEKI---------YREVQIMKMLDHPHIIKLYQVMETKSMLY 93
Cdd:PTZ00024  17 LGEGTYGKVEKAYDTLTGKIVAIKkvkIIEISNDVTKDRQLVgmcgihfttLRELKIMNEIKHENIMGLVDVYVEGDFIN 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAkNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGfgnffksgelL 173
Cdd:PTZ00024  97 LVMDIM-ASDLKKVVDRKIRLTESQVKCILLQILNGLNVLHKWYFMHRDLSPANIFINSKGICKIADFG----------L 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 ATWCGSPP-------------------------YAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG--------- 219
Cdd:PTZ00024 166 ARRYGYPPysdtlskdetmqrreemtskvvtlwYRAPELLMGAEKYHFAVDMWSVGCIFAELLTGKPLFPGeneidqlgr 245
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 929654453 220 -------PT---------LPILRQ------RVLEGRFRIPyfmSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:PTZ00024 246 ifellgtPNednwpqakkLPLYTEftprkpKDLKTIFPNA---SDDAIDLLQSLLKLNPLERISAKEALKHEY 315
STKc_LIMK2 cd14222
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the ...
26-244 2.91e-20

Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. LIMK2 activation is induced by transforming growth factor-beta l (TGFb-l) and shares the same subcellular location as the cofilin family member twinfilin, which may be its biological substrate. LIMK2 plays a role in spermatogenesis, and may contribute to tumor progression and metastasis formation in some cancer cells. 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 LIMK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271124 [Multi-domain]  Cd Length: 272  Bit Score: 91.93  E-value: 2.91e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKiiDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14222    1 LGKGFFGQAIKVTHKATGKVMVMK--ELIRCDEETQKTFLTEVKVMRSLDHPNVLKFIGVLYKDKRLNLLTEFIEGGTLK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA----------- 174
Cdd:cd14222   79 DFLRADDPFPWQQKVSFAKGIASGMAYLHSMSIIHRDLNSHNCLIKLDKTVVVADFGLSRLIVEEKKKPppdkpttkkrt 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 ----------TWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVcGALPFDGPTLPILRQRVLEGRFRIPYFMSEDC 244
Cdd:cd14222  159 lrkndrkkryTVVGNPYWMAPEMLNGKSYD-EKVDIFSFGIVLCEII-GQVYADPDCLPRTLDFGLNVRLFWEKFVPKDC 236
STKc_p38beta cd07878
Catalytic domain of the Serine/Threonine Kinase, p38beta Mitogen-Activated Protein Kinase ...
26-298 3.07e-20

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: 93.19  E-value: 3.07e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQV------METKSMLYLVTEYA 99
Cdd:cd07878   23 VGSGAYGSVCSAYDTRLRQKVAVKKLSRPFQSLIHARRTYRELRLLKHMKHENVIGLLDVftpatsIENFNEVYLVTNLM 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 knGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNffKSGELLATWCGS 179
Cdd:cd07878  103 --GADLNNIVKCQKLSDEHVQFLIYQLLRGLKYIHSAGIIHRDLKPSNVAVNEDCELRILDFGLAR--QADDEMTGYVAT 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG----------------PT------------------LPIL 225
Cdd:cd07878  179 RWYRAPEIMLNWMHYNQTVDIWSVGCIMAELLKGKALFPGndyidqlkrimevvgtPSpevlkkisseharkyiqsLPHM 258
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 929654453 226 RQRVLEGRFRIPYFMSEDcehLIRRMLVLDPSKRLTIAQIKEHKWML-IEVPVQRP--VLYPQEQEN-EPSIGEFNE 298
Cdd:cd07878  259 PQQDLKKIFRGANPLAID---LLEKMLVLDSDKRISASEALAHPYFSqYHDPEDEPeaEPYDESPENkERTIEEWKE 332
STKc_TEY_MAPK cd07858
Catalytic domain of the Serine/Threonine Kinases, Plant TEY Mitogen-Activated Protein Kinases; ...
26-271 3.64e-20

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: 92.82  E-value: 3.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSM-----LYLVTEYAk 100
Cdd:cd07858   13 IGRGAYGIVCSAKNSETNEKVAIKKIANAFDNRIDAKRTLREIKLLRHLDHENVIAIKDIMPPPHReafndVYIVYELM- 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-------GNFFKsgELL 173
Cdd:cd07858   92 DTDLHQIIRSSQTLSDDHCQYFLYQLLRGLKYIHSANVLHRDLKPSNLLLNANCDLKICDFGLarttsekGDFMT--EYV 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 174 AT-WcgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGP-------------------------------- 220
Cdd:cd07858  170 VTrW-----YRAPELLLNCSEYTTAIDVWSVGCIFAELLGRKPLFPGKdyvhqlklitellgspseedlgfirnekarry 244
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 929654453 221 --TLPILRQRVLEGRFriPYfMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd07858  245 irSLPYTPRQSFARLF--PH-ANPLAIDLLEKMLVFDPSKRITVEEALAHPYL 294
STKc_Nek7 cd08229
Catalytic domain of the Serine/Threonine Kinase, Never In Mitosis gene A (NIMA)-related kinase ...
20-219 4.21e-20

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: 91.63  E-value: 4.21e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQL-DAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd08229   26 FRIEKKIGRGQFSEVYRATCLLDGVPVALKKVQIFDLmDAKARADCIKEIDLLKQLNHPNVIKYYASFIEDNELNIVLEL 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFW----QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA 174
Cdd:cd08229  106 ADAGDLSRMIKHFKKQKRLIPEKTVWkyfvQLCSALEHMHSRRVMHRDIKPANVFITATGVVKLGDLGLGRFFSSKTTAA 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 929654453 175 -TWCGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPFDG 219
Cdd:cd08229  186 hSLVGTPYYMSPERIHENGYNFKS-DIWSLGCLLYEMAALQSPFYG 230
STKc_myosinIIIB_N cd06639
N-terminal Catalytic domain of the Serine/Threonine Kinase, Class IIIB myosin; STKs catalyze ...
20-271 5.18e-20

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: 91.59  E-value: 5.18e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDK-SQLDavnlEKIYREVQIMKML-DHPHIIKLYQvMETKS------M 91
Cdd:cd06639   24 WDIIETIGKGTYGKVYKVTNKKDGSLAAVKILDPiSDVD----EEIEAEYNILRSLpNHPNVVKFYG-MFYKAdqyvggQ 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  92 LYLVTEYAKNGEIFDY----LANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFF 167
Cdd:cd06639   99 LWLVLELCNGGSVTELvkglLKCGQRLDEAMISYILYGALLGLQHLHNNRIIHRDVKGNNILLTTEGGVKLVDFGVSAQL 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 168 KSGELLA-TWCGSPPYAAPEVFE-GQQYE---GPQLDIWSMGVVLYVLVcgalpfDGPTlPILRQRVLEGRFRIPYFMS- 241
Cdd:cd06639  179 TSARLRRnTSVGTPFWMAPEVIAcEQQYDysyDARCDVWSLGITAIELA------DGDP-PLFDMHPVKALFKIPRNPPp 251
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 929654453 242 ---------EDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd06639  252 tllnpekwcRGFSHFISQCLIKDFEKRPSVTHLLEHPFI 290
STKc_p38gamma cd07880
Catalytic domain of the Serine/Threonine Kinase, p38gamma Mitogen-Activated Protein Kinase ...
26-270 5.57e-20

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: 92.32  E-value: 5.57e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSML------YLVTEYA 99
Cdd:cd07880   23 VGSGAYGTVCSALDRRTGAKVAIKKLYRPFQSELFAKRAYRELRLLKHMKHENVIGLLDVFTPDLSLdrfhdfYLVMPFM 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 knGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKS---GELLATW 176
Cdd:cd07880  103 --GTDLGKLMKHEKLSEDRIQFLVYQMLKGLKYIHAAGIIHRDLKPGNLAVNEDCELKILDFGLARQTDSemtGYVVTRW 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 cgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG----------------PT------------------L 222
Cdd:cd07880  181 -----YRAPEVILNWMHYTQTVDIWSVGCIMAEMLTGKPLFKGhdhldqlmeimkvtgtPSkefvqklqsedaknyvkkL 255
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 929654453 223 PILRQRVLegRFRIPYfMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07880  256 PRFRKKDF--RSLLPN-ANPLAVNVLEKMLVLDAESRITAAEALAHPY 300
PKc_CLK cd14134
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases; Dual-specificity ...
20-270 6.44e-20

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: 91.86  E-value: 6.44e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDksqldavNLEKiYR-----EVQIMKML------DHPHIIKLYQVMET 88
Cdd:cd14134   14 YKILRLLGEGTFGKVLECWDRKRKRYVAVKIIR-------NVEK-YReaakiEIDVLETLaekdpnGKSHCVQLRDWFDY 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  89 KSMLYLVTE-YAKNgeIFDYL-ANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDN------------- 152
Cdd:cd14134   86 RGHMCIVFElLGPS--LYDFLkKNNyGPFPLEHVQHIAKQLLEAVAFLHDLKLTHTDLKPENILLVDsdyvkvynpkkkr 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 153 ------NMNIKIADFG---FGNFFKSgELLATwcgsPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPFD----- 218
Cdd:cd14134  164 qirvpkSTDIKLIDFGsatFDDEYHS-SIVST----RHYRAPEVILGLGWSYPC-DVWSIGCILVELYTGELLFQthdnl 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 219 ----------GPtLP--ILRQRVLEGRF--------------------------RIPYFMSEDCEH-----LIRRMLVLD 255
Cdd:cd14134  238 ehlammerilGP-LPkrMIRRAKKGAKYfyfyhgrldwpegsssgrsikrvckpLKRLMLLVDPEHrllfdLIRKMLEYD 316
                        330
                 ....*....|....*
gi 929654453 256 PSKRLTIAQIKEHKW 270
Cdd:cd14134  317 PSKRITAKEALKHPF 331
STKc_GRK3 cd05633
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 3; STKs ...
20-312 6.60e-20

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: 92.43  E-value: 6.60e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKML----DHPHIIKLYQVMETKSMLYLV 95
Cdd:cd05633    7 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMTYAFHTPDKLCFI 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLAT 175
Cdd:cd05633   87 LDLMNGGDLHYHLSQHGVFSEKEMRFYATEIILGLEHMHNRFVVYRDLKPANILLDEHGHVRISDLGLACDFSKKKPHAS 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 wCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPI---LRQRVLEGRFRIPYFMSEDCEHLIRRML 252
Cdd:cd05633  167 -VGTHGYMAPEVLQKGTAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDkheIDRMTLTVNVELPDSFSPELKSLLEGLL 245
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 929654453 253 VLDPSKRLTI-----AQIKEHK------WMLIEVPVQRPVLYPQEQENEPS----IGEFNEQVLRLMHSLGIDQQ 312
Cdd:cd05633  246 QRDVSKRLGChgrgaQEVKEHSffkgidWQQVYLQKYPPPLIPPRGEVNAAdafdIGSFDEEDTKGIKLLDSDQE 320
STKc_PAK2 cd06655
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 2; STKs catalyze the ...
26-277 6.84e-20

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: 91.32  E-value: 6.84e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLekIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06655   27 IGQGASGTVFTAIDVATGQEVAIKQINLQKQPKKEL--IINEILVMKELKNPNIVNFLDSFLVGDELFVVMEYLAGGSLT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DyLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGSPPYAA 184
Cdd:cd06655  105 D-VVTETCMDEAQIAAVCRECLQALEFLHANQVIHRDIKSDNVLLGMDGSVKLTDFGFcAQITPEQSKRSTMVGTPYWMA 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 185 PEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFdgptlpiLRQRVLEGRFRI----------PYFMSEDCEHLIRRMLVL 254
Cdd:cd06655  184 PEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPY-------LNENPLRALYLIatngtpelqnPEKLSPIFRDFLNRCLEM 255
                        250       260
                 ....*....|....*....|...
gi 929654453 255 DPSKRLTIAQIKEHKWMLIEVPV 277
Cdd:cd06655  256 DVEKRGSAKELLQHPFLKLAKPL 278
PTKc_Jak1_rpt2 cd05079
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 1; PTKs catalyze the ...
26-261 7.37e-20

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: 90.76  E-value: 7.37e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRI----TKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETK--SMLYLVTEYA 99
Cdd:cd05079   12 LGEGHFGKVELCRYDPegdnTGEQVAVKSL-KPESGGNHIADLKKEIEILRNLYHENIVKYKGICTEDggNGIKLIMEFL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLA-NHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATW-- 176
Cdd:cd05079   91 PSGSLKEYLPrNKNKINLKQQLKYAVQICKGMDYLGSRQYVHRDLAARNVLVESEHQVKIGDFGLTKAIETDKEYYTVkd 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 -CGSPPY-AAPE-VFEGQQYEGPqlDIWSMGVVLYVLV--CGA--------LPFDGPT---LPILRQ-RVLE--GRFRIP 237
Cdd:cd05079  171 dLDSPVFwYAPEcLIQSKFYIAS--DVWSFGVTLYELLtyCDSesspmtlfLKMIGPThgqMTVTRLvRVLEegKRLPRP 248
                        250       260
                 ....*....|....*....|....
gi 929654453 238 YFMSEDCEHLIRRMLVLDPSKRLT 261
Cdd:cd05079  249 PNCPEEVYQLMRKCWEFQPSKRTT 272
STKc_LIMK cd14154
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase; STKs catalyze the transfer ...
26-207 7.80e-20

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: 90.64  E-value: 7.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKsqLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14154    1 LGKGFFGQAIKVTHRETGEVMVMKELIR--FDEEAQRNFLKEVKVMRSLDHPNVLKFIGVLYKDKKLNLITEYIPGGTLK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQ-ILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-----------GNFFKSGELL 173
Cdd:cd14154   79 DVLKDMARPLPWAQRVRFAKdIASGMAYLHSMNIIHRDLNSHNCLVREDKTVVVADFGLarliveerlpsGNMSPSETLR 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 929654453 174 A----------TWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVL 207
Cdd:cd14154  159 HlkspdrkkryTVVGNPYWMAPEMLNGRSYD-EKVDIFSFGIVL 201
STKc_PAK1 cd06654
Catalytic domain of the Serine/Threonine Kinase, p21-activated kinase 1; STKs catalyze the ...
26-277 8.81e-20

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: 90.94  E-value: 8.81e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLekIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06654   28 IGQGASGTVYTAMDVATGQEVAIRQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DyLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGSPPYAA 184
Cdd:cd06654  106 D-VVTETCMDEGQIAAVCRECLQALEFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKRSTMVGTPYWMA 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 185 PEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFdgptlpiLRQRVLEGRFRI----------PYFMSEDCEHLIRRMLVL 254
Cdd:cd06654  185 PEVVTRKAY-GPKVDIWSLGIMAIEMIEGEPPY-------LNENPLRALYLIatngtpelqnPEKLSAIFRDFLNRCLEM 256
                        250       260
                 ....*....|....*....|...
gi 929654453 255 DPSKRLTIAQIKEHKWMLIEVPV 277
Cdd:cd06654  257 DVEKRGSAKELLQHQFLKIAKPL 279
PKc_MKK3_6 cd06617
Catalytic domain of the dual-specificity Protein Kinases, Mitogen-activated protein Kinase ...
24-271 9.74e-20

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: 90.56  E-value: 9.74e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  24 GTLGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKIYREVQI-MKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd06617    7 EELGRGAYGVVDKMRHVPTGTIMAVKRI-RATVNSQEQKRLLMDLDIsMRSVDCPYTVTFYGALFREGDVWICMEVMDTS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 --EIFDYLANHGRLNESEARRKF-WQILSAVDYCHGR-KIVHRDLKAENLLLDNNMNIKIADFGFgnffkSGELLATW-- 176
Cdd:cd06617   86 ldKFYKKVYDKGLTIPEDILGKIaVSIVKALEYLHSKlSVIHRDVKPSNVLINRNGQVKLCDFGI-----SGYLVDSVak 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 ---CGSPPYAAPEVFEG----QQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPI--LRQRVLEGRFRIPY--FmSEDCE 245
Cdd:cd06617  161 tidAGCKPYMAPERINPelnqKGYD-VKSDVWSLGITMIELATGRFPYDSWKTPFqqLKQVVEEPSPQLPAekF-SPEFQ 238
                        250       260
                 ....*....|....*....|....*.
gi 929654453 246 HLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd06617  239 DFVNKCLKKNYKERPNYPELLQHPFF 264
STKc_PAK3 cd06656
Catalytic domain of the Protein Serine/Threonine Kinase, p21-activated kinase 3; Serine ...
26-277 1.06e-19

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: 90.55  E-value: 1.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLekIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06656   27 IGQGASGTVYTAIDIATGQEVAIKQMNLQQQPKKEL--IINEILVMRENKNPNIVNYLDSYLVGDELWVVMEYLAGGSLT 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DyLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF-GNFFKSGELLATWCGSPPYAA 184
Cdd:cd06656  105 D-VVTETCMDEGQIAAVCRECLQALDFLHSNQVIHRDIKSDNILLGMDGSVKLTDFGFcAQITPEQSKRSTMVGTPYWMA 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 185 PEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFdgptlpiLRQRVLEGRFRI----------PYFMSEDCEHLIRRMLVL 254
Cdd:cd06656  184 PEVVTRKAY-GPKVDIWSLGIMAIEMVEGEPPY-------LNENPLRALYLIatngtpelqnPERLSAVFRDFLNRCLEM 255
                        250       260
                 ....*....|....*....|...
gi 929654453 255 DPSKRLTIAQIKEHKWMLIEVPV 277
Cdd:cd06656  256 DVDRRGSAKELLQHPFLKLAKPL 278
STKc_WNK4 cd14033
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 4; STKs catalyze ...
20-270 1.23e-19

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: 89.68  E-value: 1.23e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEgtLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLY----QVMETKSMLYLV 95
Cdd:cd14033    5 FNIE--IGRGSFKTVYRGLDTETTVEVAWCELQTRKLSKGERQRFSEEVEMLKGLQHPNIVRFYdswkSTVRGHKCIILV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGR--KIVHRDLKAENLLLDN-NMNIKIADFGFGNfFKSGEL 172
Cdd:cd14033   83 TELMTSGTLKTYLKRFREMKLKLLQRWSRQILKGLHFLHSRcpPILHRDLKCDNIFITGpTGSVKIGDLGLAT-LKRASF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 LATWCGSPPYAAPEVFEGQQYEGpqLDIWSMGVVLYVLVCGALPF-DGPTLPILRQRVLEGR-------FRIPYfMSEDC 244
Cdd:cd14033  162 AKSVIGTPEFMAPEMYEEKYDEA--VDVYAFGMCILEMATSEYPYsECQNAAQIYRKVTSGIkpdsfykVKVPE-LKEII 238
                        250       260
                 ....*....|....*....|....*.
gi 929654453 245 EHLIRrmlvLDPSKRLTIAQIKEHKW 270
Cdd:cd14033  239 EGCIR----TDKDERFTIQDLLEHRF 260
STKc_NDR2 cd05627
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze ...
26-268 1.91e-19

Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. NDR2 (also called STK38-like) plays a role in proper centrosome duplication. In addition, it is involved in regulating neuronal growth and differentiation, as well as in facilitating neurite outgrowth. NDR2 is also implicated in fear conditioning as it contributes to the coupling of neuronal morphological changes with fear-memory consolidation. NDR kinase contains an N-terminal regulatory (NTR) domain and an insert within the catalytic domain that contains an auto-inhibitory sequence. Like many other AGC kinases, NDR kinase requires phosphorylation at two sites, the activation loop (A-loop) and the hydrophobic motif (HM), for activity. The NDR2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270776 [Multi-domain]  Cd Length: 366  Bit Score: 91.27  E-value: 1.91e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQ-LDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05627   10 IGRGAFGEVRLVQKKDTGHIYAMKILRKADmLEKEQVAHIRAERDILVEADGAWVVKMFYSFQDKRNLYLIMEFLPGGDM 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK---------------- 168
Cdd:cd05627   90 MTLLMKKDTLSEEATQFYIAETVLAIDAIHQLGFIHRDIKPDNLLLDAKGHVKLSDFGLCTGLKkahrtefyrnlthnpp 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 ---------SGELLATW-----------CGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQR 228
Cdd:cd05627  170 sdfsfqnmnSKRKAETWkknrrqlaystVGTPDYIAPEVFMQTGYN-KLCDWWSLGVIMYEMLIGYPPFCSETPQETYRK 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 929654453 229 VLEGR----FRIPYFMSEDCEHLIRRMLVlDPSKRL---TIAQIKEH 268
Cdd:cd05627  249 VMNWKetlvFPPEVPISEKAKDLILRFCT-DAENRIgsnGVEEIKSH 294
UBA_SIK cd14338
UBA domain found in salt-inducible kinase SIK1, SIK2, SIK3 and similar proteins; ...
297-341 2.02e-19

UBA domain found in salt-inducible kinase SIK1, SIK2, SIK3 and similar proteins; Salt-inducible kinase SIK1, SIK2, SIK3 are serine/threonine kinases that belong to the AMP-activated protein kinases (AMPK) family involved in the regulation of metabolism during energy stress. SIK1, also called serine/threonine-protein kinase SNF1-like kinase 1 (SNF1LK), is required for myogenic differentiation. It is degraded by the proteasome in myoblasts which is regulated by cAMP signaling. Moreover, SIK1 acts as a class II histone deacetylase (HDAC) kinase, triggering the cytoplasmic export of the HDACs and activation of myocyte enhancer factor 2 (MEF2)-dependent transcription. It also regulates transcription through inhibitory phosphorylation of a family of cAMP responsive element binding protein (CREB) coactivators, called TORCs/CRTCs. In addition, SIK1 links LKB1 to p53-dependent anoikis and suppresses metastasis. It is also involved in a cell sodium-sensing network that regulates active sodium transport through a calcium-dependent process. SIK2, also called Qin-induced kinase or serine/threonine-protein kinase SNF1-like kinase 2 (SNF1LK2), plays an important role in the insulin-signaling pathway during adipocyte differentiation, as well as in autophagy progression. Moreover, SIK2 plays a critical role in neuronal survival and modulates cAMP responsive element binding protein (CREB)-mediated gene expression in response to hormones and nutrients. SIK2 acts as a critical determinant in autophagy progression. In addition, SIK2 localizes at the centrosome and functions as a centrosome kinase required for bipolar mitotic spindle formation. It is involved in the initiation of mitosis, and regulates the localization of the centrosome linker protein, C-Nap1, through S2392 phosphorylation. SIK3, also called salt-inducible kinase 3 or serine/threonine-protein kinase QSK, acts as a novel energy regulator that modulates cholesterol and bile acid metabolism by coupling with retinoid metabolism. It also play an essential role in facilitating chondrocyte hypertrophy during skeletogenesis and growth plate maintenance. Members in this family contain an N-terminal protein kinase catalytic domain followed by an ubiquitin-associated (UBA) domain.


Pssm-ID: 270523  Cd Length: 45  Bit Score: 82.19  E-value: 2.02e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 297 NEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAIYFLLVERLKSHR 341
Cdd:cd14338    1 NEQVLRHMASLGIDRDRTLESVKNDSYDHVSAIYHLLLDKLRQHR 45
PTKc_Hck cd05073
Catalytic domain of the Protein Tyrosine Kinase, Hematopoietic cell kinase; PTKs catalyze the ...
22-244 2.24e-19

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: 88.93  E-value: 2.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  22 IEGTLGKGNFAVVKLGRHRiTKTEVAIKIIDKSQLdavNLEKIYREVQIMKMLDHPHIIKLYQVMeTKSMLYLVTEYAKN 101
Cdd:cd05073   15 LEKKLGAGQFGEVWMATYN-KHTKVAVKTMKPGSM---SVEAFLAEANVMKTLQHDKLVKLHAVV-TKEPIYIITEFMAK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYL-ANHGRLNESEARRKF-WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGS 179
Cdd:cd05073   90 GSLLDFLkSDEGSKQPLPKLIDFsAQIAEGMAFIEQRNYIHRDLRAANILVSASLVCKIADFGLARVIEDNEYTAREGAK 169
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 929654453 180 PP--YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLPILrQRVLEGRFRIPyfMSEDC 244
Cdd:cd05073  170 FPikWTAPEAINFGSFT-IKSDVWSFGILLMEIVTyGRIPYPGMSNPEV-IRALERGYRMP--RPENC 233
PTKc_Jak3_rpt2 cd05081
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 3; PTKs catalyze the ...
26-210 2.32e-19

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: 89.57  E-value: 2.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRI----TKTEVAIKIIDKSQLDavNLEKIYREVQIMKMLDHPHIIKLYQVMET--KSMLYLVTEYA 99
Cdd:cd05081   12 LGKGNFGSVELCRYDPlgdnTGALVAVKQLQHSGPD--QQRDFQREIQILKALHSDFIVKYRGVSYGpgRRSLRLVMEYL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLA-NHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFF---KSGELLAT 175
Cdd:cd05081   90 PSGCLRDFLQrHRARLDASRLLLYSSQICKGMEYLGSRRCVHRDLAARNILVESEAHVKIADFGLAKLLpldKDYYVVRE 169
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 929654453 176 WCGSPPY-AAPEVFEGQQYEgPQLDIWSMGVVLYVL 210
Cdd:cd05081  170 PGQSPIFwYAPESLSDNIFS-RQSDVWSFGVVLYEL 204
PK_KSR cd14063
Pseudokinase domain of Kinase Suppressor of Ras; The pseudokinase domain shows similarity to ...
21-217 2.60e-19

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: 88.95  E-value: 2.60e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  21 DIEGTLGKGNFAVVKLGR-HritkTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14063    3 EIKEVIGKGRFGRVHRGRwH----GDVAIKLLNIDYLNEEQLEAFKEEVAAYKNTRHDNLVLFMGACMDPPHLAIVTSLC 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNmNIKIADFGFGNFFK---SGELLAT 175
Cdd:cd14063   79 KGRTLYSLIHERkEKFDFNKTVQIAQQICQGMGYLHAKGIIHKDLKSKNIFLENG-RVVITDFGLFSLSGllqPGRREDT 157
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 929654453 176 WCGSP---PYAAPEV---------FEGQQYEGPQLDIWSMGVVLYVLVCGALPF 217
Cdd:cd14063  158 LVIPNgwlCYLAPEIiralspdldFEESLPFTKASDVYAFGTVWYELLAGRWPF 211
PTKc_Jak2_rpt2 cd14205
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Janus kinase 2; PTKs catalyze the ...
26-210 2.84e-19

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: 89.30  E-value: 2.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRI----TKTEVAIKIIDKSQldAVNLEKIYREVQIMKMLDHPHIIKLYQVMET--KSMLYLVTEYA 99
Cdd:cd14205   12 LGKGNFGSVEMCRYDPlqdnTGEVVAVKKLQHST--EEHLRDFEREIEILKSLQHDNIVKYKGVCYSagRRNLRLIMEYL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLAT--W 176
Cdd:cd14205   90 PYGSLRDYLQKHKeRIDHIKLLQYTSQICKGMEYLGTKRYIHRDLATRNILVENENRVKIGDFGLTKVLPQDKEYYKvkE 169
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 929654453 177 CGSPP--YAAPEVFEGQQYEGPQlDIWSMGVVLYVL 210
Cdd:cd14205  170 PGESPifWYAPESLTESKFSVAS-DVWSFGVVLYEL 204
STKc_LIMK1 cd14221
Catalytic domain of the Serine/Threonine Kinase, LIM domain kinase 1; STKs catalyze the ...
26-271 3.21e-19

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: 88.47  E-value: 3.21e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKiiDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14221    1 LGKGCFGQAIKVTHRETGEVMVMK--ELIRFDEETQRTFLKEVKVMRCLEHPNVLKFIGVLYKDKRLNFITEYIKGGTLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQ-ILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFF----KSGELLA------ 174
Cdd:cd14221   79 GIIKSMDSHYPWSQRVSFAKdIASGMAYLHSMNIIHRDLNSHNCLVRENKSVVVADFGLARLMvdekTQPEGLRslkkpd 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 -----TWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVcGALPFDGPTLPilrqRVLEGRFRIPYFMSEDCEH--- 246
Cdd:cd14221  159 rkkryTVVGNPYWMAPEMINGRSYD-EKVDVFSFGIVLCEII-GRVNADPDYLP----RTMDFGLNVRGFLDRYCPPncp 232
                        250       260       270
                 ....*....|....*....|....*....|
gi 929654453 247 -----LIRRMLVLDPSKRLTIAQIKEhkWM 271
Cdd:cd14221  233 psffpIAVLCCDLDPEKRPSFSKLEH--WL 260
PTKc_Fyn cd05070
Catalytic domain of the Protein Tyrosine Kinase, Fyn; PTKs catalyze the transfer of the ...
22-266 3.54e-19

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: 88.59  E-value: 3.54e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  22 IEGTLGKGNFAVVKLGRHRiTKTEVAIKIIDKSQLDAvnlEKIYREVQIMKMLDHPHIIKLYQVMeTKSMLYLVTEYAKN 101
Cdd:cd05070   13 LIKRLGNGQFGEVWMGTWN-GNTKVAIKTLKPGTMSP---ESFLEEAQIMKKLKHDKLVQLYAVV-SEEPIYIVTEYMSK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLAN-HGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGS 179
Cdd:cd05070   88 GSLLDFLKDgEGRaLKLPNLVDMAAQVAAGMAYIERMNYIHRDLRSANILVGNGLICKIADFGLARLIEDNEYTARQGAK 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PP--YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLPILRQRVLEGrFRIPyfMSEDCEHLIRRMLV--- 253
Cdd:cd05070  168 FPikWTAPEAALYGRFT-IKSDVWSFGILLTELVTkGRVPYPGMNNREVLEQVERG-YRMP--CPQDCPISLHELMIhcw 243
                        250
                 ....*....|....
gi 929654453 254 -LDPSKRLTIAQIK 266
Cdd:cd05070  244 kKDPEERPTFEYLQ 257
PTKc_FGFR1 cd05098
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 1; PTKs ...
26-267 3.58e-19

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: 89.30  E-value: 3.58e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGR---------HRITKteVAIKIIdKSQLDAVNLEKIYREVQIMKML-DHPHIIKLYQVMETKSMLYLV 95
Cdd:cd05098   21 LGEGCFGQVVLAEaigldkdkpNRVTK--VAVKML-KSDATEKDLSDLISEMEMMKMIgKHKNIINLLGACTQDGPLYVI 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLA-----------NHGRLNESEARRK-----FWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIA 159
Cdd:cd05098   98 VEYASKGNLREYLQarrppgmeycyNPSHNPEEQLSSKdlvscAYQVARGMEYLASKKCIHRDLAARNVLVTEDNVMKIA 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 160 DFGFG------NFFK---SGELLATWcgsppyAAPEVFEGQQYEGpQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRV 229
Cdd:cd05098  178 DFGLArdihhiDYYKkttNGRLPVKW------MAPEALFDRIYTH-QSDVWSFGVLLWeIFTLGGSPYPGVPVEELFKLL 250
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 929654453 230 LEG-RFRIP-------YFMSEDCEHLIrrmlvldPSKRLTIAQIKE 267
Cdd:cd05098  251 KEGhRMDKPsnctnelYMMMRDCWHAV-------PSQRPTFKQLVE 289
PTKc_EphR_A cd05066
Catalytic domain of the Protein Tyrosine Kinases, Class EphA Ephrin Receptors; PTKs catalyze ...
22-255 3.75e-19

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: 88.38  E-value: 3.75e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  22 IEGTLGKGNFAVVKLGRHRI-TKTEVAIKIidkSQLDAVNLEKIYR----EVQIMKMLDHPHIIKLYQVMETKSMLYLVT 96
Cdd:cd05066    8 IEKVIGAGEFGEVCSGRLKLpGKREIPVAI---KTLKAGYTEKQRRdflsEASIMGQFDHPNIIHLEGVVTRSKPVMIVT 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNGEIFDYLANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLA- 174
Cdd:cd05066   85 EYMENGSLDAFLRKHdGQFTVIQLVGMLRGIASGMKYLSDMGYVHRDLAARNILVNSNLVCKVSDFGLSRVLEDDPEAAy 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 -TWCGSPP--YAAPEVFEGQQYEGPQlDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEGrFRIPYFMseDCEHLIRR 250
Cdd:cd05066  165 tTRGGKIPirWTAPEAIAYRKFTSAS-DVWSYGIVMWeVMSYGERPYWEMSNQDVIKAIEEG-YRLPAPM--DCPAALHQ 240

                 ....*
gi 929654453 251 mLVLD 255
Cdd:cd05066  241 -LMLD 244
STKc_TGFbR-like cd13998
Catalytic domain of Transforming Growth Factor beta Receptor-like Serine/Threonine Kinases; ...
27-267 4.59e-19

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: 88.65  E-value: 4.59e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  27 GKGNFAVVKlgRHRITKTEVAIKIIDKSQLDAVNLEK-IYREVqimkMLDHPHIIKL----YQVMETKSMLYLVTEYAKN 101
Cdd:cd13998    4 GKGRFGEVW--KASLKNEPVAVKIFSSRDKQSWFREKeIYRTP----MLKHENILQFiaadERDTALRTELWLVTAFHPN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLANHG-------RLNESEARrKFWQILSAVDYCHGRK--IVHRDLKAENLLLDNNMNIKIADFGFGNFFKSG-- 170
Cdd:cd13998   78 GSL*DYLSLHTidwvslcRLALSVAR-GLAHLHSEIPGCTQGKpaIAHRDLKSKNILVKNDGTCCIADFGLAVRLSPStg 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 -ELLAT--WCGSPPYAAPEVFEG----QQYEG-PQLDIWSMGVVLYVLV--CGA---------LPF-----DGPTLPILR 226
Cdd:cd13998  157 eEDNANngQVGTKRYMAPEVLEGainlRDFESfKRVDIYAMGLVLWEMAsrCTDlfgiveeykPPFysevpNHPSFEDMQ 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 929654453 227 QRVLEGRFRiPYFMSEDCEHLIRRMLVL--------DPSKRLTIAQIKE 267
Cdd:cd13998  237 EVVVRDKQR-PNIPNRWLSHPGLQSLAEtieecwdhDAEARLTAQCIEE 284
STKc_A-Raf cd14150
Catalytic domain of the Serine/Threonine Kinase, A-Raf (Rapidly Accelerated Fibrosarcoma) ...
26-217 4.70e-19

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: 88.15  E-value: 4.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRitkTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIkLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14150    8 IGTGSFGTVFRGKWH---GDVAVKILKVTEPTPEQLQAFKNEMQVLRKTRHVNIL-LFMGFMTRPNFAIITQWCEGSSLY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYL-ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNffksgeLLATWCGSPP--- 181
Cdd:cd14150   84 RHLhVTETRFDTMQLIDVARQTAQGMDYLHAKNIIHRDLKSNNIFLHEGLTVKIGDFGLAT------VKTRWSGSQQveq 157
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 182 ------YAAPEVFEGQQyEGP---QLDIWSMGVVLYVLVCGALPF 217
Cdd:cd14150  158 psgsilWMAPEVIRMQD-TNPysfQSDVYAYGVVLYELMSGTLPY 201
STKc_JNK cd07850
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase; STKs catalyze the ...
41-302 5.70e-19

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: 89.40  E-value: 5.70e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  41 ITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQV------METKSMLYLVTEY--AKNGEIFDYLANHG 112
Cdd:cd07850   23 VTGQNVAIKKLSRPFQNVTHAKRAYRELVLMKLVNHKNIIGLLNVftpqksLEEFQDVYLVMELmdANLCQVIQMDLDHE 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 113 RLNesearRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPYAAPEVFEGQQ 192
Cdd:cd07850  103 RMS-----YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYVVTRYYRAPEVILGMG 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 193 YEgPQLDIWSMGVVLYVLVCGALPFDG----------------PT-------LPILRQRVLEGRFRIPY----------F 239
Cdd:cd07850  178 YK-ENVDIWSVGCIMGEMIRGTVLFPGtdhidqwnkiieqlgtPSdefmsrlQPTVRNYVENRPKYAGYsfeelfpdvlF 256
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 929654453 240 MSEDCEH----------LIRRMLVLDPSKRLTIAQIKEHKWMLI-----EVPVQRPVLYPQE-QENEPSIGEFNEQVLR 302
Cdd:cd07850  257 PPDSEEHnklkasqardLLSKMLVIDPEKRISVDDALQHPYINVwydpsEVEAPPPAPYDHSiDEREHTVEEWKELIYK 335
STKc_TLK2 cd14041
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 2; STKs catalyze the ...
26-272 7.24e-19

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: 88.58  E-value: 7.24e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKI--IDKSQLDAV--NLEK-IYREVQIMKMLDHPHIIKLYQV--METKSMLyLVTEY 98
Cdd:cd14041   14 LGRGGFSEVYKAFDLTEQRYVAVKIhqLNKNWRDEKkeNYHKhACREYRIHKELDHPRIVKLYDYfsLDTDSFC-TVLEY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRK--IVHRDLKAENLLLDNNM---NIKIADFGFG--------N 165
Cdd:cd14041   93 CEGNDLDFYLKQHKLMSEKEARSIIMQIVNALKYLNEIKppIIHYDLKPGNILLVNGTacgEIKITDFGLSkimdddsyN 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 166 FFKSGELLATWCGSPPYAAPEVFEGQQyEGPQL----DIWSMGVVLYVLVCGALPF--DGPTLPILRQRVL----EGRFR 235
Cdd:cd14041  173 SVDGMELTSQGAGTYWYLPPECFVVGK-EPPKIsnkvDVWSVGVIFYQCLYGRKPFghNQSQQDILQENTIlkatEVQFP 251
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 929654453 236 IPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWML 272
Cdd:cd14041  252 PKPVVTPEAKAFIRRCLAYRKEDRIDVQQLACDPYLL 288
STKc_TAO3 cd06633
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 3; STKs catalyze ...
26-307 7.32e-19

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: 88.56  E-value: 7.32e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKS-QLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKnGEI 104
Cdd:cd06633   29 IGHGSFGAVYFATNSHTNEVVAIKKMSYSgKQTNEKWQDIIKEVKFLQQLKHPNTIEYKGCYLKDHTAWLVMEYCL-GSA 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEllaTWCGSPPYA 183
Cdd:cd06633  108 SDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPAN---SFVGTPYWM 184
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 184 APEVF----EGqQYEGpQLDIWSMGVvlyvlVCGALPFDGPtlPILRQRVLEGRFRI-----PYFMSEDCEHLIRRM--- 251
Cdd:cd06633  185 APEVIlamdEG-QYDG-KVDIWSLGI-----TCIELAERKP--PLFNMNAMSALYHIaqndsPTLQSNEWTDSFRGFvdy 255
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 929654453 252 -LVLDPSKRLTIAQIKEHKWMLIEVPVQrpVLYPQEQENEPSIGEFNEQVLRLMHSL 307
Cdd:cd06633  256 cLQKIPQERPSSAELLRHDFVRRERPPR--VLIDLIQRTKDAVRELDNLQYRKMKKI 310
STKc_ERK1_2_like cd07849
Catalytic domain of Extracellular signal-Regulated Kinase 1 and 2-like Serine/Threonine ...
20-268 1.04e-18

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: 88.52  E-value: 1.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIID--KSQLDAVnleKIYREVQIMKMLDHPHIIKLYQVM-----ETKSML 92
Cdd:cd07849    7 YQNLSYIGEGAYGMVCSAVHKPTGQKVAIKKISpfEHQTYCL---RTLREIKILLRFKHENIIGILDIQrpptfESFKDV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  93 YLVTEYAKNgEIFDYLANHgRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG-----NFF 167
Cdd:cd07849   84 YIVQELMET-DLYKLIKTQ-HLSNDHIQYFLYQILRGLKYIHSANVLHRDLKPSNLLLNTNCDLKICDFGLAriadpEHD 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 168 KSG---ELLAT-WcgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG----------------PTLP---- 223
Cdd:cd07849  162 HTGfltEYVATrW-----YRAPEIMLNSKGYTKAIDIWSVGCILAEMLSNRPLFPGkdylhqlnlilgilgtPSQEdlnc 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 929654453 224 ILRQRVLEGRFRIPYF-----------MSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd07849  237 IISLKARNYIKSLPFKpkvpwnklfpnADPKALDLLDKMLTFNPHKRITVEEALAH 292
PKc_like cd13968
Catalytic domain of the Protein Kinase superfamily; The PK superfamily contains the large ...
26-162 1.08e-18

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: 83.26  E-value: 1.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQldAVNLEKIYREVQIMKMLD--HPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd13968    1 MGEGASAKVFWAEGECTTIGVAVKIGDDVN--NEEGEDLESEMDILRRLKglELNIPKVLVTEDVDGPNILLMELVKGGT 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 929654453 104 IFDYLANhGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG 162
Cdd:cd13968   79 LIAYTQE-EELDEKDVESIMYQLAECMRLLHSFHLIHRDLNNDNILLSEDGNVKLIDFG 136
STKc_IRAK4 cd14158
Catalytic domain of the Serine/Threonine kinase, Interleukin-1 Receptor Associated Kinase 4; ...
26-218 1.09e-18

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: 87.55  E-value: 1.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRhrITKTEVAIK-IIDKSQLDAVNLEKIY-REVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd14158   23 LGEGGFGVVFKGY--INDKNVAVKkLAAMVDISTEDLTKQFeQEIQVMAKCQHENLVELLGYSCDGPQLCLVYTYMPNGS 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANhgrLNESEA---RRKFWQILSA---VDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNffKSGELLATW- 176
Cdd:cd14158  101 LLDRLAC---LNDTPPlswHMRCKIAQGTangINYLHENNHIHRDIKSANILLDETFVPKISDFGLAR--ASEKFSQTIm 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 929654453 177 ----CGSPPYAAPEVFEGQQyeGPQLDIWSMGVVLYVLVCGALPFD 218
Cdd:cd14158  176 teriVGTTAYMAPEALRGEI--TPKSDIFSFGVVLLEIITGLPPVD 219
PTKc_Abl cd05052
Catalytic domain of the Protein Tyrosine Kinase, Abelson kinase; PTKs catalyze the transfer of ...
26-267 1.14e-18

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: 86.71  E-value: 1.14e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLG---RHRITkteVAIKIIDKsqlDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd05052   14 LGGGQYGEVYEGvwkKYNLT---VAVKTLKE---DTMEVEEFLKEAAVMKEIKHPNLVQLLGVCTREPPFYIITEFMPYG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYL--ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSP 180
Cdd:cd05052   88 NLLDYLreCNREELNAVVLLYMATQIASAMEYLEKKNFIHRDLAARNCLVGENHLVKVADFGLSRLMTGDTYTAHAGAKF 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 181 P--YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLPILRQRvLEGRFRI--PYFMSEDCEHLIRRMLVLD 255
Cdd:cd05052  168 PikWTAPESLAYNKFS-IKSDVWAFGVLLWEIATyGMSPYPGIDLSQVYEL-LEKGYRMerPEGCPPKVYELMRACWQWN 245
                        250
                 ....*....|..
gi 929654453 256 PSKRLTIAQIKE 267
Cdd:cd05052  246 PSDRPSFAEIHQ 257
PKc_MKK5 cd06619
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
25-268 1.21e-18

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: 87.24  E-value: 1.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLGRHRITKTEVAIKIIdksQLD-AVNLEK-IYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd06619    8 ILGHGNGGTVYKAYHLLTRRILAVKVI---PLDiTVELQKqIMSELEILYKCDSPYIIGFYGAFFVENRISICTEFMDGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYlanhGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSgELLATWCGSPPY 182
Cdd:cd06619   85 SLDVY----RKIPEHVLGRIAVAVVKGLTYLWSLKILHRDVKPSNMLVNTRGQVKLCDFGVSTQLVN-SIAKTYVGTNAY 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 183 AAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPF------DGPTLPI--LRQRVLEGRFRIP-YFMSEDCEHLIRRMLV 253
Cdd:cd06619  160 MAPERISGEQY-GIHSDVWSLGISFMELALGRFPYpqiqknQGSLMPLqlLQCIVDEDPPVLPvGQFSEKFVHFITQCMR 238
                        250
                 ....*....|....*
gi 929654453 254 LDPSKRLTIAQIKEH 268
Cdd:cd06619  239 KQPKERPAPENLMDH 253
PTKc_Trk cd05049
Catalytic domain of the Protein Tyrosine Kinases, Tropomyosin Related Kinases; PTKs catalyze ...
24-267 1.32e-18

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: 87.14  E-value: 1.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  24 GTLGKGNFAVVKLG--RHRITKTE---VAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd05049   11 RELGEGAFGKVFLGecYNLEPEQDkmlVAVKTLKDASSPDAR-KDFEREAELLTNLQHENIVKFYGVCTEGDPLLMVFEY 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHG--------------RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG 164
Cdd:cd05049   90 MEHGDLNKFLRSHGpdaaflasedsapgELTLSQLLHIAVQIASGMVYLASQHFVHRDLATRNCLVGTNLVVKIGDFGMS 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 165 ------NFFKSG---ELLATWCgsPPyaapevfEGQQYE--GPQLDIWSMGVVLY-VLVCGALPF----DGPTLPILRQR 228
Cdd:cd05049  170 rdiystDYYRVGghtMLPIRWM--PP-------ESILYRkfTTESDVWSFGVVLWeIFTYGKQPWfqlsNTEVIECITQG 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 929654453 229 VLEGRFRipyfmseDCEHLIRRMLV----LDPSKRLTIAQIKE 267
Cdd:cd05049  241 RLLQRPR-------TCPSEVYAVMLgcwkREPQQRLNIKDIHK 276
PTZ00266 PTZ00266
NIMA-related protein kinase; Provisional
7-264 1.39e-18

NIMA-related protein kinase; Provisional


Pssm-ID: 173502 [Multi-domain]  Cd Length: 1021  Bit Score: 91.34  E-value: 1.39e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453    7 PRHLQRGPVRVGFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVM 86
Cdd:PTZ00266    2 PGKYDDGESRLNEYEVIKKIGNGRFGEVFLVKHKRTQEFFCWKAISYRGLKEREKSQLVIEVNVMRELKHKNIVRYIDRF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   87 ETKS--MLYLVTEYAKNGEIFDYLAN----HGRLNESEARRKFWQILSAVDYCH-------GRKIVHRDLKAENLLLD-- 151
Cdd:PTZ00266   82 LNKAnqKLYILMEFCDAGDLSRNIQKcykmFGKIEEHAIVDITRQLLHALAYCHnlkdgpnGERVLHRDLKPQNIFLStg 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  152 -----------NNMN----IKIADFGFGNFFKSGELLATWCGSPPYAAPEVF--EGQQYEGPQlDIWSMGVVLYVLVCGA 214
Cdd:PTZ00266  162 irhigkitaqaNNLNgrpiAKIGDFGLSKNIGIESMAHSCVGTPYYWSPELLlhETKSYDDKS-DMWALGCIIYELCSGK 240
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 929654453  215 LPFD--------------GPTLPIlrqrvlEGRfripyfmSEDCEHLIRRMLVLDPSKRLTIAQ 264
Cdd:PTZ00266  241 TPFHkannfsqliselkrGPDLPI------KGK-------SKELNILIKNLLNLSAKERPSALQ 291
PTKc_Tyk2_rpt2 cd05080
Catalytic (repeat 2) domain of the Protein Tyrosine Kinase, Tyrosine kinase 2; PTKs catalyze ...
26-220 1.43e-18

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: 86.88  E-value: 1.43e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTE----VAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETK--SMLYLVTEYA 99
Cdd:cd05080   12 LGEGHFGKVSLYCYDPTNDGtgemVAVKAL-KADCGPQHRSGWKQEIDILKTLYHENIVKYKGCCSEQggKSLQLIMEYV 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHgRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELL--ATWC 177
Cdd:cd05080   91 PLGSLRDYLPKH-SIGLAQLLLFAQQICEGMAYLHSQHYIHRDLAARNVLLDNDRLVKIGDFGLAKAVPEGHEYyrVRED 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 178 GSPP--YAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPFDGP 220
Cdd:cd05080  170 GDSPvfWYAPECLKEYKFYYAS-DVWSFGVTLYELLTHCDSSQSP 213
PTKc_Yes cd05069
Catalytic domain of the Protein Tyrosine Kinase, Yes; PTKs catalyze the transfer of the ...
22-266 1.55e-18

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: 87.05  E-value: 1.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  22 IEGTLGKGNFAVVKLGRHRITkTEVAIKIIDKSQLDAvnlEKIYREVQIMKMLDHPHIIKLYQVMeTKSMLYLVTEYAKN 101
Cdd:cd05069   16 LDVKLGQGCFGEVWMGTWNGT-TKVAIKTLKPGTMMP---EAFLQEAQIMKKLRHDKLVPLYAVV-SEEPIYIVTEFMGK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYL--ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGS 179
Cdd:cd05069   91 GSLLDFLkeGDGKYLKLPQLVDMAAQIADGMAYIERMNYIHRDLRAANILVGDNLVCKIADFGLARLIEDNEYTARQGAK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PP--YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLPILRQRVLEG-RFRIPYFMSEDCEHLIRRMLVLD 255
Cdd:cd05069  171 FPikWTAPEAALYGRFT-IKSDVWSFGILLTELVTkGRVPYPGMVNREVLEQVERGyRMPCPQGCPESLHELMKLCWKKD 249
                        250
                 ....*....|.
gi 929654453 256 PSKRLTIAQIK 266
Cdd:cd05069  250 PDERPTFEYIQ 260
STKc_MLK1 cd14145
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 1; STKs catalyze the ...
22-219 1.69e-18

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: 86.63  E-value: 1.69e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  22 IEGTLGKGNFAvvKLGRHRITKTEVAIKII--DKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd14145   10 LEEIIGIGGFG--KVYRAIWIGDEVAVKAArhDPDEDISQTIENVRQEAKLFAMLKHPNIIALRGVCLKEPNLCLVMEFA 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHgRLNESEARRKFWQILSAVDYCHGRKIV---HRDLKAENLLL----DN----NMNIKIADFGFG-NFF 167
Cdd:cd14145   88 RGGPLNRVLSGK-RIPPDILVNWAVQIARGMNYLHCEAIVpviHRDLKSSNILIlekvENgdlsNKILKITDFGLArEWH 166
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 929654453 168 KSGELLATwcGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPFDG 219
Cdd:cd14145  167 RTTKMSAA--GTYAWMAPEVIRSSMFSKGS-DVWSYGVLLWELLTGEVPFRG 215
PTKc_EGFR cd05108
Catalytic domain of the Protein Tyrosine Kinase, Epidermal Growth Factor Receptor; PTKs ...
26-259 2.08e-18

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: 87.39  E-value: 2.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLG----RHRITKTEVAIKIIDKSQLDAVNLEkIYREVQIMKMLDHPHIIKLYQVMETkSMLYLVTEYAKN 101
Cdd:cd05108   15 LGSGAFGTVYKGlwipEGEKVKIPVAIKELREATSPKANKE-ILDEAYVMASVDNPHVCRLLGICLT-STVQLITQLMPF 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLANHgRLNESEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE-LLATWCG 178
Cdd:cd05108   93 GCLLDYVREH-KDNIGSQYLLNWcvQIAKGMNYLEDRRLVHRDLAARNVLVKTPQHVKITDFGLAKLLGAEEkEYHAEGG 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPP--YAAPEVFEGQQYEGpQLDIWSMGVVLYVLVC-GALPFDG-PTLPIlrQRVLEGRFRIPY--FMSEDCEHLIRRML 252
Cdd:cd05108  172 KVPikWMALESILHRIYTH-QSDVWSYGVTVWELMTfGSKPYDGiPASEI--SSILEKGERLPQppICTIDVYMIMVKCW 248

                 ....*..
gi 929654453 253 VLDPSKR 259
Cdd:cd05108  249 MIDADSR 255
STKc_NDR1 cd05628
Catalytic domain of the Serine/Threonine Kinase, Nuclear Dbf2-Related kinase 1; STKs catalyze ...
26-250 2.21e-18

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: 88.17  E-value: 2.21e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQ-LDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEI 104
Cdd:cd05628    9 IGRGAFGEVRLVQKKDTGHVYAMKILRKADmLEKEQVGHIRAERDILVEADSLWVVKMFYSFQDKLNLYLIMEFLPGGDM 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK---------------- 168
Cdd:cd05628   89 MTLLMKKDTLTEEETQFYIAETVLAIDSIHQLGFIHRDIKPDNLLLDSKGHVKLSDFGLCTGLKkahrtefyrnlnhslp 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 ---------SGELLATW-----------CGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQR 228
Cdd:cd05628  169 sdftfqnmnSKRKAETWkrnrrqlafstVGTPDYIAPEVFMQTGYN-KLCDWWSLGVIMYEMLIGYPPFCSETPQETYKK 247
                        250       260
                 ....*....|....*....|....*.
gi 929654453 229 VLEGR----FRIPYFMSEDCEHLIRR 250
Cdd:cd05628  248 VMNWKetliFPPEVPISEKAKDLILR 273
STKc_MLK2 cd14148
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 2; STKs catalyze the ...
26-217 2.24e-18

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: 85.81  E-value: 2.24e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRitKTEVAIKII--DKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd14148    2 IGVGGFGKVYKGLWR--GEEVAVKAArqDPDEDIAVTAENVRQEARLFWMLQHPNIIALRGVCLNPPHLCLVMEYARGGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLAN-----HGRLNesearrkfW--QILSAVDYCHGRKIV---HRDLKAENLLL------DN--NMNIKIADFGFG- 164
Cdd:cd14148   80 LNRALAGkkvppHVLVN--------WavQIARGMNYLHNEAIVpiiHRDLKSSNILIlepienDDlsGKTLKITDFGLAr 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 929654453 165 NFFKSGELLATwcGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPF 217
Cdd:cd14148  152 EWHKTTKMSAA--GTYAWMAPEVIRLSLFSKSS-DVWSFGVLLWELLTGEVPY 201
STKc_RIP4_like cd14025
Catalytic domain of the Serine/Threonine kinases, Receptor Interacting Protein 4 and similar ...
26-276 2.27e-18

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: 86.01  E-value: 2.27e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVmeTKSMLYLVTEYAKNGEIF 105
Cdd:cd14025    4 VGSGGFGQVYKVRHKHWKTWLAIKCPPSLHVDDSERMELLEEAKKMEMAKFRHILPVYGI--CSEPVGLVMEYMETGSLE 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGrLNESEARRKFWQILSAVDYCHGRK--IVHRDLKAENLLLDNNMNIKIADFGFG--NFFKSGELLA--TWCGS 179
Cdd:cd14025   82 KLLASEP-LPWELRFRIIHETAVGMNFLHCMKppLLHLDLKPANILLDAHYHVKISDFGLAkwNGLSHSHDLSrdGLRGT 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVF-EGQQYEGPQLDIWSMGVVLYVLVCGALPFDG--PTLPILrQRVLEGRF----RIPYFMSEDCEHLIRRML 252
Cdd:cd14025  161 IAYLPPERFkEKNRCPDTKHDVYSFAIVIWGILTQKKPFAGenNILHIM-VKVVKGHRpslsPIPRQRPSECQQMICLMK 239
                        250       260
                 ....*....|....*....|....*..
gi 929654453 253 VL---DPSKRLTIAQIKEHKWMLIEVP 276
Cdd:cd14025  240 RCwdqDPRKRPTFQDITSETENLLSLL 266
STKc_TLK1 cd14040
Catalytic domain of the Serine/Threonine kinase, Tousled-Like Kinase 1; STKs catalyze the ...
26-272 2.63e-18

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: 86.65  E-value: 2.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKI--IDKSQLDAV--NLEK-IYREVQIMKMLDHPHIIKLYQVMETKSMLY-LVTEYA 99
Cdd:cd14040   14 LGRGGFSEVYKAFDLYEQRYAAVKIhqLNKSWRDEKkeNYHKhACREYRIHKELDHPRIVKLYDYFSLDTDTFcTVLEYC 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRK--IVHRDLKAENLLLDNNM---NIKIADFGFGNFFKSG---- 170
Cdd:cd14040   94 EGNDLDFYLKQHKLMSEKEARSIVMQIVNALRYLNEIKppIIHYDLKPGNILLVDGTacgEIKITDFGLSKIMDDDsygv 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 ---ELLATWCGSPPYAAPEVFEGQQyEGPQL----DIWSMGVVLYVLVCGALPF--DGPTLPILRQRVL----EGRFRIP 237
Cdd:cd14040  174 dgmDLTSQGAGTYWYLPPECFVVGK-EPPKIsnkvDVWSVGVIFFQCLYGRKPFghNQSQQDILQENTIlkatEVQFPVK 252
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 929654453 238 YFMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWML 272
Cdd:cd14040  253 PVVSNEAKAFIRRCLAYRKEDRFDVHQLASDPYLL 287
STKc_JNK2 cd07876
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 2; STKs catalyze the ...
26-300 3.09e-18

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: 87.39  E-value: 3.09e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd07876   29 IGSGAQGIVCAAFDTVLGINVAVKKLSRPFQNQTHAKRAYRELVLLKCVNHKNIISLLNVFTPQKSLEEFQDVYLVMELM 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DylAN-----HGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSP 180
Cdd:cd07876  109 D--ANlcqviHMELDHERMSYLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTACTNFMMTPYVVTR 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 181 PYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDG----------------PTL-------PILRQRVlEGRFRIP 237
Cdd:cd07876  187 YYRAPEVILGMGYK-ENVDIWSVGCIMGELVKGSVIFQGtdhidqwnkvieqlgtPSAefmnrlqPTVRNYV-ENRPQYP 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 238 ----------YFMSEDCEH----------LIRRMLVLDPSKRLTIAQIKEHKWMLI-----EVPVQRPVLY-PQEQENEP 291
Cdd:cd07876  265 gisfeelfpdWIFPSESERdklktsqardLLSKMLVIDPDKRISVDEALRHPYITVwydpaEAEAPPPQIYdAQLEEREH 344

                 ....*....
gi 929654453 292 SIGEFNEQV 300
Cdd:cd07876  345 AIEEWKELI 353
PTZ00036 PTZ00036
glycogen synthase kinase; Provisional
10-261 3.73e-18

glycogen synthase kinase; Provisional


Pssm-ID: 173333 [Multi-domain]  Cd Length: 440  Bit Score: 88.17  E-value: 3.73e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  10 LQRGPVRVgfYDIEGTLGKGNFAVVKLGRHRITKTEVAIK-IIDKSQLDAvnlekiyREVQIMKMLDHPHIIKLYQVMET 88
Cdd:PTZ00036  60 INRSPNKS--YKLGNIIGNGSFGVVYEAICIDTSEKVAIKkVLQDPQYKN-------RELLIMKNLNHINIIFLKDYYYT 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  89 KSM--------LYLVTEYAKNgEIFDYLANHGRLNESE----ARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD-NNMN 155
Cdd:PTZ00036 131 ECFkkneknifLNVVMEFIPQ-TVHKYMKHYARNNHALplflVKLYSYQLCRALAYIHSKFICHRDLKPQNLLIDpNTHT 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 156 IKIADFGFGNFFKSGELLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG---------------- 219
Cdd:PTZ00036 210 LKLCDFGSAKNLLAGQRSVSYICSRFYRAPELMLGATNYTTHIDLWSLGCIIAEMILGYPIFSGqssvdqlvriiqvlgt 289
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 929654453 220 PT---------------LPILRQRVLEGRFriPYFMSEDCEHLIRRMLVLDPSKRLT 261
Cdd:PTZ00036 290 PTedqlkemnpnyadikFPDVKPKDLKKVF--PKGTPDDAINFISQFLKYEPLKRLN 344
PKc_MEK cd06615
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
23-221 3.83e-18

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: 86.34  E-value: 3.83e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  23 EGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVnLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd06615    6 LGELGAGNGGVVTKVLHRPSGLIMARKLIHLEIKPAI-RNQIIRELKVLHECNSPYIVGFYGAFYSDGEISICMEHMDGG 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNEsearrkfwQILSAVDYC---------HGRKIVHRDLKAENLLLDNNMNIKIADFGFgnffkSGELL 173
Cdd:cd06615   85 SLDQVLKKAGRIPE--------NILGKISIAvlrgltylrEKHKIMHRDVKPSNILVNSRGEIKLCDFGV-----SGQLI 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 929654453 174 ----ATWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPT 221
Cdd:cd06615  152 dsmaNSFVGTRSYMSPERLQGTHYT-VQSDIWSLGLSLVEMAIGRYPIPPPD 202
STKc_MAP4K4_6_N cd06636
N-terminal Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinase ...
18-217 4.84e-18

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: 85.44  E-value: 4.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  18 GFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAvnlEKIYREVQIMKMLDH-PHIIKLYQVMETKS------ 90
Cdd:cd06636   16 GIFELVEVVGNGTYGQVYKGRHVKTGQLAAIKVMDVTEDEE---EEIKLEINMLKKYSHhRNIATYYGAFIKKSppghdd 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  91 MLYLVTEYAKNGEIFDYLANhgrlNESEARRKFW------QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF- 163
Cdd:cd06636   93 QLWLVMEFCGAGSVTDLVKN----TKGNALKEDWiayicrEILRGLAHLHAHKVIHRDIKGQNVLLTENAEVKLVDFGVs 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 164 GNFFKSGELLATWCGSPPYAAPEVFEGQqyEGP------QLDIWSMGVVLYVLVCGALPF 217
Cdd:cd06636  169 AQLDRTVGRRNTFIGTPYWMAPEVIACD--ENPdatydyRSDIWSLGITAIEMAEGAPPL 226
STKc_MLK cd14061
Catalytic domain of the Serine/Threonine Kinases, Mixed Lineage Kinases; STKs catalyze the ...
26-219 5.39e-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: 84.75  E-value: 5.39e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRitKTEVAIKI--IDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd14061    2 IGVGGFGKVYRGIWR--GEEVAVKAarQDPDEDISVTLENVRQEARLFWMLRHPNIIALRGVCLQPPNLCLVMEYARGGA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 ifdylanhgrLNESEARRKF-------W--QILSAVDYCHGRK---IVHRDLKAENLLLDN--------NMNIKIADFGF 163
Cdd:cd14061   80 ----------LNRVLAGRKIpphvlvdWaiQIARGMNYLHNEApvpIIHRDLKSSNILILEaienedleNKTLKITDFGL 149
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 929654453 164 G-NFFKSGELLATwcGSPPYAAPEVFEGQQYEGPQlDIWSMGVVLYVLVCGALPFDG 219
Cdd:cd14061  150 ArEWHKTTRMSAA--GTYAWMAPEVIKSSTFSKAS-DVWSYGVLLWELLTGEVPYKG 203
STKc_MAPK4_6 cd07854
Catalytic domain of the Serine/Threonine Kinases, Mitogen-Activated Protein Kinases 4 (also ...
46-290 6.00e-18

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: 86.37  E-value: 6.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  46 VAIKIIdkSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKS--------------MLYLVTEYAKNGeiFDYLANH 111
Cdd:cd07854   33 VAVKKI--VLTDPQSVKHALREIKIIRRLDHDNIVKVYEVLGPSGsdltedvgsltelnSVYIVQEYMETD--LANVLEQ 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 112 GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD-NNMNIKIADFGFGNF---------FKSGELLATWcgspp 181
Cdd:cd07854  109 GPLSEEHARLFMYQLLRGLKYIHSANVLHRDLKPANVFINtEDLVLKIGDFGLARIvdphyshkgYLSEGLVTKW----- 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 182 YAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGP-----------TLPILRQRVLEGRFR-IPYFMSED------ 243
Cdd:cd07854  184 YRSPRLLLSPNNYTKAIDMWAAGCIFAEMLTGKPLFAGAheleqmqlileSVPVVREEDRNELLNvIPSFVRNDggeprr 263
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929654453 244 ----------CE--HLIRRMLVLDPSKRLTIAQIKEHKWMLI-EVPVQRPV-LYPQEQENE 290
Cdd:cd07854  264 plrdllpgvnPEalDFLEQILTFNPMDRLTAEEALMHPYMSCySCPFDEPVsLHPFHIEDE 324
UBA_SIK1 cd14408
UBA domain found in salt-inducible kinase 1 (SIK1); SIK1, also called serine/threonine-protein ...
292-341 6.22e-18

UBA domain found in salt-inducible kinase 1 (SIK1); SIK1, also called serine/threonine-protein kinase SNF1-like kinase 1 (SNF1LK), is a serine/threonine kinase abundant in adrenal glands. It belongs to the AMP-activated protein kinases (AMPK) family involved in the regulation of metabolism during energy stress. SIK1 is required for myogenic differentiation. It is degraded by the proteasome in myoblasts which is regulated by cAMP signaling. Moreover, SIK1 acts as a class II histone deacetylase (HDAC) kinase, triggering the cytoplasmic export of the HDACs and activation of myocyte enhancer factor 2 (MEF2)-dependent transcription. It also regulates transcription through inhibitory phosphorylation of a family of cAMP responsive element binding protein (CREB) coactivators, called TORCs/CRTCs. In addition, SIK1 links LKB1 to p53-dependent anoikis and suppresses metastasis. It is also involved in a cell sodium-sensing network that regulates active sodium transport through a calcium-dependent process. SIK1 contains an N-terminal protein kinase catalytic domain followed by an ubiquitin-associated (UBA) domain and a putative PEST domain.


Pssm-ID: 270591  Cd Length: 50  Bit Score: 78.12  E-value: 6.22e-18
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 929654453 292 SIGEFNEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAIYFLLVERLKSHR 341
Cdd:cd14408    1 NLGDYSEQVLGIMQTLGIDRQRTVESLQNSSYNHFAAIYYLLLERLKEYR 50
STKc_GRK2 cd14223
Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs ...
20-312 6.37e-18

Catalytic domain of the Serine/Threonine Kinase, G protein-coupled Receptor Kinase 2; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. GRK2, also called beta-adrenergic receptor kinase (beta-ARK) or beta-ARK1, is important in regulating several cardiac receptor responses. It plays a role in cardiac development and in hypertension. Deletion of GRK2 in mice results in embryonic lethality, caused by hypoplasia of the ventricular myocardium. GRK2 also plays important roles in the liver (as a regulator of portal blood pressure), in immune cells, and in the nervous system. Altered GRK2 expression has been reported in several disorders including major depression, schizophrenia, bipolar disorder, and Parkinsonism. GRK2 contains an N-terminal RGS homology (RH) domain, a central catalytic domain, and C-terminal pleckstrin homology (PH) domain that mediates PIP2 and G protein betagamma-subunit translocation to the membrane. GRKs phosphorylate and regulate G protein-coupled receptors (GPCRs), the largest superfamily of cell surface receptors which regulate some part of nearly all physiological functions. Phosphorylated GPCRs bind to arrestins, which prevents further G protein signaling despite the presence of activating ligand. TheGRK2 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271125 [Multi-domain]  Cd Length: 321  Bit Score: 85.87  E-value: 6.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKML----DHPHIIKLYQVMETKSMLYLV 95
Cdd:cd14223    2 FSVHRIIGRGGFGEVYGCRKADTGKMYAMKCLDKKRIKMKQGETLALNERIMLSLvstgDCPFIVCMSYAFHTPDKLSFI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLAT 175
Cdd:cd14223   82 LDLMNGGDLHYHLSQHGVFSEAEMRFYAAEIILGLEHMHSRFVVYRDLKPANILLDEFGHVRISDLGLACDFSKKKPHAS 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 wCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPI---LRQRVLEGRFRIPYFMSEDCEHLIRRML 252
Cdd:cd14223  162 -VGTHGYMAPEVLQKGVAYDSSADWFSLGCMLFKLLRGHSPFRQHKTKDkheIDRMTLTMAVELPDSFSPELRSLLEGLL 240
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 929654453 253 VLDPSKRLTI-----AQIKEH------KWMLIEVPVQRPVLYPQEQENEPS----IGEFNEQVLRLMHSLGIDQQ 312
Cdd:cd14223  241 QRDVNRRLGCmgrgaQEVKEEpffrglDWQMVFLQKYPPPLIPPRGEVNAAdafdIGSFDEEDTKGIKLLESDQE 315
PTKc_FGFR2 cd05101
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs ...
46-267 7.26e-18

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. There are many splice variants of FGFR2 which show differential expression and binding to FGF ligands. Disruption of either FGFR2 or FGFR2b is lethal in mice, due to defects in the placenta or severe impairment of tissue development including lung, limb, and thyroid, respectively. Disruption of FGFR2c in mice results in defective bone and skull development. Genetic alterations of FGFR2 are associated with many human skeletal disorders including Apert syndrome, Crouzon syndrome, Jackson-Weiss syndrome, and Pfeiffer syndrome. FGFR2 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 FGFR2 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: 270679 [Multi-domain]  Cd Length: 313  Bit Score: 85.45  E-value: 7.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  46 VAIKIIdKSQLDAVNLEKIYREVQIMKML-DHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDYLANH-----------GR 113
Cdd:cd05101   59 VAVKML-KDDATEKDLSDLVSEMEMMKMIgKHKNIINLLGACTQDGPLYVIVEYASKGNLREYLRARrppgmeysydiNR 137
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 114 LNESEARRK-----FWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG------NFFK---SGELLATWcgs 179
Cdd:cd05101  138 VPEEQMTFKdlvscTYQLARGMEYLASQKCIHRDLAARNVLVTENNVMKIADFGLArdinniDYYKkttNGRLPVKW--- 214
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 ppyAAPEVFEGQQYEGpQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEG-RFRIP-------YFMSEDCEHLIrr 250
Cdd:cd05101  215 ---MAPEALFDRVYTH-QSDVWSFGVLMWeIFTLGGSPYPGIPVEELFKLLKEGhRMDKPanctnelYMMMRDCWHAV-- 288
                        250
                 ....*....|....*..
gi 929654453 251 mlvldPSKRLTIAQIKE 267
Cdd:cd05101  289 -----PSQRPTFKQLVE 300
STKc_JNK3 cd07874
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 3; STKs catalyze the ...
26-302 7.55e-18

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: 86.30  E-value: 7.55e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSML------YLVTEY- 98
Cdd:cd07874   25 IGSGAQGIVCAAYDAVLDRNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIISLLNVFTPQKSLeefqdvYLVMELm 104
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 -AKNGEIFDYLANHGRLNesearRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWC 177
Cdd:cd07874  105 dANLCQVIQMELDHERMS-----YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYV 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 GSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGPTLPILRQRVLEGR-FRIPYFMSE-------------- 242
Cdd:cd07874  180 VTRYYRAPEVILGMGYK-ENVDIWSVGCIMGEMVRHKILFPGRDYIDQWNKVIEQLgTPCPEFMKKlqptvrnyvenrpk 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 243 -----------------DCEH----------LIRRMLVLDPSKRLTIAQIKEHKWMLI-----EVPVQRPVLYPQE-QEN 289
Cdd:cd07874  259 yagltfpklfpdslfpaDSEHnklkasqardLLSKMLVIDPAKRISVDEALQHPYINVwydpaEVEAPPPQIYDKQlDER 338
                        330
                 ....*....|...
gi 929654453 290 EPSIGEFNEQVLR 302
Cdd:cd07874  339 EHTIEEWKELIYK 351
STKc_WNK3 cd14031
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 3; STKs catalyze ...
20-217 8.42e-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: 84.77  E-value: 8.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEgtLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLY----QVMETKSMLYLV 95
Cdd:cd14031   14 FDIE--LGRGAFKTVYKGLDTETWVEVAWCELQDRKLTKAEQQRFKEEAEMLKGLQHPNIVRFYdsweSVLKGKKCIVLV 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRK--IVHRDLKAENLLLDNNM-NIKIADFGFGNFFKSgEL 172
Cdd:cd14031   92 TELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLATLMRT-SF 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 173 LATWCGSPPYAAPEVFEgQQYEgPQLDIWSMGVVLYVLVCGALPF 217
Cdd:cd14031  171 AKSVIGTPEFMAPEMYE-EHYD-ESVDVYAFGMCMLEMATSEYPY 213
STKc_ERK5 cd07855
Catalytic domain of the Serine/Threonine Kinase, Extracellular signal-Regulated Kinase 5; ...
20-268 9.84e-18

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: 85.50  E-value: 9.84e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSML------Y 93
Cdd:cd07855    7 YEPIETIGSGAYGVVCSAIDTKSGQKVAIKKIPNAFDVVTTAKRTLRELKILRHFKHDNIIAIRDILRPKVPYadfkdvY 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKNgEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG--------- 164
Cdd:cd07855   87 VVLDLMES-DLHHIIHSDQPLTLEHIRYFLYQLLRGLKYIHSANVIHRDLKPSNLLVNENCELKIGDFGMArglctspee 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 165 -NFFKSgELLATwcgsPPYAAPEV-FEGQQYEgPQLDIWSMGVVLYVLVCGALPFDG----------------PTLPILR 226
Cdd:cd07855  166 hKYFMT-EYVAT----RWYRAPELmLSLPEYT-QAIDMWSVGCIFAEMLGRRQLFPGknyvhqlqliltvlgtPSQAVIN 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 929654453 227 Q----RV------LEGRFRIPY---FMSEDCE--HLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd07855  240 AigadRVrryiqnLPNKQPVPWetlYPKADQQalDLLSQMLRFDPSERITVAEALQH 296
PTKc_EphR_A10 cd05064
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A10; PTKs catalyze the ...
22-265 1.18e-17

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: 83.82  E-value: 1.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  22 IEGTLGKGNFAVVKLGRHRI-TKTE--VAIKIIDKSQLDAVNLeKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd05064    9 IERILGTGRFGELCRGCLKLpSKRElpVAIHTLRAGCSDKQRR-GFLAEALTLGQFDHSNIVRLEGVITRGNTMMIVTEY 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWC 177
Cdd:cd05064   88 MSNGALDSFLRKHeGQLVAGQLMGMLPGLASGMKYLSEMGYVHKGLAAHKVLVNSDLVCKISGFRRLQEDKSEAIYTTMS 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 GSPP--YAAPEVFEGQQYEgPQLDIWSMGVVLY-VLVCGALPF-DGPTLPILrqRVLEGRFRIPyfMSEDCEHLIRRMLV 253
Cdd:cd05064  168 GKSPvlWAAPEAIQYHHFS-SASDVWSFGIVMWeVMSYGERPYwDMSGQDVI--KAVEDGFRLP--APRNCPNLLHQLML 242
                        250
                 ....*....|....*.
gi 929654453 254 ----LDPSKRLTIAQI 265
Cdd:cd05064  243 dcwqKERGERPRFSQI 258
STKc_WNK2_like cd14032
Catalytic domain of With No Lysine (WNK) 2-like Serine/Threonine kinases; STKs catalyze the ...
20-217 1.33e-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: 83.97  E-value: 1.33e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEgtLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMET----KSMLYLV 95
Cdd:cd14032    5 FDIE--LGRGSFKTVYKGLDTETWVEVAWCELQDRKLTKVERQRFKEEAEMLKGLQHPNIVRFYDFWEScakgKRCIVLV 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRK--IVHRDLKAENLLLDNNM-NIKIADFGFGNfFKSGEL 172
Cdd:cd14032   83 TELMTSGTLKTYLKRFKVMKPKVLRSWCRQILKGLLFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLAT-LKRASF 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 173 LATWCGSPPYAAPEVFEgqQYEGPQLDIWSMGVVLYVLVCGALPF 217
Cdd:cd14032  162 AKSVIGTPEFMAPEMYE--EHYDESVDVYAFGMCMLEMATSEYPY 204
PTKc_EphR_B cd05065
Catalytic domain of the Protein Tyrosine Kinases, Class EphB Ephrin Receptors; PTKs catalyze ...
15-217 1.49e-17

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: 83.77  E-value: 1.49e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  15 VRVGFYDIEGTLGKGNFAVVKLGRHRIT---KTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSM 91
Cdd:cd05065    1 IDVSCVKIEEVIGAGEFGEVCRGRLKLPgkrEIFVAIKTL-KSGYTEKQRRDFLSEASIMGQFDHPNIIHLEGVVTKSRP 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  92 LYLVTEYAKNGEIFDYL-ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSG 170
Cdd:cd05065   80 VMIITEFMENGALDSFLrQNDGQFTVIQLVGMLRGIAAGMKYLSEMNYVHRDLAARNILVNSNLVCKVSDFGLSRFLEDD 159
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 929654453 171 ELLATWCGS-----P-PYAAPEVFEGQQYEGPQlDIWSMGVVLY-VLVCGALPF 217
Cdd:cd05065  160 TSDPTYTSSlggkiPiRWTAPEAIAYRKFTSAS-DVWSYGIVMWeVMSYGERPY 212
PKc_MKK4 cd06616
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
23-219 1.51e-17

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: 84.34  E-value: 1.51e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  23 EGTLGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKIYREVQ-IMKMLDHPHIIKLY-------------QVMET 88
Cdd:cd06616   11 LGEIGRGAFGTVNKMLHKPSGTIMAVKRI-RSTVDEKEQKRLLMDLDvVMRSSDCPYIVKFYgalfregdcwicmELMDI 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  89 kSM--LYLvteyakngeiFDYLANHGRLNEsearrkfwQILSAVDYCHGR---------KIVHRDLKAENLLLDNNMNIK 157
Cdd:cd06616   90 -SLdkFYK----------YVYEVLDSVIPE--------EILGKIAVATVKalnylkeelKIIHRDVKPSNILLDRNGNIK 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 158 IADFGFgnffkSGELLATWC-----GSPPYAAPEVFEGQQYEGP---QLDIWSMGVVLYVLVCGALPFDG 219
Cdd:cd06616  151 LCDFGI-----SGQLVDSIAktrdaGCRPYMAPERIDPSASRDGydvRSDVWSLGITLYEVATGKFPYPK 215
PTKc_FGFR4 cd05099
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs ...
26-267 1.53e-17

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 4; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Unlike other FGFRs, there is only one splice form of FGFR4. It binds FGF1, FGF2, FGF6, FGF19, and FGF23. FGF19 is a selective ligand for FGFR4. Although disruption of FGFR4 in mice causes no obvious phenotype, in vivo inhibition of FGFR4 in cultured skeletal muscle cells resulted in an arrest of muscle progenitor differentiation. FGF6 and FGFR4 are uniquely expressed in myofibers and satellite cells. FGF6/FGFR4 signaling appears to play a key role in the regulation of muscle regeneration. A polymorphism in FGFR4 is found in head and neck squamous cell carcinoma. FGFR4 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 FGFR4 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: 133230 [Multi-domain]  Cd Length: 314  Bit Score: 84.63  E-value: 1.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFA-VVKLGRHRITK------TEVAIKIIDKSQLDAvNLEKIYREVQIMKMLD-HPHIIKLYQVMETKSMLYLVTE 97
Cdd:cd05099   20 LGEGCFGqVVRAEAYGIDKsrpdqtVTVAVKMLKDNATDK-DLADLISEMELMKLIGkHKNIINLLGVCTQEGPLYVIVE 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYL----------------ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADF 161
Cdd:cd05099   99 YAAKGNLREFLrarrppgpdytfditkVPEEQLSFKDLVSCAYQVARGMEYLESRRCIHRDLAARNVLVTEDNVMKIADF 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 162 GFG------NFFK---SGELLATWcgsppyAAPEVFEGQQYEGpQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLE 231
Cdd:cd05099  179 GLArgvhdiDYYKktsNGRLPVKW------MAPEALFDRVYTH-QSDVWSFGILMWeIFTLGGSPYPGIPVEELFKLLRE 251
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 929654453 232 G-RFRIP-------YFMSEDCEHLIrrmlvldPSKRLTIAQIKE 267
Cdd:cd05099  252 GhRMDKPsncthelYMLMRECWHAV-------PTQRPTFKQLVE 288
STKc_NLK cd07853
Catalytic domain of the Serine/Threonine Kinase, Nemo-Like Kinase; STKs catalyze the transfer ...
46-271 1.99e-17

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: 85.18  E-value: 1.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  46 VAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSM-----LYLVTEYAKNgEIFDYLANHGRLNESEAR 120
Cdd:cd07853   28 VALKKMPNVFQNLVSCKRVFRELKMLCFFKHDNVLSALDILQPPHIdpfeeIYVVTELMQS-DLHKIIVSPQPLSSDHVK 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 121 RKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK-------SGELLATWcgsppYAAPEVFEGQQY 193
Cdd:cd07853  107 VFLYQILRGLKYLHSAGILHRDIKPGNLLVNSNCVLKICDFGLARVEEpdeskhmTQEVVTQY-----YRAPEILMGSRH 181
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 194 EGPQLDIWSMGVVLYVLVCGALPFDG----------------PTLPIL-------RQRVLEGRFRIP-----YFMS---- 241
Cdd:cd07853  182 YTSAVDIWSVGCIFAELLGRRILFQAqspiqqldlitdllgtPSLEAMrsacegaRAHILRGPHKPPslpvlYTLSsqat 261
                        250       260       270
                 ....*....|....*....|....*....|
gi 929654453 242 EDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd07853  262 HEAVHLLCRMLVFDPDKRISAADALAHPYL 291
STKc_JNK1 cd07875
Catalytic domain of the Serine/Threonine Kinase, c-Jun N-terminal Kinase 1; STKs catalyze the ...
26-302 2.34e-17

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: 84.71  E-value: 2.34e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQV------METKSMLYLVTEY- 98
Cdd:cd07875   32 IGSGAQGIVCAAYDAILERNVAIKKLSRPFQNQTHAKRAYRELVLMKCVNHKNIIGLLNVftpqksLEEFQDVYIVMELm 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 -AKNGEIFDYLANHGRLNesearRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWC 177
Cdd:cd07875  112 dANLCQVIQMELDHERMS-----YLLYQMLCGIKHLHSAGIIHRDLKPSNIVVKSDCTLKILDFGLARTAGTSFMMTPYV 186
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 GSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDG-----------------------PTLPILRQRVlEGRF 234
Cdd:cd07875  187 VTRYYRAPEVILGMGYK-ENVDIWSVGCIMGEMIKGGVLFPGtdhidqwnkvieqlgtpcpefmkKLQPTVRTYV-ENRP 264
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 235 RIPYFMSE----------DCEH----------LIRRMLVLDPSKRLTIAQIKEHKWMLI-------EVPvqrPVLYPQEQ 287
Cdd:cd07875  265 KYAGYSFEklfpdvlfpaDSEHnklkasqardLLSKMLVIDASKRISVDEALQHPYINVwydpseaEAP---PPKIPDKQ 341
                        330
                 ....*....|....*..
gi 929654453 288 --ENEPSIGEFNEQVLR 302
Cdd:cd07875  342 ldEREHTIEEWKELIYK 358
PTKc_Tyro3 cd05074
Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the ...
25-267 2.52e-17

Catalytic domain of the Protein Tyrosine Kinase, Tyro3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tyro3 (or Sky) is predominantly expressed in the central nervous system and the brain, and functions as a neurotrophic factor. It is also expressed in osteoclasts and has a role in bone resorption. Tyro3 is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Tyro3 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: 270659 [Multi-domain]  Cd Length: 284  Bit Score: 83.43  E-value: 2.52e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVK---LGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQV---METKSML---YLV 95
Cdd:cd05074   16 MLGKGEFGSVReaqLKSEDGSFQKVAVKMLKADIFSSSDIEEFLREAACMKEFDHPNVIKLIGVslrSRAKGRLpipMVI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLAnHGRLNESEAR-------RKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK 168
Cdd:cd05074   96 LPFMKHGDLHTFLL-MSRIGEEPFTlplqtlvRFMIDIASGMEYLSSKNFIHRDLAARNCMLNENMTVCVADFGLSKKIY 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 SGELLATWCGSP---PYAAPEVFEGQQYEgPQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEG-RFRIPYFMSED 243
Cdd:cd05074  175 SGDYYRQGCASKlpvKWLALESLADNVYT-THSDVWAFGVTMWeIMTRGQTPYAGVENSEIYNYLIKGnRLKQPPDCLED 253
                        250       260
                 ....*....|....*....|....
gi 929654453 244 CEHLIRRMLVLDPSKRLTIAQIKE 267
Cdd:cd05074  254 VYELMCQCWSPEPKCRPSFQHLRD 277
STKc_Raf cd14062
Catalytic domain of the Serine/Threonine Kinases, Raf (Rapidly Accelerated Fibrosarcoma) ...
26-219 2.76e-17

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: 82.44  E-value: 2.76e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGR-HRItkteVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMeTKSMLYLVTEYAKNGEI 104
Cdd:cd14062    1 IGSGSFGTVYKGRwHGD----VAVKKLNVTDPTPSQLQAFKNEVAVLRKTRHVNILLFMGYM-TKPQLAIVTQWCEGSSL 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGRLNESE-----ARrkfwQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGfgnffksgelLAT---- 175
Cdd:cd14062   76 YKHLHVLETKFEMLqlidiAR----QTAQGMDYLHAKNIIHRDLKSNNIFLHEDLTVKIGDFG----------LATvktr 141
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 929654453 176 WCGSPP---------YAAPEVFEGQQYE--GPQLDIWSMGVVLYVLVCGALPFDG 219
Cdd:cd14062  142 WSGSQQfeqptgsilWMAPEVIRMQDENpySFQSDVYAFGIVLYELLTGQLPYSH 196
STKc_MPK1 cd07857
Catalytic domain of the Serine/Threonine Kinase, Fungal Mitogen-Activated Protein Kinase MPK1; ...
20-302 2.91e-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: 83.99  E-value: 2.91e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTE--VAIK----IIDKSQLdavnLEKIYREVQIMKML-DHPHIIKLYQvMEtksml 92
Cdd:cd07857    2 YELIKELGQGAYGIVCSARNAETSEEetVAIKkitnVFSKKIL----AKRALRELKLLRHFrGHKNITCLYD-MD----- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  93 yLVTEYAKNG-----EIFDY-----LANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG 162
Cdd:cd07857   72 -IVFPGNFNElylyeELMEAdlhqiIRSGQPLTDAHFQSFIYQILCGLKYIHSANVLHRDLKPGNLLVNADCELKICDFG 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 163 FG-----NFFKSGELLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDG----------------PT 221
Cdd:cd07857  151 LArgfseNPGENAGFMTEYVATRWYRAPEIMLSFQSYTKAIDVWSVGCILAELLGRKPVFKGkdyvdqlnqilqvlgtPD 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 222 LPILR----QRVLEGRFRIPY-----------FMSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWMLI-EVPVQRPVL--- 282
Cdd:cd07857  231 EETLSrigsPKAQNYIRSLPNipkkpfesifpNANPLALDLLEKLLAFDPTKRISVEEALEHPYLAIwHDPDDEPVCqkp 310
                        330       340
                 ....*....|....*....|
gi 929654453 283 YPQEQENEPSIGEFNEQVLR 302
Cdd:cd07857  311 FDFSFESEDSMEELRDMIIE 330
PKc_MEK1 cd06650
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
26-220 2.95e-17

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: 83.95  E-value: 2.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06650   13 LGAGNGGVVFKVSHKPSGLVMARKLIHLEIKPAIR-NQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHGR-KIVHRDLKAENLLLDNNMNIKIADFGFgnffkSGELL----ATWCGSP 180
Cdd:cd06650   92 QVLKKAGRIPEQILGKVSIAVIKGLTYLREKhKIMHRDVKPSNILVNSRGEIKLCDFGV-----SGQLIdsmaNSFVGTR 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 929654453 181 PYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGP 220
Cdd:cd06650  167 SYMSPERLQGTHYS-VQSDIWSMGLSLVEMAVGRYPIPPP 205
PKc_TNNI3K cd14064
Catalytic domain of the Dual-specificity protein kinase, TNNI3-interacting kinase; ...
26-265 3.27e-17

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: 82.19  E-value: 3.27e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRitKTEVAIK------IIDKSQLDAvnlekIYREVQIMKMLDHPHIIKLY-QVMETKSMLYLVTEY 98
Cdd:cd14064    1 IGSGSFGKVYKGRCR--NKIVAIKryrantYCSKSDVDM-----FCREVSILCRLNHPCVIQFVgACLDDPSQFAIVTQY 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLANHGRLNESEARrkfwqILSAVDYCHG--------RKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKS- 169
Cdd:cd14064   74 VSGGSLFSLLHEQKRVIDLQSK-----LIIAVDVAKGmeylhnltQPIIHRDLNSHNILLYEDGHAVVADFGESRFLQSl 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 170 -GELLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFD--GPTLPILRQRVLEGRFRIPYFMSEDCEH 246
Cdd:cd14064  149 dEDNMTKQPGNLRWMAPEVFTQCTRYSIKADVFSYALCLWELLTGEIPFAhlKPAAAAADMAYHHIRPPIGYSIPKPISS 228
                        250
                 ....*....|....*....
gi 929654453 247 LIRRMLVLDPSKRLTIAQI 265
Cdd:cd14064  229 LLMRGWNAEPESRPSFVEI 247
STKc_ACVR2 cd14053
Catalytic domain of the Serine/Threonine Kinase, Activin Type II Receptor; STKs catalyze the ...
28-252 3.74e-17

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: 83.15  E-value: 3.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  28 KGNFAVVKLGRhrITKTEVAIKIIDKSQLDA-VNLEKIYREvQIMKmldHPHIIKLY---QVME-TKSMLYLVTEYAKNG 102
Cdd:cd14053    5 RGRFGAVWKAQ--YLNRLVAVKIFPLQEKQSwLTEREIYSL-PGMK---HENILQFIgaeKHGEsLEAEYWLITEFHERG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHgRLNESEARRKFWQILSAVDYCH--------GRK--IVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL 172
Cdd:cd14053   79 SLCDYLKGN-VISWNELCKIAESMARGLAYLHedipatngGHKpsIAHRDFKSKNVLLKSDLTACIADFGLALKFEPGKS 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 173 LAT---WCGSPPYAAPEVFEG----QQYEGPQLDIWSMGVVLYVLV--CGA---------LPF-----DGPTLPILRQRV 229
Cdd:cd14053  158 CGDthgQVGTRRYMAPEVLEGainfTRDAFLRIDMYAMGLVLWELLsrCSVhdgpvdeyqLPFeeevgQHPTLEDMQECV 237
                        250       260
                 ....*....|....*....|...
gi 929654453 230 LEGRFRiPYFMSEDCEHLIRRML 252
Cdd:cd14053  238 VHKKLR-PQIRDEWRKHPGLAQL 259
PKc_TESK cd14155
Catalytic domain of the Dual-specificity protein kinase, Testicular protein kinase; ...
26-272 3.77e-17

Catalytic domain of the Dual-specificity protein kinase, Testicular 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. TESK proteins phosphorylate cofilin and induce actin cytoskeletal reorganization. In the Drosphila eye, TESK is required for epithelial cell organization. Mammals contain two TESK proteins, TESK1 and TESK2, which are highly expressed in testis and play roles in spermatogenesis. TESK1 is found in testicular germ cells while TESK2 is expressed mainly in nongerminal Sertoli cells. TESK1 is stimulated by integrin-mediated signaling pathways. It regulates cell spreading and focal adhesion formation. The TESK 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: 271057 [Multi-domain]  Cd Length: 253  Bit Score: 82.14  E-value: 3.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIidkSQLDAvNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14155    1 IGSGFFSEVYKVRHRTSGQVMALKM---NTLSS-NRANMLREVQLMNRLSHPNILRFMGVCVHQGQLHALTEYINGGNLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL---DNNMNIKIADFGFGNFFKS----GELLATwCG 178
Cdd:cd14155   77 QLLDSNEPLSWTVRVKLALDIARGLSYLHSKGIFHRDLTSKNCLIkrdENGYTAVVGDFGLAEKIPDysdgKEKLAV-VG 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 SPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVcGALPFDGPTLPilrqRVLEGRFRIPYF--MSEDCEHLIRRMLV--- 253
Cdd:cd14155  156 SPYWMAPEVLRGEPYN-EKADVFSYGIILCEII-ARIQADPDYLP----RTEDFGLDYDAFqhMVGDCPPDFLQLAFncc 229
                        250       260
                 ....*....|....*....|.
gi 929654453 254 -LDPSKRLTIAQIKEH-KWML 272
Cdd:cd14155  230 nMDPKSRPSFHDIVKTlEEIL 250
PKc_MKK7 cd06618
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-activated protein Kinase ...
24-273 3.95e-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: 83.19  E-value: 3.95e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  24 GTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQlDAVNLEKIYREVQI-MKMLDHPHIIKLYQVMETKSMLYLVTEyaKNG 102
Cdd:cd06618   21 GEIGSGTCGQVYKMRHKKTGHVMAVKQMRRSG-NKEENKRILMDLDVvLKSHDCPYIVKCYGYFITDSDVFICME--LMS 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLAN--HGRLNESEARRKFWQILSAVDYC---HGrkIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWC 177
Cdd:cd06618   98 TCLDKLLKriQGPIPEDILGKMTVSIVKALHYLkekHG--VIHRDVKPSNILLDESGNVKLCDFGISGRLVDSKAKTRSA 175
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 178 GSPPYAAPEVFEGQQYegPQLDI----WSMGVVLYVLVCGALPFDGPT--LPILRQRVLEGRFRIPYFM--SEDCEHLIR 249
Cdd:cd06618  176 GCAAYMAPERIDPPDN--PKYDIradvWSLGISLVELATGQFPYRNCKteFEVLTKILNEEPPSLPPNEgfSPDFCSFVD 253
                        250       260
                 ....*....|....*....|....
gi 929654453 250 RMLVLDPSKRLTIAQIKEHKWMLI 273
Cdd:cd06618  254 LCLTKDHRYRPKYRELLQHPFIRR 277
PK_STRAD cd08216
Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows ...
26-229 5.54e-17

Pseudokinase domain of STE20-related kinase adapter protein; The pseudokinase domain shows similarity to protein kinases but lacks crucial residues for catalytic activity. STRAD forms a complex with the scaffolding protein MO25, and the serine/threonine kinase (STK), LKB1, resulting in the activation of the kinase. In the complex, LKB1 phosphorylates and activates adenosine monophosphate-activated protein kinases (AMPKs), which regulate cell energy metabolism and cell polarity. LKB1 is a tumor suppressor linked to the rare inherited disease, Peutz-Jeghers syndrome, which is characterized by a predisposition to benign polyps and hyperpigmentation of the buccal mucosa. There are two forms of STRAD, alpha and beta, that complex with LKB1 and MO25. The structure of STRAD-alpha is available and shows that this protein binds ATP, has an ordered activation loop, and adopts a closed conformation typical of fully active protein kinases. It does not possess activity due to nonconservative substitutions of essential catalytic residues. ATP binding enhances the affinity of STRAD for MO25. The conformation of STRAD-alpha stabilized through ATP and MO25 may be needed to activate LKB1. The STRAD 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: 270856 [Multi-domain]  Cd Length: 315  Bit Score: 83.11  E-value: 5.54e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNF--AVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd08216    6 IGKCFKggGVVHLAKHKPTNTLVAVKKINLESDSKEDLKFLQQEILTSRQLQHPNILPYVTSFVVDNDLYVVTPLMAYGS 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANH---GrLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG-NFFKSGELLATWCGS 179
Cdd:cd08216   86 CRDLLKTHfpeG-LPELAIAFILRDVLNALEYIHSKGYIHRSVKASHILISGDGKVVLSGLRYAySMVKHGKRQRVVHDF 164
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 P-------PYAAPEVFEgQQYEG--PQLDIWSMGVVLYVLVCGALPF-DGPTLPILRQRV 229
Cdd:cd08216  165 PksseknlPWLSPEVLQ-QNLLGynEKSDIYSVGITACELANGVVPFsDMPATQMLLEKV 223
STKc_MLK3 cd14147
Catalytic domain of the Serine/Threonine Kinase, Mixed Lineage Kinase 3; STKs catalyze the ...
22-219 5.73e-17

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: 82.00  E-value: 5.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  22 IEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKN 101
Cdd:cd14147    7 LEEVIGIGGFGKVYRGSWRGELVAVKAARQDPDEDISVTAESVRQEARLFAMLAHPNIIALKAVCLEEPNLCLVMEYAAG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLAN-----HGRLNesearrkfW--QILSAVDYCHGRKIV---HRDLKAENLLLDNN--------MNIKIADFGF 163
Cdd:cd14147   87 GPLSRALAGrrvppHVLVN--------WavQIARGMHYLHCEALVpviHRDLKSNNILLLQPienddmehKTLKITDFGL 158
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 929654453 164 GNFFKSGELLATwCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDG 219
Cdd:cd14147  159 AREWHKTTQMSA-AGTYAWMAPEVIKASTF-SKGSDVWSFGVLLWELLTGEVPYRG 212
STK_BAK1_like cd14664
Catalytic domain of the Serine/Threonine Kinase, BRI1 associated kinase 1 and related STKs; ...
26-218 6.01e-17

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: 81.77  E-value: 6.01e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRiTKTEVAIKIIDKSQLDAVNLEkIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14664    1 IGRGGAGTVYKGVMP-NGTLVAVKRLKGEGTQGGDHG-FQAEIQTLGMIRHRNIVRLRGYCSNPTTNLLVYEYMPNGSLG 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLanHGRLNES-----EARRKFwqilsAVDYCHG---------RKIVHRDLKAENLLLDNNMNIKIADFGFGNFF--KS 169
Cdd:cd14664   79 ELL--HSRPESQppldwETRQRI-----ALGSARGlaylhhdcsPLIIHRDVKSNNILLDEEFEAHVADFGLAKLMddKD 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 929654453 170 GELLATWCGSPPYAAPE-VFEGQQYEgpQLDIWSMGVVLYVLVCGALPFD 218
Cdd:cd14664  152 SHVMSSVAGSYGYIAPEyAYTGKVSE--KSDVYSYGVVLLELITGKRPFD 199
STKc_PRP4 cd14135
Catalytic domain of the Serine/Threonine Kinase, Pre-mRNA-Processing factor 4; STKs catalyze ...
20-269 7.17e-17

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: 82.66  E-value: 7.17e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFA-VVK---LGRhriTKTEVAIKIIDKSQLdavnLEKI-YREVQIMKML------DHPHIIKLYQVMET 88
Cdd:cd14135    2 YRVYGYLGKGVFSnVVRardLAR---GNQEVAIKIIRNNEL----MHKAgLKELEILKKLndadpdDKKHCIRLLRHFEH 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  89 KSMLYLVTE-YAKNgeIFDYLANHGR---LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMN-IKIADFGF 163
Cdd:cd14135   75 KNHLCLVFEsLSMN--LREVLKKYGKnvgLNIKAVRSYAQQLFLALKHLKKCNILHADIKPDNILVNEKKNtLKLCDFGS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 164 GNFFKSGELLAtWCGSPPYAAPEVFEGQQYEGPqLDIWSMGVVLYVLVCGALPFDGPT--------------LP--ILRQ 227
Cdd:cd14135  153 ASDIGENEITP-YLVSRFYRAPEIILGLPYDYP-IDMWSVGCTLYELYTGKILFPGKTnnhmlklmmdlkgkFPkkMLRK 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 228 rvleGRFRIPYFmSEDC-----EH--------------------------------------------LIRRMLVLDPSK 258
Cdd:cd14135  231 ----GQFKDQHF-DENLnfiyrEVdkvtkkevrrvmsdikptkdlktlligkqrlpdedrkkllqlkdLLDKCLMLDPEK 305
                        330
                 ....*....|.
gi 929654453 259 RLTIAQIKEHK 269
Cdd:cd14135  306 RITPNEALQHP 316
STKc_LATS1 cd05625
Catalytic domain of the Serine/Threonine Kinase, Large Tumor Suppressor 1; STKs catalyze the ...
25-217 8.99e-17

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: 83.17  E-value: 8.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVN-LEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd05625    8 TLGIGAFGEVCLARKVDTKALYATKTLRKKDVLLRNqVAHVKAERDILAEADNEWVVRLYYSFQDKDNLYFVMDYIPGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF---------GNFFKSGE--- 171
Cdd:cd05625   88 MMSLLIRMGVFPEDLARFYIAELTCAVESVHKMGFIHRDIKPDNILIDRDGHIKLTDFGLctgfrwthdSKYYQSGDhlr 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 ------------------------------------LLATWCGSPPYAAPEVFEGQQYEgpQL-DIWSMGVVLYVLVCGA 214
Cdd:cd05625  168 qdsmdfsnewgdpencrcgdrlkplerraarqhqrcLAHSLVGTPNYIAPEVLLRTGYT--QLcDWWSVGVILFEMLVGQ 245

                 ...
gi 929654453 215 LPF 217
Cdd:cd05625  246 PPF 248
STKc_B-Raf cd14151
Catalytic domain of the Serine/Threonine Kinase, B-Raf (Rapidly Accelerated Fibrosarcoma) ...
26-217 9.09e-17

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: 81.65  E-value: 9.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRitkTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIkLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14151   16 IGSGSFGTVYKGKWH---GDVAVKMLNVTAPTPQQLQAFKNEVGVLRKTRHVNIL-LFMGYSTKPQLAIVTQWCEGSSLY 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLanHGRLNESEARRKF---WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNF---FKSGELLATWCGS 179
Cdd:cd14151   92 HHL--HIIETKFEMIKLIdiaRQTAQGMDYLHAKSIIHRDLKSNNIFLHEDLTVKIGDFGLATVksrWSGSHQFEQLSGS 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 929654453 180 PPYAAPEVFEGQQyEGP---QLDIWSMGVVLYVLVCGALPF 217
Cdd:cd14151  170 ILWMAPEVIRMQD-KNPysfQSDVYAFGIVLYELMTGQLPY 209
PTKc_Src cd05071
Catalytic domain of the Protein Tyrosine Kinase, Src; PTKs catalyze the transfer of the ...
22-219 1.16e-16

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: 81.27  E-value: 1.16e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  22 IEGTLGKGNFAVVKLGRHRITkTEVAIKIIDKSQLDAvnlEKIYREVQIMKMLDHPHIIKLYQVMeTKSMLYLVTEYAKN 101
Cdd:cd05071   13 LEVKLGQGCFGEVWMGTWNGT-TRVAIKTLKPGTMSP---EAFLQEAQVMKKLRHEKLVQLYAVV-SEEPIYIVTEYMSK 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLANH--GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGS 179
Cdd:cd05071   88 GSLLDFLKGEmgKYLRLPQLVDMAAQIASGMAYVERMNYVHRDLRAANILVGENLVCKVADFGLARLIEDNEYTARQGAK 167
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 929654453 180 PP--YAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDG 219
Cdd:cd05071  168 FPikWTAPEAALYGRFT-IKSDVWSFGILLTELTTkGRVPYPG 209
STKc_LATS2 cd05626
Catalytic domain of the Protein Serine/Threonine Kinase, Large Tumor Suppressor 2; STKs ...
25-237 1.23e-16

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: 82.75  E-value: 1.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLGRHRITKTEVAIKIIDKSQ-LDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGE 103
Cdd:cd05626    8 TLGIGAFGEVCLACKVDTHALYAMKTLRKKDvLNRNQVAHVKAERDILAEADNEWVVKLYYSFQDKDNLYFVMDYIPGGD 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFF---------------- 167
Cdd:cd05626   88 MMSLLIRMEVFPEVLARFYIAELTLAIESVHKMGFIHRDIKPDNILIDLDGHIKLTDFGLCTGFrwthnskyyqkgshir 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 168 ----------------KSGELLAT----------------WCGSPPYAAPEVFEGQQYEgpQL-DIWSMGVVLYVLVCGA 214
Cdd:cd05626  168 qdsmepsdlwddvsncRCGDRLKTleqratkqhqrclahsLVGTPNYIAPEVLLRKGYT--QLcDWWSVGVILFEMLVGQ 245
                        250       260
                 ....*....|....*....|....*
gi 929654453 215 LPFDGPTLPILRQRVL--EGRFRIP 237
Cdd:cd05626  246 PPFLAPTPTETQLKVInwENTLHIP 270
PK_SCY1_like cd14011
Pseudokinase domain of Scy1-like proteins; The pseudokinase domain shows similarity to protein ...
37-270 1.28e-16

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: 81.21  E-value: 1.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  37 GRHRITKTEVAIKIIDKSQLDAVN-------LEKIYREVQIMKMLDHPHIIKLYQVMET-KSMLYLVTEyakngEIFDYL 108
Cdd:cd14011   15 GSKKSTKQEVSVFVFEKKQLEEYSkrdreqiLELLKRGVKQLTRLRHPRILTVQHPLEEsRESLAFATE-----PVFASL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 109 AN--HGRLNES--------------EARRKFWQILSAVDYCHGR-KIVHRDLKAENLLLDNNMNIKIADFGF-------- 163
Cdd:cd14011   90 ANvlGERDNMPspppelqdyklydvEIKYGLLQISEALSFLHNDvKLVHGNICPESVVINSNGEWKLAGFDFcisseqat 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 164 GNFFKSGEL---LATWCG-SPPYAAPEVFEgQQYEGPQLDIWSMGVVLYVLVC-GALPFDGPT--------LPILRQRVL 230
Cdd:cd14011  170 DQFPYFREYdpnLPPLAQpNLNYLAPEYIL-SKTCDPASDMFSLGVLIYAIYNkGKPLFDCVNnllsykknSNQLRQLSL 248
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 929654453 231 EGRFRIPYFMSEdcehLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd14011  249 SLLEKVPEELRD----HVKTLLNVTPEVRPDAEQLSKIPF 284
STKc_EIF2AK1_HRI cd14049
Catalytic domain of the Serine/Threonine kinase, eukaryotic translation Initiation Factor ...
26-207 1.40e-16

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: 81.01  E-value: 1.40e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQV-ME-TKSMLY---------- 93
Cdd:cd14049   14 LGKGGYGKVYKVRNKLDGQYYAIKKILIKKVTKRDCMKVLREVKVLAGLQHPNIVGYHTAwMEhVQLMLYiqmqlcelsl 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 ---LVTEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD-NNMNIKIADFG------- 162
Cdd:cd14049   94 wdwIVERNKRPCEEEFKSAPYTPVDVDVTTKILQQLLEGVTYIHSMGIVHRDLKPRNIFLHgSDIHVRIGDFGlacpdil 173
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 929654453 163 ------FGNFFKSGELLATWCGSPPYAAPEVFEGQQYEgPQLDIWSMGVVL 207
Cdd:cd14049  174 qdgndsTTMSRLNGLTHTSGVGTCLYAAPEQLEGSHYD-FKSDMYSIGVIL 223
STKc_Vps15 cd13980
Catalytic domain of the Serine/Threonine kinase, Vacuolar protein sorting-associated protein ...
26-261 1.77e-16

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


Pssm-ID: 270882 [Multi-domain]  Cd Length: 278  Bit Score: 80.76  E-value: 1.77e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRitKTEVAIKIIDKsQLDAVNLEKIYREVQ--IMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNgE 103
Cdd:cd13980    8 LGSTRFLKVARARHD--EGLVVVKVFVK-PDPALPLRSYKQRLEeiRDRLLELPNVLPFQKVIETDKAAYLIRQYVKY-N 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 104 IFDYLANHGRLNESEarRKF--WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG--------------FGNFF 167
Cdd:cd13980   84 LYDRISTRPFLNLIE--KKWiaFQLLHALNQCHKRGVCHGDIKTENVLVTSWNWVYLTDFAsfkptylpednpadFSYFF 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 168 KSGELLATwcgsppYAAPEVF-EGQQYEG----------PQLDIWSMGVVL-YVLVCGALPFDGPTLPILRQ------RV 229
Cdd:cd13980  162 DTSRRRTC------YIAPERFvDALTLDAeserrdgeltPAMDIFSLGCVIaELFTEGRPLFDLSQLLAYRKgefspeQV 235
                        250       260       270
                 ....*....|....*....|....*....|..
gi 929654453 230 LEgrfRIPyfmSEDCEHLIRRMLVLDPSKRLT 261
Cdd:cd13980  236 LE---KIE---DPNIRELILHMIQRDPSKRLS 261
STKc_TNIK cd06637
Catalytic domain of the Serine/Threonine Kinase, Traf2- and Nck-Interacting Kinase; STKs ...
18-281 1.82e-16

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: 80.92  E-value: 1.82e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  18 GFYDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAvnlEKIYREVQIMKMLDHPHIIKLYQVMETKS------- 90
Cdd:cd06637    6 GIFELVELVGNGTYGQVYKGRHVKTGQLAAIKVMDVTGDEE---EEIKQEINMLKKYSHHRNIATYYGAFIKKnppgmdd 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  91 MLYLVTEYAKNGEIFDYLANhgrlNESEARRKFW------QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF- 163
Cdd:cd06637   83 QLWLVMEFCGAGSVTDLIKN----TKGNTLKEEWiayicrEILRGLSHLHQHKVIHRDIKGQNVLLTENAEVKLVDFGVs 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 164 GNFFKSGELLATWCGSPPYAAPEVFEGQqyEGP------QLDIWSMGVVLYVLVCGALPFdgPTLPILRQRVLEGRFRIP 237
Cdd:cd06637  159 AQLDRTVGRRNTFIGTPYWMAPEVIACD--ENPdatydfKSDLWSLGITAIEMAEGAPPL--CDMHPMRALFLIPRNPAP 234
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 929654453 238 YFMSEDC----EHLIRRMLVLDPSKRLTIAQIKEHKWMLiEVPVQRPV 281
Cdd:cd06637  235 RLKSKKWskkfQSFIESCLVKNHSQRPSTEQLMKHPFIR-DQPNERQV 281
STKc_SRPK cd14136
Catalytic domain of the Serine/Threonine Kinase, Serine-aRginine Protein Kinase; STKs catalyze ...
14-271 2.43e-16

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: 81.08  E-value: 2.43e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  14 PVRVG--F---YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIdKSQ-------------LDAVNL--EKIYREVQIMKM 73
Cdd:cd14136    1 PVKIGevYngrYHVVRKLGWGHFSTVWLCWDLQNKRFVALKVV-KSAqhyteaaldeiklLKCVREadPKDPGREHVVQL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  74 LDH--------PHIIKLYQVMeTKSMLYLVTEYakngeifDYlanHGrLNESEARRKFWQILSAVDYCHGR-KIVHRDLK 144
Cdd:cd14136   80 LDDfkhtgpngTHVCMVFEVL-GPNLLKLIKRY-------NY---RG-IPLPLVKKIARQVLQGLDYLHTKcGIIHTDIK 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 145 AENLLLD-NNMNIKIADfgFGNffksgellATWCGSP--------PYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGAL 215
Cdd:cd14136  148 PENVLLCiSKIEVKIAD--LGN--------ACWTDKHftediqtrQYRSPEVILGAGY-GTPADIWSTACMAFELATGDY 216
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 216 PFDgP------------------TL-PILRQRVLEGRFRIPYFMSEDCEHLIRR-------------------------- 250
Cdd:cd14136  217 LFD-PhsgedysrdedhlaliieLLgRIPRSIILSGKYSREFFNRKGELRHISKlkpwpledvlvekykwskeeakefas 295
                        330       340
                 ....*....|....*....|....*
gi 929654453 251 ----MLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14136  296 fllpMLEYDPEKRATAAQCLQHPWL 320
PTKc_FGFR3 cd05100
Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs ...
4-267 3.00e-16

Catalytic domain of the Protein Tyrosine Kinase, Fibroblast Growth Factor Receptor 3; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Many FGFR3 splice variants have been reported with the IIIb and IIIc isoforms being the predominant forms. FGFR3 IIIc is the isoform expressed in chondrocytes, the cells affected in dwarfism, while IIIb is expressed in epithelial cells. FGFR3 ligands include FGF1, FGF2, FGF4, FGF8, FGF9, and FGF23. It is a negative regulator of long bone growth. In the cochlear duct and in the lens, FGFR3 is involved in differentiation while it appears to have a role in cell proliferation in epithelial cells. Germline mutations in FGFR3 are associated with skeletal disorders including several forms of dwarfism. Some missense mutations are associated with multiple myeloma and carcinomas of the bladder and cervix. Overexpression of FGFR3 is found in thyroid carcinoma. FGFR3 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 FGFR3 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: 173652 [Multi-domain]  Cd Length: 334  Bit Score: 81.22  E-value: 3.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   4 ADGPRHLQRGPVRVGFYDIEGTLGKGNFA-VVKLGRHRITK-TEVAIKIIDKSQLDAvNLEKIYREVQIMKML-DHPHII 80
Cdd:cd05100    3 ADPKWELSRTRLTLGKPLGEGCFGQVVMAeAIGIDKDKPNKpVTVAVKMLKDDATDK-DLSDLVSEMEMMKMIgKHKNII 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  81 KLYQVMETKSMLYLVTEYAKNGEI-----------FDYLANHGRLNESEARRK-----FWQILSAVDYCHGRKIVHRDLK 144
Cdd:cd05100   82 NLLGACTQDGPLYVLVEYASKGNLreylrarrppgMDYSFDTCKLPEEQLTFKdlvscAYQVARGMEYLASQKCIHRDLA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 145 AENLLLDNNMNIKIADFGFG------NFFK---SGELLATWcgsppyAAPEVFEGQQYEGpQLDIWSMGVVLY-VLVCGA 214
Cdd:cd05100  162 ARNVLVTEDNVMKIADFGLArdvhniDYYKkttNGRLPVKW------MAPEALFDRVYTH-QSDVWSFGVLLWeIFTLGG 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 929654453 215 LPFDGPTLPILRQRVLEG-RFRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKE 267
Cdd:cd05100  235 SPYPGIPVEELFKLLKEGhRMDKPANCTHELYMIMRECWHAVPSQRPTFKQLVE 288
STKc_Mos cd13979
Catalytic domain of the Serine/Threonine kinase, Oocyte maturation factor Mos; STKs catalyze ...
26-262 3.23e-16

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: 79.74  E-value: 3.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRitKTEVAIKIIDKSQLDAVNLEKIYREVQIMKmLDHPHIIKLY---QVMETKSMLYLVTEYAKNG 102
Cdd:cd13979   11 LGSGGFGSVYKATYK--GETVAVKIVRRRRKNRASRQSFWAELNAAR-LRHENIVRVLaaeTGTDFASLGLIIMEYCGNG 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIfdylanHGRLNESEAR-------RKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG----FGNFFKSGE 171
Cdd:cd13979   88 TL------QQLIYEGSEPlplahriLISLDIARALRFCHSHGIVHLDVKPANILISEQGVCKLCDFGcsvkLGEGNEVGT 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 LLATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGptlpiLRQRVLEG----RFRIPYFMSED---- 243
Cdd:cd13979  162 PRSHIGGTYTYRAPELLKGERV-TPKADIYSFGITLWQMLTRELPYAG-----LRQHVLYAvvakDLRPDLSGLEDsefg 235
                        250       260
                 ....*....|....*....|.
gi 929654453 244 --CEHLIRRMLVLDPSKRLTI 262
Cdd:cd13979  236 qrLRSLISRCWSAQPAERPNA 256
pknD PRK13184
serine/threonine-protein kinase PknD;
20-301 5.07e-16

serine/threonine-protein kinase PknD;


Pssm-ID: 183880 [Multi-domain]  Cd Length: 932  Bit Score: 82.90  E-value: 5.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIY-REVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:PRK13184   4 YDIIRLIGKGGMGEVYLAYDPVCSRRVALKKIREDLSENPLLKKRFlREAKIAADLIHPGIVPVYSICSDGDPVYYTMPY 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKnGEIFDYLANHGRLNESEAR------------RKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG---- 162
Cdd:PRK13184  84 IE-GYTLKSLLKSVWQKESLSKelaektsvgaflSIFHKICATIEYVHSKGVLHRDLKPDNILLGLFGEVVILDWGaaif 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 163 -------------------FGNFFKSGELLatwcGSPPYAAPEVFEGQQyEGPQLDIWSMGVVLYVLVCGALPF---DGP 220
Cdd:PRK13184 163 kkleeedlldidvdernicYSSMTIPGKIV----GTPDYMAPERLLGVP-ASESTDIYALGVILYQMLTLSFPYrrkKGR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 221 TLPiLRQRVLE----GRFR-IPYFMSEdcehLIRRMLVLDPSKRLT-----IAQIKEH-----KWMLievpvqRPVLYPQ 285
Cdd:PRK13184 238 KIS-YRDVILSpievAPYReIPPFLSQ----IAMKALAVDPAERYSsvqelKQDLEPHlqgspEWTV------KATLMTK 306
                        330
                 ....*....|....*.
gi 929654453 286 EQENepsiGEFNEQVL 301
Cdd:PRK13184 307 KKSC----WKFYEPIL 318
STKc_RIP1 cd14027
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 1; STKs catalyze ...
26-218 5.52e-16

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: 79.08  E-value: 5.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRiTKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14027    1 LDSGGFGKVSLCFHR-TQGLVVLKTVYTGPNCIEHNEALLEEGKMMNRLRHSRVVKLLGVILEEGKYSLVMEYMEKGNLM 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHgRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL------------- 172
Cdd:cd14027   80 HVLKKV-SVPLSVKGRIILEIIEGMAYLHGKGVIHKDLKPENILVDNDFHIKIADLGLASFKMWSKLtkeehneqrevdg 158
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 929654453 173 -LATWCGSPPYAAPEVFEGQQYEGPQ-LDIWSMGVVLYVLVCGALPFD 218
Cdd:cd14027  159 tAKKNAGTLYYMAPEHLNDVNAKPTEkSDVYSFAIVLWAIFANKEPYE 206
STKc_RIP2 cd14026
Catalytic domain of the Serine/Threonine kinase, Receptor Interacting Protein 2; STKs catalyze ...
26-298 7.28e-16

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: 79.19  E-value: 7.28e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIdksQLDAVNLEK----IYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKN 101
Cdd:cd14026    5 LSRGAFGTVSRARHADWRVTVAIKCL---KLDSPVGDSerncLLKEAEILHKARFSYILPILGICNEPEFLGIVTEYMTN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLanHGRLNESEAR-----RKFWQILSAVDYCHGRK--IVHRDLKAENLLLDNNMNIKIADFGFGNFFK------ 168
Cdd:cd14026   82 GSLNELL--HEKDIYPDVAwplrlRILYEIALGVNYLHNMSppLLHHDLKTQNILLDGEFHVKIADFGLSKWRQlsisqs 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 SGELLATWCGSPPYAAPEVFEGQQYEGPQL--DIWSMGVVLYVLVCGALPFDGPTLPI-LRQRVLEGRFRIpyfMSEDCe 245
Cdd:cd14026  160 RSSKSAPEGGTIIYMPPEEYEPSQKRRASVkhDIYSYAIIMWEVLSRKIPFEEVTNPLqIMYSVSQGHRPD---TGEDS- 235
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 929654453 246 hlirrmLVLDPSKRLTIAQIKEHKWMliEVPVQRPVLYPQEQENEPSIGEFNE 298
Cdd:cd14026  236 ------LPVDIPHRATLINLIESGWA--QNPDERPSFLKCLIELEPVLRTFDE 280
PTKc_Tie cd05047
Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the ...
26-265 9.15e-16

Catalytic domain of Tie Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie proteins, consisting of Tie1 and Tie2, are receptor PTKs (RTKs) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2, while no specific ligand has been identified for Tie1. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. In vivo studies of Tie1 show that it is critical in vascular development. The Tie 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: 270641 [Multi-domain]  Cd Length: 270  Bit Score: 78.54  E-value: 9.15e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRI--TKTEVAIKIIdKSQLDAVNLEKIYREVQIM-KMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd05047    3 IGEGNFGQVLKARIKKdgLRMDAAIKRM-KEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYAPHG 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRL---------NESEARRKFWQIL-------SAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGN- 165
Cdd:cd05047   82 NLLDFLRKSRVLetdpafaiaNSTASTLSSQQLLhfaadvaRGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGLSRg 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 166 ---FFKS--GELLATWcgsppyAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLPILRQRVLEG-RFRIPY 238
Cdd:cd05047  162 qevYVKKtmGRLPVRW------MAIESLNYSVYT-TNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRLEKPL 234
                        250       260
                 ....*....|....*....|....*..
gi 929654453 239 FMSEDCEHLIRRMLVLDPSKRLTIAQI 265
Cdd:cd05047  235 NCDDEVYDLMRQCWREKPYERPSFAQI 261
PTKc_TrkA cd05092
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase A; PTKs catalyze ...
26-208 9.89e-16

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: 78.47  E-value: 9.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGR-HRIT----KTEVAIKIIDKSQLDAvnLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAK 100
Cdd:cd05092   13 LGEGAFGKVFLAEcHNLLpeqdKMLVAVKALKEATESA--RQDFQREAELLTVLQHQHIVRFYGVCTEGEPLIMVFEYMR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLANH---------------GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG- 164
Cdd:cd05092   91 HGDLNRFLRSHgpdakildggegqapGQLTLGQMLQIASQIASGMVYLASLHFVHRDLATRNCLVGQGLVVKIGDFGMSr 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 929654453 165 -----NFFKSG---ELLATWcgsppyAAPEVFEGQQYEgPQLDIWSMGVVLY 208
Cdd:cd05092  171 diystDYYRVGgrtMLPIRW------MPPESILYRKFT-TESDIWSFGVVLW 215
STKc_LRRK cd14000
Catalytic domain of the Serine/Threonine kinase, Leucine-Rich Repeat Kinase; STKs catalyze the ...
26-267 1.07e-15

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: 78.42  E-value: 1.07e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKlgRHRITKTEVAIKIIDK---------------SQLDAVNLEKIYR----EVQIMKMLDHPHIIKLyqVM 86
Cdd:cd14000    2 LGDGGFGSVY--RASYKGEPVAVKIFNKhtssnfanvpadtmlRHLRATDAMKNFRllrqELTVLSHLHHPSIVYL--LG 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  87 ETKSMLYLVTEYAKNGEIFDYLANHGRLNESEARRKF----WQILSAVDYCHGRKIVHRDLKAENLLL-----DNNMNIK 157
Cdd:cd14000   78 IGIHPLMLVLELAPLGSLDHLLQQDSRSFASLGRTLQqriaLQVADGLRYLHSAMIIYRDLKSHNVLVwtlypNSAIIIK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 158 IADFGFGNF-FKSGELlaTWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGpTLPILRQRVLEGRFRI 236
Cdd:cd14000  158 IADYGISRQcCRMGAK--GSEGTPGFRAPEIARGNVIYNEKVDVFSFGMLLYEILSGGAPMVG-HLKFPNEFDIHGGLRP 234
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 929654453 237 PYFMSED-----CEHLIRRMLVLDPSKRLTIAQIKE 267
Cdd:cd14000  235 PLKQYECapwpeVEVLMKKCWKENPQQRPTAVTVVS 270
PKc_MEK2 cd06649
Catalytic domain of the dual-specificity Protein Kinase, Mitogen-Activated Protein (MAP) ...
26-220 1.12e-15

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: 79.32  E-value: 1.12e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06649   13 LGAGNGGVVTKVQHKPSGLIMARKLIHLEIKPAIR-NQIIRELQVLHECNSPYIVGFYGAFYSDGEISICMEHMDGGSLD 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHGR-KIVHRDLKAENLLLDNNMNIKIADFGFgnffkSGELL----ATWCGSP 180
Cdd:cd06649   92 QVLKEAKRIPEEILGKVSIAVLRGLAYLREKhQIMHRDVKPSNILVNSRGEIKLCDFGV-----SGQLIdsmaNSFVGTR 166
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 929654453 181 PYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDGP 220
Cdd:cd06649  167 SYMSPERLQGTHYS-VQSDIWSMGLSLVELAIGRYPIPPP 205
PKc_DYRK1 cd14226
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
20-219 1.14e-15

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: 79.29  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIdKSQLDAVNLEKIyrEVQIMKMLDHP------HIIKLYQVMETKSMLY 93
Cdd:cd14226   15 YEIDSLIGKGSFGQVVKAYDHVEQEWVAIKII-KNKKAFLNQAQI--EVRLLELMNKHdtenkyYIVRLKRHFMFRNHLC 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTE---YakngEIFDYLAN---HG-RLNESearRKF-WQILSAVDYCHGR--KIVHRDLKAENLLLDN--NMNIKIADf 161
Cdd:cd14226   92 LVFEllsY----NLYDLLRNtnfRGvSLNLT---RKFaQQLCTALLFLSTPelSIIHCDLKPENILLCNpkRSAIKIID- 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 929654453 162 gFGNFFKSGELLATWCGSPPYAAPEVFEGQQYEGPqLDIWSMGVVLYVLVCGALPFDG 219
Cdd:cd14226  164 -FGSSCQLGQRIYQYIQSRFYRSPEVLLGLPYDLA-IDMWSLGCILVEMHTGEPLFSG 219
STKc_MAP4K3 cd06645
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
26-271 1.18e-15

Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase kinase kinase 3; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. MAP4K3 plays a role in the nutrient-responsive pathway of mTOR (mammalian target of rapamycin) signaling. MAP4K3 is required in the activation of S6 kinase by amino acids and for the phosphorylation of the mTOR-regulated inhibitor of eukaryotic initiation factor 4E. mTOR regulates ribosome biogenesis and protein translation, and is frequently deregulated in cancer. MAP4Ks are involved in MAPK signaling pathways by activating a MAPK kinase kinase. Each MAPK cascade is activated either by a small GTP-binding protein or by an adaptor protein, which transmits the signal either directly to a MAP3K to start the triple kinase core cascade or indirectly through a mediator kinase, a MAP4K. Members of this subfamily contain an N-terminal catalytic domain and a C-terminal citron homology (CNH) regulatory domain. The MAP4K3 subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270812 [Multi-domain]  Cd Length: 272  Bit Score: 78.16  E-value: 1.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDavNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd06645   19 IGSGTYGDVYKARNVNTGELAAIKVIKLEPGE--DFAVVQQEIIMMKDCKHSNIVAYFGSYLRRDKLWICMEFCGGGSLQ 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFgnffkSGELLAT------WCGS 179
Cdd:cd06645   97 DIYHVTGPLSESQIAYVSRETLQGLYYLHSKGKMHRDIKGANILLTDNGHVKLADFGV-----SAQITATiakrksFIGT 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 PPYAAPEVFEGQQYEG-PQL-DIWSMGVVLYVLVcgalPFDGPTLPILRQRVL----EGRFRIPYFM-----SEDCEHLI 248
Cdd:cd06645  172 PYWMAPEVAAVERKGGyNQLcDIWAVGITAIELA----ELQPPMFDLHPMRALflmtKSNFQPPKLKdkmkwSNSFHHFV 247
                        250       260
                 ....*....|....*....|...
gi 929654453 249 RRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd06645  248 KMALTKNPKKRPTAEKLLQHPFV 270
PTKc_HER4 cd05110
Catalytic domain of the Protein Tyrosine Kinase, HER4; PTKs catalyze the transfer of the ...
26-237 1.22e-15

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: 78.57  E-value: 1.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLG----RHRITKTEVAIKIIDKSQLDAVNLEkIYREVQIMKMLDHPHIIKLYQVMETKSmLYLVTEYAKN 101
Cdd:cd05110   15 LGSGAFGTVYKGiwvpEGETVKIPVAIKILNETTGPKANVE-FMDEALIMASMDHPHLVRLLGVCLSPT-IQLVTQLMPH 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLANHgRLNESEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGS 179
Cdd:cd05110   93 GCLLDYVHEH-KDNIGSQLLLNWcvQIAKGMMYLEERRLVHRDLAARNVLVKSPNHVKITDFGLARLLEGDEKEYNADGG 171
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 929654453 180 P---PYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVC-GALPFDG-PTLPIlrQRVLEGRFRIP 237
Cdd:cd05110  172 KmpiKWMALECIHYRKFTH-QSDVWSYGVTIWELMTfGGKPYDGiPTREI--PDLLEKGERLP 231
PTKc_Axl cd05075
Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the ...
25-219 1.40e-15

Catalytic domain of the Protein Tyrosine Kinase, Axl; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Axl is widely expressed in a variety of organs and cells including epithelial, mesenchymal, hematopoietic, as well as non-transformed cells. It is important in many cellular functions such as survival, anti-apoptosis, proliferation, migration, and adhesion. Axl was originally isolated from patients with chronic myelogenous leukemia and a chronic myeloproliferative disorder. It is overexpressed in many human cancers including colon, squamous cell, thyroid, breast, and lung carcinomas. Axl is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to its ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Axl 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: 270660 [Multi-domain]  Cd Length: 277  Bit Score: 78.13  E-value: 1.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVVKLGRhrITKTEVAIKIIDKSQLDAV----NLEKIYREVQIMKMLDHPHIIKLYQV--METKSMLY----L 94
Cdd:cd05075    7 TLGEGEFGSVMEGQ--LNQDDSVLKVAVKTMKIAIctrsEMEDFLSEAVCMKEFDHPNVMRLIGVclQNTESEGYpspvV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAKNGEIFDYLAnHGRLNE------SEARRKFW-QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF---- 163
Cdd:cd05075   85 ILPFMKHGDLHSFLL-YSRLGDcpvylpTQMLVKFMtDIASGMEYLSSKNFIHRDLAARNCMLNENMNVCVADFGLskki 163
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 929654453 164 --GNFFKSGELLATwcgSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDG 219
Cdd:cd05075  164 ynGDYYRQGRISKM---PVKWIAIESLADRVYT-TKSDVWSFGVTMWEIATrGQTPYPG 218
STKc_TGFbR2_like cd14055
Catalytic domain of the Serine/Threonine Kinase, Transforming Growth Factor beta Type II ...
26-267 1.77e-15

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: 78.19  E-value: 1.77e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVV---KLGRHRITKTE-VAIKIIDKSQLDAVNLEK-IYREVQimkmLDHPHIIKLYQVMETKSML----YLVT 96
Cdd:cd14055    3 VGKGRFAEVwkaKLKQNASGQYEtVAVKIFPYEEYASWKNEKdIFTDAS----LKHENILQFLTAEERGVGLdrqyWLIT 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  97 EYAKNGEIFDYLANHgRLNESEARRKFWQILSAVDYCH------GRK---IVHRDLKAENLLLDNNMNIKIADFGFG--- 164
Cdd:cd14055   79 AYHENGSLQDYLTRH-ILSWEDLCKMAGSLARGLAHLHsdrtpcGRPkipIAHRDLKSSNILVKNDGTCVLADFGLAlrl 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 165 -------NFFKSGELlatwcGSPPYAAPEVFEG----QQYEG-PQLDIWSMGVVLYVLV--CGA--------LPF----- 217
Cdd:cd14055  158 dpslsvdELANSGQV-----GTARYMAPEALESrvnlEDLESfKQIDVYSMALVLWEMAsrCEAsgevkpyeLPFgskvr 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 218 DGPTLPILRQRVLEGRFR--IPyfmSEDCEHLIRRMLVL--------DPSKRLTIAQIKE 267
Cdd:cd14055  233 ERPCVESMKDLVLRDRGRpeIP---DSWLTHQGMCVLCDtitecwdhDPEARLTASCVAE 289
STKc_C-Raf cd14149
Catalytic domain of the Serine/Threonine Kinase, C-Raf (Rapidly Accelerated Fibrosarcoma) ...
26-217 2.16e-15

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: 77.76  E-value: 2.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRitkTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIkLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14149   20 IGSGSFGTVYKGKWH---GDVAVKILKVVDPTPEQFQAFRNEVAVLRKTRHVNIL-LFMGYMTKDNLAIVTQWCEGSSLY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLanhgrlNESEARRKFWQIL-------SAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNF---FKSGELLAT 175
Cdd:cd14149   96 KHL------HVQETKFQMFQLIdiarqtaQGMDYLHAKNIIHRDMKSNNIFLHEGLTVKIGDFGLATVksrWSGSQQVEQ 169
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 176 WCGSPPYAAPEVFEGQQyEGP---QLDIWSMGVVLYVLVCGALPF 217
Cdd:cd14149  170 PTGSILWMAPEVIRMQD-NNPfsfQSDVYSYGIVLYELMTGELPY 213
STKc_TDY_MAPK cd07859
Catalytic domain of the Serine/Threonine Kinases, Plant TDY Mitogen-Activated Protein Kinases; ...
20-219 2.28e-15

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: 78.28  E-value: 2.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSM-----LYL 94
Cdd:cd07859    2 YKIQEVIGKGSYGVVCSAIDTHTGEKVAIKKINDVFEHVSDATRILREIKLLRLLRHPDIVEIKHIMLPPSRrefkdIYV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAKNgEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGN--FFKSG-- 170
Cdd:cd07859   82 VFELMES-DLHQVIKANDDLTPEHHQFFLYQLLRALKYIHTANVFHRDLKPKNILANADCKLKICDFGLARvaFNDTPta 160
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 929654453 171 ----ELLAT-WcgsppYAAPEV---FEGQQyeGPQLDIWSMGVVLYVLVCGALPFDG 219
Cdd:cd07859  161 ifwtDYVATrW-----YRAPELcgsFFSKY--TPAIDIWSIGCIFAEVLTGKPLFPG 210
STKc_MAP4K5 cd06646
Catalytic domain of the Serine/Threonine Kinase, Mitogen-activated protein kinase kinase ...
20-205 2.50e-15

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: 76.99  E-value: 2.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLekIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd06646   11 YELIQRVGSGTYGDVYKARNLHTGELAAVKIIKLEPGDDFSL--IQQEIFMVKECKHCNIVAYFGSYLSREKLWICMEYC 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFgnffkSGELLAT---- 175
Cdd:cd06646   89 GGGSLQDIYHVTGPLSELQIAYVCRETLQGLAYLHSKGKMHRDIKGANILLTDNGDVKLADFGV-----AAKITATiakr 163
                        170       180       190
                 ....*....|....*....|....*....|....
gi 929654453 176 --WCGSPPYAAPEVFEGQQYEG-PQL-DIWSMGV 205
Cdd:cd06646  164 ksFIGTPYWMAPEVAAVEKNGGyNQLcDIWAVGI 197
STKc_CDK4 cd07863
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 4; STKs ...
20-271 2.61e-15

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: 77.31  E-value: 2.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKIID-KSQLDAVNLEKIyREVQIMKML---DHPHIIKLYQVMET-----KS 90
Cdd:cd07863    2 YEPVAEIGVGAYGTVYKARDPHSGHFVALKSVRvQTNEDGLPLSTV-REVALLKRLeafDHPNIVRLMDVCATsrtdrET 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  91 MLYLVTEYAkNGEIFDYL--ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK 168
Cdd:cd07863   81 KVTLVFEHV-DQDLRTYLdkVPPPGLPAETIKDLMRQFLRGLDFLHANCIVHRDLKPENILVTSGGQVKLADFGLARIYS 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 SGELLATWCGSPPYAAPEVFEGQQYEGPqLDIWSMGVVLY------VLVCG--------------ALPF--DGPTLPILR 226
Cdd:cd07863  160 CQMALTPVVVTLWYRAPEVLLQSTYATP-VDMWSVGCIFAemfrrkPLFCGnseadqlgkifdliGLPPedDWPRDVTLP 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 929654453 227 QRVLEGRFRIPYF-----MSEDCEHLIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd07863  239 RGAFSPRGPRPVQsvvpeIEESGAQLLLEMLTFNPHKRISAFRALQHPFF 288
PKc_YAK1 cd14212
Catalytic domain of the Dual-specificity protein kinase, YAK1; Dual-specificity PKs catalyze ...
20-206 3.06e-15

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: 78.06  E-value: 3.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFA-VVKLgRHRITKTEVAIKIIdKSQLDAVNLEKIyrEVQIMKML-------DHPHIIKLYQVMETKSM 91
Cdd:cd14212    1 YLVLDLLGQGTFGqVVKC-QDLKTNKLVAVKVL-KNKPAYFRQAML--EIAILTLLntkydpeDKHHIVRLLDHFMHHGH 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  92 LYLVTE-YAKNgeIFDYLA---NHGrLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNM--NIKIADFGFGN 165
Cdd:cd14212   77 LCIVFElLGVN--LYELLKqnqFRG-LSLQLIRKFLQQLLDALSVLKDARIIHCDLKPENILLVNLDspEIKLIDFGSAC 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 929654453 166 FfkSGELLATWCGSPPYAAPEVFEGQQYEGPqLDIWSMGVV 206
Cdd:cd14212  154 F--ENYTLYTYIQSRFYRSPEVLLGLPYSTA-IDMWSLGCI 191
PTKc_EphR_A2 cd05063
Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2; PTKs catalyze the ...
23-253 3.16e-15

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: 76.94  E-value: 3.16e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  23 EGTLGKGNFAVVKLGRHRIT-KTEVAIKIidkSQLDAVNLEK----IYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTE 97
Cdd:cd05063   10 QKVIGAGEFGEVFRGILKMPgRKEVAVAI---KTLKPGYTEKqrqdFLSEASIMGQFSHHNIIRLEGVVTKFKPAMIITE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE--LLA 174
Cdd:cd05063   87 YMENGALDKYLRDHdGEFSSYQLVGMLRGIAAGMKYLSDMNYVHRDLAARNILVNSNLECKVSDFGLSRVLEDDPegTYT 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 175 TWCGSPP--YAAPEVFEGQQYEGPQlDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEGrFRIPYFMseDCEHLIRRM 251
Cdd:cd05063  167 TSGGKIPirWTAPEAIAYRKFTSAS-DVWSFGIVMWeVMSFGERPYWDMSNHEVMKAINDG-FRLPAPM--DCPSAVYQL 242

                 ..
gi 929654453 252 LV 253
Cdd:cd05063  243 ML 244
STKc_p38delta cd07879
Catalytic domain of the Serine/Threonine Kinase, p38delta Mitogen-Activated Protein Kinase ...
26-270 3.33e-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: 78.02  E-value: 3.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSML------YLVTEYA 99
Cdd:cd07879   23 VGSGAYGSVCSAIDKRTGEKVAIKKLSRPFQSEIFAKRAYRELTLLKHMQHENVIGLLDVFTSAVSGdefqdfYLVMPYM 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNgEIFDYLANHgrLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK---SGELLATW 176
Cdd:cd07879  103 QT-DLQKIMGHP--LSEDKVQYLVYQMLCGLKYIHSAGIIHRDLKPGNLAVNEDCELKILDFGLARHADaemTGYVVTRW 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 177 cgsppYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGP----------------------------------TL 222
Cdd:cd07879  180 -----YRAPEVILNWMHYNQTVDIWSVGCIMAEMLTGKTLFKGKdyldqltqilkvtgvpgpefvqkledkaaksyikSL 254
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 929654453 223 PILRQRVLEGRFRIPYFMSEDcehLIRRMLVLDPSKRLTIAQIKEHKW 270
Cdd:cd07879  255 PKYPRKDFSTLFPKASPQAVD---LLEKMLELDVDKRLTATEALEHPY 299
PTKc_Chk cd05083
Catalytic domain of the Protein Tyrosine Kinase, Csk homologous kinase; PTKs catalyze the ...
26-267 3.54e-15

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: 76.45  E-value: 3.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHriTKTEVAIKIIdKSQLDAVNLekiYREVQIMKMLDHPHIIKLYQVMeTKSMLYLVTEYAKNGEIF 105
Cdd:cd05083   14 IGEGEFGAVLQGEY--MGQKVAVKNI-KCDVTAQAF---LEETAVMTKLQHKNLVRLLGVI-LHNGLYIVMELMSKGNLV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHGR--LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSG----ELLATWcgs 179
Cdd:cd05083   87 NFLRSRGRalVPVIQLLQFSLDVAEGMEYLESKKLVHRDLAARNILVSEDGVAKISDFGLAKVGSMGvdnsRLPVKW--- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 180 ppyAAPEVFEGQQYEGpQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEG-RFRIPYFMSEDCEHLIRRMLVLDPS 257
Cdd:cd05083  164 ---TAPEALKNKKFSS-KSDVWSYGVLLWeVFSYGRAPYPKMSVKEVKEAVEKGyRMEPPEGCPPDVYSIMTSCWEAEPG 239
                        250
                 ....*....|
gi 929654453 258 KRLTIAQIKE 267
Cdd:cd05083  240 KRPSFKKLRE 249
STKc_TAO1 cd06635
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 1; STKs catalyze ...
26-307 3.61e-15

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: 77.40  E-value: 3.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKS-QLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKnGEI 104
Cdd:cd06635   33 IGHGSFGAVYFARDVRTSEVVAIKKMSYSgKQSNEKWQDIIKEVKFLQRIKHPNSIEYKGCYLREHTAWLVMEYCL-GSA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEllaTWCGSPPYA 183
Cdd:cd06635  112 SDLLEVHKKpLQEIEIAAITHGALQGLAYLHSHNMIHRDIKAGNILLTEPGQVKLADFGSASIASPAN---SFVGTPYWM 188
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 184 APEVF----EGqQYEGpQLDIWSMGVvlyvlVCGALPFDGPtlPILRQRVLEGRFRI-----PYFMSEDCEHLIRRM--- 251
Cdd:cd06635  189 APEVIlamdEG-QYDG-KVDVWSLGI-----TCIELAERKP--PLFNMNAMSALYHIaqnesPTLQSNEWSDYFRNFvds 259
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 929654453 252 -LVLDPSKRLTIAQIKEHKWMLIEVPvqRPVLYPQEQENEPSIGEFNEQVLRLMHSL 307
Cdd:cd06635  260 cLQKIPQDRPTSEELLKHMFVLRERP--ETVLIDLIQRTKDAVRELDNLQYRKMKKL 314
STKc_WNK1 cd14030
Catalytic domain of the Serine/Threonine protein kinase, With No Lysine (WNK) 1; STKs catalyze ...
20-217 4.39e-15

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: 77.01  E-value: 4.39e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEgtLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMET----KSMLYLV 95
Cdd:cd14030   29 FDIE--IGRGSFKTVYKGLDTETTVEVAWCELQDRKLSKSERQRFKEEAGMLKGLQHPNIVRFYDSWEStvkgKKCIVLV 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRK--IVHRDLKAENLLLDNNM-NIKIADFGFGNfFKSGEL 172
Cdd:cd14030  107 TELMTSGTLKTYLKRFKVMKIKVLRSWCRQILKGLQFLHTRTppIIHRDLKCDNIFITGPTgSVKIGDLGLAT-LKRASF 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 173 LATWCGSPPYAAPEVFEgQQYEgPQLDIWSMGVVLYVLVCGALPF 217
Cdd:cd14030  186 AKSVIGTPEFMAPEMYE-EKYD-ESVDVYAFGMCMLEMATSEYPY 228
PTKc_c-ros cd05044
Catalytic domain of the Protein Tyrosine Kinase, C-ros; PTKs catalyze the transfer of the ...
43-267 5.17e-15

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: 76.30  E-value: 5.17e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  43 KTEVAIKIIDKSQLDAvNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDYLanhgRLNESEARRK 122
Cdd:cd05044   26 ETKVAVKTLRKGATDQ-EKAEFLKEAHLMSNFKHPNILKLLGVCLDNDPQYIILELMEGGDLLSYL----RAARPTAFTP 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 123 FWQILS-----AVDYCHGRK------IVHRDLKAENLLLDNN----MNIKIADFGFGN-------FFKSGE--LLATWcg 178
Cdd:cd05044  101 PLLTLKdllsiCVDVAKGCVyledmhFVHRDLAARNCLVSSKdyreRVVKIGDFGLARdiykndyYRKEGEglLPVRW-- 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 179 sppyAAPE-----VFEGQQyegpqlDIWSMGVVLY-VLVCGALPFDGPT-LPILRQRVLEGRFRIPYFMSEDCEHLIRRM 251
Cdd:cd05044  179 ----MAPEslvdgVFTTQS------DVWAFGVLMWeILTLGQQPYPARNnLEVLHFVRAGGRLDQPDNCPDDLYELMLRC 248
                        250
                 ....*....|....*.
gi 929654453 252 LVLDPSKRLTIAQIKE 267
Cdd:cd05044  249 WSTDPEERPSFARILE 264
PTKc_PDGFR cd05055
Catalytic domain of the Protein Tyrosine Kinases, Platelet Derived Growth Factor Receptors; ...
25-265 6.38e-15

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: 76.37  E-value: 6.38e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFA-VVKLGRHRITKTEVAIKI---IDKSQLDAVNLEKIYREVQIMKML-DHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd05055   42 TLGAGAFGkVVEATAYGLSKSDAVMKVavkMLKPTAHSSEREALMSELKIMSHLgNHENIVNLLGACTIGGPILVITEYC 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANhgrlnESEARRKFWQILS-------AVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG-------N 165
Cdd:cd05055  122 CYGDLLNFLRR-----KRESFLTLEDLLSfsyqvakGMAFLASKNCIHRDLAARNVLLTHGKIVKICDFGLArdimndsN 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 166 FFKSGE--LLATWcgsppyAAPE-VFEGqqYEGPQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEGRFRI--PYF 239
Cdd:cd05055  197 YVVKGNarLPVKW------MAPEsIFNC--VYTFESDVWSYGILLWeIFSLGSNPYPGMPVDSKFYKLIKEGYRMaqPEH 268
                        250       260
                 ....*....|....*....|....*.
gi 929654453 240 MSEDCEHLIRRMLVLDPSKRLTIAQI 265
Cdd:cd05055  269 APAEIYDIMKTCWDADPLKRPTFKQI 294
STKc_Cdc7 cd14019
Catalytic domain of the Serine/Threonine Kinase, Cell Division Cycle 7 kinase; STKs catalyze ...
20-268 6.51e-15

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: 75.72  E-value: 6.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKT-------EVAIKIIDKSQLDAvnleKIYREVQIMKMLD-HPHIIKLYQVMETKSM 91
Cdd:cd14019    3 YRIIEKIGEGTFSSVYKAEDKLHDLydrnkgrLVALKHIYPTSSPS----RILNELECLERLGgSNNVSGLITAFRNEDQ 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  92 LYLVTEYAKNGEIFDYLANhgrLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLdnnmNIK-----IADFGFGNF 166
Cdd:cd14019   79 VVAVLPYIEHDDFRDFYRK---MSLTDIRIYLRNLFKALKHVHSFGIIHRDVKPGNFLY----NREtgkgvLVDFGLAQR 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 167 FKS-GELLATWCGSPPYAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGALPFDGPTLPIlrQRVLEgrfRIPYFMSEDCE 245
Cdd:cd14019  152 EEDrPEQRAPRAGTRGFRAPEVLFKCPHQTTAIDIWSAGVILLSILSGRFPFFFSSDDI--DALAE---IATIFGSDEAY 226
                        250       260
                 ....*....|....*....|...
gi 929654453 246 HLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14019  227 DLLDKLLELDPSKRITAEEALKH 249
PTKc_TAM cd05035
Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer ...
25-267 7.27e-15

Catalytic Domain of TAM (Tyro3, Axl, Mer) Protein Tyrosine Kinases; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. The TAM subfamily consists of Tyro3 (or Sky), Axl, Mer (or Mertk), and similar proteins. TAM subfamily members are receptor tyr kinases (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. TAM proteins are implicated in a variety of cellular effects including survival, proliferation, migration, and phagocytosis. They are also associated with several types of cancer as well as inflammatory, autoimmune, vascular, and kidney diseases. The TAM 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: 270631 [Multi-domain]  Cd Length: 273  Bit Score: 76.03  E-value: 7.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  25 TLGKGNFAVV---KLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSML------YLV 95
Cdd:cd05035    6 ILGEGEFGSVmeaQLKQDDGSQLKVAVKTMKVDIHTYSEIEEFLSEAACMKDFDHPNVMRLIGVCFTASDLnkppspMVI 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNGEIFDYLAnHGRLNES------EARRKFW-QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFK 168
Cdd:cd05035   86 LPFMKHGDLHSYLL-YSRLGGLpeklplQTLLKFMvDIAKGMEYLSNRNFIHRDLAARNCMLDENMTVCVADFGLSRKIY 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 169 SGELLATWCGSP---PYAAPEVFEGQQYEgPQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEG-RFRIPYFMSED 243
Cdd:cd05035  165 SGDYYRQGRISKmpvKWIALESLADNVYT-SKSDVWSFGVTMWeIATRGQTPYPGVENHEIYDYLRNGnRLKQPEDCLDE 243
                        250       260
                 ....*....|....*....|....
gi 929654453 244 CEHLIRRMLVLDPSKRLTIAQIKE 267
Cdd:cd05035  244 VYFLMYFCWTVDPKDRPTFTKLRE 267
PHA03211 PHA03211
serine/threonine kinase US3; Provisional
67-208 7.83e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 223009 [Multi-domain]  Cd Length: 461  Bit Score: 78.01  E-value: 7.83e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  67 EVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNgEIFDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKA 145
Cdd:PHA03211 210 EARLLRRLSHPAVLALLDVRVVGGLTCLVLPKYRS-DLYTYLGARLRpLGLAQVTAVARQLLSAIDYIHGEGIIHRDIKT 288
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 929654453 146 ENLLLDNNMNIKIADFGFGNFFKsgellATWCGSPPYA--------APEVFEGQQYEgPQLDIWSMGVVLY 208
Cdd:PHA03211 289 ENVLVNGPEDICLGDFGAACFAR-----GSWSTPFHYGiagtvdtnAPEVLAGDPYT-PSVDIWSAGLVIF 353
PHA03212 PHA03212
serine/threonine kinase US3; Provisional
67-213 8.01e-15

serine/threonine kinase US3; Provisional


Pssm-ID: 165478 [Multi-domain]  Cd Length: 391  Bit Score: 77.34  E-value: 8.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  67 EVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNgEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAE 146
Cdd:PHA03212 133 EAHILRAINHPSIIQLKGTFTYNKFTCLILPRYKT-DLYCYLAAKRNIAICDILAIERSVLRAIQYLHENRIIHRDIKAE 211
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 929654453 147 NLLLDNNMNIKIADFGFGNFFK--SGELLATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCG 213
Cdd:PHA03212 212 NIFINHPGDVCLGDFGAACFPVdiNANKYYGWAGTIATNAPELLARDPY-GPAVDIWSAGIVLFEMATC 279
PTKc_Ror cd05048
Catalytic Domain of the Protein Tyrosine Kinases, Receptor tyrosine kinase-like Orphan ...
26-268 8.58e-15

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: 75.87  E-value: 8.58e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGR-----HRITKTEVAIKIIDKSQLDAVNlEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAK 100
Cdd:cd05048   13 LGEGAFGKVYKGEllgpsSEESAISVAIKTLKENASPKTQ-QDFRREAELMSDLQHPNIVCLLGVCTKEQPQCMLFEYMA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLANHGRLNESEA-------RRKFW---------QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG 164
Cdd:cd05048   92 HGDLHEFLVRHSPHSDVGVssdddgtASSLDqsdflhiaiQIAAGMEYLSSHHYVHRDLAARNCLVGDGLTVKISDFGLS 171
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 165 NFFKSGELLATWCGSP-P--YAAPEVFEGQQYEgPQLDIWSMGVVLY-VLVCGALPFDGPTlpilRQRVLEG-RFRIPYF 239
Cdd:cd05048  172 RDIYSSDYYRVQSKSLlPvrWMPPEAILYGKFT-TESDVWSFGVVLWeIFSYGLQPYYGYS----NQEVIEMiRSRQLLP 246
                        250       260       270
                 ....*....|....*....|....*....|...
gi 929654453 240 MSEDCEHLIRRMLV----LDPSKRLTIAQIKEH 268
Cdd:cd05048  247 CPEDCPARVYSLMVecwhEIPSRRPRFKEIHTR 279
STKc_PDIK1L cd13977
Catalytic domain of the Serine/Threonine kinase, PDLIM1 interacting kinase 1 like; STKs ...
20-266 1.68e-14

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: 75.67  E-value: 1.68e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFAVVKLGRHRITKTEVAIKiidKSQLDAV-NLEKIYREVQIMKMLD--HPHIIKL----------YQVM 86
Cdd:cd13977    2 YSLIREVGRGSYGVVYEAVVRRTGARVAVK---KIRCNAPeNVELALREFWALSSIQrqHPNVIQLeecvlqrdglAQRM 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  87 E---TKSMLYL-VTEYAKNGEI-FDY-----------LANHGRLNESEARRK---------FWQILSAVDYCHGRKIVHR 141
Cdd:cd13977   79 ShgsSKSDLYLlLVETSLKGERcFDPrsacylwfvmeFCDGGDMNEYLLSRRpdrqtntsfMLQLSSALAFLHRNQIVHR 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 142 DLKAENLLLDNNMN---IKIADFGFGNFFKSGEL------------LATWCGSPPYAAPEVFEGqqYEGPQLDIWSMGVV 206
Cdd:cd13977  159 DLKPDNILISHKRGepiLKVADFGLSKVCSGSGLnpeepanvnkhfLSSACGSDFYMAPEVWEG--HYTAKADIFALGII 236
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 207 LYVLV--------------CGALPFDGPTLPILRQRVLEG---RFRIP----YFMSEDCEHLIRRMLVLDPSKRLTIAQI 265
Cdd:cd13977  237 IWAMVeritfrdgetkkelLGTYIQQGKEIVPLGEALLENpklELQIPlkkkKSMNDDMKQLLRDMLAANPQERPDAFQL 316

                 .
gi 929654453 266 K 266
Cdd:cd13977  317 E 317
PTKc_Tie1 cd05089
Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; ...
23-265 2.09e-14

Catalytic domain of the Protein Tyrosine Kinase, Tie1; Protein Tyrosine Kinase (PTK) family; Tie1; 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. Tie1 is a receptor tyr kinase (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie receptors are specifically expressed in endothelial cells and hematopoietic stem cells. No specific ligand has been identified for Tie1, although the angiopoietin, Ang-1, binds to Tie1 through integrins at high concentrations. In vivo studies of Tie1 show that it is critical in vascular development.


Pssm-ID: 270671 [Multi-domain]  Cd Length: 297  Bit Score: 75.04  E-value: 2.09e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  23 EGTLGKGNFAVV--KLGRHRITKTEVAIKIIdKSQLDAVNLEKIYREVQIM-KMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd05089    7 EDVIGEGNFGQVikAMIKKDGLKMNAAIKML-KEFASENDHRDFAGELEVLcKLGHHPNIINLLGACENRGYLYIAIEYA 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYL-------------ANHGR---LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF 163
Cdd:cd05089   86 PYGNLLDFLrksrvletdpafaKEHGTastLTSQQLLQFASDVAKGMQYLSEKQFIHRDLAARNVLVGENLVSKIADFGL 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 164 GN----FFKS--GELLATWcgsppyAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLPILRQRVLEG-RFR 235
Cdd:cd05089  166 SRgeevYVKKtmGRLPVRW------MAIESLNYSVYT-TKSDVWSFGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRME 238
                        250       260       270
                 ....*....|....*....|....*....|
gi 929654453 236 IPYFMSEDCEHLIRRMLVLDPSKRLTIAQI 265
Cdd:cd05089  239 KPRNCDDEVYELMRQCWRDRPYERPPFSQI 268
PHA03209 PHA03209
serine/threonine kinase US3; Provisional
67-208 2.30e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 177557 [Multi-domain]  Cd Length: 357  Bit Score: 75.68  E-value: 2.30e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  67 EVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNgEIFDYLANH-GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKA 145
Cdd:PHA03209 107 EAMLLQNVNHPSVIRMKDTLVSGAITCMVLPHYSS-DLYTYLTKRsRPLPIDQALIIEKQILEGLRYLHAQRIIHRDVKT 185
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 929654453 146 ENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPYAAPEVFEGQQYEGpQLDIWSMGVVLY 208
Cdd:PHA03209 186 ENIFINDVDQVCIGDLGAAQFPVVAPAFLGLAGTVETNAPEVLARDKYNS-KADIWSAGIVLF 247
PKc_CLK3 cd14214
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 3; Dual-specificity ...
20-268 3.59e-14

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: 74.66  E-value: 3.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFA-VVKLGRHRITKTEVAIKII-------DKSQLDAVNLEKIYREVQIMK-----MLD----HPHIIKL 82
Cdd:cd14214   15 YEIVGDLGEGTFGkVVECLDHARGKSQVALKIIrnvgkyrEAARLEINVLKKIKEKDKENKflcvlMSDwfnfHGHMCIA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  83 YQVMETKSMlylvtEYAKNGEIFDYLANHgrlneseARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDN---------- 152
Cdd:cd14214   95 FELLGKNTF-----EFLKENNFQPYPLPH-------IRHMAYQLCHALKFLHENQLTHTDLKPENILFVNsefdtlynes 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 153 ---------NMNIKIADFGFGNFfkSGELLATWCGSPPYAAPEVFEGQQYEGPqLDIWSMGVVLYVLVCGALPFD----- 218
Cdd:cd14214  163 ksceeksvkNTSIRVADFGSATF--DHEHHTTIVATRHYRPPEVILELGWAQP-CDVWSLGCILFEYYRGFTLFQthenr 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 219 ----------GPtLP---ILRQR---------------VLEGRF------RIPYFMSEDC-EH-----LIRRMLVLDPSK 258
Cdd:cd14214  240 ehlvmmekilGP-IPshmIHRTRkqkyfykgslvwdenSSDGRYvsenckPLMSYMLGDSlEHtqlfdLLRRMLEFDPAL 318
                        330
                 ....*....|
gi 929654453 259 RLTIAQIKEH 268
Cdd:cd14214  319 RITLKEALLH 328
PHA03207 PHA03207
serine/threonine kinase US3; Provisional
20-265 4.63e-14

serine/threonine kinase US3; Provisional


Pssm-ID: 165473 [Multi-domain]  Cd Length: 392  Bit Score: 75.27  E-value: 4.63e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGN----FAVVKLGRhrITKTEVAIKIIDKSQldavNLEkiyREVQIMKMLDHPHIIKLYQVMETKSMLYLV 95
Cdd:PHA03207  94 YNILSSLTPGSegevFVCTKHGD--EQRKKVIVKAVTGGK----TPG---REIDILKTISHRAIINLIHAYRWKSTVCMV 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  96 TEYAKNgEIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGnfFKSGELLAT 175
Cdd:PHA03207 165 MPKYKC-DLFTYVDRSGPLPLEQAITIQRRLLEALAYLHGRGIIHRDVKTENIFLDEPENAVLGDFGAA--CKLDAHPDT 241
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 176 -----WCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDGPTLP--------ILR---------------- 226
Cdd:PHA03207 242 pqcygWSGTLETNSPELLALDPY-CAKTDIWSAGLVLFEMSVKNVTLFGKQVKssssqlrsIIRcmqvhplefpqngstn 320
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 929654453 227 --------QRVLEGRFRIP-----YFMSEDCEHLIRRMLVLDPSKRLTIAQI 265
Cdd:PHA03207 321 lckhfkqyAIVLRPPYTIPpvirkYGMHMDVEYLIAKMLTFDQEFRPSAQDI 372
PTKc_Wee1 cd14051
Catalytic domain of the Protein Tyrosine Kinase, Wee1; PTKs catalyze the transfer of the ...
24-268 5.00e-14

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: 73.21  E-value: 5.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  24 GTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKML-DHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd14051    6 EKIGSGEFGSVYKCINRLDGCVYAIKKSKKPVAGSVDEQNALNEVYAHAVLgKHPHVVRYYSAWAEDDHMIIQNEYCNGG 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANH----GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIA---DFGFGNF--------- 166
Cdd:cd14051   86 SLADAISENekagERFSEAELKDLLLQVAQGLKYIHSQNLVHMDIKPGNIFISRTPNPVSSeeeEEDFEGEednpesnev 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 167 -FKSGELLATWCGSPP--------YAAPEVFEGQQYEGPQLDIWSMGVVLYVLVCGA-LPFDGPTLPILRQrvleGRFri 236
Cdd:cd14051  166 tYKIGDLGHVTSISNPqveegdcrFLANEILQENYSHLPKADIFALALTVYEAAGGGpLPKNGDEWHEIRQ----GNL-- 239
                        250       260       270
                 ....*....|....*....|....*....|....
gi 929654453 237 PYF--MSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14051  240 PPLpqCSPEFNELLRSMIHPDPEKRPSAAALLQH 273
STKc_TAO2 cd06634
Catalytic domain of the Serine/Threonine Kinase, Thousand-and-One Amino acids 2; STKs catalyze ...
26-205 5.72e-14

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: 73.90  E-value: 5.72e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKS-QLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKnGEI 104
Cdd:cd06634   23 IGHGSFGAVYFARDVRNNEVVAIKKMSYSgKQSNEKWQDIIKEVKFLQKLRHPNTIEYRGCYLREHTAWLVMEYCL-GSA 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 105 FDYLANHGR-LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEllaTWCGSPPYA 183
Cdd:cd06634  102 SDLLEVHKKpLQEVEIAAITHGALQGLAYLHSHNMIHRDVKAGNILLTEPGLVKLGDFGSASIMAPAN---SFVGTPYWM 178
                        170       180
                 ....*....|....*....|....*.
gi 929654453 184 APEVF----EGqQYEGpQLDIWSMGV 205
Cdd:cd06634  179 APEVIlamdEG-QYDG-KVDVWSLGI 202
PTKc_Wee1a cd14138
Catalytic domain of the Protein Tyrosine Kinase, Wee1a; PTKs catalyze the transfer of the ...
19-268 6.45e-14

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: 73.13  E-value: 6.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEgTLGKGNFAVVKLGRHRITKTEVAIKIIDKSQLDAVNLEKIYREVQIMKML-DHPHIIKLYQVMETKSMLYLVTE 97
Cdd:cd14138    7 FHELE-KIGSGEFGSVFKCVKRLDGCIYAIKRSKKPLAGSVDEQNALREVYAHAVLgQHSHVVRYYSAWAEDDHMLIQNE 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLANHGR----LNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLD-------------------NNM 154
Cdd:cd14138   86 YCNGGSLADAISENYRimsyFTEPELKDLLLQVARGLKYIHSMSLVHMDIKPSNIFISrtsipnaaseegdedewasNKV 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 155 NIKIADFGFGNFFKSGELLAtwcGSPPYAAPEVFEGQQYEGPQLDIWSMGVvlyVLVCGA----LPFDGPTLPILRQRVL 230
Cdd:cd14138  166 IFKIGDLGHVTRVSSPQVEE---GDSRFLANEVLQENYTHLPKADIFALAL---TVVCAAgaepLPTNGDQWHEIRQGKL 239
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 929654453 231 EgrfRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14138  240 P---RIPQVLSQEFLDLLKVMIHPDPERRPSAVALVKH 274
PTKc_DDR2 cd05095
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 2; PTKs catalyze ...
26-171 1.23e-13

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: 72.72  E-value: 1.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKL----GRHRITKTEVAIKI-IDKSQLDAVNLEK----------IYREVQIMKMLDHPHIIKLYQVMETKS 90
Cdd:cd05095   13 LGEGQFGEVHLceaeGMEKFMDKDFALEVsENQPVLVAVKMLRadanknarndFLKEIKIMSRLKDPNIIRLLAVCITDD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  91 MLYLVTEYAKNGEIFDYLANH---GRLNESEARR-------KFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKI 158
Cdd:cd05095   93 PLCMITEYMENGDLNQFLSRQqpeGQLALPSNALtvsysdlRFMaaQIASGMKYLSSLNFVHRDLATRNCLVGKNYTIKI 172
                        170
                 ....*....|...
gi 929654453 159 ADFGFGNFFKSGE 171
Cdd:cd05095  173 ADFGMSRNLYSGD 185
PKc_CLK1_4 cd14213
Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; ...
9-268 1.33e-13

Catalytic domain of the Dual-specificity protein kinases, CDC-like kinases 1 and 4; Dual-specificity PKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine as well as tyrosine residues on protein substrates. CLK1 plays a role in neuronal differentiation. 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 CLK1/4 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: 271115 [Multi-domain]  Cd Length: 330  Bit Score: 72.96  E-value: 1.33e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453   9 HL--QRGPVRVGFYDIEGTLGKGNFA-VVKLGRHRITKTEVAIKIIDK---------------SQLDAVNLEKIYREVQI 70
Cdd:cd14213    1 HLicQSGDVLRARYEIVDTLGEGAFGkVVECIDHKMGGMHVAVKIVKNvdryreaarseiqvlEHLNTTDPNSTFRCVQM 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  71 MKMLDH-PHIIKLYQvmetksMLYLVT-EYAKNGEIFDYLANHgrlneseARRKFWQILSAVDYCHGRKIVHRDLKAENL 148
Cdd:cd14213   81 LEWFDHhGHVCIVFE------LLGLSTyDFIKENSFLPFPIDH-------IRNMAYQICKSVNFLHHNKLTHTDLKPENI 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 149 LLDN-------------------NMNIKIADFGFGNFfkSGELLATWCGSPPYAAPEVFEGQQYEGPqLDIWSMGVVLYV 209
Cdd:cd14213  148 LFVQsdyvvkynpkmkrdertlkNPDIKVVDFGSATY--DDEHHSTLVSTRHYRAPEVILALGWSQP-CDVWSIGCILIE 224
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 210 LVCGALPF---DGPTLPILRQRVL-----------------------------EGRF-------RIPYFMSEDCEH---- 246
Cdd:cd14213  225 YYLGFTVFqthDSKEHLAMMERILgplpkhmiqktrkrkyfhhdqldwdehssAGRYvrrrckpLKEFMLSQDVDHeqlf 304
                        330       340
                 ....*....|....*....|...
gi 929654453 247 -LIRRMLVLDPSKRLTIAQIKEH 268
Cdd:cd14213  305 dLIQKMLEYDPAKRITLDEALKH 327
STKc_TGFbR1_ACVR1b_ACVR1c cd14143
Catalytic domain of the Serine/Threonine Kinases, Transforming Growth Factor beta Type I ...
26-267 1.65e-13

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: 72.09  E-value: 1.65e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRitKTEVAIKIIdkSQLDAVNLekiYREVQIMK--MLDHPHIIKLYQVME----TKSMLYLVTEYA 99
Cdd:cd14143    3 IGKGRFGEVWRGRWR--GEDVAVKIF--SSREERSW---FREAEIYQtvMLRHENILGFIAADNkdngTWTQLWLVSDYH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLaNHGRLNESEARRKFWQILSAVDYCH-------GR-KIVHRDLKAENLLLDNNMNIKIADFGFGnfFKSGE 171
Cdd:cd14143   76 EHGSLFDYL-NRYTVTVEGMIKLALSIASGLAHLHmeivgtqGKpAIAHRDLKSKNILVKKNGTCCIADLGLA--VRHDS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 172 LLATW-------CGSPPYAAPEVFEG----QQYEG-PQLDIWSMGVVLYVLV--CGA--------LPF-----DGPTLPI 224
Cdd:cd14143  153 ATDTIdiapnhrVGTKRYMAPEVLDDtinmKHFESfKRADIYALGLVFWEIArrCSIggihedyqLPYydlvpSDPSIEE 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 929654453 225 LRQRVLEGRFR--IPYFMSEdCEHLiRRMLVL-------DPSKRLTIAQIKE 267
Cdd:cd14143  233 MRKVVCEQKLRpnIPNRWQS-CEAL-RVMAKImrecwyaNGAARLTALRIKK 282
PTK_HER3 cd05111
Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) is a member of the EGFR ...
26-223 2.05e-13

Pseudokinase domain of the Protein Tyrosine Kinase, HER3; HER3 (ErbB3) 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. HER3 contains an impaired tyr kinase domain, which lacks crucial residues for catalytic activity against exogenous substrates but is still able to bind ATP and autophosphorylate. HER3 binds the neuregulin ligands, NRG1 and NRG2, and it relies on its heterodimerization partners for activity following ligand binding. The HER2-HER3 heterodimer constitutes a high affinity co-receptor capable of potent mitogenic signaling. HER3 participates in a signaling pathway involved in the proliferation, survival, adhesion, and motility of tumor cells. The HER3 subfamily is part of a larger superfamily that includes other pseudokinases and the the catalytic domains of active kinases such as protein serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 173656 [Multi-domain]  Cd Length: 279  Bit Score: 71.53  E-value: 2.05e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLG----RHRITKTEVAIKII-DKSQLDAvnLEKIYREVQIMKMLDHPHIIKLYQVMETKSmLYLVTEYAK 100
Cdd:cd05111   15 LGSGVFGTVHKGiwipEGDSIKIPVAIKVIqDRSGRQS--FQAVTDHMLAIGSLDHAYIVRLLGICPGAS-LQLVTQLLP 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLANHgRLNESEARRKFW--QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFF--KSGELLATW 176
Cdd:cd05111   92 LGSLLDHVRQH-RGSLGPQLLLNWcvQIAKGMYYLEEHRMVHRNLAARNVLLKSPSQVQVADFGVADLLypDDKKYFYSE 170
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 929654453 177 CGSP-PYAAPEVFEGQQYEGpQLDIWSMGVVLYVLVC-GALPFDGPTLP 223
Cdd:cd05111  171 AKTPiKWMALESIHFGKYTH-QSDVWSYGVTVWEMMTfGAEPYAGMRLA 218
STKc_CK1 cd14016
Catalytic domain of the Serine/Threonine protein kinase, Casein Kinase 1; STKs catalyze the ...
26-168 2.74e-13

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: 70.95  E-value: 2.74e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIiDKSQLDAVNLEkiyREVQIMKML-DHPHIIKLYQVMETKSMLYLVTEY-AKNGE 103
Cdd:cd14016    8 IGSGSFGEVYLGIDLKTGEEVAIKI-EKKDSKHPQLE---YEAKVYKLLqGGPGIPRLYWFGQEGDYNVMVMDLlGPSLE 83
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 929654453 104 ifDYLANHGRlnesearrKF---------WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIK---IADFGFGNFFK 168
Cdd:cd14016   84 --DLFNKCGR--------KFslktvlmlaDQMISRLEYLHSKGYIHRDIKPENFLMGLGKNSNkvyLIDFGLAKKYR 150
PTK_Jak_rpt1 cd05037
Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak ...
26-265 3.45e-13

Pseudokinase (repeat 1) domain of the Protein Tyrosine Kinases, Janus kinases; The Jak subfamily is composed of Jak1, Jak2, Jak3, TYK2, and similar proteins. They 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. The pseudokinase domain shows similarity to tyr kinases but lacks crucial residues for catalytic activity and ATP binding. It modulates the kinase activity of the C-terminal catalytic domain. In the case of Jak2, the presumed pseudokinase (repeat 1) domain exhibits dual-specificity kinase activity, phosphorylating two negative regulatory sites in Jak2: Ser523 and Tyr570. 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 serine/threonine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 270633 [Multi-domain]  Cd Length: 259  Bit Score: 70.59  E-value: 3.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHR------ITKTEVAIKIIDKSQLDAvnLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLyLVTEYA 99
Cdd:cd05037    7 LGQGTFTNIYDGILRevgdgrVQEVEVLLKVLDSDHRDI--SESFFETASLMSQISHKHLVKLYGVCVADENI-MVQEYV 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLanHGRLNESEARRKF---WQILSAVDYCHGRKIVHRDLKAENLLL------DNNMNIKIADFGFGnffkSG 170
Cdd:cd05037   84 RYGPLDKYL--RRMGNNVPLSWKLqvaKQLASALHYLEDKKLIHGNVRGRNILLaregldGYPPFIKLSDPGVP----IT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 171 ELLATWCGSP-PYAAPEVFEG-QQYEGPQLDIWSMGVVLYVLVCGAlpfDGPTLPILRQRVL---EGRFRIPYFMSEDCE 245
Cdd:cd05037  158 VLSREERVDRiPWIAPECLRNlQANLTIAADKWSFGTTLWEICSGG---EEPLSALSSQEKLqfyEDQHQLPAPDCAELA 234
                        250       260
                 ....*....|....*....|
gi 929654453 246 HLIRRMLVLDPSKRLTIAQI 265
Cdd:cd05037  235 ELIMQCWTYEPTKRPSFRAI 254
PTKc_DDR_like cd05097
Catalytic domain of Discoidin Domain Receptor-like Protein Tyrosine Kinases; PTKs catalyze the ...
46-171 4.12e-13

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: 71.16  E-value: 4.12e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  46 VAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDYLAnhgrlnESEARRKFW- 124
Cdd:cd05097   47 VAVKML-RADVTKTARNDFLKEIKIMSRLKNPNIIRLLGVCVSDDPLCMITEYMENGDLNQFLS------QREIESTFTh 119
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 929654453 125 -----------------QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE 171
Cdd:cd05097  120 annipsvsianllymavQIASGMKYLASLNFVHRDLATRNCLVGNHYTIKIADFGMSRNLYSGD 183
PTKc_HER2 cd05109
Catalytic domain of the Protein Tyrosine Kinase, HER2; PTKs catalyze the transfer of the ...
26-219 4.50e-13

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: 70.82  E-value: 4.50e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLG----RHRITKTEVAIKIIDKSQLDAVNLEkIYREVQIMKMLDHPHIIKLYQVMETkSMLYLVTEYAKN 101
Cdd:cd05109   15 LGSGAFGTVYKGiwipDGENVKIPVAIKVLRENTSPKANKE-ILDEAYVMAGVGSPYVCRLLGICLT-STVQLVTQLMPY 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYL-ANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGEL-LATWCGS 179
Cdd:cd05109   93 GCLLDYVrENKDRIGSQDLLNWCVQIAKGMSYLEEVRLVHRDLAARNVLVKSPNHVKITDFGLARLLDIDETeYHADGGK 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 929654453 180 PP--YAAPEVFEGQQYEGpQLDIWSMGVVLYVLVC-GALPFDG 219
Cdd:cd05109  173 VPikWMALESILHRRFTH-QSDVWSYGVTVWELMTfGAKPYDG 214
PTKc_Mer cd14204
Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the ...
26-274 4.88e-13

Catalytic Domain of the Protein Tyrosine Kinase, Mer; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Mer (or Mertk) is named after its original reported expression pattern (monocytes, epithelial, and reproductive tissues). It is required for the ingestion of apoptotic cells by phagocytes such as macrophages, retinal pigment epithelial cells, and dendritic cells. Mer is also important in maintaining immune homeostasis. Mer is a member of the TAM subfamily, composed of receptor PTKs (RTKs) containing an extracellular ligand-binding region with two immunoglobulin-like domains followed by two fibronectin type III repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands, Gas6 and protein S, leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. The Mer 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: 271106 [Multi-domain]  Cd Length: 284  Bit Score: 70.73  E-value: 4.88e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRI---TKTEVAIKIIDKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQV-METKSMLY----LVTE 97
Cdd:cd14204   15 LGEGEFGSVMEGELQQpdgTNHKVAVKTMKLDNFSQREIEEFLSEAACMKDFNHPNVIRLLGVcLEVGSQRIpkpmVILP 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYLAnHGRLNES------EARRKFW-QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF------G 164
Cdd:cd14204   95 FMKYGDLHSFLL-RSRLGSGpqhvplQTLLKFMiDIALGMEYLSSRNFLHRDLAARNCMLRDDMTVCVADFGLskkiysG 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 165 NFFKSGELLATwcgSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLPILRQRVLEG-RFRIPYFMSE 242
Cdd:cd14204  174 DYYRQGRIAKM---PVKWIAVESLADRVYT-VKSDVWAFGVTMWEIATrGMTPYPGVQNHEIYDYLLHGhRLKQPEDCLD 249
                        250       260       270
                 ....*....|....*....|....*....|..
gi 929654453 243 DCEHLIRRMLVLDPSKRLTIAQIKEHKWMLIE 274
Cdd:cd14204  250 ELYDIMYSCWRSDPTDRPTFTQLRENLEKLLE 281
PTKc_Met_Ron cd05058
Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of ...
26-217 5.16e-13

Catalytic domain of the Protein Tyrosine Kinases, Met and Ron; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Met and Ron are receptor PTKs (RTKs) composed of an alpha-beta heterodimer. The extracellular alpha chain is disulfide linked to the beta chain, which contains an extracellular ligand-binding region with a sema domain, a PSI domain and four IPT repeats, a transmembrane segment, and an intracellular catalytic domain. Binding to their ligands leads to receptor dimerization, autophosphorylation, activation, and intracellular signaling. Met binds to the ligand, hepatocyte growth factor/scatter factor (HGF/SF), and is also called the HGF receptor. HGF/Met signaling plays a role in growth, transformation, cell motility, invasion, metastasis, angiogenesis, wound healing, and tissue regeneration. Aberrant expression of Met through mutations or gene amplification is associated with many human cancers including hereditary papillary renal and gastric carcinomas. The ligand for Ron is macrophage stimulating protein (MSP). Ron signaling is important in regulating cell motility, adhesion, proliferation, and apoptosis. Aberrant Ron expression is implicated in tumorigenesis and metastasis. The Met/Ron 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: 270649 [Multi-domain]  Cd Length: 262  Bit Score: 70.20  E-value: 5.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRIT---KTEVAIKIIDKSQlDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVT-EYAKN 101
Cdd:cd05058    3 IGKGHFGCVYHGTLIDSdgqKIHCAVKSLNRIT-DIEEVEQFLKEGIIMKDFSHPNVLSLLGICLPSEGSPLVVlPYMKH 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 102 GEIFDYLANHGRLNESEARRKF-WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG------NFF-----KS 169
Cdd:cd05058   82 GDLRNFIRSETHNPTVKDLIGFgLQVAKGMEYLASKKFVHRDLAARNCMLDESFTVKVADFGLArdiydkEYYsvhnhTG 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 929654453 170 GELLATWcgsppyAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPF 217
Cdd:cd05058  162 AKLPVKW------MALESLQTQKFT-TKSDVWSFGVLLWELMTrGAPPY 203
PKc_DYRK4 cd14225
Catalytic domain of the protein kinase, Dual-specificity tYrosine-phosphorylated and ...
20-271 5.70e-13

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: 71.27  E-value: 5.70e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFA-VVKLGRHRiTKTEVAIKIIdksqldaVNLEKIYR----EVQIMKMLDHPHIIKLYQVMETKSMLYL 94
Cdd:cd14225   45 YEILEVIGKGSFGqVVKALDHK-TNEHVAIKII-------RNKKRFHHqalvEVKILDALRRKDRDNSHNVIHMKEYFYF 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  95 VTEYAKNGEI-----FDYLANHGRLNESEA--RRKFWQILSAVDYCHGRKIVHRDLKAENLLLDN--NMNIKIADFGFGN 165
Cdd:cd14225  117 RNHLCITFELlgmnlYELIKKNNFQGFSLSliRRFAISLLQCLRLLYRERIIHCDLKPENILLRQrgQSSIKVIDFGSSC 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 166 FfkSGELLATWCGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALPFDG----------------PTLPIL---- 225
Cdd:cd14225  197 Y--EHQRVYTYIQSRFYRSPEVILGLPY-SMAIDMWSLGCILAELYTGYPLFPGeneveqlacimevlglPPPELIenaq 273
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 226 RQRVL-------------EGRFRIPyfMSEDCEH-----------LIRRMLVLDPSKRLTIAQIKEHKWM 271
Cdd:cd14225  274 RRRLFfdskgnprcitnsKGKKRRP--NSKDLASalktsdplfldFIRRCLEWDPSKRMTPDEALQHEWI 341
PKc_LIMK_like_unk cd14156
Catalytic domain of an unknown subfamily of LIM domain kinase-like protein kinases; PKs ...
26-223 7.37e-13

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: 69.47  E-value: 7.37e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKTEVAIKIIDKSqldaVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIF 105
Cdd:cd14156    1 IGSGFFSKVYKVTHGATGKVMVVKIYKND----VDQHKIVREISLLQKLSHPNIVRYLGICVKDEKLHPILEYVSGGCLE 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 106 DYLANHG-RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIK---IADFGFGNFF-----KSGELLATW 176
Cdd:cd14156   77 ELLAREElPLSWREKVELACDISRGMVYLHSKNIYHRDLNSKNCLIRVTPRGReavVTDFGLAREVgempaNDPERKLSL 156
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 929654453 177 CGSPPYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVcGALPFDGPTLP 223
Cdd:cd14156  157 VGSAFWMAPEMLRGEPYD-RKVDVFSFGIVLCEIL-ARIPADPEVLP 201
STKc_CDK6 cd07862
Catalytic domain of the Serine/Threonine Kinase, Cyclin-Dependent protein Kinase 6; STKs ...
66-207 1.05e-12

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: 69.68  E-value: 1.05e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  66 REVQIMKMLD---HPHIIKLYQV-----METKSMLYLVTEYAkNGEIFDYL--ANHGRLNESEARRKFWQILSAVDYCHG 135
Cdd:cd07862   50 REVAVLRHLEtfeHPNVVRLFDVctvsrTDRETKLTLVFEHV-DQDLTTYLdkVPEPGVPTETIKDMMFQLLRGLDFLHS 128
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 929654453 136 RKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLATWCGSPPYAAPEVFEGQQYEGPqLDIWSMGVVL 207
Cdd:cd07862  129 HRVVHRDLKPQNILVTSSGQIKLADFGLARIYSFQMALTSVVVTLWYRAPEVLLQSSYATP-VDLWSVGCIF 199
PKc_CLK2 cd14215
Catalytic domain of the Dual-specificity protein kinase, CDC-like kinase 2; Dual-specificity ...
20-268 1.13e-12

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: 70.05  E-value: 1.13e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  20 YDIEGTLGKGNFA-VVKLGRHRITKTEVAIKII-------DKSQLDAVNLEKIYRE--------VQIMKMLD-HPHIIKL 82
Cdd:cd14215   14 YEIVSTLGEGTFGrVVQCIDHRRGGARVALKIIknvekykEAARLEINVLEKINEKdpenknlcVQMFDWFDyHGHMCIS 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  83 YQVMETKSMLYLvteyaKNGEIFDYLANhgrlnesEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDN---------- 152
Cdd:cd14215   94 FELLGLSTFDFL-----KENNYLPYPIH-------QVRHMAFQVCQAVKFLHDNKLTHTDLKPENILFVNsdyeltynle 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 153 ---------NMNIKIADFGFGNFfkSGELLATWCGSPPYAAPEVFEGQQYEGPqLDIWSMGVVLYVLVCGALPF---DGP 220
Cdd:cd14215  162 kkrdersvkSTAIRVVDFGSATF--DHEHHSTIVSTRHYRAPEVILELGWSQP-CDVWSIGCIIFEYYVGFTLFqthDNR 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 221 TLPILRQRVL-----------------------------EGRFRIP-------YFMSEDCEH-----LIRRMLVLDPSKR 259
Cdd:cd14215  239 EHLAMMERILgpipsrmirktrkqkyfyhgrldwdentsAGRYVREnckplrrYLTSEAEEHhqlfdLIESMLEYEPSKR 318

                 ....*....
gi 929654453 260 LTIAQIKEH 268
Cdd:cd14215  319 LTLAAALKH 327
STKc_BMPR1a cd14220
Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; ...
26-267 1.91e-12

Catalytic domain of the Serine/Threonine Kinase, Bone Morphogenetic Protein Type IA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. BMPR1a, also called Activin receptor-Like Kinase 3 (ALK3), functions as a receptor for bone 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. Germline mutations in BMPR1a are associated with an increased risk to Juvenile Polyposis Syndrome, a hamartomatous disorder that may lead to gastrointestinal cancer. BMPR1a may also play an indirect role in the development of hematopoietic stem cells (HSCs) as osteoblasts are a major component of the HSC niche within the bone marrow. BMPR1a belongs to a group of receptors for the TGFbeta family of secreted signaling molecules that includes TGFbeta, BMPs, 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 BMPR1a, 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 BMPR1a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271122 [Multi-domain]  Cd Length: 287  Bit Score: 68.91  E-value: 1.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHRITKteVAIKIIDKSQLDAvnlekIYREVQIMK--MLDHPHIIKLYQV----METKSMLYLVTEYA 99
Cdd:cd14220    3 IGKGRYGEVWMGKWRGEK--VAVKVFFTTEEAS-----WFRETEIYQtvLMRHENILGFIAAdikgTGSWTQLYLITDYH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRLNESEARRKFwqiLSAVDYCH---------GR-KIVHRDLKAENLLLDNNMNIKIADFGFGNFFKS 169
Cdd:cd14220   76 ENGSLYDFLKCTTLDTRALLKLAY---SAACGLCHlhteiygtqGKpAIAHRDLKSKNILIKKNGTCCIADLGLAVKFNS 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 170 --GEL---LATWCGSPPYAAPEVFE---GQQYEGPQL--DIWSMGVVLYVL----VCGA------LPF-----DGPTLPI 224
Cdd:cd14220  153 dtNEVdvpLNTRVGTKRYMAPEVLDeslNKNHFQAYImaDIYSFGLIIWEMarrcVTGGiveeyqLPYydmvpSDPSYED 232
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 929654453 225 LRQRVLEGRFRIPYFMSEDCEHLIRRMLVL-------DPSKRLTIAQIKE 267
Cdd:cd14220  233 MREVVCVKRLRPTVSNRWNSDECLRAVLKLmsecwahNPASRLTALRIKK 282
PTKc_DDR cd05051
Catalytic domain of the Protein Tyrosine Kinases, Discoidin Domain Receptors; PTKs catalyze ...
40-208 2.09e-12

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: 68.90  E-value: 2.09e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  40 RITKTEVAIKIIdKSQLDAVNLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDYLANH-GRLNESE 118
Cdd:cd05051   43 KDEPVLVAVKML-RPDASKNAREDFLKEVKIMSQLKDPNIVRLLGVCTRDEPLCMIVEYMENGDLNQFLQKHeAETQGAS 121
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 119 ARRKFW-----------QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE---------LLATWcg 178
Cdd:cd05051  122 ATNSKTlsygtllymatQIASGMKYLESLNFVHRDLATRNCLVGPNYTIKIADFGMSRNLYSGDyyriegravLPIRW-- 199
                        170       180       190
                 ....*....|....*....|....*....|
gi 929654453 179 sppyAAPEVFEGQQYEgPQLDIWSMGVVLY 208
Cdd:cd05051  200 ----MAWESILLGKFT-TKSDVWAFGVTLW 224
PTKc_VEGFR2 cd05103
Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; ...
124-268 3.73e-12

Catalytic domain of the Protein Tyrosine Kinase, Vascular Endothelial Growth Factor Receptor 2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. VEGFR2 (or Flk1) binds the ligands VEGFA, VEGFC, VEGFD and VEGFE. VEGFR2 signaling is implicated in all aspects of normal and pathological vascular endothelial cell biology. It induces a variety of cellular effects including migration, survival, and proliferation. It is critical in regulating embryonic vascular development and angiogenesis. VEGFR2 is the major signal transducer in pathological angiogenesis including cancer and diabetic retinopathy, and is a target for inhibition in cancer therapy. The carboxyl terminus of VEGFR2 plays an important role in its autophosphorylation and activation. VEGFR2 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 VEGFR2 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: 270681 [Multi-domain]  Cd Length: 343  Bit Score: 68.85  E-value: 3.73e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 124 WQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG-NFFKSGELLATWCGSPP--YAAPEVFEGQQYEgPQLDI 200
Cdd:cd05103  186 FQVAKGMEFLASRKCIHRDLAARNILLSENNVVKICDFGLArDIYKDPDYVRKGDARLPlkWMAPETIFDRVYT-IQSDV 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 201 WSMGVVLY-VLVCGALPFdgPTLPILRQ---RVLEG-RFRIP-YFMSE------DCEHlirrmlvLDPSKRLTIAQIKEH 268
Cdd:cd05103  265 WSFGVLLWeIFSLGASPY--PGVKIDEEfcrRLKEGtRMRAPdYTTPEmyqtmlDCWH-------GEPSQRPTFSELVEH 335
PHA03210 PHA03210
serine/threonine kinase US3; Provisional
42-211 3.78e-12

serine/threonine kinase US3; Provisional


Pssm-ID: 165476 [Multi-domain]  Cd Length: 501  Bit Score: 69.72  E-value: 3.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  42 TKTEVAIKIIDKSQLdAVNLEKiyrEVQIMKMLDHPHIIKLYQVMETKSMLYLVTEyAKNGEIFDYLANHG-----RLNE 116
Cdd:PHA03210 192 CERLIAKRVKAGSRA-AIQLEN---EILALGRLNHENILKIEEILRSEANTYMITQ-KYDFDLYSFMYDEAfdwkdRPLL 266
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 117 SEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGELLAT--WCGSPPYAAPEVFEGQQYe 194
Cdd:PHA03210 267 KQTRAIMKQLLCAVEYIHDKKLIHRDIKLENIFLNCDGKIVLGDFGTAMPFEKEREAFDygWVGTVATNSPEILAGDGY- 345
                        170
                 ....*....|....*..
gi 929654453 195 GPQLDIWSMGVVLYVLV 211
Cdd:PHA03210 346 CEITDIWSCGLILLDML 362
PTKc_TrkC cd05094
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase C; PTKs catalyze ...
26-267 3.80e-12

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: 68.11  E-value: 3.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGR-HRITKTE----VAIKIIDKSQLDAvnLEKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAK 100
Cdd:cd05094   13 LGEGAFGKVFLAEcYNLSPTKdkmlVAVKTLKDPTLAA--RKDFQREAELLTNLQHDHIVKFYGVCGDGDPLIMVFEYMK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 101 NGEIFDYLANH----------------GRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG 164
Cdd:cd05094   91 HGDLNKFLRAHgpdamilvdgqprqakGELGLSQMLHIATQIASGMVYLASQHFVHRDLATRNCLVGANLLVKIGDFGMS 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 165 ------NFFKSG---ELLATWcgsppyAAPEVFEGQQYEgPQLDIWSMGVVLY-VLVCGALPFD--GPTLP---ILRQRV 229
Cdd:cd05094  171 rdvystDYYRVGghtMLPIRW------MPPESIMYRKFT-TESDVWSFGVILWeIFTYGKQPWFqlSNTEViecITQGRV 243
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 929654453 230 LEGrfriPYFMSEDCEHLIRRMLVLDPSKRLTIAQIKE 267
Cdd:cd05094  244 LER----PRVCPKEVYDIMLGCWQREPQQRLNIKEIYK 277
STKc_ACVR2b cd14140
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the ...
92-220 4.46e-12

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIB Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2b (or ActRIIB) 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. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors 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. The ACVR2b subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271042 [Multi-domain]  Cd Length: 291  Bit Score: 67.75  E-value: 4.46e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  92 LYLVTEYAKNGEIFDYLANHG-------RLNESEARRKFWqILSAVDYCHGR----KIVHRDLKAENLLLDNNMNIKIAD 160
Cdd:cd14140   68 LWLITAFHDKGSLTDYLKGNIvswnelcHIAETMARGLSY-LHEDVPRCKGEghkpAIAHRDFKSKNVLLKNDLTAVLAD 146
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 929654453 161 FGFGNFFKSGELLAT---WCGSPPYAAPEVFEG----QQYEGPQLDIWSMGVVLYVLVCGALPFDGP 220
Cdd:cd14140  147 FGLAVRFEPGKPPGDthgQVGTRRYMAPEVLEGainfQRDSFLRIDMYAMGLVLWELVSRCKAADGP 213
PTKc_Tie2 cd05088
Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the ...
23-265 4.54e-12

Catalytic domain of the Protein Tyrosine Kinase, Tie2; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Tie2 is a receptor PTK (RTK) containing an extracellular region, a transmembrane segment, and an intracellular catalytic domain. The extracellular region contains an immunoglobulin (Ig)-like domain, three epidermal growth factor (EGF)-like domains, a second Ig-like domain, and three fibronectin type III repeats. Tie2 is expressed mainly in endothelial cells and hematopoietic stem cells. It is also found in a subset of tumor-associated monocytes and eosinophils. The angiopoietins (Ang-1 to Ang-4) serve as ligands for Tie2. The binding of Ang-1 to Tie2 leads to receptor autophosphorylation and activation, promoting cell migration and survival. In contrast, Ang-2 binding to Tie2 does not result in the same response, suggesting that Ang-2 may function as an antagonist. Tie2 signaling plays key regulatory roles in vascular integrity and quiescence, and in inflammation. The Tie2 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: 133219 [Multi-domain]  Cd Length: 303  Bit Score: 68.10  E-value: 4.54e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  23 EGTLGKGNFAVVKLGRHRIT--KTEVAIKIIdKSQLDAVNLEKIYREVQIM-KMLDHPHIIKLYQVMETKSMLYLVTEYA 99
Cdd:cd05088   12 QDVIGEGNFGQVLKARIKKDglRMDAAIKRM-KEYASKDDHRDFAGELEVLcKLGHHPNIINLLGACEHRGYLYLAIEYA 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHGRL---------NESEARRKFWQILS-------AVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF 163
Cdd:cd05088   91 PHGNLLDFLRKSRVLetdpafaiaNSTASTLSSQQLLHfaadvarGMDYLSQKQFIHRDLAARNILVGENYVAKIADFGL 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 164 GN----FFKS--GELLATWcgsppyAAPEVFEGQQYEgPQLDIWSMGVVLYVLVC-GALPFDGPTLPILRQRVLEG-RFR 235
Cdd:cd05088  171 SRgqevYVKKtmGRLPVRW------MAIESLNYSVYT-TNSDVWSYGVLLWEIVSlGGTPYCGMTCAELYEKLPQGyRLE 243
                        250       260       270
                 ....*....|....*....|....*....|
gi 929654453 236 IPYFMSEDCEHLIRRMLVLDPSKRLTIAQI 265
Cdd:cd05088  244 KPLNCDDEVYDLMRQCWREKPYERPSFAQI 273
STKc_BMPR2_AMHR2 cd14054
Catalytic domain of the Serine/Threonine Kinases, Bone Morphogenetic Protein and ...
26-208 1.10e-11

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: 66.62  E-value: 1.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRhrITKTEVAIKII-DKSQLDAVNLEKIYRevqiMKMLDHPHIIKLY-----QVMETKSMLYLVTEYA 99
Cdd:cd14054    3 IGQGRYGTVWKGS--LDERPVAVKVFpARHRQNFQNEKDIYE----LPLMEHSNILRFIgaderPTADGRMEYLLVLEYA 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 100 KNGEIFDYLANHgRLNESEARRKFWQILSAVDYCHGRK---------IVHRDLKAENLLLDNNMNIKIADFGF-----GN 165
Cdd:cd14054   77 PKGSLCSYLREN-TLDWMSSCRMALSLTRGLAYLHTDLrrgdqykpaIAHRDLNSRNVLVKADGSCVICDFGLamvlrGS 155
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 929654453 166 FFKSGELLA------TWCGSPPYAAPEVFEG----QQYEGP--QLDIWSMGVVLY 208
Cdd:cd14054  156 SLVRGRPGAaenasiSEVGTLRYMAPEVLEGavnlRDCESAlkQVDVYALGLVLW 210
UBA_SIK3 cd14410
UBA domain found in salt-inducible kinase 3 (SIK3); SIK3, also called salt-inducible kinase 3 ...
297-341 1.30e-11

UBA domain found in salt-inducible kinase 3 (SIK3); SIK3, also called salt-inducible kinase 3 or serine/threonine-protein kinase QSK, is a serine/threonine kinase ubiquitously expressed. It belongs to the AMP-activated protein kinases (AMPK) family involved in the regulation of metabolism during energy stress. It acts as a novel energy regulator that modulates cholesterol and bile acid metabolism by coupling with retinoid metabolism. It also play an essential role in facilitating chondrocyte hypertrophy during skeletogenesis and growth plate maintenance. SIK3 contains an N-terminal protein kinase catalytic domain followed by an ubiquitin-associated (UBA) domain.


Pssm-ID: 270593  Cd Length: 45  Bit Score: 60.03  E-value: 1.30e-11
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 297 NEQVLRLMHSLGIDQQKTIESLQNKSYNHFAAIYFLLVERLKSHR 341
Cdd:cd14410    1 NEQVLLAMAEMGLDRERTLQSLRADAYDHYSAIYSLLCDRLKRHK 45
STKc_CDC2L6 cd07867
Catalytic domain of Serine/Threonine Kinase, Cell Division Cycle 2-like 6; STKs catalyze the ...
19-211 1.71e-11

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: 66.63  E-value: 1.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  19 FYDIEG-TLGKGNFAVVKLGRHRITK--TEVAIKIIDKSQLDAvnleKIYREVQIMKMLDHPHIIKLYQVMETKS--MLY 93
Cdd:cd07867    2 LFEYEGcKVGRGTYGHVYKAKRKDGKdeKEYALKQIEGTGISM----SACREIALLRELKHPNVIALQKVFLSHSdrKVW 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  94 LVTEYAKNgEIFDYLANHG---------RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL----DNNMNIKIAD 160
Cdd:cd07867   78 LLFDYAEH-DLWHIIKFHRaskankkpmQLPRSMVKSLLYQILDGIHYLHANWVLHRDLKPANILVmgegPERGRVKIAD 156
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 929654453 161 FGFGNFFKSGelLATWCGSPP------YAAPEVFEGQQYEGPQLDIWSMGVVLYVLV 211
Cdd:cd07867  157 MGFARLFNSP--LKPLADLDPvvvtfwYRAPELLLGARHYTKAIDIWAIGCIFAELL 211
PTKc_TrkB cd05093
Catalytic domain of the Protein Tyrosine Kinase, Tropomyosin Related Kinase B; PTKs catalyze ...
26-208 2.00e-11

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: 65.83  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGR-HRITKTEVAIKIIDKSQLDAVNLEK--IYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd05093   13 LGEGAFGKVFLAEcYNLCPEQDKILVAVKTLKDASDNARkdFHREAELLTNLQHEHIVKFYGVCVEGDPLIMVFEYMKHG 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHG-------------RLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFG----- 164
Cdd:cd05093   93 DLNKFLRAHGpdavlmaegnrpaELTQSQMLHIAQQIAAGMVYLASQHFVHRDLATRNCLVGENLLVKIGDFGMSrdvys 172
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 929654453 165 -NFFKSG---ELLATWcgsppyAAPEVFEGQQYEgPQLDIWSMGVVLY 208
Cdd:cd05093  173 tDYYRVGghtMLPIRW------MPPESIMYRKFT-TESDVWSLGVVLW 213
STKc_ACVR2a cd14141
Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the ...
92-220 2.20e-11

Catalytic domain of the Serine/Threonine Kinase, Activin Type IIA Receptor; STKs catalyze the transfer of the gamma-phosphoryl group from ATP to serine/threonine residues on protein substrates. ACVR2a (or ActRIIA) 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. ACVR2b is one of two ACVR2 receptors found in vertebrates. Type II receptors 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. The ACVR2a subfamily is part of a larger superfamily that includes the catalytic domains of other STKs, protein tyrosine kinases, RIO kinases, aminoglycoside phosphotransferase, choline kinase, and phosphoinositide 3-kinase.


Pssm-ID: 271043 [Multi-domain]  Cd Length: 290  Bit Score: 65.83  E-value: 2.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  92 LYLVTEYAKNGEIFDYL-ANHGRLNE------SEAR--RKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFG 162
Cdd:cd14141   68 LWLITAFHEKGSLTDYLkANVVSWNElchiaqTMARglAYLHEDIPGLKDGHKPAIAHRDIKSKNVLLKNNLTACIADFG 147
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 929654453 163 FGNFFKSGELLAT---WCGSPPYAAPEVFEG----QQYEGPQLDIWSMGVVLYVLVCGALPFDGP 220
Cdd:cd14141  148 LALKFEAGKSAGDthgQVGTRRYMAPEVLEGainfQRDAFLRIDMYAMGLVLWELASRCTASDGP 212
PTKc_DDR1 cd05096
Catalytic domain of the Protein Tyrosine Kinase, Discoidin Domain Receptor 1; PTKs catalyze ...
46-217 2.37e-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: 65.73  E-value: 2.37e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  46 VAIKII--DKSQlDAVNleKIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDYLANHgRLNESEARRKF 123
Cdd:cd05096   49 VAVKILrpDANK-NARN--DFLKEVKILSRLKDPNIIRLLGVCVDEDPLCMITEYMENGDLNQFLSSH-HLDDKEENGND 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 124 W--------------------QILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGFGNFFKSGE---------LLA 174
Cdd:cd05096  125 AvppahclpaisyssllhvalQIASGMKYLSSLNFVHRDLATRNCLVGENLTIKIADFGMSRNLYAGDyyriqgravLPI 204
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 929654453 175 TWcgsppYAAPEVFEGQQYEGPqlDIWSMGVVLY--VLVCGALPF 217
Cdd:cd05096  205 RW-----MAWECILMGKFTTAS--DVWAFGVTLWeiLMLCKEQPY 242
STKc_MAP3K8 cd13995
Catalytic domain of the Serine/Threonine kinase, Mitogen-Activated Protein Kinase (MAPK) ...
28-269 3.01e-11

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: 64.65  E-value: 3.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  28 KGNFAVVKLGRHRITKTEVAIKIIDKSQLDAvnlekiyREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNGEIFDY 107
Cdd:cd13995   14 RGAFGKVYLAQDTKTKKRMACKLIPVEQFKP-------SDVEIQACFRHENIAELYGALLWEETVHLFMEAGEGGSVLEK 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 108 LANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLLdnnMNIK--IADFGFG-----NFFKSGELLatwcGSP 180
Cdd:cd13995   87 LESCGPMREFEIIWVTKHVLKGLDFLHSKNIIHHDIKPSNIVF---MSTKavLVDFGLSvqmteDVYVPKDLR----GTE 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 181 PYAAPEVFEGQQYEgPQLDIWSMGVVLYVLVCGALPFDG-------PT-LPILRQRV--LEGrfripyfMSEDCEHLIRR 250
Cdd:cd13995  160 IYMSPEVILCRGHN-TKADIYSLGATIIHMQTGSPPWVRryprsayPSyLYIIHKQAppLED-------IAQDCSPAMRE 231
                        250       260
                 ....*....|....*....|...
gi 929654453 251 M----LVLDPSKRLTIAQIKEHK 269
Cdd:cd13995  232 LleaaLERNPNHRSSAAELLKHE 254
PTKc_InsR cd05061
Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer ...
26-267 4.11e-11

Catalytic domain of the Protein Tyrosine Kinase, Insulin Receptor; PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. InsR is a receptor PTK (RTK) that is composed of two alphabeta heterodimers. Binding of the insulin ligand 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 signaling plays an important role in many cellular processes including glucose homeostasis, glycogen synthesis, lipid and protein metabolism, ion and amino acid transport, cell cycle and proliferation, cell differentiation, gene transcription, and nitric oxide synthesis. Insulin resistance, caused by abnormalities in InsR signaling, has been described in diabetes, hypertension, cardiovascular disease, metabolic syndrome, heart failure, and female infertility. The InsR 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: 133192 [Multi-domain]  Cd Length: 288  Bit Score: 64.99  E-value: 4.11e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  26 LGKGNFAVVKLGRHR-ITK----TEVAIKIIDKSqldAVNLEKI--YREVQIMKMLDHPHIIKLYQVMETKSMLYLVTEY 98
Cdd:cd05061   14 LGQGSFGMVYEGNARdIIKgeaeTRVAVKTVNES---ASLRERIefLNEASVMKGFTCHHVVRLLGVVSKGQPTLVVMEL 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  99 AKNGEIFDYLA--------NHGRLNES--EARRKFWQILSAVDYCHGRKIVHRDLKAENLLLDNNMNIKIADFGF----- 163
Cdd:cd05061   91 MAHGDLKSYLRslrpeaenNPGRPPPTlqEMIQMAAEIADGMAYLNAKKFVHRDLAARNCMVAHDFTVKIGDFGMtrdiy 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 164 -GNFFKSGE---LLATWcgsppyAAPEVFEGQQYEgPQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLEGRFripY 238
Cdd:cd05061  171 eTDYYRKGGkglLPVRW------MAPESLKDGVFT-TSSDMWSFGVVLWeITSLAEQPYQGLSNEQVLKFVMDGGY---L 240
                        250       260       270
                 ....*....|....*....|....*....|...
gi 929654453 239 FMSEDCEHLIRRMLVL----DPSKRLTIAQIKE 267
Cdd:cd05061  241 DQPDNCPERVTDLMRMcwqfNPKMRPTFLEIVN 273
STKc_RPK118_like cd05576
Catalytic domain of the Serine/Threonine Kinase, RPK118, and similar proteins; STKs catalyze ...
77-268 5.82e-11

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: 64.10  E-value: 5.82e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  77 PHIIKLYQVMETKSMLYLVTEYAKNGEIFDYLANHgrLNESEARRKF----------------------W--QILSAVDY 132
Cdd:cd05576   51 PNMVCLRKYIISEESVFLVLQHAEGGKLWSYLSKF--LNDKEIHQLFadlderlaaasrfyipeeciqrWaaEMVVALDA 128
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 133 CHGRKIVHRDLKAENLLLDNNMNIKIADFGfgnffKSGELLATWCG---SPPYAAPEVfEGQQYEGPQLDIWSMGVVLYV 209
Cdd:cd05576  129 LHREGIVCRDLNPNNILLNDRGHIQLTYFS-----RWSEVEDSCDSdaiENMYCAPEV-GGISEETEACDWWSLGALLFE 202
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 929654453 210 LVCGALPFDGPTLPILRQRVLEgrfrIPYFMSEDCEHLIRRMLVLDPSKRL-----TIAQIKEH 268
Cdd:cd05576  203 LLTGKALVECHPAGINTHTTLN----IPEWVSEEARSLLQQLLQFNPTERLgagvaGVEDIKSH 262
PTKc_Musk cd05050
Catalytic domain of the Protein Tyrosine Kinase, Muscle-specific kinase; PTKs catalyze the ...
23-265 7.09e-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: 64.08  E-value: 7.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  23 EGTLGKGNFAVVKLGRH-----RITKTEVAIKIIDKSQLDAVNLEkIYREVQIMKMLDHPHIIKLYQVMETKSMLYLVTE 97
Cdd:cd05050   10 VRDIGQGAFGRVFQARApgllpYEPFTMVAVKMLKEEASADMQAD-FQREAALMAEFDHPNIVKLLGVCAVGKPMCLLFE 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  98 YAKNGEIFDYL-ANHGRLNESEARRKFW---------------------QILSAVDYCHGRKIVHRDLKAENLLLDNNMN 155
Cdd:cd05050   89 YMAYGDLNEFLrHRSPRAQCSLSHSTSSarkcglnplplscteqlciakQVAAGMAYLSERKFVHRDLATRNCLVGENMV 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 156 IKIADFGFG-NFFKSGELLATWCGSPP--YAAPEVFEGQQYEgPQLDIWSMGVVLY-VLVCGALPFDGPTLPILRQRVLE 231
Cdd:cd05050  169 VKIADFGLSrNIYSADYYKASENDAIPirWMPPESIFYNRYT-TESDVWAYGVVLWeIFSYGMQPYYGMAHEEVIYYVRD 247
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 929654453 232 GR-FRIPYFMSEDCEHLIRRMLVLDPSKRLTIAQI 265
Cdd:cd05050  248 GNvLSCPDNCPLELYNLMRLCWSKLPSDRPSFASI 282
STKc_NIK cd13991
Catalytic domain of the Serine/Threonine kinase, NF-kappaB Inducing Kinase (NIK); STKs ...
23-267 8.87e-11

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: 63.68  E-value: 8.87e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453  23 EGTLGKGNFAVVKLGRHRITKTEVAIKiidKSQLDAVNLEkiyrEVQIMKMLDHPHIIKLYQVMETKSMLYLVTEYAKNG 102
Cdd:cd13991   11 QLRIGRGSFGEVHRMEDKQTGFQCAVK---KVRLEVFRAE----ELMACAGLTSPRVVPLYGAVREGPWVNIFMDLKEGG 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 103 EIFDYLANHGRLNESEARRKFWQILSAVDYCHGRKIVHRDLKAENLLL-DNNMNIKIADFGF---------------GNF 166
Cdd:cd13991   84 SLGQLIKEQGCLPEDRALHYLGQALEGLEYLHSRKILHGDVKADNVLLsSDGSDAFLCDFGHaecldpdglgkslftGDY 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 929654453 167 FKsgellatwcGSPPYAAPEVFEGQQYeGPQLDIWSMGVVLYVLVCGALP----FDGPTL-------PILRQrvlegrfr 235
Cdd:cd13991  164 IP---------GTETHMAPEVVLGKPC-DAKVDVWSSCCMMLHMLNGCHPwtqyYSGPLClkianepPPLRE-------- 225
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 929654453 236 IPyfmsEDCEHL----IRRMLVLDPSKRLTIAQIKE 267
Cdd:cd13991  226 IP----PSCAPLtaqaIQAGLRKEPVHRASAAELRR 257
 
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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